CN101128580A - Enzymes for Starch Processing - Google Patents

Abstract

The present invention relates to polypeptides having glucoamylase activity and isolated polynucleotides encoding said polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods for producing and using the polypeptides. The invention also relates to the composition comprising a glucoamylase of the invention as well as the use such compositions for starch conversion processes, brewing, including processes for producing fermentation products or syrups.

Description

Enzymes for Starch Processing

Cross-References to Sequence Listings and Deposited Microorganisms

This application contains information in the form of a Sequence Listing, which is appended to this application, and a data carrier thereof is also filed with this application. Furthermore, the present application relates to deposited microorganisms. The contents of the data carrier and the deposited microorganisms are hereby fully incorporated by reference.

Field of invention

The present invention relates to polypeptides comprising a carbohydrate binding module ("CBM") and an alpha-amylase catalytic domain. In addition, the invention relates to wild-type alpha-amylase polypeptides comprising useful alpha-amylase catalytic domains and/or CBMs, and also to catalytic domain sequences and/or CBM sequences. The invention also relates to the use of these polypeptides in a starch liquefaction process which degrades starch into smaller oligosaccharide and/or polysaccharide fragments.

Background of the invention

A number of enzymes and methods have been described for the conversion of starch into starch hydrolysates, such as maltose, glucose or specialty syrups, which are used either as sweeteners or as precursors for other sugars such as fructose. Glucose can also be fermented into ethanol or other fermentation products such as citric acid, monosodium glutamate, gluconic acid, sodium gluconate, calcium gluconate, potassium gluconate, gluconodelta lactone ), or sodium erythorbate, itaconic acid, lactic acid, gluconic acid; ketones; amino acids, glutamic acid (sodium monoglutaminate), penicillin, tetracycline; enzymes; vitamins such as riboflavin, B12 , β-carotene or hormones.

Starch is a high molecular weight polymer composed of chains of glucose units. It usually consists of about 80% amylopectin and 20% amylose. Amylopectin is a branched polysaccharide in which linear chains of α-1,4 D-glucose residues are linked by α-1,6 glycosidic bonds.

Amylose is a linear polysaccharide consisting of D-glucopyranose units linked together by α-1,4 glycosidic bonds. In the case of converting starch into soluble starch hydrolysates, the starch is depolymerized. Conventional depolymerization methods consist of a gelatinization step and two consecutive processing steps, liquefaction and saccharification.

Granular starch consists of fine granules that are insoluble in water at room temperature. When the aqueous starch slurry is heated, the granules swell and eventually rupture, dispersing the starch molecules into solution. During this "gelatinization" the viscosity increases dramatically. With solids levels of 30-40% in typical industrial processes, the starch must be diluted or "liquefied" to allow it to be processed. Today, this reduction in viscosity is mostly obtained by enzymatic degradation. During the liquefaction step, the long-chain starches are degraded by alpha-amylases into smaller branched and linear units (maltodextrins). Typically, the liquefaction process is carried out at about 105-110°C for about 5 to 10 minutes, followed by about 95°C for about 1-2 hours. The temperature is then lowered to 60°C, glucoamylase (also known as GA or AMG) or beta-amylase and optionally a debranching enzyme such as isoamylase or pullulanase are added, and the saccharification process is carried out for about 24 to 72 hours.

From the above discussion it is evident that the traditional starch conversion process is very energy intensive due to the different demands in terms of temperature during the different steps. It is therefore desirable to be able to select and/or design enzymes for the process so that the entire process can be carried out without gelatinizing the starch. US patents 4,591,560, 4,727,026, and 4,009,074, EP patent 0171218 and Danish patent application PA 2003 00949 have such "raw starch" processes. The present invention discloses polypeptides specifically designed for such processes, comprising the amino acid sequence of a CBM and the amino acid sequence of a starch degrading enzyme. Hybrid enzymes are the subject of WO9814601, WO0077165, and PCT/US2004/020499.

Summary of the invention

The inventors have surprisingly found that the activity and specificity can be altered by adding a carbohydrate binding module (CBM) to a specific alpha-amylase, thereby enhancing the efficacy of different starch degradation processes, including, for example, raw, such as non-gelatinized starch and/or degradation of gelatinized starch. Activity and specificity can also be altered by substituting one CBM for another.

These hybrids consisting of polypeptides having α-amylase activity and predominantly carbohydrate-binding modules with an affinity for starch have advantages over existing α-amylases by selecting a catalytic domain with the desired properties. To achieve, desired properties such as pH profile, temperature profile, oxidation resistance, calcium stability, substrate affinity or product profile, the catalytic domain can be combined with a carbohydrate binding module that has a stronger or Weaker binding affinity, such as specific affinity for amylose, specific affinity for amylopectin, or affinity for specific structures in carbohydrates. The present invention therefore relates to hybrids having altered properties relative to CBM-free alpha-amylases and/or relative to amylases of the prior art, such as at low pH, for example, at a pH below 4, such as at 3.5 having enhanced stability and/or activity, enhanced activity against granular starch and/or enhanced degradation of granular starch at low pH even in the absence or at low glucoamylase levels, and /or have an altered product profile.

Due to the superior hydrolytic activity of these polypeptides, the entire starch conversion process can be performed without gelatinized starch, ie the polypeptides hydrolyze granular starch in raw starch processing and fully or partially gelatinized starch in conventional starch processing.

Thus in a first aspect the invention provides a polypeptide comprising a first amino acid sequence comprising a catalytic moiety and a second amino acid sequence comprising a carbohydrate binding moiety, said catalytic moiety having alpha-amylase activity, wherein said second The amino acid sequence has at least 60% homology to any amino acid sequence selected from the group consisting of: SEQ ID NO: 52, SEQ ID NO: 76, SEQ ID NO: 78, SEQ ID NO: 80, SEQ ID NO: 82 , SEQ ID NO: 84, SEQ ID NO: 86, SEQ ID NO: 88, SEQ ID NO: 90, SEQ ID NO: 92, SEQ ID NO: 94, SEQ ID NO: 96, SEQ ID NO: 98, SEQ ID NO: 109, SEQ ID NO: 137, SEQ ID NO: 139, SEQ ID NO: 141 and SEQ ID NO: 143.

In a second aspect, the present invention provides a polypeptide having alpha-amylase activity selected from the group consisting of: (a) a polypeptide having an amino acid sequence with at least 75% homology to an amino acid of a mature polypeptide selected from the group consisting of: SEQ Amino acids 1-441 in ID NO:14, Amino acids 1-471 in SEQ ID NO:18, Amino acids 1-450 in SEQ ID NO:20, Amino acids 1-445 in SEQ ID NO:22, SEQ ID NO: Amino acids 1-498 of 26, amino acids 18-513 of SEQ ID NO:28, amino acids 1-507 of SEQ ID NO:30, amino acids 1-481 of SEQ ID NO:32, amino acids 1-481 of SEQ ID NO:34 Amino acids 1-495 of, amino acids 1-477 of SEQ ID NO:38, amino acids 1-449 of SEQ ID NO:42, amino acids 1-442 of SEQ ID NO:115, amino acids of SEQ ID NO:117 1-441, amino acids 1-477 in SEQ ID NO: 125, amino acids 1-446 in SEQ ID NO: 131, amino acids 41-481 in SEQ ID NO: 157, amino acids 22-626 in SEQ ID NO: 159, Amino acids 24-630 in SEQ ID NO: 161, amino acids 27-602 in SEQ ID NO: 163, amino acids 21-643 in SEQ ID NO: 165, amino acids 29-566 in SEQ ID NO: 167, SEQ ID NO: 169 Amino acids 22-613 in, amino acids 21-463 in SEQ ID NO: 171, amino acids 21-587 in SEQ ID NO: 173, amino acids 30-773 in SEQ ID NO: 175, amino acids 22 in SEQ ID NO: 177 -586, amino acid 20-582 in SEQ ID NO: 179, (b) the polypeptide encoded by nucleotide sequence, described nucleotide sequence (i) under at least low stringency condition and the nucleus in SEQ ID NO: 13 Nucleotides 1-1326, nucleotides 1-1413 in SEQ ID NO: 17, nucleotides 1-1350 in SEQ ID NO: 19, nucleotides 1-1338 in SEQ ID NO: 21, SEQ ID NO: Nucleotides 1-1494 of 25, nucleotides 52-1539 of SEQ ID NO:27, nucleotides 1-1521 of SEQ ID NO:29, nucleotides 1-1443 of SEQ ID NO:31 , Nucleotides 1-1485 in SEQ ID NO:33, Nucleotides 1-1431 in SEQ ID NO:37, Nucleotides 1-1347 in SEQ ID NO:41, Nucleosides in SEQ ID NO:114 Acid 1-1326, Nucleotides 1-1323 in SEQ ID NO:116, Nucleotides 1-1431 in SEQ ID NO:124, Nucleotides 1-1338 in SEQ ID NO:130, SEQ ID NO:156 Nucleotides 121-1443 in, nucleotides 64-1878 in SEQ ID NO: 158, nucleotides 70-1890 in SEQ ID NO: 160, nucleotides 79-1806 in SEQ ID NO: 162, SEQ ID NO: 162 Nucleotides 61-1929 in ID NO:164, Nucleotides 85-1701 in SEQ ID NO:166, Nucleotides 64-1842 in SEQ ID NO:168, Nucleotides 61 in SEQ ID NO:170 -1389, nucleotides 61-1764 in SEQ ID NO:172, nucleotides 61-2322 in SEQ ID NO:174, nucleotides 64-1761 in SEQ ID NO:176, nucleotides in SEQ ID NO:178 Nucleotides 58-1749 hybridize, or (ii) under conditions of at least moderate stringency to nucleotides 1-1326 in SEQ ID NO: 13, nucleotides 1-1413 in SEQ ID NO: 17, nucleosides in SEQ ID NO: 19 Acid 1-1350, Nucleotides 1-1338 in SEQ ID NO:21, Nucleotides 1-1494 in SEQ ID NO:25, Nucleotides 52-1539 in SEQ ID NO:27, Nucleotide 1 in SEQ ID NO:29 -1521, nucleotides 1-1443 in SEQ ID NO: 31, nucleotides 1-1485 in SEQ ID NO: 33, nucleotides 1-1431 in SEQ ID NO: 37, nucleotides 1-1347 in SEQ ID NO: 41, SEQ ID NO: nucleotides 1-1326 in 114, nucleotides 1-1323 in SEQ ID NO: 116, nucleotides 1-1431 in SEQ ID NO: 124, nucleotides 1-1338 in SEQ ID NO: 130, SEQ ID NO: nucleotides 121-1443 in 156, nucleotides 64-1878 in SEQ ID NO: 158, nucleotides 70-1890 in SEQ ID NO: 160, nucleotides 79-1806 in SEQ ID NO: 162, SEQ ID NO: Nucleotides 61-1929 in 164, nucleotides 85-1701 in SEQ ID NO: 166, nucleotides 64-1842 in SEQ ID NO: 168, nucleotides 61-1389 in SEQ ID NO: 170, nucleus in SEQ ID NO: 172 cDNA contained in polynucleotides shown in nucleotides 61-1764, nucleotides 61-2322 in SEQ ID NO: 174, nucleotides 64-1761 in SEQ ID NO: 176, nucleotides 58-1749 in SEQ ID NO: 178 sequence hybridization, or (iii), the complementary strand of (i) or (ii); and (c) comprising conservative substitutions, deletions, and/or insertions of one or more amino acids in an amino acid sequence selected from the group consisting of Variant: amino acids 1-441 in SEQ ID NO: 14, amino acids 1-471 in SEQ ID NO: 18, amino acids 1-450 in SEQ ID NO: 20, amino acids 1-445 in SEQ ID NO: 22 , amino acids 1-498 in SEQ ID NO:26, amino acids 18-513 in SEQ ID NO:28, amino acids 1-507 in SEQ ID NO:30, amino acids 1-481 in SEQ ID NO:32, SEQ ID NO: Amino acids 1-495 in ID NO:34, Amino acids 1-477 in SEQ ID NO:38, Amino acids 1-449 in SEQ ID NO:42, Amino acids 1-442 in SEQ ID NO:115, SEQ ID NO: Amino acids 1-441 in 117, amino acids 1-477 in SEQ ID NO: 125, amino acids 1-446 in SEQ ID NO: 131, amino acids 41-481 in SEQ ID NO: 157, amino acids in SEQ ID NO: 159 Amino acids 22-626, amino acids 24-630 in SEQ ID NO: 161, amino acids 27-602 in SEQ ID NO: 163, amino acids 21-643 in SEQ ID NO: 165, amino acids 29 in SEQ ID NO: 167 -566, amino acids 22-613 in SEQ ID NO: 169, amino acids 21-463 in SEQ ID NO: 171, amino acids 21-587 in SEQ ID NO: 173, amino acids 30-773 in SEQ ID NO: 175 , amino acids 22-586 of SEQ ID NO:177 and amino acids 20-582 of SEQ ID NO:179.

In a second aspect the present invention provides a polypeptide having carbohydrate binding affinity selected from the group consisting of: (a)i) a polypeptide comprising an amino acid sequence having at least 60% homology to a sequence selected from the group consisting of: SEQ ID NO : amino acids 529-626 of 159, amino acids 533-630 of SEQ ID NO: 161, amino acids 508-602 of SEQ ID NO: 163, amino acids 540-643 of SEQ ID NO: 165, amino acids 502-566 of SEQ ID NO: 167 , amino acids 513-613 of SEQ ID NO: 169, amino acids 492-587 of SEQ ID NO: 173, amino acids 30-287 of SEQ ID NO: 175, amino acids 487-586 of SEQ ID NO: 177, and amino acids of SEQ ID NO: 179 Amino acids 482-582; (b) a polypeptide encoded by a nucleotide sequence that hybridizes to a polynucleotide probe under low stringency conditions, and the polynucleotide probe is selected from the group consisting of: (i) selected from the group The complementary strand of the sequence: nucleotides 1585-1878 in SEQ ID NO: 158, nucleotides 1597-1890 in SEQ ID NO: 160, nucleotides 1522-1806 in SEQ ID NO: 162, SEQ ID Nucleotides 1618-1929 in NO:164, nucleotides 1504-1701 in SEQ ID NO:166, nucleotides 1537-1842 in SEQ ID NO:168, nucleotides in SEQ ID NO:172 1474-1764, nucleotides 61-861 in SEQ ID NO: 174, nucleotides 1459-1761 in SEQ ID NO: 176, and nucleotides 1444-1749 in SEQ ID NO: 178, (c) A fragment of (a) or (b) having carbohydrate binding affinity.

In other aspects the invention provides the polypeptides of the first, second and/or third aspects for use in saccharification, in a process involving fermentation, in a starch conversion process, in a process for the production of oligosaccharides, e.g. In the process of maltodextrin or glucose and/or fructose syrup, for the production of fuel or drinking ethanol, for the production of beverages, and/or for the fermentation of organic compounds such as citric acid, ascorbic acid, lysine, glutamic acid usage in the method.

In a further aspect the invention provides a composition comprising a polypeptide of the first, second and/or third aspect.

In another aspect the invention provides a method of saccharifying starch, wherein the starch is treated with the polypeptide of the first, second and/or third aspect.

In yet another aspect the invention provides a method comprising: a) contacting starch with a polypeptide comprising a catalytic moiety having alpha-amylase activity and a carbohydrate binding moiety, e.g., a first, a second and/or or the polypeptide of the third aspect; b) incubating the starch with the polypeptide; c) fermenting to produce a fermentation product, d) optionally recovering the fermentation product, wherein the enzyme with glucoamylase activity is either missing, or in the form of There is an amount less than 0.5 AGU/g DS starch substrate, and wherein steps a, b, c, and/or d can be carried out separately or simultaneously.

In another aspect the invention provides a method comprising: a) contacting a starch substrate with a yeast cell transformed to express a polypeptide comprising a catalytic moiety having alpha-amylase activity and a carbohydrate binding moiety, e.g., The polypeptide of the first and/or second aspect; b) preserving said starch substrate with said yeast; c) fermenting to produce ethanol; d) optionally recovering ethanol, wherein steps a), b), and c) separately or simultaneously. A preferred embodiment comprises maintaining said starch substrate with said yeast for a time and at a temperature sufficient to convert at least 90% w/w of said starch substrate to fermentable sugars.

In yet another aspect the present invention provides a method of producing ethanol from starch-containing material by fermentation, said method comprising: (i) liquefying said starch-containing material with a polypeptide comprising a catalytic moiety having alpha-amylase activity and a carbohydrate binding moiety, For example, a polypeptide of the first and/or second aspect; (ii) liquefied mash obtained by saccharification; (iii) fermenting the material obtained in step (ii) in the presence of a fermenting organism and optionally including recovering ethanol.

In further aspects the present invention provides a DNA sequence encoding a polypeptide according to the first, second and/or third aspect, a DNA construct comprising said DNA sequence, a recombinant expression vector carrying said DNA construct, A host cell transformed with the DNA construct or the vector, the host cell is a microorganism, especially a bacterial or fungal cell, a yeast or a plant cell.

Detailed description of the invention

The term "granular starch" is understood as raw, uncooked starch, ie starch which has not yet undergone gelatinization. Starch forms in plants as tiny water-insoluble granules. These granules are preserved in starch at temperatures below the initial gelatinization temperature. When placed in cold water, the pellets can absorb small amounts of liquid. The swelling is reversible up to 50°C to 70°C, the degree of reversibility depends on the particular starch. At higher temperatures, an irreversible swelling called gelatinization begins.

The term "initial gelatinization temperature" is understood as the lowest temperature at which starch begins to gelatinize. Starch heated in water begins to gelatinize between 50°C and 75°C, the precise temperature of gelatinization being dependent on the particular starch and readily determined by the skilled artisan. Thus, the initial gelatinization temperature may vary according to the plant species, the particular variety of the plant species, and the growing conditions. In the context of the present invention, the initial gelatinization temperature of a given starch refers to that described by Gorinstein S.and Lii.C., Starch/Störke, Vol.44(12)pp.461-466(1992) The temperature at which 5% of the birefringence in the starch granules is lost when measured by the method.

The term "soluble starch hydrolyzate" is understood as the soluble product of the process of the invention, which may comprise monosaccharides, disaccharides, and oligosaccharides, such as glucose, maltose, maltodextrin, cyclodextrin and any mixtures of these. Preferably, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or at least 98% of the dry solids of the granular starch are converted to soluble starch Hydrolyzate.

The term polypeptide "homology" is understood as the degree of identity between two sequences, which indicates that the first sequence is derived from the second sequence. This can be done by means of computer programs known in the art such as GAP provided in the GCG program package (Program Manual for the Wisconsin (Wisconsin) Program Package, 8th Edition, August 1994, Genetics Computer Group, 575 Science Drive, Madison, Wisconsin , USA 53711) suitably determine homology (Needleman, S Band Wunsch, CD, (1970), Journal of Molecular Biology, 48, 443-453). Amino acid sequence comparisons used the following settings: gap construction penalty 3.0, gap extension penalty 0.1. The relevant portion of the amino acid sequence used for homology determinations is the mature polypeptide, ie without a signal peptide. Suitable experimental conditions for determining the hybridization of a nucleotide probe to a homologous DNA or RNA sequence at low, medium, or high stringency include pre-soaking the filter containing the DNA fragment or RNA to be hybridized in 5x SSC (chlorinated Sodium/sodium citrate, Sambrook et al.1989) in 10min, filter in 5x SSC, 5x Denhardt's solution (Sambrook et al.1989), 0.5% SDS and 100 μg/ml denatured sonicated salmon sperm DNA (Sambrook et al. 1989) in the solution of prehybridization, followed by (Feinberg, AP and Vogelstein, B. (1983) Anal. Biochem. 132: 6-13), ³² P-dCTP labeled ( Specific activity >1×10 ⁹ cpm/microgram) probes were hybridized at about 45° C. for 12 hours in the same solution. The filter is then heated in 2x SSC, 0.5% SDS at about 55°C (low stringency), more preferably at about 60°C (medium stringency), still more preferably at about 65°C (medium/high stringency), still more Two washes at about 70°C (high stringency), even more preferably at about 75°C (very high stringency), are preferred.

Molecules that hybridize to the oligonucleotide probes under these conditions are detected on x-ray film.

polypeptide

A polypeptide of the invention may be a hybrid enzyme, or the polypeptide may be a wild-type enzyme that already comprises a catalytic moiety having alpha-amylase activity and a carbohydrate binding moiety. The polypeptides of the invention may also be variants of this wild-type enzyme. Hybrids can be produced by fusion of a first DNA sequence encoding a first amino acid sequence with a second DNA sequence encoding a second amino acid sequence, or hybrids can be based on knowledge of the appropriate CBM, linker and catalytic domain. Knowledge of the amino acid sequence is produced as a fully synthetic gene.

The term "hybrid enzyme" or "hybrid polypeptide" is used herein to characterize those polypeptides of the invention comprising a first amino acid sequence comprising at least one catalytic moiety and a second amino acid sequence comprising at least one carbohydrate binding moiety, so The catalytic module has alpha-amylase activity, wherein the first and second amino acid sequences are from different sources. The term "source" is understood as eg, but not limited to, a parent enzyme, such as an amylase or glucoamylase, or other catalytic activity comprising a suitable catalytic module and/or a suitable CBM and/or a suitable linker.

Enzyme classification numbers (EC numbers) are in accordance with the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (Recommendations (1992) of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology , Academic Press Inc, 1992).

Reference to polypeptides herein includes polypeptide species comprising the amino acid sequence of an alpha-amylase (EC 3.2.1.1) linked (i.e., covalently bound) to a protein comprising a carbohydrate binding module (CBM). amino acid sequence.

CBM-containing hybrid enzymes, and detailed descriptions of their preparation and purification are known in the art [see, e.g., WO 90/00609, WO 94/24158, and WO 95/16782, and Greenwood et al. Biotechnology and Bioengineering 44 (1994) pp. 1295-1305]. They can be prepared, for example, by transforming a DNA construct comprising at least a protein encoding a polypeptide of interest linked with or without a linker into a host cell and culturing the transformed host cell to express the fusion gene. DNA Sequence A DNA fragment encoding a carbohydrate binding module. The CBM in the polypeptide of the present invention can be located at the C-terminal, N-terminal or internal of the polypeptide. In one embodiment the polypeptide may comprise more than one CBM, for example, two CBMs; one at the C-terminus and the other at the N-terminus, or two CBMs in tandem at the C-terminus, N-terminus or internal. However, polypeptides with more than two CBMs are also contemplated.

Alpha-amylase of the present invention

The present invention relates to alpha-amylase polypeptides useful as CBMs, linkers and/or donors (parent amylases) for catalytic modules. The polypeptide of the invention may be a wild-type alpha-amylase (EC 3.2.1.1) or the polypeptide may be a variant of this wild-type enzyme. In addition the polypeptides of the invention may be fragments of such enzymes, e.g. the catalytic domain, i.e. a fragment having alpha-amylase activity but separated from the CBM when present in the wild-type enzyme, or e.g. the CBM, i.e. having a carbohydrate binding module fragments. It may also be a hybrid enzyme comprising a fragment of such an alpha-amylase, for example comprising a catalytic domain, a linker and/or a CBM derived from an alpha-amylase of the invention.

In addition, a polypeptide of the invention may be a fragment of such an enzyme, e.g., still comprising a functional catalytic domain and the CBM if present in said wild-type enzyme, or, e.g., a fragment of the wild-type enzyme, the wild-type type enzyme does not comprise a CBM, and wherein said fragment comprises a functional catalytic domain.

Alpha-Amylases: The present invention relates to novel polypeptides comprising a carbohydrate binding module ("CBM") and possessing alpha-amylase activity. These polypeptides may originate from any organism, preferably those of fungal or bacterial origin.

The α-amylases of the present invention include α-amylases obtainable from species selected from the group consisting of Absidia, Acremonium, Coniochaeta, Leather Coriolus, Cryptosporiopsis, Dichotomocladium, Dinemasporium, Diplodia, Fusarium, Gliocladium, Malbranchea, Ash tree Meriplilus, Necteria, Penicillium, Rhizomucor, Stereum, Streptomyces, Subulispora, Syncephalum (Syncephalastrum), Thamindium, Thermoascus, Thermomyces, Trametes, Trichophaea, and Valsaria. The alpha-amylase may be derived from any of the genus, species or sequences listed in Table 1.

Preferably said α-amylase is derived from any species selected from the group consisting of: Thermomyces lanuginosus, in particular a polypeptide having amino acids 1-441 in SEQ ID NO: 14; bacteria of the genus Malbranchea Species (Malbranchea sp.), particularly a polypeptide having amino acids 1-471 among SEQ ID NO: 18; Rhizomucor pusillus, particularly a polypeptide having amino acids 1-450 among SEQ ID NO: 20; Dichotomocladium hesseltinei, especially a polypeptide having amino acids 1-445 among SEQ ID NO: 22; Stereum sp., especially a polypeptide having amino acids 1-498 among SEQ ID NO: 26; Trametes Trametes sp., especially polypeptides having amino acids 18-513 among SEQ ID NO:28; Coriolus consors, especially having amino acids 1-507 among SEQ ID NO:30 Polypeptides; Dinemasporium sp., especially polypeptides with amino acids 1-481 in SEQ ID NO: 32; Cryptosporiopsis, especially amino acids in SEQ ID NO: 34 Polypeptides of 1-495; Diplidia sp., especially polypeptides with amino acids 1-477 in SEQ ID NO: 38; Gliocladium sp., In particular a polypeptide having amino acids 1-449 in SEQ ID NO: 42; Nectria sp., in particular a polypeptide having amino acids 1-442 in SEQ ID NO: 115; Fusarium Species of the genus (Fusarium sp.), especially a polypeptide having amino acids 1-441 among SEQ ID NO: 117; Thermoascus auranticus, especially having amino acids 1-477 among SEQ ID NO: 125 Thamindium elegans, particularly a polypeptide having amino acids 1-446 among SEQ ID NO: 131; Absidiacristatata, particularly a polypeptide having amino acids 41-481 among SEQ ID NO: 157; Acremonium sp., especially a polypeptide having amino acids 22-626 in SEQ ID NO: 159; Coniochaeta sp., especially a polypeptide having SEQ ID NO: The polypeptide of amino acid 24-630 in 161; Megaporus (Meripilus giganteus), particularly the polypeptide with amino acid 27-602 among the SEQ ID NO:163; Penicillium sp. (Penicillium sp.), particularly with SEQ ID NO: ID NO: polypeptides of amino acids 21-643 in 165; Streptomyces limosus, in particular polypeptides with amino acids 29-566 in SEQ ID NO: 167; Subulispora procurvata, in particular those in SEQ ID NO: 169 A polypeptide of amino acids 22-613 of Syncephalastrum racemosum, in particular a polypeptide having amino acids 21-463 in SEQ ID NO: 171 ; Trametes currugata, in particular a polypeptide having SEQ ID NO: A polypeptide of amino acids 21-587 in 173; Trichophaea saccata, in particular a polypeptide with amino acids 30-773 in SEQ ID NO: 175; Valsaria rubricosa, in particular a polypeptide with amino acids 22-586 in SEQ ID NO: 177 and Valsaria spartii, in particular a polypeptide having amino acids 20-582 of SEQ ID NO: 179.

It is also preferred to have at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or even at least 98% of the mature peptide of any of the aforementioned polypeptides Homologous α-amylase amino acid sequences. In another preferred embodiment, the α-amylase amino acid sequence has no more than 10 positions, no more than 9 positions, no more than 8 positions, no more than 7 positions, no more than 6 positions position, no more than 5 positions, no more than 4 positions, no more than 3 positions, no more than 2 positions, or even no more than 1 position of an amino acid different from any of the aforementioned amino acid sequences sequence.

Also preferred is an alpha-amylase amino acid sequence encoded by a DNA sequence that shares at least 50%, at least 60%, at least 65%, at least 70%, at least 75% with any sequence of a polynucleotide selected from the group consisting of %, at least 80%, at least 85%, at least 90%, at least 95%, or even at least 98% homology, said polynucleotide sequence is represented as: SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 19, SEQ ID NO: 21 , SEQ ID NO: 23, SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 29, SEQ ID NO: 31, SEQ ID NO: 33, SEQ ID NO: 35, SEQ ID NO: 37, SEQ ID NO: 39, SEQ ID NO: 41, SEQ ID NO: 43, SEQ ID NO: 110, SEQ ID NO: 112, SEQ ID NO: 114, SEQ ID NO: 116, SEQ ID NO: 118, SEQ ID NO: 120 , SEQ ID NO: 122, SEQ ID NO: 124, SEQ ID NO: 126, SEQ ID NO: 128, SEQ ID NO: 130, SEQ ID NO: 132, SEQ ID NO: 134, SEQ ID NO: 154, and SEQ ID NO: 156. SEQ ID NO: 13, SEQ ID NO: 17, SEQ ID NO: 19, SEQ ID NO: 21, SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 29, SEQ ID NO: 31, SEQ ID NO: 33, SEQ ID NO: 37, SEQ ID NO: 41, SEQ ID NO: 114, SEQ ID NO: 116, SEQ ID NO: 124, SEQ ID NO: 130, SEQ ID NO: 156, SEQ ID NO: 158. SEQ ID NO: 160, SEQ ID NO: 162, SEQ ID NO: 164, SEQ ID NO: 166, SEQ ID NO: 168, SEQ ID NO: 170, SEQ ID NO: 172, SEQ ID NO: 174, SEQ ID NO: 176 and SEQ ID NO: 178. More preferred is any alpha-amylase amino acid sequence encoded by a DNA sequence that hybridizes at low, medium, medium/high, high and/or very high stringency to any of the aforementioned alpha-amylase DNA sequences. It is also preferred that the amino acid sequence encoding an alpha-amylase has at least 50%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85% of any of the aforementioned alpha-amylase DNA sequences , at least 90%, at least 95%, at least 99%, or even 100% homologous DNA sequences.

Alpha-amylase catalytic domain: In one embodiment the invention relates to a catalytic domain derived from a polypeptide comprising a carbohydrate binding module ("CBM") and having alpha-amylase activity, such as derived from a group selected from SEQ ID NO: 14. SEQ ID NO: 18, SEQ ID NO: 20, SEQ ID NO: 22, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO: 38, SEQ ID NO: 42, SEQ ID NO: 115, SEQ ID NO: 117, SEQ ID NO: 125, SEQ ID NO: 131, SEQ ID NO: 157, SEQ ID NO: 159, SEQ ID NO: 161, SEQ ID NO: 163, SEQ ID NO: 165, SEQ ID NO: 167, SEQ ID NO: 169, SEQ ID NO: 171, SEQ ID NO: 173, SEQ ID NO: 175, SEQ ID NO: 177 and SEQ ID NO: The catalytic domain of the polypeptide of α-amylase shown in 179. Amino acids 1-441 in SEQ ID NO: 14, amino acids 1-471 in SEQ ID NO: 18, amino acids 1-450 in SEQ ID NO: 20, amino acids 1-445 in SEQ ID NO: 22, SEQ ID Amino acids 1-498 in NO:26, amino acids 18-513 in SEQ ID NO:28, amino acids 1-507 in SEQ ID NO:30, amino acids 1-481 in SEQ ID NO:32, SEQ ID NO:34 Amino acids 1-495 in, amino acids 1-477 in SEQ ID NO:38, amino acids 1-449 in SEQ ID NO:42, amino acids 1-442 in SEQ ID NO:115, amino acids 1-442 in SEQ ID NO:117 Amino acids 1-441, amino acids 1-477 in SEQ ID NO: 125, amino acids 1-446 in SEQ ID NO: 131, amino acids 41-481 in SEQ ID NO: 157, amino acids 22 in SEQ ID NO: 159 -502, amino acids 24-499 in SEQ ID NO: 161, amino acids 27-492 in SEQ ID NO: 163, amino acids 21-496 in SEQ ID NO: 165, amino acids 29-501 in SEQ ID NO: 167 , amino acids 22-487 in SEQ ID NO: 169, amino acids 21-463 in SEQ ID NO: 171, amino acids 21-477 in SEQ ID NO: 173, amino acids 288-773 in SEQ ID NO: 175, SEQ ID NO: 175 The catalytic domain represented by amino acids 22-471 in ID NO: 177 and amino acids 20-470 in SEQ ID NO: 179 is preferred. A catalytic domain having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, or even at least 95% homology to any of the aforementioned catalytic domain sequences Sequences are also preferred. In another preferred embodiment, the catalytic domain sequence has no more than 10 positions, no more than 9 positions, no more than 8 positions, no more than 7 positions, no more than 6 positions , no more than 5 positions, no more than 4 positions, no more than 3 positions, no more than 2 positions, or even no more than 1 position differs from any of the aforementioned catalytic domain sequences amino acid sequence.

It is also preferred to have at least 50%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least The amino acid sequence of the catalytic domain encoded by the DNA sequence of 95% homology, said polynucleotide is such as nucleotides 1-1326 in SEQ ID NO: 13, nucleotides 1-1413 in SEQ ID NO: 17 , nucleotides 1-1350 in SEQ ID NO: 19, nucleotides 1-1338 in SEQ ID NO: 21, nucleotides 1-1494 in SEQ ID NO: 25, nucleotides in SEQ ID NO: 27 Nucleotides 52-1539, nucleotides 1-1521 in SEQ ID NO:29, nucleotides 1-1443 in SEQ ID NO:31, nucleotides 1-1485 in SEQ ID NO:33, SEQ ID NO: Nucleotides 1-1431 in ID NO:37, Nucleotides 1-1347 in SEQ ID NO:41, Nucleotides 1-1326 in SEQ ID NO:114, Nucleosides in SEQ ID NO:116 Acid 1-1323, Nucleotides 1-1431 in SEQ ID NO:124, Nucleotides 1-1338 in SEQ ID NO:130, Nucleotides 121-1443 in SEQ ID NO:156, SEQ ID NO : nucleotides 64-1506 in 158, nucleotides 70-1497 in SEQ ID NO: 160, nucleotides 79-1476 in SEQ ID NO: 162, nucleotides 61 in SEQ ID NO: 164 -1488, nucleotides 85-1503 of SEQ ID NO:166, nucleotides 64-1461 of SEQ ID NO:168, nucleotides 61-1389 of SEQ ID NO:170, SEQ ID NO:172 Nucleotides 61-1431 in, nucleotides 862-2322 in SEQ ID NO: 174, nucleotides 64-1413 in SEQ ID NO: 176, and nucleotides 58-1410 in SEQ ID NO: 178 shown. More preferred is any catalytic domain amino acid sequence encoded by a DNA sequence that hybridizes to any of the aforementioned DNA sequences at low, medium, medium/high, high and/or very high stringency. It is also preferred that the amino acid sequence encoding the catalytic domain has at least 50%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least DNA sequences that are 90%, at least 95%, at least 99%, or even 100% homologous.

Linker sequences: In one embodiment the invention relates to linker sequences derived from polypeptides comprising a carbohydrate binding module ("CBM") and having alpha-amylase activity. Linker amino acid sequences preferably selected from the group consisting of amino acids 503-528 in SEQ ID NO: 159, amino acids 500-532 in SEQ ID NO: 161, amino acids 493-507 in SEQ ID NO: 163, SEQ ID NO : amino acids 497-539 in 165, amino acids 488-512 in SEQ ID NO: 169, amino acids 478-491 in SEQ ID NO: 173, amino acids 472-486 in SEQ ID NO: 177 and SEQ ID NO: 179 The linker amino acid sequence shown in amino acids 471-481. Linker amino acid sequences having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, or even at least 95% homology to any of the aforementioned linker sequences are also preferred . In another preferred embodiment, the linker sequence has no more than 10 positions, no more than 9 positions, no more than 8 positions, no more than 7 positions, no more than 6 positions, no more than An amino acid sequence that differs from any of the aforementioned linker sequences by more than 5 positions, by no more than 4 positions, by no more than 3 positions, by no more than 2 positions, or even by no more than 1 position.

Carbohydrate binding module: In one embodiment the present invention relates to a CBM derived from a polypeptide comprising a carbohydrate binding module ("CBM") and having alpha-amylase activity, said CBM being derived from a group selected from the group consisting of SEQ ID NO: 14, SEQ ID NO: 18, SEQ ID NO: 20, SEQ ID NO: 22, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO : 38, SEQ ID NO: 42, SEQ ID NO: 115, SEQ ID NO: 117, SEQ ID NO: 125, SEQ ID NO: 131, SEQ ID NO: 157, SEQ ID NO: 159, SEQ ID NO: 161, SEQ ID NO: 163, SEQ ID NO: 165, SEQ ID NO: 167, SEQ ID NO: 169, SEQ ID NO: 171, SEQ ID NO: 173, SEQ ID NO: 175, SEQ ID NO: 177 and SEQ ID NO: The polypeptide of α-amylase shown in 179. A CBM amino acid sequence preferably selected from the group consisting of amino acids 529-626 in SEQ ID NO: 159, amino acids 533-630 in SEQ ID NO: 161, amino acids 508-602 in SEQ ID NO: 163, amino acids 508-602 in SEQ ID NO: 163, Amino acids 540-643 in NO: 165, amino acids 502-566 in SEQ ID NO: 167, amino acids 513-613 in SEQ ID NO: 169, amino acids 492-587 in SEQ ID NO: 173, SEQ ID NO: Sequence of amino acids 30-287 in 175, amino acids 487-586 in SEQ ID NO: 177, and amino acids 482-582 in SEQ ID NO: 179. Also preferred are CBM amino acids having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, or even at least 95% homology to any of the aforementioned CBM amino acid sequences sequence. In another preferred embodiment, the CBM sequence has no more than 10 positions, no more than 9 positions, no more than 8 positions, no more than 7 positions, no more than 6 positions, no more than An amino acid sequence that differs by more than 5 positions, by no more than 4 positions, by no more than 3 positions, by no more than 2 positions, or even by no more than 1 position from any of the aforementioned CBM sequences.

It is also preferred to have at least 50%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least The CBM amino acid sequence encoded by the DNA sequence of 95% homology, said polynucleotide is as nucleotide 1585-1878 in SEQ ID NO: 158, nucleotide 1597-1890 in SEQ ID NO: 160, SEQ ID NO: Nucleotides 1522-1806 in ID NO:162, Nucleotides 1618-1929 in SEQ ID NO:164, Nucleotides 1504-1701 in SEQ ID NO:166, Nucleosides in SEQ ID NO:168 Acids 1537-1842, nucleotides 1474-1764 in SEQ ID NO: 172, nucleotides 61-861 in SEQ ID NO: 174, nucleotides 1459-1761 in SEQ ID NO: 176, and SEQ ID NO : Nucleotides 1444-1749 in 178, SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NO: 13. SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 19, SEQ ID NO: 21, SEQ ID NO: 23, SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 29, SEQ ID NO: 31, SEQ ID NO: 33, SEQ ID NO: 35, SEQ ID NO: 37, SEQ ID NO: 39, SEQ ID NO: 41, SEQ ID NO: 43, SEQ ID NO: 110, SEQ ID NO: 112. SEQ ID NO: 114, SEQ ID NO: 116, SEQ ID NO: 118, SEQ ID NO: 120, SEQ ID NO: 122, SEQ ID NO: 124, SEQ ID NO: 126, SEQ ID NO: 128, Shown in SEQ ID NO: 130, SEQ ID NO: 132, SEQ ID NO: 134, SEQ ID NO: 154 and SEQ ID NO: 156. More preferred is any CBM amino acid sequence encoded by a DNA sequence that hybridizes at low, medium, medium/high, high and/or very high stringency to the complementary DNA sequence of any of the aforementioned CBM DNA sequences. It is also preferred to encode a CBM amino acid sequence and have at least 50%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% of any of the aforementioned CBM DNA sequences %, at least 99%, or even 100% homologous DNA sequences.

The DNA sequence shown in nucleotides 1504-1701 in SEQ ID NO: 166 and nucleotides 61-861 in SEQ ID NO: 174 and the encoded amino acid sequence also includes a linker sequence in addition to the CBM.

Table 1

Alpha-amylases used as catalytic domains and CBM donors. Location of catalytic domain, linker and CBM sequences. species Strain number SEQ ID NO mature peptide catalytic domain Connector CBM type Absidia crescendo NN047841 SEQ ID NO: 156 121-1443 121-1443 DNA Absidia croupatum NN047841 SEQ ID NO: 157 41-481 41-481 amino acid Acremonium sp. NN045509 SEQ ID NO: 158 64-1878 64-1506 1507-1584 1585-1878 DNA Acremonium sp. NN045509 SEQ ID NO: 159 22-626 22-502 503-528 529-626 amino acid Species of the genus Chaetomium NN047603 SEQ ID NO: 160 70-1890 70-1497 1498-1596 1597-1890 DNA Species of the genus Chaetomium NN047603 SEQ ID NO: 161 24-630 24-499 500-532 533-630 amino acid Coriolus salmonella NN048884 SEQ ID NO: 29 1-1521 1-1521 DNA Coriolus salmonella NN048884 SEQ ID NO: 30 1-507 1-507 amino acid Species of the genus Cryptosporiopsis NN047117 SEQ ID NO: 33 1-1485 1-1485 DNA Species of the genus Cryptosporiopsis NN047117 SEQ ID NO: 34 1-495 1-495 amino acid Dichotomocladium hesseltinei NN103100 SEQ ID NO: 21 1-1338 1-1338 DNA

Dichotomocladium hesseltinei NN103100 SEQ ID NO: 22 1-445 1-445 amino acid Species of the genus Dichaete NN043050 SEQ ID NO: 31 1-1443 1-1443 DNA Species of the genus Dichaete NN043050 SEQ ID NO: 32 1-481 1-481 amino acid Species of the genus Chrodispora NN047649 SEQ ID NO: 37 1-1431 1-1431 DNA Species of the genus Chrodispora NN047649 SEQ ID NO: 38 1-477 1-477 amino acid Fusarium sp. NN046318 SEQ ID NO: 116 1-1323 1-1323 dna Fusarium sp. NN046318 SEQ ID NO: 117 1-441 1-441 amino acid Species of the genus Gliosis NN047683 SEQ ID NO: 41 1-1347 1-1347 DNA Species of the genus Gliosis NN047683 SEQ ID NO: 42 1-449 1-449 amino acid Species of the genus Malbranchea NN046840 SEQ ID NO: 17 1-1413 1-1413 DNA Species of the genus Malbranchea NN046840 SEQ ID NO: 18 1-471 1-471 amino acid Megaporus NN006040 SEQ ID NO: 162 79-1806 79-1476 1477-1521 1522-1806 DNA

Megaporus NN006040 SEQ ID NO: 163 27-602 27-492 493-507 508-602 amino acid Bacteria of the genus Cliff NN047728 SEQ ID NO: 114 1-1326 1-1326 DNA Bacteria of the genus Cliff NN047728 SEQ ID NO: 115 1-442 1-442 amino acid Penicillium species NN050730 SEQ ID NO: 164 61-1929 61-1488 1489-1617 1618-1929 DNA Penicillium species NN050730 SEQ ID NO: 165 21-643 21-496 497-539 540-643 amino acid Rhizomucor micromyces NN101459 SEQ ID NO: 19 1-1350 1-1350 DNA Rhizomucor micromyces NN101459 SEQ ID NO: 20 1-450 1-450 amino acid Bacteria of the genus Resus NN048875 SEQ ID NO: 25 1-1494 1-1494 DNA Bacteria of the genus Resus NN048875 SEQ ID NO: 26 1-498 1-498 amino acid Streptomyces militosa ATCC19778 SEQ ID NO: 166 85-1701 85-1503 ¹⁾ 1504-1701 DNA Streptomyces militosa ATCC19778 SEQ ID NO: 167 29-566 29-501 ¹⁾ 502-566 amino acid Subulispora procurvata NN042875 SEQ ID NO: 169 22-613 22-487 488-512 513-613 amino acid Subulisporaprovurvata NN042875 SEQ ID NO: 168 64-1842 64-1461 1462-1536 1537-1842 DNA

Cocephalus racemosa NN047920 SEQ ID NO: 170 61-1389 61-1389 DNA Cocephalus racemosa NN047920 SEQ ID NO: 171 21-463 21-463 amino acid Thamindiumelegans NN050372 SEQ ID NO: 130 1-1338 1-1338 DNA Thamindiumelegans NN050372 SEQ ID NO: 131 1-446 1-446 amino acid Thermoascomycetes NN047354 SEQ ID NO: 124 1-1431 1-1431 DNA Thermoascomycetes NN047354 SEQ ID NO: 125 1-477 1-477 amino acid Thermomyces lanuginosa NN044958 SEQ ID NO: 13 1-1326 1-1326 DNA Thermomyces lanuginosa NN044958 SEQ ID NO: 14 1-441 1-441 amino acid Trametes rugosa CGMCC5.61 SEQ ID NO: 172 61-1764 61-1431 1432-1473 1474-1764 DNA Trametes rugosa CGMCC5.61 SEQ ID NO: 173 21-587 21-477 478-491 492-587 amino acid Trametes species NN048968 SEQ ID NO: 27 52-1539 52-1539 DNA Trametes species NN048968 SEQ ID NO: 28 18-513 18-513 amino acid

Trichophaea saccata NN102806 SEQ ID NO: 174 61-2322 862-2322 ¹⁾ 61-861 DNA Trichophaea saccata NN102806 SEQ ID NO: 175 30-773 288-773 ¹⁾ 30-287 amino acid Valsaria rubricosa NN046835 SEQ ID NO: 176 64-1761 64-1413 1414-1458 1459-1761 DNA Valsaria rubricosa NN046835 SEQ ID NO: 177 22-586 22-471 472-486 487-586 amino acid Valsaria spartii NN050508 SEQ ID NO: 178 58-1749 58-1410 1411-1443 1444-1749 DNA Valsaria spartii NN050508 SEQ ID NO: 179 20-582 20-470 471-481 482-582 amino acid ¹⁾ The sequence contains both the CBM and the linker

Alpha-amylase polypeptides can be used in starch degradation processes and/or as donors for catalytic domains and/or CBMs of hybrid polypeptides. Preferred polypeptides of the invention, e.g., hybrid polypeptides, comprise a first amino acid sequence comprising a catalytic moiety and a second amino acid sequence comprising a carbohydrate binding moiety, said catalytic moiety having alpha-amylase activity, wherein said first The two amino acid sequences have at least 60%, at least 70%, at least 80%, at least 85%, at least 90%, such as at least 95% homology to any amino acid sequence selected from the group consisting of amino acids in SEQ ID NO: 159 529-626, amino acids 533-630 in SEQ ID NO: 161, amino acids 508-602 in SEQ ID NO: 163, amino acids 540-643 in SEQ ID NO: 165, amino acids 502-566 in SEQ ID NO: 167, Amino acids 513-613 in SEQ ID NO: 169, amino acids 492-587 in SEQ ID NO: 173, amino acids 30-287 in SEQ ID NO: 175, amino acids 487-586 in SEQ ID NO: 177 and SEQ ID NO: 179 Amino acids 482-582 in. More preferred polypeptides, e.g., hybrid polypeptides, wherein said first amino acid sequence shares at least 60%, at least 70%, at least 80%, at least 85%, at least 90%, such as at least 95% homology: amino acids 1-441 in SEQ ID NO:14, amino acids 1-471 in SEQ ID NO:18, amino acids 1-450 in SEQ ID NO:20, amino acids in SEQ ID NO:22 1-445, amino acids 1-498 in SEQ ID NO:26, amino acids 18-513 in SEQ ID NO:28, amino acids 1-507 in SEQ ID NO:30, amino acids 1-481 in SEQ ID NO:32 , amino acids 1-495 in SEQ ID NO: 34, amino acids 1-477 in SEQ ID NO: 38, amino acids 1-449 in SEQ ID NO: 42, amino acids 1-442 in SEQ ID NO: 115, SEQ ID NO: Amino acids 1-441 in ID NO:117, Amino acids 1-477 in SEQ ID NO:125, Amino acids 1-446 in SEQ ID NO:131, Amino acids 41-481 in SEQ ID NO:157, SEQ ID NO : amino acids 22-502 in 159, amino acids 24-499 in SEQ ID NO: 161, amino acids 27-492 in SEQ ID NO: 163, amino acids 21-496 in SEQ ID NO: 165, SEQ ID NO: 167 Amino acids 29-501 in, amino acids 22-487 in SEQ ID NO: 169, amino acids 21-463 in SEQ ID NO: 171, amino acids 21-477 in SEQ ID NO: 173, amino acids in SEQ ID NO: 175 Amino acids 288-773, amino acids 22-471 in SEQ ID NO: 177, and amino acids 20-470 in SEQ ID NO: 179. Also preferred are polypeptides, e.g., hybrid polypeptides, wherein a linker sequence is present at a position between said first and said second amino acid sequence, said linker sequence sharing at least 60% of any amino acid sequence selected from the group consisting of , at least 70%, at least 80%, at least 85%, at least 90%, such as at least 95% homology: amino acids 503-528 in SEQ ID NO: 159, amino acids 500-532 in SEQ ID NO: 161, SEQ ID NO: 161 Amino acids 493-507 in ID NO: 163, Amino acids 497-539 in SEQ ID NO: 165, Amino acids 488-512 in SEQ ID NO: 169, Amino acids 478-491 in SEQ ID NO: 173, SEQ ID NO : amino acids 472-486 in 177 and amino acids 471-481 in SEQ ID NO: 179.

Alpha-amylase sequence

Catalytic domains suitable for constructing polypeptides of the type according to the invention, ie alpha-amylase catalytic domains (in particular acid stable alpha-amylases) may be derived from any organism, preferably those of fungal or bacterial origin.

Preferably the alpha-amylase is a wild type enzyme. More preferably said alpha-amylase is a variant alpha-amylase comprising amino acid modifications resulting in enhanced activity, enhanced protein stability at low pH and/or high pH, enhanced stabilization against calcium depletion properties, and/or enhanced stability at elevated temperatures.

Related alpha-amylases for use in the hybrids of the present invention include alpha-amylases obtainable from species selected from the group listed below: Absidia, Acremonium, Aspergillus, Chaetomium, Trichodomonas Shell, Cryptosporiopsis, Dichotomocladium, Dichotomocladium sp., Chromospora, Fusarium, Gliocladium, Malbranchea, Meripilus, Trametes, C. Shell, Penicillium, Phanerochaete, Rhizomucor, Rhizopus, Streptomyces, Subulispora, Syncephalum, Thaminidium, Thermoascus, Thermomyces, Trametes, Trichophaea and Valsaria. The alpha-amylase catalytic domain may also be of bacterial origin, eg, Bacillus.

Preferably the amino acid sequence of the selected α-amylase is derived from any species selected from the group consisting of Absidia pilosa, species of the genus Acremonium, Aspergillus niger, Aspergillus kawachii, Aspergillus oryzae (Aspergillus oryzae), Conechaetomium sp., Conechaetomium sp., Cryptosporiopsis sp., Dichotomocladium hesseltinei, Echinocladium hesseltinei, Echinocladium sp., Chromodiospora sp. , species of Fusarium, species of Gliocladium, species of Malbranchea, species of Megaporus, species of C. , Phanerochaete chrysosporium (Phanerochaete chrysosporium), Rhizopus microspermum, Rhizopus oryzae (Rhizopus oryzae), strains of the genus Steinus, Streptomycesthermocyaneoviolaceus, Streptomyces silt, Subulispora procurvata, Cocephalus racemosa, Thaminidium elegans, Thermoascus, species of the genus Thermoascus, Thermomyces lanuginosa, Trametes rugosa, species of the genus Trametes, Trichophaea saccata, Valsaria rubricosa, Valsaria spartii, and Bacillus flavothermus (synonym: Anoxybacillus contaminans).

Preferably, the hybrid comprises an α-amylase amino acid sequence selected from the α-amylase catalytic modules listed in Table 1 or 2.

Most preferably, said hybrid comprises an α-amylase amino acid sequence selected from the group consisting of Aspergillus niger (SEQ ID NO: 2), Aspergillus oryzae (SEQ ID NO: 4 and SEQ ID NO: 6) , Trichophaea saccata (SEQ ID NO: 8), Subulispora procurvata (SEQ ID NO: 10), Valsaria rubricosa (SEQ ID NO: 12), Thermomyces lanuginosa (SEQ ID NO: 14), Acremonium Mycobacterium (SEQ ID NO: 16), the strain of Malbranchea (SEQ ID NO: 18), Rhizomucor micromus (SEQ ID NO: 20), Dichotomocladium hesseltinei (SEQ ID NO: 22), Megaporus (SEQ ID NO: 24), strain AMY1179 (SEQ ID NO: 26) of the genus Resus, strains of the genus Trametes (SEQ ID NO: 28), Coriolus censors (Coriolus censors) (SEQ ID NO: 30) , Dichaeta spinosa (SEQ ID NO: 32), Cryptosporiopsis species (SEQ ID NO: 34), Chaetomium genus (SEQ ID NO: 36), Chromospora Bacterial species (SEQ ID NO:38) of the genus Bacillus (SEQ ID NO:38), the bacterial species (SEQ ID NO:40) of the genus Gliocladium, the bacterial species (SEQ ID NO:42) of the genus Gliosis, Streptomyces thermocyaneoviolaceus (SEQ ID NO : 44), the bacterial classification II (SEQ ID NO: 111) of Thermoascus genus, the bacterial classification (SEQ ID NO: 113) of Chaetomium genus, the bacterial classification (SEQ ID NO: 115) of the genus Echinococcus genus, Fusarium sp. (SEQ ID NO: 117), Trametes rugosa (SEQ ID NO: 119), Penicillium sp. (SEQ ID NO: 121), Valsariaspartii (SEQ ID NO: 123), Thermoascus aurantiacus (SEQ ID NO: 125), Phanerochaete chrysosporium (SEQ ID NO: 127), Rhizopus oryzae (SEQ ID NO: 129), Thaminidiumelegans (SEQ ID NO: 131), Absidia chrysosporium (SEQ ID NO: 129), ID NO: 133), Syntocephalus racemosa (SEQ ID NO: 135) and Streptomyces militaris (SEQ ID NO: 155) alpha-amylase.

The present invention also preferably comprises a hybrid of an α-amylase amino acid sequence having at least 60%, at least 65%, at least 70%, at least 75%, at least 80% of any sequence selected from the group consisting of %, at least 85%, at least 90% or even at least 95% homology to: SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO : 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 20, SEQ ID NO: 22, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28 , SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO: 36, SEQ ID NO: 38, SEQ ID NO: 40, SEQ ID NO: 42, SEQ ID NO: 44, SEQ ID NO: 111, SEQ ID NO: 113, SEQ ID NO: 115, SEQ ID NO: 117, SEQ ID NO: 119, SEQ ID NO: 121, SEQ ID NO: 123, SEQ ID NO: 125, SEQ ID NO: 127 , SEQ ID NO: 129, SEQ ID NO: 131, SEQ ID NO: 133, SEQ ID NO: 135 and SEQ ID NO: 155.

In another preferred embodiment, the hybrid enzyme has no more than 10 positions, no more than 9 positions, no more than 8 positions, no more than 7 positions, no more than 6 positions, no more than An alpha-amylase sequence that is different from an amino acid sequence selected from the group consisting of more than 5 positions, no more than 4 positions, no more than 3 positions, no more than 2 positions, and no more than 1 position: SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18. SEQ ID NO: 20, SEQ ID NO: 22, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO: 36, SEQ ID NO: 38, SEQ ID NO: 40, SEQ ID NO: 42, SEQ ID NO: 44, SEQ ID NO: 111, SEQ ID NO: 113, SEQ ID NO: 115, SEQ ID NO : 117, SEQ ID NO: 119, SEQ ID NO: 121, SEQ ID NO: 123, SEQ ID NO: 125, SEQ ID NO: 127, SEQ ID NO: 129, SEQ ID NO: 131, SEQ ID NO: 133, SEQ ID NO: 135 and SEQ ID NO: 155.

Also preferred are hybrids comprising an amino acid sequence of an α-amylase having at least 50%, at least 60%, at least 65%, at least 70%, at least 75% of any sequence selected from the group consisting of , at least 80%, at least 85%, at least 90% or even at least 95% homology to: SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9. SEQ ID NO: 11, SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 19, SEQ ID NO: 21, SEQ ID NO: 23, SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 29, SEQ ID NO: 31, SEQ ID NO: 33, SEQ ID NO: 35, SEQ ID NO: 37, SEQ ID NO: 39, SEQ ID NO: 41, SEQ ID NO: 43. SEQ ID NO: 110, SEQ ID NO: 112, SEQ ID NO: 114, SEQ ID NO: 116, SEQ ID NO: 118, SEQ ID NO: 120, SEQ ID NO: 122, SEQ ID NO: 124, SEQ ID NO: 126, SEQ ID NO: 128, SEQ ID NO: 130, SEQ ID NO: 132, SEQ ID NO: 134, and SEQ ID NO: 154.

More preferred is a hybrid comprising an alpha-amylase derived from a DNA sequence that hybridizes to any DNA sequence selected from the group consisting of low, medium, medium/high, high and/or very high stringency Encoding: SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 19, SEQ ID NO: 21, SEQ ID NO: 23, SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 29, SEQ ID NO: 31, SEQ ID NO: 33. SEQ ID NO: 35, SEQ ID NO: 37, SEQ ID NO: 39, SEQ ID NO: 41, SEQ ID NO: 43, SEQ ID NO: 110, SEQ ID NO: 112, SEQ ID NO: 114, SEQ ID NO: 116, SEQ ID NO: 118, SEQ ID NO: 120, SEQ ID NO: 122, SEQ ID NO: 124, SEQ ID NO: 126, SEQ ID NO: 128, SEQ ID NO: 130, SEQ ID NO : 132, SEQ ID NO: 134 and SEQ ID NO: 154.

linker sequence

The linker sequence may be any suitable linker sequence, for example, a linker sequence derived from an alpha-amylase or a glucoamylase. The linker may be a bond, or a short linking group comprising about 2 to about 100 carbon atoms, especially 2 to 40 carbon atoms. However, the linker is preferably a sequence of about 2 to about 100 amino acid residues, more preferably 4 to 40 amino acid residues, eg 6 to 15 amino acid residues.

Preferably the hybrid comprises a linker sequence derived from any species selected from the group consisting of Acremonium, Chaetomium, Chaetomium, Meripilus, Pachykytospora , Penicillium, Sublispora, Trametes, Trichophaea, Valsaria, Athelia, Aspergillus, Trametes and Leucopaxillus. The linker may also be of bacterial origin, for example from a strain of the Bacillus species. More preferably, the linker is derived from a species selected from the group consisting of Acremonium species, Conechaetomium species, Conechaetomium species, Megapora, Penicillium species species, Sublispora provurvata, Trametes rugosa, Trichophaea saccata, Valsaiarubricosa, Valsario spartii, Aspergillus jaundice, Aspergillus niger, Athelia rolfsii, Leucopaxillus gigantus, Pachykytospora papayracea ), Trametes cingulata and Bacillus flavothermus.

Preferably, the hybrid comprises a linker amino acid sequence selected from linkers listed in Table 1 or 2.

More preferably said linker is a linker from a glucoamylase selected from the group consisting of: S. papyrus (SEQ ID NO: 46), Trametes cingularis (SEQ ID NO: 48), Pleurotus grandis (SEQ ID NO: 50), A. roerii (SEQ ID NO: 68), Aspergillus basilica (SEQ ID NO: 70), Aspergillus niger (SEQ ID NO: 72), or an α-amylase from the group selected from Linkers of: Sublispora provurvata (SEQ ID NO: 54), Valsaria rubricosa (SEQ ID NO: 56), Acremonium sp. (SEQ ID NO: 58), Megaporus (SEQ ID NO: 60), Bacillus flavothermus (SEQ ID NO: 62, SEQ ID NO: 64 or SEQ ID NO: 66), the strain AM603 (SEQ ID NO: 74) of the genus Cone Chaetomium, the bacterial strain of the genus Cone Chaetomium (SEQ ID NO: 145 ), Trametes rugosa (SEQ ID NO: 147), Valsario spartii (SEQ ID NO: 149), Penicillium species (SEQ ID NO: 151), Trichophaea saccata (SEQ ID NO: 52).

The present invention also preferably has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% homology to any sequence selected from the group Any linker amino acid sequence: SEQ ID NO: 46, SEQ ID NO: 48, SEQ ID NO: 50, SEQ ID NO: 52, SEQ ID NO: 54, SEQ ID NO: 56, SEQ ID NO: 58, SEQ ID NO : 60, SEQ ID NO: 62, SEQ ID NO: 64, SEQ ID NO: 66, SEQ ID NO: 68, SEQ ID NO: 70, SEQ ID NO: 72, SEQ ID NO: 74, SEQ ID NO: 145, SEQ ID NO: 147, SEQ ID NO: 149 and SEQ ID NO: 151.

In another preferred embodiment, the hybrid enzyme has no more than 10 positions, no more than 9 positions, no more than 8 positions, no more than 7 positions, no more than 6 positions, no more than More than 5 positions, no more than 4 positions, no more than 3 positions, no more than 2 positions, no more than 1 position is different from the linker sequence selected from the amino acid sequence of the following group: SEQ ID NO: 46. SEQ ID NO: 48, SEQ ID NO: 50, SEQ ID NO: 52, SEQ ID NO: 54, SEQ ID NO: 56, SEQ ID NO: 58, SEQ ID NO: 60, SEQ ID NO: 62, SEQ ID NO: 64, SEQ ID NO: 66, SEQ ID NO: 68, SEQ ID NO: 70, SEQ ID NO: 72, SEQ ID NO: 74, SEQ ID NO: 145, SEQ ID NO: 147, SEQ ID NO : 149 and SEQ ID NO: 151.

Also preferred is a hybrid comprising a linker sequence consisting of at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% of any sequence selected from the group consisting of % or even at least 95% homologous DNA sequences encoded by: SEQ ID NO: 45, SEQ ID NO: 47, SEQ ID NO: 49, SEQ ID NO: 51, SEQ ID NO: 53, SEQ ID NO: 55, SEQ ID NO: 57, SEQ ID NO: 59, SEQ ID NO: 61, SEQ ID NO: 63, SEQ ID NO: 65, SEQ ID NO: 67, SEQ ID NO: 69, SEQ ID NO: 71, SEQ ID NO : 73, SEQ ID NO: 144, SEQ ID NO: 146, SEQ ID NO: 148, and SEQ ID NO: 150.

More preferred is a hybrid comprising a linker sequence encoded by a DNA sequence that hybridizes to any DNA sequence selected from the group consisting of high, medium or low stringency: SEQ ID NO: 45, SEQ ID NO: 47 , SEQ ID NO: 49, SEQ ID NO: 51, SEQ ID NO: 53, SEQ ID NO: 55, SEQ ID NO: 57, SEQ ID NO: 59, SEQ ID NO: 61, SEQ ID NO: 63, SEQ ID NO: 65, SEQ ID NO: 67, SEQ ID NO: 69, SEQ ID NO: 71, SEQ ID NO: 73, SEQ ID NO: 144, SEQ ID NO: 146, SEQ ID NO: 148, and SEQ ID NO: 150.

In a preferred embodiment a linker originating from a CBM source is used, for example, when using a CBM from A. raciferi glucoamylase, a linker sequence from A. racii glucoamylase is also used for the hybrid.

carbohydrate binding module

A carbohydrate binding module (CBM), or commonly referred to as a carbohydrate binding domain (CBM), refers to the preferential binding of polysaccharides or oligosaccharides (carbohydrates), often - but not necessarily exclusively - their water-insoluble (including crystalline ) form of the polypeptide amino acid sequence.

The CBM derived from starch-degrading enzymes is usually called starch-binding module (starch-binding module) or SBM (can be present in specific starch-degrading enzymes, such as specific glucoamylase (GA), or in enzymes such as cyclic in dextrin glycosyltransferases, or CBM in alpha-amylases). Likewise, other subclasses of CBM will include, for example, cellulose-binding modules (CBMs from cellulolytic enzymes), chitin-binding modules (CBMs typically present in chitinases), xylan-binding modules (CBM typically found in xylanases), Mannan Binding Module (CBM typically found in mannanases). SBM is usually called SBD (StarchBinding Domain) (starch binding domain).

A CBM is found to be a major part of a large polypeptide or protein consisting of two or more amino acid sequence regions of polypeptides, especially in hydrolytic enzymes (hydrolases) that typically contain a catalytic module and a carbohydrate binding module (CBM), in which The catalytic module contains the active site for substrate hydrolysis and the carbohydrate binding module (CBM) is used to bind the carbohydrate substrate in question. These enzymes may comprise more than one catalytic module and one, two or three CBMs and optionally further comprise one or more polypeptide amino acid sequences linking together one or more CBMs and one or more catalytic modules, the latter type The regions are often referred to as "joints". Examples of CBM-containing hydrolytic enzymes, some of which were mentioned above, are cellulases, xylanases, mannanases, arabinofuranosidases, acetylesterases and chitinases. CBMs are also found in algae, for example, in the red alga Porphyrapurpurea in the form of non-hydrolyzable polysaccharide-binding proteins.

In a protein/polypeptide (eg, an enzyme, typically a hydrolytic enzyme) in which a CBM is present, the CBM may be located at the N- or C-terminus or at an internal position.

Portions of polypeptides or proteins (eg, hydrolytic enzymes) that make up the CBM itself consist of more than about 30 and less than about 250 amino acid residues.

"Carbohydrate binding module family 20" or CBM-20 module in the context of the present invention is defined as a sequence of about 100 amino acids, which is similar to that in Figure 1 by Joergensen et al. (1997) in Biotechnol. Lett. 19: 1027-1031 The carbohydrate binding modules (CBM) of the disclosed polypeptides share at least 45% homology. The CBM comprises the last 102 amino acids of the polypeptide, a subsequence from amino acid 582 to amino acid 683. The numbering of the glycoside hydrolase family applied in this specification follows Coutinho, PM & Henrissat, B. (1999) CAZy-Carbohydrate at URL: http://afmb.cnrs-mrs.fr/~cazy/CAZY/index.html - Active Enzymes server, or alternatively follow Coutinho, PM & Henrissat, B.1999; The modular structure of cells and other carbohydrate-active enzymes: an integrated database approach. In "Genetics, Biochemistry and Ecology of Cellulose Degradation", K. Ohmiya, K. Hayashi, K. Sakka, Y. Kobayashi, S. Karita and T. Kimura eds., Uni Publishers Co., Tokyo, pp.15-23, and Bourne, Y. & Henrissat, B. 2001; Glycosidehydrolases and glycosyltransferases: families and functional modules, ideas from Current Opinion in Structural Biology 11:593-600.

Examples of enzymes comprising CBMs suitable for use in the context of the present invention are alpha-amylases, maltogenic alpha-amylases, cellulases, xylanases, mannanases, arabinofuranosidases, acetylesterases and several Butinase. Further CBMs of interest in relation to the present invention include CBMs derived from glucoamylases (EC 3.2.1.3) or cyclodextrin glycosyltransferases (CGTases) (EC 2.4.1.19).

CBMs derived from fungal, bacterial or plant sources will generally be suitable for use in the hybrids of the invention. CBMs of fungal origin are preferred. In this regard, techniques suitable for isolating the genes of interest are well known in the art.

Hybrids comprising CBMs of families 20, 21 or 25 of carbohydrate binding modules are preferred. CBMs suitable for the carbohydrate binding module family 20 of the present invention may be derived from the glucose Amylase, α-amylase from Aspergillus kawaii (EMBL: #_AB008370), Aspergillus nidulans (NCBIAAF17100.1), β-amylase from Bacillus cereus (SWISSPROTP36924) , or CGTases derived from Bacillus circulans (SWISSPROTP43379). Preferably CBM from and with CBM from Aspergillus basilica (EMBL: #_AB008370) alpha-amylase is at least 60%, at least 65%, at least 70%, at least 75%, at least CBMs that are 80%, at least 85%, at least 90% or even at least 95% homologous. More preferred CBMs include glucoamylase CBMs from species of the genus Hormoconis, such as from Hormoconis resinae (synonymous with Creosote fungi, or Amorphotheca resinae), such as CBMs from SWISSPROT: Q03045 , from Lentinula ), such as from Lentinula edodes (shiitake mushroom), such as SPTREMBL: Q9P4C5 CBM, from Neurospora, such as from Neurospora crassa, such as SWISSPROT: P14804 CBM from Talaromyces sp., such as from Talaromycesbyssochlamydioides, from Geosmithia sp., such as from Geosmithiacylindrospora, from the genus (Scorias sp.), such as from Scorias spongiosa, from Eupenicillium sp., such as from Eupenicillium ludwigii, from Aspergillus, such as from Aspergillus japonicus, from the genus Penicillium Species from Penicillium cf.miczynskii, from the genus Thysanophora sp., and from Humicola sp., such as from Humicolagrisea var.Thermoidea ), such as the CBM of SPTREMBL: Q12623.

Preferably the hybrid comprises a CBM derived from any family or species selected from the group consisting of: Acremonium, Aspergillus, Atheneum, Conechaetomium, Cryptosporiopsis, Dichotomocladium, Trichumella , Chrodispora, Gliocladium, Pleurotus spp., Malbranchea, Grifolarum cinerea, Clifferia, Pachypora, Penicillium, Rhizomucor, Rhizomucor minutum, Streptomyces, Subulispora, Thermomyces, Trametes, Trichophaea saccata, and Valsaria. CBM can also be derived from plants such as corn (e.g., Zea mays) or from bacteria such as Bacillus. More preferably, the hybrid comprises CBM derived from any species selected from the group consisting of species of Acremonium, Aspergillus albicans, Aspergillus niger, Aspergillus oryzae, Athelia rouille, Bacillus flavothermus, Chaetomium Species of the genus, Cryptosporiopsis sp. (Cryptosporiopsis sp.), Dichotomocladium hesseltinei, Dichotomocladium hesseltinei, Chlorodispora sp., Gliocladium sp., Malbranchea sp. (Malbranchea sp.), Megapora, Clifex sp., Papyrus spp., Penicillium sp., Rhizomucor micromyces, Streptomyces thermocyaneoviolaceus, Streptomyces silt, Subulisporaprovurvata, Thermomyces lanuginosa, Trametes annuli, Trametes rugosa, Trichophaeasaccata, Valsaria rubricosa, Valsario spartii, and corn.

Preferably said hybrid comprises a CBM amino acid sequence selected from the CBMs listed in Table 1 or 2.

Most preferably, said hybrid comprises CBM from a glucoamylase selected from the group consisting of: S. papyrus (SEQ ID NO: 76), Trametes cingularis (SEQ ID NO: 78), Pleurotus grandis (SEQ ID NO: 78), ID NO: 80), Athena rotundum (SEQ ID NO: 92), Aspergillus basilica (SEQ ID NO: 94), Aspergillus niger (SEQ IDNO: 96), or from the α-amylase selected from the following group CBM: Trichopheraea saccata (SEQ ID NO: 52), Subulispora provurvata (SEQ ID NO: 82), Valsaria rubricosa (SEQ ID NO: 84), Acremonium species (SEQ ID NO: 86), Macropora ( SEQ ID NO: 88), Bacillus flavothermus (SEQ ID NO: 90), Chaetomium sp. (SEQ ID NO: 98), Maize (SEQ ID NO: 109), Chaetomium sp. (SEQ ID NO: 137), Trametes rugosa (SEQ ID NO: 139), Valsario spartii (SEQ ID NO: 141) and Penicillium sp. (SEQ ID NO: 143).

In another preferred embodiment, the hybrid enzyme has no more than 10 positions, no more than 9 positions, no more than 8 positions, no more than 7 positions, no more than 6 positions, no more than A CBM sequence that differs by more than 5 positions, no more than 4 positions, no more than 3 positions, no more than 2 positions, or even no more than 1 position from an amino acid sequence selected from the group consisting of: SEQ ID NO: 52, SEQ ID NO: 76, SEQ ID NO: 78, SEQ ID NO: 80, SEQ ID NO: 82, SEQ ID NO: 84, SEQ ID NO: 86, SEQ ID NO: 88, SEQ ID NO : 90, SEQ ID NO: 92, SEQ ID NO: 94, SEQ ID NO: 96, SEQ ID NO: 98, SEQ ID NO: 109, SEQ ID NO: 137, SEQ ID NO: 139, SEQ ID NO: 141 and SEQ ID NO: 143.

It is also preferred to consist of a DNA sequence having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% homology to any sequence selected from the group consisting of Any CBM encoded: SEQ ID NO: 75, SEQ ID NO: 77, SEQ ID NO: 79, SEQ ID NO: 81, SEQ ID NO: 83, SEQ ID NO: 85, SEQ ID NO: 87, SEQ ID NO: 89. SEQ ID NO: 91, SEQ ID NO: 93, SEQ ID NO: 95, SEQ ID NO: 97, SEQ ID NO: 108, SEQ ID NO: 136, SEQ ID NO: 140, SEQ ID NO: 142. More preferably any CBM encoded by a DNA sequence that hybridizes under high, medium or low stringency to any DNA sequence selected from the group: SEQ ID NO: 75, SEQ ID NO: 77, SEQ ID NO: 79, SEQ ID NO: 79, SEQ ID NO: ID NO: 81, SEQ ID NO: 83, SEQ ID NO: 85, SEQ ID NO: 87, SEQ ID NO: 89, SEQ ID NO: 91, SEQ ID NO: 93, SEQ ID NO: 95, SEQ ID NO: 97. SEQ ID NO: 108, SEQ ID NO: 136, SEQ ID NO: 138, SEQ ID NO: 140, and SEQ ID NO: 142.

More suitable CBMs of carbohydrate binding module family 20, 21 or 25 can be found at URL: http://afmb.cnrs-mrs.fr/~cazy/CAZY/index.html) .

Once a nucleotide sequence encoding a substrate-binding (carbohydrate binding) region has been identified, either as cDNA or as chromosomal DNA, it can then be manipulated in various ways to fuse it to a DNA sequence encoding a polypeptide of interest. The DNA fragment encoding the carbohydrate-binding amino acid sequence and the DNA encoding the polypeptide of interest are then ligated with or without a linker. The resulting ligated DNA can then be manipulated in various ways to effect expression.

specific implementation

In a preferred embodiment, the polypeptide comprises a CBM derived from A. papillium, A. papyrus, Valsaria rubricosa, or A. macroporus. Preferably, any polypeptide comprising a CBM amino acid sequence selected from the group consisting of A. rotiae glucoamylase (SEQ ID NO: 92), A. papyrus glucoamylase (SEQ ID NO: 76), Valsaria rubricosa α - Amylase (SEQ ID NO: 84) and Macroporus alpha-amylase (SEQ ID NO: 88).

In another preferred embodiment, the polypeptide comprises an α-amylase sequence (SEQ ID NO: 4) derived from Aspergillus oryzae acid α-amylase, preferably wherein said Aspergillus oryzae amino acid sequence comprises one selected from the following group or multiple amino acid substitutions: A128P, K138V, S141N, Q143A, D144S, Y155W, E156D, D157N, N244E, M246L, G446D, D448S, and N450D. Most preferably, said polypeptide comprises a catalytic domain having the amino acid sequence shown in SEQ ID NO:6. In a preferred embodiment, the polypeptide further comprises a CBM derived from A. rotundum, preferably the polypeptide further comprises a CBM having the amino acid sequence shown in SEQ ID NO: 92. Most preferably, the polypeptide has the amino acid sequence shown in SEQ ID NO: 100, or the polypeptide has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, Amino acid sequences of at least 90% or even at least 95% homology.

It is also preferably composed of a DNA sequence having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% homology to the DNA sequence shown in SEQ ID NO:99 Any polypeptide encoded by a DNA sequence.

In another preferred embodiment, said polypeptide comprises a catalytic module derived from Rhizomucor pumila alpha-amylase and/or a CBM derived from A. roxitum. In a particularly preferred embodiment, the polypeptide has the amino acid sequence shown in SEQ ID NO: 101 or the polypeptide has at least 60%, at least 65%, at least 70%, at least 75%, Amino acid sequences of at least 80%, at least 85%, at least 90% or even at least 95% homology.

In another preferred embodiment, the polypeptide comprises a catalytic module derived from the α-amylase of Polyporus macroporus and/or a CBM derived from Athena rotiae. In a particularly preferred embodiment, the polypeptide has the amino acid sequence shown in SEQ ID NO: 102 or the polypeptide has at least 60%, at least 65%, at least 70%, at least 75%, at least 80% of the aforementioned amino acid sequence %, at least 85%, at least 90%, or even at least 95% homologous amino acid sequences.

In another preferred embodiment, the polypeptide has no more than 10 positions, no more than 9 positions, no more than 8 positions, no more than 7 positions, no more than 6 positions, no more than 5 positions, no more than 4 positions, no more than 3 positions, no more than 2 positions, or even no more than 1 position different from SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID Amino acid sequence of any amino acid sequence shown in NO: 102.

Also preferred is any polypeptide encoded by a DNA sequence that is at least 60%, at least 65%, At least 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% homology.

More preferably any CBM encoded by a DNA sequence that hybridizes under high, medium or low stringency to any DNA sequence encoding any of the amino acid sequences set forth in SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102 .

Other preferred embodiments of the polypeptides of the invention are shown in Tables 3, 4, 5 and 6 of the Examples section. Also preferred is any polypeptide having at least 70%, more preferably at least 80% and even more preferably at least 90% homology to any of the amino acid sequences of the polypeptides shown in Tables 1 to 7. More preferred is any polypeptide encoded by a DNA sequence that hybridizes under low, medium, or high stringency to a DNA sequence encoding any of the amino acid sequences of the polypeptides shown in Tables 1-7.

In a preferred embodiment, the polypeptide comprises a catalytic domain with at least 75% homology to Aspergillus oryzae catalytic domain (SEQ ID NO: 6) and a CBM selected from the group consisting of at least 75% homology CBM: SEQ ID NO: 82, SEQ ID NO: 84, SEQ ID NO: 86, SEQ ID NO: 76, SEQ ID NO: 78, SEQ ID NO: 80, SEQ ID NO: 88, SEQ ID NO: 52, SEQ ID NO: 92, SEQ ID NO: 52, and SEQ ID NO: 90. In a more preferred embodiment, the polypeptide comprises an Aspergillus oryzae catalytic domain (SEQ ID NO: 6) and a CBM selected from the group consisting of: SEQ ID NO: 82, SEQ ID NO: 84, SEQ ID NO: 86, SEQ ID NO: 86, SEQ ID NO: ID NO: 76, SEQ ID NO: 78, SEQ ID NO: 80, SEQ ID NO: 88, SEQ ID NO: 52, SEQ ID NO: 92, SEQ ID NO: 52, and SEQ ID NO: 90.

In a preferred embodiment, the polypeptide comprises a CBM having at least 75% homology to the A. roxitum glucoamylase CBM (SEQ ID NO: 92) and at least 75% homology to a catalytic domain selected from the group consisting of Homologous catalytic domains: SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 20, SEQ ID NO: 22, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 155, SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO: 36, SEQ ID NO : 38, SEQ ID NO: 40, SEQ ID NO: 42, SEQ ID NO: 44, SEQ ID NO: 111, SEQ ID NO: 113, SEQ ID NO: 115, SEQ ID NO: 117, SEQ ID NO: 119, SEQ ID NO: 123, SEQ ID NO: 125, SEQ ID NO: 121, SEQ ID NO: 127, SEQ ID NO: 129, SEQ ID NO: 131, SEQ ID NO: 133, and SEQ ID NO: 135. In a more preferred embodiment, the polypeptide comprises A. roxarii glucoamylase CBM (SEQ ID NO: 92) and a catalytic domain selected from the group consisting of SEQ ID NO: 8, SEQ ID NO: 10 , SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 20, SEQ ID NO: 22, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 155, SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO: 36, SEQ ID NO: 38, SEQ ID NO: 40, SEQ ID NO: 42, SEQ ID NO: 44 , SEQ ID NO: 111, SEQ ID NO: 113, SEQ ID NO: 115, SEQ ID NO: 117, SEQ ID NO: 119, SEQ ID NO: 123, SEQ ID NO: 125, SEQ ID NO: 121, SEQ ID NO: 127, SEQ ID NO: 129, SEQ ID NO: 131, SEQ ID NO: 133 and SEQ ID NO: 135.

In a preferred embodiment, the polypeptide comprises a CBM having at least 75% homology to the CBM of the sp. Derived catalytic domain: Alpha-amylase CBM of Acremonium sp. in SEQ ID NO: 16, Rhizomucor pumila alpha-amylase CBM in SEQ ID NO: 20, and in SEQ ID NO: 24 Megaporus α-amylase CBM. In a more preferred embodiment, the polypeptide comprises the CBM of Acremonium glucoamylase in SEQ ID NO: 145 and the CBM selected from the group consisting of Acremonium in SEQ ID NO: 16 The α-amylase CBM of the strain, the Rhizomucor pumila α-amylase CBM in SEQ ID NO: 20, and the Megaporus α-amylase CBM in SEQ ID NO: 24.

In a preferred embodiment, the polypeptide comprises a catalytic domain having at least 75% homology to the catalytic domain of Rhizomucor pumilus alpha-amylase (SEQ ID NO: 20) and at least 75% homology to a CBM selected from the group consisting of CBM of % homology: Aspergillus glucoamylase CBM in SEQ ID NO:94 and Aspergillus niger glucoamylase CBM in SEQ ID NO:96. In a more preferred embodiment, the polypeptide comprises Rhizomucor pumilus α-amylase catalytic domain (SEQ ID NO: 20) and a CBM selected from the group consisting of: Aspergillus glabra glucoamylase in SEQ ID NO: 94 Aspergillus niger glucoamylase CBM in CBM and SEQ ID NO:96.

In a preferred embodiment, the polypeptide comprises a catalytic domain having at least 75% homology to the catalytic domain of Megaporus α-amylase (SEQ ID NO: 24) and at least 75% homology to a CBM selected from the group consisting of CBMs of % homology: the CBM of Papyrus magna glucoamylase CBM in SEQ ID NO:145, the Valsaria rubricosa alpha-amylase CBM in SEQ ID NO:84 and the maize CBM in SEQ ID NO:109. In a more preferred embodiment, the polypeptide comprises a macroporus α-amylase catalytic domain (SEQ ID NO: 24) and a CBM selected from the group consisting of: Glucospora spp. in SEQ ID NO: 145 Glucoamylase, Valsaria rubricosa alpha-amylase CBM in SEQ ID NO:84 and maize CBM in SEQ ID NO:109.

In a preferred embodiment, the polypeptide comprises a catalytic domain having at least 75% homology to the catalytic domain of Rhizomucor pumilus alpha-amylase (SEQ ID NO: 20) and at least 75% homology to a CBM selected from the group consisting of CBM of % homology: A. roerii glucoamylase CBM in SEQ ID NO: 92 and maize CBM in SEQ ID NO: 109, Chaetomium species in SEQ ID NO: 113 α-amylase CBM, Trametes rugosa α-amylase CBM in SEQ ID NO: 119, Valsaria spartii α-amylase CBM in SEQ ID NO: 123, Penicillium in SEQ ID NO: 121 The α-amylase CBM of species and the Megaporus α-amylase CBM in SEQ ID NO:88. In a more preferred embodiment, the polypeptide comprises Rhizomucor pumilus α-amylase catalytic domain (SEQ ID NO: 20) and a CBM selected from the group consisting of: Glycoamylase CBM and the corn CBM in SEQ ID NO:109, the α-amylase CBM of the bacterial species of Chaetomium in SEQ ID NO:113, Trametes rugosa α-amylase in SEQ ID NO:119 Amylase CBM, Valsaria spartii α-amylase CBM in SEQ ID NO:123, α-amylase CBM of Penicillium species in SEQ ID NO:121 and Macroporus α-amylase in SEQ ID NO:88 Enzyme CBM.

In a particularly preferred embodiment, the polypeptide is selected from the group consisting of V001, V002, V003, V004, V005, V006, V007, V008, V009, V010, V011, V012, V013, V014, V015, V016, V017, V018 , V019, V021, V022, V023, V024, V025, V026, V027, V028, V029, V030, V031, V032, V033, V034, V035, V036, V037, V038, V039, V040, V041, V042, V043, V047 , V048, V049, V050, V051, V052, V054, V055, V057, V059, V060, V061, V063, V064, V065, V066, V067, V068 and V069.

Expression vector

The present invention also relates to a recombinant expression vector, which may comprise a DNA sequence encoding a polypeptide, a promoter, a signal peptide sequence and a transcription and translation stop signal. The various DNA and control sequences described above may be joined together to prepare recombinant expression vectors, which may include one or more convenient restriction sites to allow insertion or replacement of the DNA sequence encoding the polypeptide at these sites. Alternatively, expression can be performed by inserting a DNA sequence or DNA construct comprising the sequence into a suitable vector. During the construction of an expression vector, the coding sequence is located in the vector so that it is operably linked with appropriate control sequences for expression and possible secretion.

The recombinant expression vector may be any vector (eg, a plasmid or virus) that can be conveniently used in recombinant DNA procedures and that is capable of causing expression of the DNA sequence. The choice of vector typically depends on the compatibility of the vector with the host cell into which the vector is to be introduced. The vector can be a linear or closed circular plasmid. The vector may be an autonomously replicating vector, ie, a vector that exists as an extrachromosomal entity that replicates independently of chromosomal replication, eg, a plasmid, extrachromosomal module, minichromosome, cosmid or artificial chromosome. The vector may contain any means for ensuring self-replication. Alternatively, the vector may be one that, when introduced into a host cell, integrates into the genome and replicates with the chromosome or chromosomes into which it has integrated. The vector system may be a single vector or plasmid or two or more vectors or plasmids containing all of the DNA to be introduced into the genome of the host cell, or a transposon.

mark

The vectors of the invention preferably comprise one or more selectable markers which allow easy selection of transformed cells. Selectable markers are genes whose products confer antimicrobial or viral resistance, heavy metal resistance, prototrophy to auxotrophy, and the like.

Examples of selectable markers for filamentous fungal host cells can be selected from including, but not limited to: amdS (acetamidase), argB (ornithine carbamoyltransferase), bar (glufosinate-ammonium acetyltransferase) , hygB (hygromycin phosphotransferase), niaD (nitrate reductase), pyrG (orotidine-5'-phosphate decarboxylase), sC (sulfate adenyltransferase), trpC (o-amino Benzoate synthase), and glufosinate resistance markers, and sets of equivalents from other species. Preferred for Aspergillus cells are the amdS and pyrG markers for A. nidulans or A. oryzae and the bar marker for Streptomyces hygroscopicus. Alternatively, selection can be accomplished by co-transformation, eg as described in WO 91/17243, wherein the selectable marker is on a separate vector.

The vectors of the present invention preferably comprise one or more elements that permit stable integration of the vector into the genome of the host cell or autonomous replication of the vector in the cell independent of the genome of the cell.

When introduced into a host cell, the vector of the present invention can integrate into the host cell genome. For integration, the vector may rely on the DNA sequence encoding the polypeptide of interest or any other vector element for stable integration of the vector into the genome by homologous or non-homologous recombination. Alternatively, the vector may contain additional DNA sequences for targeted integration into the genome of the host cell by homologous recombination. The additional DNA sequences enable integration of the vector into the host cell genome at one or more precise locations in one or more chromosomes. To increase the likelihood of integration at precise locations, the integration module should preferably comprise a sufficient amount of DNA, such as 100 to 1,500 base pairs, preferably 400 to 1,500 base pairs, most preferably 800 to 1,500 base pairs, It is highly homologous to the corresponding target sequence to increase the probability of homologous recombination. The integrating element can be any sequence homologous to the target sequence in the genome of the host cell. Additionally, the integrating elements may be non-coding or coding DNA sequences. On the other hand, the vector can be integrated into the genome of the host cell by non-homologous recombination. These DNA sequences can be any sequence homologous to the target sequence in the genome of the host cell. In addition, these DNA sequences can be non-coding or coding sequences.

For autonomous replication, the vector may further comprise an origin of replication enabling the vector to replicate autonomously in the host cell in question.

Episomal replication of the AMA1 plasmid vector disclosed in WO 00/24883 can be used.

More than one copy of a DNA sequence encoding a polypeptide of interest can be inserted into a host cell to increase expression of the DNA sequence. Stable amplification of the DNA sequence can be obtained by integrating at least one additional copy of the sequence into the host cell genome and selecting transformants using methods well known in the art.

Methods for linking the above elements to construct the recombinant expression vector of the present invention are well known to those skilled in the art (see, for example, Sambrook et al, 1989, Molecular Cloning, A Laboratory Manual, ^2nd edition, Cold Spring Harbor , New York).

host cell

Host cells of the invention comprising a DNA construct or comprising an expression vector comprising a DNA sequence encoding said polypeptide are advantageous in the recombinant production of a polypeptide (e.g., a hybrid enzyme, a wild-type enzyme, or a genetically modified wild-type enzyme) used as host cells. The cells can be transformed with the expression vector. Alternatively, the invention encoding the polypeptide (e.g., hybrid enzyme, wild-type enzyme, or genetically modified wild-type enzyme) can be conveniently incorporated by integrating the DNA construct (in one or more copies) into the host chromosome. The DNA construct transforms the cells. Integration of the DNA construct into the host chromosome may follow conventional methods, for example, by homologous or heterologous recombination.

The host cell may be any suitable prokaryotic or eukaryotic cell, eg, bacterial cells, filamentous fungal cells, yeast, plant cells or mammalian cells.

In a preferred embodiment, the host cell is a filamentous fungus represented by the class of Ascomycota including, for example, Neurospora, Eupenicillium (=Penicillium), naked cell (Emericella) (=Aspergillus), Eurotium (=Aspergillus).

In a more preferred embodiment, said filamentous fungi include all filamentous fungi of the subdivision Eumycota and Oomycota (such as Hawksworth et al. In, Ainsworth and Bisby's Dictionary of The Fungi, 8 ^th edition, 1995, CAB International, University Press, Cambridge, UK). The filamentous fungi are characterized by a vegetative mycelium composed of chitin, cellulose, glucan, chitosan, mannan, and other complex polysaccharides. Vegetative growth occurs by hyphal extension and carbon catabolism is strictly aerobic.

In an even more preferred embodiment, said filamentous fungal host cell is a cell of a species including but not limited to a cell selected from the group consisting of Aspergillus species, preferably strains of Aspergillus oryzae, Aspergillus niger, Aspergillus awamori, Aspergillus bursa, or strains of the genus Bacillus, or strains of the genus Fusarium, such as Fusarium oxysporium, Fusarium graminearum (more precisely expressed as Gribberella zeae), formerly known as Sphaeria zeae, Synonymous with Gibberella roseum and Gibberella roseum f.sp. cerealis), or Fusarium sulphureum (more precisely Gibberella puricaris, with Fusarium trichothecioides, Fusarium A strain of bactridioides, Fusarium sambucium, Fusarium roseum (synonymous with Fusarium roseum var. graminearum), Fusarium cerealis (synonymous with Fusarium crookwellense), or Fusarium venenatum.

In a most preferred embodiment, the filamentous fungal host cell is a cell of an Aspergillus species, preferably a strain of Aspergillus oryzae or Aspergillus niger.

The filamentous fungal host cell may be a wild-type filamentous fungal host cell or a variant, mutated or genetically modified filamentous fungal host cell. In a preferred embodiment of the invention said host cell is a protease deficient or protease negative strain. Also specifically contemplated are Aspergillus strains, such as Aspergillus niger strains, which have been genetically modified to disrupt or reduce the expression of glucoamylase, acid stable alpha-amylase, alpha-1,6 transglucosidase, and protease activities.

Transformation of filamentous fungal host cells

Filamentous fungal host cells can be transformed by methods involving protoplast formation, protoplast transformation, and cell wall regeneration in a manner known in the art. Suitable methods for transforming Aspergillus host cells are described in EP 238 023, EP 184 438, and Yelton et al. 1984, Proceedings of the National Academy of Sciences USA 81: 1470-1474. Suitable methods for transforming Fusarium species are described in Malardier et al. 1989, Gene 78: 147-156 or U.S. Patent 6,060,305.

Isolation and cloning of the DNA sequence encoding the parental alpha-amylase

Techniques for isolating or cloning a DNA sequence encoding a polypeptide of interest are known in the art and include isolation from genomic DNA, preparation from cDNA, or combinations thereof. Cloning of the DNA sequences of the invention from such genomic DNA may be performed, for example, using the well-known polymerase chain reaction (PCR) or antibody screening of expression libraries to detect cloned DNA fragments sharing common structural features. See, e.g., Innis et al., 1990, PCR: A Guide to Methods and Application, Academic Press, New York. Other DNA amplification methods such as ligase chain reaction (LCR), ligation-activated transcription (LAT) and DNA sequence-based amplification (NASBA) can be used.

The DNA sequence encoding the parent alpha-amylase can be isolated from any cell or microorganism that produces the alpha-amylase using a variety of methods well known in the art. First, genomic DNA and/or cDNA libraries should be constructed using chromosomal DNA or messenger RNA from the organism producing the alpha-amylase of interest. Then, if the amino acid sequence of the alpha-amylase is known, labeled oligonucleotide probes can be synthesized and used to identify alpha-amylase-encoding clones from genomic libraries derived from the biological preparation. Alternatively, using very low to very high stringency hybridization and wash conditions, a labeled oligonucleotide probe comprising a sequence homologous to another known α-amylase gene can be used as a probe to identify genes encoding α-amylases. - Cloning of amylases.

Another method of identifying α-amylase-encoding clones would involve inserting fragments of genomic DNA into expression vectors such as plasmids, transforming α-amylase-negative bacteria with the resulting genomic DNA library, and then using the transformed bacteria in cells containing α- The substrate for amylase (ie, maltose) was plated on agar, allowing the identification of alpha-amylase expressing clones.

Alternatively, the DNA sequence encoding the polypeptide can be prepared synthetically by established standard methods, for example, the phosphoroamidite method described in S.L.Beaucage and M.H.Caruthers, (1981), Tetrahedron Letters 22, p.1859-1869, or by Matthes et al. al. (1984), the method described in EMBO J.3, p.801-805. In the phosphoroamidite method, oligonucleotides are synthesized, eg, in an automatic DNA synthesizer, purified, annealed, ligated, and cloned into a suitable vector.

Finally, the DNA sequence may be of mixed genomic and synthetic origin, of mixed synthetic and cDNA origin, or of mixed genomic and cDNA origin by ligating fragments of synthetic, genomic or cDNA origin (corresponding, where appropriate, to the entire DNA sequence) according to standard techniques. Fragments from different parts) were prepared. The DNA sequence can also be prepared by polymerase chain reaction (PCR) using specific primers, such as described in US Pat.

isolated DNA sequence

In particular, the invention relates to an isolated DNA sequence comprising a DNA sequence encoding a polypeptide comprising the amino acid sequence of a catalytic moiety having alpha-amylase activity and Amino acid sequence of a carbohydrate binding module, wherein the catalytic module is of fungal origin.

The term "isolated DNA sequence" as used herein refers to a DNA sequence that is substantially free of other DNA sequences, e.g., at least about 20% pure, preferably at least about 40% pure, more preferably at least about 60% pure, as determined by agarose electrophoresis Pure, more preferably at least about 80% pure, most preferably at least about 90% pure.

For example, an isolated DNA sequence can be obtained by standard cloning methods used in genetic engineering, which relocate the DNA sequence from its natural location to a different site where it will replicate. The cloning method may involve excision and isolation of the desired DNA fragment comprising the DNA sequence encoding the polypeptide of interest, insertion of the fragment into a vector molecule, incorporation of the recombinant vector into multiple copies of the DNA sequence, or The host cell in which the clone will replicate. An isolated DNA sequence can be manipulated in a variety of ways to provide for expression of a polypeptide of interest. Depending on the expression vector, manipulation of the DNA sequence may be desired or necessary prior to its insertion into the vector. Techniques for modifying DNA sequences utilizing recombinant DNA methods are well known in the art.

DNA construct

The invention relates in particular to a DNA construct comprising a DNA sequence encoding a polypeptide, such as a hybrid enzyme or a wild-type enzyme, wherein the hybrid enzyme comprises a first amino acid sequence comprising a catalytic moiety and a carbohydrate binding moiety comprising The second amino acid sequence of said catalytic moiety having alpha-amylase activity, or wherein said wild-type enzyme comprises a first amino acid sequence comprising a catalytic moiety and a second amino acid sequence comprising a carbohydrate binding moiety, said The catalytic module has alpha-amylase activity. A "DNA construct" is defined herein as a single- or double-stranded DNA molecule isolated from a naturally occurring gene or modified to include DNA segments combined and juxtaposed in a manner not found in nature. The term DNA construct is synonymous with the term expression cassette when the DNA construct comprises all the control sequences required for expression of the coding sequence of the invention.

site-directed mutagenesis

Once the DNA sequence encoding the parental alpha-amylase has been isolated and the desired mutation sites identified, mutations can be introduced using synthetic oligonucleotides. These oligonucleotides contain nucleotide sequences flanking the desired mutation sites. In a particular method, a single-stranded gap in the DNA that is the alpha-amylase coding sequence is created in a vector carrying the alpha-amylase gene. Synthetic nucleotides carrying the desired mutation are then annealed to the homologous portion of the single-stranded DNA. The remaining gap was then filled with DNA polymerase I (Klenow fragment) and the construct was ligated using T4 ligase. A specific example of this method is described in Morinaga et al. (1984), Biotechnology 2, p.646-639. US Patent 4,760,025 discloses the introduction of oligonucleotides encoding multiple mutations through minor changes in the expression cassette. However, a greater variety of mutations can be introduced at any one time by the Morinaga method because many oligonucleotides of different lengths can be introduced.

Another method for introducing mutations into a DNA sequence encoding an alpha-amylase is described by Nelson and Long, (1989), Analyticai Biochemistry 180, p.147-151. It involves the 3-step production of a PCR fragment containing the desired mutation, where a chemically synthesized DNA strand is used as one of the primers in a PCR reaction to introduce the desired mutation. DNA fragments carrying the mutations can be isolated from PCR-produced fragments by cleavage with restriction enzymes and reinsertion into expression plasmids.

localized random mutagenesis

Random mutagenesis may advantageously be restricted to a portion of the parent alpha-amylase in question. This may be advantageous, for example, when a particular region of the enzyme has been identified as being particularly important for a given property of the enzyme and is expected to be modified to produce a variation with improved properties. Normally, these regions can be identified when the tertiary structure of the parent enzyme has been elucidated and is relevant to the function of the enzyme.

Localized or region-specific random mutagenesis is conveniently performed using PCR-induced mutagenesis techniques as described above, or any other suitable technique known in the art. Alternatively, the DNA sequence encoding a portion of the DNA sequence to be modified may be isolated, for example by insertion into a suitable vector, and said portion may subsequently be mutagenized using any of the mutagenesis methods discussed above.

Hybrid or variant of wild-type enzyme

The performance of wild-type or hybrid enzymes containing a carbohydrate binding module ("CBM") and an alpha-amylase catalytic module in starch degradation methods can be improved by protein engineering, such as by site-directed mutagenesis, by Localized random mutagenesis, by synthetically making new variants of the parental wild-type enzyme or the parental hybrid enzyme, or by any other suitable protein engineering technique.

Such variants can be produced using conventional protein engineering techniques.

Expression of polypeptides in host cells

The nucleotide sequence to be introduced into the DNA of the host cell can be incorporated into a nucleic acid construct comprising a nucleotide sequence operably linked to one or more control sequences directing the coding sequence Expression is in a suitable host cell under conditions compatible with the control sequences.

A nucleotide sequence encoding a polypeptide can be manipulated for expression of the polypeptide in a variety of ways. Depending on the expression vector, manipulation of the nucleotide sequence may be desired or necessary prior to its insertion into the vector. Techniques for modifying nucleotide sequences utilizing recombinant DNA methods are well known in the art.

The control sequence may be a suitable promoter sequence, which is a nucleotide sequence recognized by a host cell to express a nucleotide sequence. The promoter sequence contains transcriptional control sequences which mediate the expression of the polypeptide. The promoter can be any nucleotide sequence that shows transcriptional activity in the host cell of choice, including mutant, truncated, and hybrid promoters, which can be encoded by homologous or heterologous Genetic acquisition of extracellular or intracellular polypeptides.

Examples of suitable promoters that direct transcription of the nucleic acid constructs of the invention, especially in bacterial host cells, are the lactose operon from Escherichia coli, the agarase gene (dagA) from Streptomycescoelicolor, Bacillus subtilis Levansucrase gene (sacB), Bacillus licheniformis α-amylase gene (amyL), Bacillus stearothermophilus maltogenicamylase gene (amyM), Promoters derived from the Bacillus amyloliquefaciens α-amylase gene (amyQ), the Bacillus licheniformis penicillinase gene (penP), the Bacillus subtilis xylA and xylB genes, and the prokaryotic β-lactamase gene (Villa -Kamaroff et al., 1978, Proceedings of the National Academy of Sciences USA75: 3727-3731), and the tac promoter (DeBoer et al., 1983, Proceedings of the National Academy of Sciences USA80: 21-25). Further promoters are described in "Useful proteins from recombinant bacteria" in Scientific American, 1980, 242:74-94; and Sambrook et al., 1989, supra.

Examples of suitable promoters for directing the transcription of nucleic acid constructs of the present invention in filamentous fungal host cells are Aspergillus oryzae TAKA amylase, Rhizomucor miehei (Rhizomucor miehei) aspartic protease, Aspergillus niger neutral Alpha-amylase, Aspergillus niger acid-stabilized alpha-amylase, Aspergillus niger or Aspergillus awamori glucoamylase (glaA), Rhizomucor miehei lipase, Aspergillus oryzae alkaline protease, Aspergillus oryzae triose phosphate isomerase, Promoters derived from the genes of Aspergillus nidulans acetamidase, and Fusarium oxysporum trypsin-like protease (WO 96/00787), and the NA2-tpi promoter (from Aspergillus niger neutral alpha-amylase and Aspergillus oryzae triphosphate The hybrid of the promoter of the gene of sugar isomerase), and mutant, truncated, and hybrid promoters thereof.

In yeast hosts, useful promoters are composed of Saccharomyces cerevisiae enolase (ENO-1), S. cerevisiae galactokinase (GAL1), S. cerevisiae alcohol dehydrogenase/glyceraldehyde-3-phosphate dehydrogenase (ADH2/GAP), and Saccharomyces cerevisiae 3-phosphoglycerate kinase gene acquisition. Romanos et al., 1992, Yeast 8:423-488 describe other useful promoters for yeast host cells.

The control sequence may also be a suitable transcription terminator sequence recognized by the host cell to terminate transcription. The terminator sequence is operably linked to the 3' end of the nucleotide sequence encoding the polypeptide. Any terminator that is functional in the host cell of choice may be used in the present invention.

Preferred terminators for filamentous fungal host cells are from Aspergillus oryzae TAKA amylase, Aspergillus niger glucoamylase, Aspergillus nidulans anthranilate synthase, Aspergillus niger alpha-glucosidase, and Fusarium oxysporum pancreatic Genetic acquisition of protease-like proteases.

Preferred terminators for use in yeast host cells are obtained from the genes for S. cerevisiae enolase, S. cerevisiae cytochrome C (CYC1 ), and S. cerevisiae glyceraldehyde-3-phosphate dehydrogenase. Romanos et al., 1992, supra describe other useful terminators for yeast host cells.

The control sequence may also be a suitable leader sequence, which is an untranslated region of an mRNA important for translation by the host cell. The leader sequence is operably linked to the 5' end of the nucleotide sequence encoding the polypeptide. Any terminator that is functional in the host cell of choice may be used in the present invention.

Preferred leader sequences for use in filamentous fungal host cells are derived from the genes for Aspergillus oryzae TAKA amylase and Aspergillus nidulans triose phosphate isomerase.

Suitable leader sequences for yeast host cells are composed of S. cerevisiae enolase (ENO-1), S. cerevisiae 3-phosphoglycerate kinase, S. cerevisiae alpha-factor, and S. cerevisiae alcohol dehydrogenase/glyceraldehyde-3- Gene acquisition of phosphate dehydrogenase (ADH2/GAP).

The control sequence may also be a polyadenylation sequence operably linked to the 3' end of the nucleotide sequence which, when transcribed, is recognized by the host cell as an mRNA transcribed to Signal for the addition of polyadenosine residues. Any polyadenylation sequence that is functional in the host cell of choice may be used in the present invention.

Preferred polyadenylation sequences for filamentous fungal host cells consist of Aspergillus oryzae TAKA amylase, Aspergillus niger glucoamylase, Aspergillus nidulans anthranilate synthase, Fusarium oxysporum trypsin-like protease, and Gene acquisition of Aspergillus niger alpha-glucosidase.

Guo and Sherman, 1995, Molecular Cellular Biology 15:5983-5990 describe polyadenylation sequences useful in yeast host cells.

The control sequence may also be a signal peptide coding region encoding an amino acid sequence linked to the amino terminus of the polypeptide and directing the encoded polypeptide into the secretory pathway of the cell. The 5' end of the coding sequence of the nucleotide sequence may itself contain a signal peptide coding region naturally linked in translation reading frame with the segment of the coding region which encodes the secreted polypeptide. Alternatively, the 5' end of the coding sequence may contain a signal peptide coding region foreign to the coding sequence. Where the coding sequence does not naturally contain a signal peptide coding region, a foreign signal peptide coding region may be required. Alternatively, the foreign signal peptide coding region can simply replace the native signal peptide coding region to enhance secretion of the polypeptide. However, any signal peptide coding region that directs the expressed polypeptide into the secretory pathway of the host cell of choice may be used in the present invention.

The signal peptide coding region effective for bacterial host cells is composed of Bacillus NCIB 11837 maltogenic amylase, Bacillus stearothermophilus α-amylase, Bacillus licheniformis subtilisin, Bacillus licheniformis β-lactamase, Bacillus stearothermophilus Bacillus neutral protease (nprT, nprS, nprM), and the signal peptide coding region obtained from the gene of Bacillus subtilis prsA. Simonen and Palva, 1993, Microbiological Reviews 57: 109-137 describe more signal peptides.

The effective signal peptide coding region for filamentous fungal host cells is composed of Aspergillus oryzae TAKA amylase, Aspergillus niger neutral amylase, Aspergillus niger glucoamylase, Rhizomucor miehei aspartic protease, Humicola insolens insolens) cellulase, and Humicola lanuginose (Humicola lanuginose) lipase gene obtained signal peptide coding region.

Signal peptides useful for yeast host cells are derived from the S. cerevisiae alpha-factor and S. cerevisiae invertase genes. Romanos et al., 1992, supra describe other useful signal peptide coding regions.

The control sequence may also be a propeptide coding region that codes for an amino acid sequence located at the amino terminus of the polypeptide. The resulting polypeptide is called a proenzyme or propolypeptide (in some contexts a zymogen). Propolypeptides are generally inactive and can be converted to mature active polypeptides by catalytic or autocatalytic cleavage of the propeptide from the propolypeptide. The propeptide coding region can be composed of Bacillus subtilis alkaline protease (aprE), Bacillus subtilis neutral protease (nprT), Saccharomyces cerevisiae alpha-factor, Rhizomucor miehei aspartic protease, and Myceliophthora thermophila (Myceliophthora Thermophila) laccase (WO 95/33836) gene acquisition.

When both the signal peptide and propeptide regions are present at the amino terminus of the polypeptide, the propeptide region is located immediately adjacent to the amino terminus of the polypeptide, and the signal peptide region is located immediately adjacent to the amino terminus of the propeptide region.

It may also be desirable to add regulatory sequences that allow regulation of expression of the polypeptide relative to the growth of the host cell. Examples of regulatory systems are those that cause the expression of a gene to be turned on or off in response to a chemical or physical stimulus, including the presence of a regulatory compound. Regulatory systems in prokaryotic systems include the lac, tac, and trp operator systems. In yeast, the ADH2 system or the GAL1 system can be used. In filamentous fungi, the TAKA alpha-amylase promoter, the Aspergillus niger glucoamylase promoter, and the Aspergillus oryzae glucoamylase promoter can be used as regulatory sequences. Examples of other regulatory sequences are those that allow gene amplification. In eukaryotic systems these include the dihydrofolate reductase gene amplified in the presence of methotrexate, and the metallothionein gene amplified with heavy metals. In these instances, the nucleotide sequence encoding the polypeptide is operably linked to regulatory sequences.

The various nucleotide and control sequences described above may be joined together to prepare a recombinant expression vector, which may include one or more convenient restriction sites to allow insertion of the nucleotide sequence encoding the polypeptide at these sites or replace. Alternatively, the nucleotide sequence of the present invention can be expressed by inserting the nucleotide sequence or nucleic acid construct comprising the sequence into a suitable vector for expression. During construction of an expression vector, the coding sequence is placed in a vector so that the coding sequence is operably linked with appropriate control sequences for expression.

The recombinant expression vector may be any vector (eg, a plasmid or virus) that can be conveniently used in recombinant DNA procedures and that is capable of causing expression of the nucleotide sequence. The choice of vector typically depends on the compatibility of the vector with the host cell into which the vector is to be introduced. The vector can be a linear or closed circular plasmid.

The vector may be an autonomously replicating vector, ie, a vector that exists as an extrachromosomal entity that replicates independently of chromosomal replication, eg, a plasmid, extrachromosomal element, minichromosome, or artificial chromosome.

The vector may contain any means for ensuring self-replication. Alternatively, the vector may be one that, when introduced into a host cell, integrates into the genome and replicates with the chromosome or chromosomes into which it has integrated. In addition, a single vector or plasmid or two or more vectors or plasmids containing the entire DNA to be introduced into the host cell genome, or a transposon may be used.

The vectors of the invention preferably comprise one or more selectable markers which allow easy selection of transformed cells. Selectable markers are genes whose products confer antimicrobial or viral resistance, heavy metal resistance, prototrophy to auxotrophy, and the like.

Suitable markers for yeast host cells are ADE2, HIS3, LEU2, LYS2, MET3, TRP1, and URA3. Selectable markers for filamentous fungal host cells include, but are not limited to, amdS (acetamidase), argB (ornithine carbamoyltransferase), bar (glufosinate-ammonium acetyltransferase), hygB (hygromycin phosphotransferase), niaD (nitrate reductase), pyrG (orotidine-5'-phosphate decarboxylase), sC (sulfate adenylyltransferase), trpC (anthranilate synthase), and equivalents thereof.

Preferred for use in Aspergillus cells are the amdS and pyrG genes of Aspergillus nidulans or Aspergillus oryzae and the bar gene of Streptomyces hygroscopicus.

The vectors of the present invention preferably comprise one or more elements that permit stable integration of the vector into the host cell genome or autonomous replication of the vector in the cell independent of the genome.

For integration into the host cell genome, the vector may rely on a nucleotide sequence encoding a polypeptide or any other vector element for stable integration of the vector into the genome by homologous or non-homologous recombination. Alternatively, the vector may contain additional nucleotide sequences for directing directed integration by homologous recombination into the genome of the host cell. The additional nucleotide sequence enables integration of the vector at one or more precise locations in one or more chromosomes in the genome of the host cell. To increase the likelihood of integration at precise locations, the integrating element should preferably comprise a sufficient number of nucleotides, such as 100 to 1,500 base pairs, preferably 400 to 1,500 base pairs, most preferably 800 to 1,500 base pairs Yes, it is highly homologous to the corresponding target sequence to increase the probability of homologous recombination. The integrating element can be any sequence homologous to the target sequence in the genome of the host cell. Additionally, the integrating elements may be non-coding or coding nucleotide sequences. On the other hand, the vector can be integrated into the genome of the host cell by non-homologous recombination.

For autonomous replication, the vector may further comprise an origin of replication enabling the vector to replicate autonomously in the host cell in question. Examples of bacterial origins of replication are the origins of replication of plasmids pBR322, pUC19, pACYC177, and pACYC184, which permit replication in E. coli, and the origins of replication of pUB110, pE194, pTA1060, and pAMβ1, which permit replication in Bacillus. Examples of origins of replication for yeast host cells are the 2 micron origin of replication, ARS1, ARS4, the combination of ARS1 and CEN3, and the combination of ARS4 and CEN6. The origin of replication may be one with a mutation that renders it temperature sensitive in the host cell (see, e.g., Ehrlich, 1978, Proceedings of the National Academy of Sciences USA 75:1433).

More than one copy of a nucleotide sequence of the invention may be inserted into a host cell to increase production of a gene product. An increase in copy number of a nucleotide sequence can be obtained by integrating at least one additional copy of the sequence into the host cell genome, or by including an amplifiable selectable marker gene with the nucleotide sequence; Cells are grown in the presence of a suitable selectable agent to select for cells containing an amplified copy of the selectable marker gene, and thus additional copies of the nucleotide sequence.

Methods for linking the above elements to construct recombinant expression vectors of the present invention are well known to those skilled in the art (see, eg, Sambrook et al., 1989, supra).

Host cells: The present invention also relates to recombinant fermenting fungi, or host cells comprising the nucleic acid constructs of the present invention, which are advantageously used for the on site recombinant production of polypeptides. A vector comprising a nucleotide sequence of the invention is introduced into a host cell so that the vector exists as a chromosomal component or as a self-replicating extrachromosomal vector as previously described.

The host cell is a fungal cell. "Fungi" as used herein includes Ascomycota, Basidiomycota, Chytridiomycota, and Zygomycota (e.g. Hawksworth et al., in Ainsworth and Bisby's Dictionary of The Fungi, pp. 8 edition, 1995, CAB International, University Press, Cambridge, UK) and Oomycota (as cited in Hawksworth et al., 1995, supra, p. 171) and all mitotic spore fungi (Hawksworth et al., 1995, supra).

In a more preferred embodiment, the fungal host cell is a filamentous fungal cell. "Filamentous fungi" include all filamentous forms of the fungi and oomycetes (as defined by Hawksworth et al., 1995, supra). The filamentous fungi are characterized by a mycelial wall composed of chitin, cellulose, glucan, chitosan, mannan, and other complex polysaccharides. Vegetative growth occurs by hyphal extension and carbon catabolism is strictly aerobic.

In a preferred embodiment, the filamentous fungal host cell is a cell of a thermophilic or thermotolerant fungus, such as a species of Ascomycotina, Basidiomycotina, Zygomycotina or Chytridiomycotina, in particular A species in the group consisting of Chaetomium, Thermoascus, Malbranchea, or Thielavia (such as Thielavia terrestris), or Trichophaea . Even more preferably said host cell is Trichophaea saccata or a Humicola such as a strain of Humicola insolens.

Fungal cells can be transformed by methods involving the formation of protoplasts, transformation of the protoplasts, and regeneration of the cell wall in a manner known per se. Suitable methods for transforming Aspergillus host cells are described in EP 238 023 and Yelton et al., 1984, Proceedings of the National Academy of Sciences USA 81: 1470-1474. Malardier et al., 1989, Gene 78:147-156 and WO 96/00787 describe suitable methods for transformation of Fusarium species. Available from Becker and Guarente, In Abelson, J.N. and Simon, M.I., editors, Guide to Yeast Genetics and Molecular Biology, Methods in Enzymology, Volume 194, pp 182-187, Academic Press, Inc., New York; Ito et al., 1983 , Journal of Bacteriology 153: 163; and Hinnen et al., 1978, Proceedings of the National Academy of Sciences USA 75: 1920 to transform yeast.

Enzyme Expression in Plants

A DNA sequence encoding a polypeptide of interest, such as a hybrid enzyme of the invention or a variant or hybrid of a wild-type enzyme, can be transformed and expressed in transgenic plants as described below.

The transgenic plant can be dicotyledonous or monocotyledonous, referred to as dicotyledonous or monocotyledonous. Examples of monocots are grasses such as blue grass (Poa), forage grasses such as Festuca, Lolium, temperate grasses such as bentgrass genus (Agrostis), and cereals such as wheat, oats, rye, barley, rice, sorghum and maize (corn).

Examples of dicots are tobacco, legumes (such as lupine), potatoes, sugar beets, peas, beans and soybeans, and cruciferous plants (Brassicaceae) such as cauliflower, Rapeseed rape and the closely related model organism Arabidopsis thaliana.

Examples of plant parts are stem, callus, leaf, root, fruit, seed, and tuber and the individual tissues comprising these parts, e.g., epidermis, mesophyll, parenchyme, vascular tissue, branch living tissue. In this context, specific plant cell compartments such as chloroplasts, apoplasts, mitochondria, vacuoles, peroxisomes and cytoplasm are also considered plant parts. Additionally, any plant cell, regardless of tissue origin, is considered a plant part. Likewise, plant parts such as specific tissues and cells isolated for use in the present invention are also considered plant parts, for example, embryos, endosperms, aleurone and seed coats.

Progeny of these plants, plant parts and plant cells are also included within the scope of the present invention.

Transgenic plants or plant cells expressing a polypeptide of interest can be constructed according to methods known in the art. Briefly, plants or plant cells are constructed by integrating one or more expression constructs encoding a polypeptide of interest into the plant host genome and propagating the resulting engineered plants or plant cells into transgenic plants or plant cells.

Conveniently, the expression construct is a DNA construct comprising a gene encoding a polypeptide of interest operably associated with suitable regulatory sequences required for expression of the gene in the plant or plant part of choice of. Furthermore, the expression construct may comprise a selectable marker for identifying the host cell into which the expression construct has been integrated and the DNA sequences necessary for introduction of the construct into the plant in question (the latter depending on the intended use). DNA introduction method).

The choice of regulatory sequences (such as promoter and terminator sequences and optionally signal or transit sequences) is determined, for example, by when, where and how the enzyme in question is desired to be expressed. For example, expression of a gene encoding an enzyme of the invention may be constitutive or inducible, or may be developmental, stage, or tissue specific, and may direct the gene product to a specific cellular compartment, tissue, or plant part such as a seed or leaves. Regulatory sequences are described in Tague et al, Plant Phys., 86, 506, 1988.

For constitutive expression, the 35S-CaMV, maize ubiquitin 1 and rice actin 1 promoters can be used (Franck et al. 1980. Cell 21: 285-294, Christensen AH, Sharrock RA and Quail 1992. Maize polyubiquitin genes: structure, thermal perturbation of expression and transcript splicing, and promoter activity following transfer toprotoplasts by electroporation. Plant Mo. Biol. 18, 675-689.; Zhang W, McElroyD. and Wu R 1991, Analysis of rice Actl 5'region transgenic activity riceplants. Plant Cell 3, 1155-1165). Organ-specific promoters can be, for example, from storage sink tissues such as seeds, potato tubers, and fruits (Edwards & Coruzzi, 1990. Annu. Rev. Genet. 24:275-303), or from metabolic sinks. sink) tissues such as meristem (Ito et al., 1994, Plant Mol. Biol. 24:863-878), seed-specific promoters such as glutelin, gliadin, globulin or albumin from rice (Wu et al., Plant and Cell Physiology Vol.39, No.8pp.885-889 (1998)), Conrad U.et al, Journal of Plant Physiology Vol.152, No.6, pp.708-711 (1998) described the broad bean promoter from legumin B4 of Vicia faba (Viciafaba) and an unknown seed protein, the promoter from seed oleosin (Chen et al., Plant and Cell Physiology, Vol.39, No.9 , pp.935-941 (1998), the storage protein napA promoter from Brassica napus, or any other seed-specific promoter known in the art, e.g., as described in WO 91/14772. In addition, the promoter may be a leaf-specific promoter from rice or tomato such as the rbcs promoter (Kyozuka et al., Plant Physiology, Vol.102, No.3, pp.991-1000 (1993), Chlorella Viral adenine methyltransferase gene promoter (Mitra, A.and Higgins, DW, Plant Molecular Biology, Vol.26, No.1, pp.85-93 (1994), or the aldP gene promoter from rice ( Kagaya et al., Molecular and General Genetics, Vol.248, No.6, pp.668-674 (1995) or wound-inducible promoters such as the potato pin2 promoter (Xu et al, Plant Molecular Biology, Vol.22 , No.4, pp.573-588 (1993).Equally, the promoter can be induced by abiotic treatments such as temperature, drought or salinity changes, or by an externally applied substance that activates the promoter, For example, ethanol, estrogen, phytohormones like ethylene, abscisic acid and gibberellic acid, and heavy metals induce.

Promoter enhancer elements can be used to obtain higher enzyme expression in plants. For example, the promoter enhancer component may be an intron located between the promoter and the nucleotide sequence encoding the enzyme. For example, Xu et al. op cit discloses the use of the first intron of the rice actin 1 gene to enhance expression.

The selectable marker gene and any other part of the expression construct can be selected from those available in the art.

The DNA constructs are incorporated into the plant genome following conventional techniques known in the art, including Agrobacterium-mediated transformation, virus-mediated transformation, microinjection, particle bombardment, biolistic transformation, and electroporation. Perforation (Gasser et al, Science, 244, 1293; Potrykus, Bio/Techn. 8, 535, 1990; Shimamoto et al, Nature, 338, 274, 1989).

Currently, Agrobacterium tumefaciens-mediated gene transfer is the method of choice for the production of transgenic dicotyledonous plants (for review see Hooykas & Schilperoort, 1992, Plant Mol. Biol., 19: 15-38), or for the transformation of monocots, although other transformation methods are commonly used for these plants. Currently, the ideal method for producing transgenic monocots supplemented by the Agrobacterium approach is particle bombardment (microscopic gold or tungsten particles coated with transforming DNA) of embryonic callus or developing embryos (Christou, 1992, Plant J., 2: 275-281; Shimamoto, 1994, Curr. Opin. Biotechnol., 5: 158-162; Vasil et al., 1992, Bio/Technology 10: 667-674). An alternative method for transformation of monocots is based on the transformation of protoplasts as described by Omirulleh S, et al., Plant Molecular Biology, Vol. 21, No. 3, pp. 415-428 (1993).

After transformation, transformants that have incorporated the expression construct are selected and propagated as whole plants according to methods well known in the art. The transformation method is generally designed for use during regeneration or in subsequent production using, for example, co-transformation with two separate T-DNA constructs or site-specific excision of the selection gene by specific recombinases. Selective removal of select genes.

starch processing

The polypeptide of the first, second and/or third aspect may be used in a method of liquefying starch, wherein a gelatinized or granular starch substrate is treated with said hybrid enzyme in an aqueous medium. The polypeptides of the first, second and/or third aspects may also be used in a process for saccharification of liquefied starch substrates. A preferred use is in a fermentation process in which a starch substrate is liquefied and/or saccharified in the presence of a polypeptide of the first, second and/or third aspect to produce Glucose and/or maltose converted into fermentation products. These fermentation methods include methods for the production of fuel ethanol or portable alcohol, methods for the production of beverages, methods for the production of desired organic compounds such as citric acid, itaconic acid, lactic acid, gluconic acid, sodium gluconate, Calcium gluconate, potassium gluconate, glucono delta lactone, or sodium erythorbate; ketones; amino acids, such as glutamic acid (sodium monoglutaminate), and those that are difficult to produce synthetically More complex compounds such as antibiotics, such as penicillin, tetracycline; enzymes; vitamins, such as riboflavin, B12, beta-carotene; hormones.

The starch to be processed may be of highly refined starch quality, preferably at least 90%, at least 95%, at least 97% or at least 99.5% pure, or it may be a coarser starch-containing material comprising ground whole grains, which Includes non-starch fractions such as germ residue and fibers. Raw materials such as whole grains are ground to open up the tissue so that further processing can be performed. Two milling methods are preferred according to the invention: wet milling and dry milling. Corn grits, preferably ground corn grits, may also be used.

In addition to starch, dry ground grain will also contain significant amounts of non-starch carbohydrates. When such heterogeneous materials are processed by jet cooking, usually only partial gelatinization of the starch is achieved. Due to their high activity against non-gelatinized starches, the polypeptides of the invention are advantageously used in processes involving liquefaction and/or saccharification of jet-cooked dried and ground starch.

Furthermore, due to the superior hydrolytic activity of the polypeptide of the first aspect, the need for glucoamylase during the saccharification step is greatly reduced. This allows saccharification to be carried out at very low levels of glucoamylase activity, and preferably absent or if present, at no more than or even less than 0.5 AGU/g DS, more preferably no more than or even less The starch substrate is present in an amount of 0.4 AGU/g DS, more preferably no more than or even less than 0.3 AGU/g DS, most preferably less than 0.1 AGU/g DS, such as no more than or even less than 0.05 AGU/g DS starch substrate. Enzymes with glucoamylase activity expressed in mg enzyme protein or missing, or at no more than or even less than 0.5mg EP/g DS, more preferably no more than or even less than 0.4mg EP/g DS, more preferably no More than or even less than 0.3 mg EP/g DS, most preferably no more than or even less than 0.1 mg EP/g DS, such as no more than or even less than 0.05 mg EP/g DS or no more than or even less than 0.02 mg EP The amount of/g DS starch substrate present. The glucoamylase can preferably be derived from bacterial strains in the bacterial species of Aspergillus, Talaromyces, Pachypora or Trametes, more preferably derived from Aspergillus niger, Talaromyces emersonii, Trametes annuli or Pachykytospora papyracea.

Also due to the superior hydrolytic activity of the polypeptides of the first aspect, the need for alpha-amylase in the liquefaction and/or saccharification steps is greatly reduced. The polypeptide of the first aspect expressed in mg enzyme protein may be no more than or even less than 0.5 mg EP/g DS, more preferably no more than or even less than 0.4 mg EP/gDS, still more preferably no more than or even less than 0.3 mg EP/g DS, most preferably no more than or even less than 0.1 mg EP/g DS, such as no more than or even less than 0.05 mg EP/g DS or no more than or even less than 0.02 mg EP/g DS of starch substrate Quantity preparation. The polypeptide of the first aspect may be formulated in an amount of 0.05 to 10.0 AFAU/g DS, preferably 0.1 to 5.0 AFAU/g DS, more preferably 0.25 to 2.5 AFAU/g DS starch. The method may comprise: a) contacting a starch substrate with a polypeptide comprising a catalytic moiety having alpha-amylase activity and a carbohydrate binding moiety, e.g., the polypeptide of the first aspect; Or at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99.5% w/w of said starch substrate is converted into fermentable sugar temperature and time Within, incubating said starch substrate with said polypeptide; c) fermenting to produce a fermentation product, d) optionally recovering the fermentation product. During processing steps b) and/or c), the enzyme with glucoamylase activity is either absent, or at 0.001 to 2.0 AGU/gDS, 0.01 to 1.5 AGU/g DS, 0.05 to 1.0 AGU/g DS, 0.01 to An amount of 0.5 AGU/g DS is present. Preferably there is the enzyme of glucoamylase activity or deletion, or with no more than or even less than 0.5AGU/gDS, more preferably no more than or even less than 0.4AGU/gDS, more preferably no more than or even less than 0.3AGU/gDS, Most preferably no more than or even less than 0.1 AGU, such as no more than or even less than 0.05 AGU/g DS starch substrate is present. Enzymes with glucoamylase activity expressed in mg enzyme protein or missing, or at no more than or even less than 0.5mgEP/g DS, more preferably no more than or even less than 0.4mgEP/gDS, more preferably no more than Or even less than 0.3mg EP/g DS, most preferably no more than or even less than 0.1mg EP/g DS, such as no more than or even less than 0.05mg EP/g DS or no more than or even less than 0.02mg EP/g DS The amount of g DS starch substrate present. Steps a, b, c, and/or d in the method may be performed individually or simultaneously.

In another aspect the method may comprise: a) contacting a starch substrate with a yeast cell transformed to express a polypeptide comprising a catalytic moiety having alpha-amylase activity and a carbohydrate binding moiety, e.g., a first and/or the polypeptide of the second aspect; b) incubating said starch substrate with said yeast at a temperature and for a time sufficient to convert at least 90% w/w of said starch substrate to fermentable sugars; c) fermentation to produce ethanol; d) optional recovery of ethanol. Steps a, b, and c can be performed individually or simultaneously.

In yet another aspect the method comprises hydrolysis of gelatinized or granular starch slurry, in particular hydrolysis of granular starch to a soluble starch hydrolyzate at a temperature below the initial gelatinization temperature of said granular starch. In addition to being contacted with a polypeptide comprising a catalytic moiety having alpha-amylase activity and a carbohydrate binding moiety, e.g., the polypeptide of the first aspect, the starch may be contacted with an enzyme selected from the group consisting of fungal alpha-amylase enzymes (EC 3.2.1.1), beta-amylases (E.C.3.2.1.2), and glucoamylases (E.C.3.2.1.3). In embodiments further bacterial alpha-amylases or debranching enzymes may be added, such as isoamylase (E.C. 3.2.1.68) or pullulanase (E.C. 3.2.1.41). A bacterial alpha-amylase in the context of the present invention is an alpha-amylase as defined on page 3, line 18 to page 6, line 27 of WO 99/19467.

In embodiments the method is carried out at a temperature below the initial gelatinization temperature. Preferably the method is carried out at a temperature of at least 30°C, at least 31°C, at least 32°C, at least 33°C, at least 34°C, at least 35°C, at least 36°C, at least 37°C, at least 38°C, at least 39°C, at least 40°C, at least 41°C, at least 42°C, at least 43°C, at least 44°C, at least 45°C, at least 46°C, at least 47°C, at least 48°C, at least 49°C, at least 50°C, at least 51°C, at least 52°C , at least 53°C, at least 54°C, at least 55°C, at least 56°C, at least 57°C, at least 58°C, at least 59°C, or preferably at least 60°C. The pH at which the method is carried out may be in the range of 3.0 to 7.0, preferably 3.5 to 6.0, or more preferably 4.0-5.0. In a preferred embodiment, the method comprises fermentation with eg yeast to produce ethanol, eg at a temperature of about 32°C, such as 30 to 35°C.

In another preferred embodiment, the method comprises simultaneous saccharification and fermentation, for example at a temperature of 30 to 35°C, for example at about 32°C, for example with yeast to produce ethanol, or with another suitable fermenting organism to produce the desired organic compounds.

In the above fermentation process, the ethanol content reaches at least 7%, at least 8%, at least 9%, at least 10%, at least 11%, at least 12%, at least 13%, at least 14%, at least 15%, such as at least 16% ethanol .

The starch slurry used in any of the above aspects may have 20-55% dry solids granular starch, preferably 25-40% dry solids granular starch, more preferably 30-35% dry solids granular starch. At least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or preferably at least 99% converted It is a soluble starch hydrolyzate.

In another preferred embodiment, a polypeptide comprising a catalytic moiety having α-amylase activity and a carbohydrate binding moiety, for example, the polypeptide of the first aspect is used in a process for liquefaction and saccharification of gelatinized starch, such as but not Limited to gelatinization by jet cooking. The method may include fermentation to produce a fermentation product such as ethanol. This method of producing ethanol from starch-containing material by fermentation comprises: (i) liquefying said starch-containing material with a polypeptide comprising a catalytic moiety having alpha-amylase activity and a carbohydrate binding moiety, e.g., the polypeptide of the first aspect (ii) liquefied mash obtained by saccharification; (iii) fermenting the material obtained in step (ii) in the presence of a fermenting organism. Optionally the method further comprises recovering ethanol. Saccharification and fermentation can be carried out as a simultaneous saccharification and fermentation process (SSF process). The ethanol content reaches at least 7%, at least 8%, at least 9%, at least 10%, at least 11%, at least 12%, at least 13%, at least 14%, at least 15%, such as at least 16% ethanol during fermentation.

In particular, in the method of the above aspects, the starch to be processed may be obtained from tubers, roots, stems, legumes, cereals or whole grains. More particularly, the granular starch may be obtained from corn, cobs, wheat, barley, rye, milo, sago, cassava, tapioca, sorghum, rice, peas, beans, bananas or potatoes get. Special consideration is given to waxy and non-waxy corn and barley.

The invention also relates to compositions comprising a polypeptide of the first and/or second aspect. In a particularly preferred embodiment the composition comprises the polypeptide of the first aspect selected from the group consisting of V001, V002, V003, V004, V005, V006, V007, V008, V009, V010, V011, V012, V013, V014, V015, V016, V017, V018, V019, V021, V022, V023, V024, V025, V026, V027, V028, V029, V030, V031, V032, V033, V034, V035, V036, V037, V038, V039, Group of V040, V041, V042, V043, V047, V048, V049, V050, V051, V052, V054, V055, V057, V059, V060, V061, V063, V064, V065, V066, V067, V068 and V069. The composition may further comprise an enzyme selected from the group consisting of fungal alpha-amylase (EC 3.2.1.1), beta-amylase (E.C.3.2.1.2), glucoamylase (E.C.3.2.1.3) and branched chain Amylase (E.C. 3.2.1.41). The glucoamylase may preferably be derived from a strain of Aspergillus, such as Aspergillus niger, or from a strain of Talaromyces leycettanus, as disclosed in U.S. Patent Re.32,153 Glucoamylases, derived from Talaromyces duponti and/or Talaromyces thermopiles, such as those disclosed in US Patent 4,587,215, and more preferably derived from T. emersonii. Most preferably the glucoamylase is derived from T. emersonii strain CBS 793.97 and/or has the sequence disclosed in WO 99/28448 as SEQ ID NO: 7. More preferred are glucoamylases having amino acid sequences that are at least 50%, at least 60%, at least 70%, at least 80%, at least 90% or even at least 95% homologous to the aforementioned amino acid sequences. A commercial Talaromyces glucoamylase preparation was supplied by Novozymes A/S as Spirizyme Fuel.

For compositions comprising a polypeptide of the first and/or second aspect and a glucoamylase, preference is also given to a polypeptide having glucoamylase activity originating from a strain of Trametes, preferably Trametes cerevisiae. More preferably have glucoamylase activity and at least 50%, at least 60%, at least 70%, at least 80%, Polypeptides that are at least 90% or even at least 95% homologous.

For a composition comprising a polypeptide of the first and/or second aspect and a glucoamylase, a strain having glucoamylase activity derived from the genus Pachypora, preferably M. papyrii, is also preferred, or Polypeptide derived from the E. coli strain deposited at DSMZ and given accession number DSM 17105. More preferably have glucoamylase activity and at least 50%, at least 60%, at least 70%, at least 80%, Polypeptides that are at least 90% or even at least 95% homologous.

The composition described above can be used to liquefy and/or saccharify gelatinized or granular starch, as well as partially gelatinized starch. Partially gelatinized starch refers to starch that has been gelatinized to some extent, that is, part of the starch has been irreversibly swollen and gelatinized while part of the starch still exists in a granular state.

The above compositions may preferably comprise acid alpha-amylase present in an amount of 0.01 to 10 AFAU/g DS, preferably 0.1 to 5 AFAU/g DS, more preferably 0.5 to 3 AFAU/g DS, most preferably 0.3 to 2 AFAU/g DS . The composition can be applied in any of the above-mentioned starch processing methods.

Materials and methods

Determination of acid alpha-amylase activity

When used according to the invention, the activity of any acid alpha-amylase may be measured in AFAU (Acid Fungal Alpha-amylase Units), which is determined relative to an enzyme standard. 1 AFAU is defined as the amount of enzyme that degrades 5.260 mg of starch dry matter per hour under the standard conditions mentioned below.

Acid alpha-amylase, acid-stable alpha-amylase, an endo-alpha-amylase (1,4-alpha-D-glucan-glucosidyl-hydrolase (1,4-alpha- D-glucan-glucano-hydrolase), E.C.3.2.1.1), hydrolyzes α-1,4-glycosidic bonds in the internal region of the starch molecule to form dextrins and oligosaccharides with different chain lengths. The intensity of the color formed with iodine is directly proportional to the concentration of starch. Amylase activity was determined by reverse colorimetry with decreasing starch concentration under the specified assay conditions.

Blue/purple t=23 seconds to decolorize

Standard Conditions/Reaction Conditions:

Substrate: Soluble starch, about 0.17g/L

Buffer: citrate, about 0.03M

Iodine (I2): 0.03g/L

CaCl ₂ : 1.85mM

pH: 2.50±0.05

Incubation temperature: 40°C

Response time: 23 seconds

Wavelength: 590nm

Enzyme concentration: 0.025AFAU/mL

Enzyme working range: 0.01-0.04AFAU/mL

A brochure EB-SM-0259.02/01 describing the analytical method in more detail is available from Novozymes A/S, Denmark and is hereby incorporated by reference.

Glucoamylase activity

Glucoamylase activity can be measured in amyloglucosidase units (AGU). AGU is defined as the amount of enzyme that hydrolyzes 1 micromole of maltose per minute under the standard conditions of 37°C, pH 4.3, substrate: maltose 23.2mM, buffer: acetate 0.1M, and reaction time 5 minutes.

An automated analyzer system may be used. Mutarotase is added to the glucose dehydrogenase reagent to convert any α-D-glucose present to β-D-glucose. In the above reaction, glucose dehydrogenase specifically reacts with β-D-glucose to form NADH, which is measured by a photometer at 340 nm as a measure of the initial glucose concentration.

AMG incubation:

Substrate: Maltose 23.2mM

Buffer: Acetate 0.1M

Ph: 4.30±0.05

Incubation temperature: 37℃±1

Response time: 5 minutes

Enzyme working range: 0.5-4.0AGU/mL

Color reaction:

GlucDH: 430U/L

Mutarotase: 9U/L

NAD: 0.21mM

Buffer: Phosphate 0.12M; 0.15M NaCl

pH: 7.60±0.05

Incubation temperature: 37℃±1

Response time: 5 minutes

Wavelength: 340nm

A brochure (EB-SM-0131.02/01) describing the analytical method in more detail is available from Novozymes A/S, Denmark and is hereby incorporated by reference.

Strains and plasmids

E. coli DH12S (available from Gibco BRL) was used for yeast plasmid rescue.

pLA1 is a S. cerevisiae and E. coli shuttle vector under the control of the TPI promoter, constructed from pJC039 as described in WO 01/92502. Into this has been inserted the A. acid niger alpha-amylase signal sequence, the A. acid niger alpha-amylase gene (SEQ ID NO: 1) and the portion containing the linker (SEQ ID NO: 67) and the CBM (SEQ ID NO: 91) Sequence of the glucoamylase gene from Athena rotundum. The complete sequence of the plasmid is given in SEQ ID NO:103. The alpha-amylase gene is the sequence from 5029 to 6468, the linker is the sequence from 6469 to 6501, and the CBM is the sequence from 6502 to 6795. The vector is used for the construction of α-amylase CBM hybrid.

Saccharomyces cerevisiae YNG318: MATa Dpep4[cir+]ura3-52, leu2-D2, his 4-539 were used for α-amylase variant expression. It is described in J. Biol. Chem. 272(15), pp 9720-9727, 1997.

Media and Substrates

10X base solution: yeast nitrogen base without amino acid (DIFCO) 66.8g/l, succinate (salt) 100g/l, NaOH 60g/l.

SC-Glucose: 20% Glucose (ie 2% final concentration = 2g/100ml) 100ml/l, 5% Threonine 4ml/l, 1% Tryptophan 10ml/l, 20% Casamino acids 25ml/l , 10X base solution 100ml/l. The solution was sterilized using a filter with a pore size of 0.20 microns. The agar was autoclaved together with _H2O (approximately 761 ml), and the separately sterilized SC-glucose solution was added to the agar solution.

YPD: Bacto peptone 20g/l, yeast extract 10g/l, 20% glucose 100ml/l.

PEG/LiAc solution: 40% PEG4000 50ml, 5M lithium acetate 1ml.

DNA manipulation

Unless otherwise stated, DNA manipulations and transformations were performed using Sambrook et al. (1989) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Lab., Cold Spring Harbor, NY; Ausubel, F.M.et al. (eds.) "Current Protocols in Molecular Biology", John Wiley and Sons, 1995; Harwood, C.R. and Cutting, S.M. (eds.) described in the standard method of molecular biology.

yeast transformation

Yeast transformation was performed using the lithium acetate method. Mix 0.5 μL of vector (digested by restriction endonucleases) with 1 μL of PCR fragment. Thaw YNG318 competent cells on ice. Mix 100 μL of cells, DNA mixture and 10 μL of carrier DNA (Clontech) in a 12 ml polypropylene test tube (Falcon 2059). Add 0.6ml PEG/LiAc solution and mix gently. Incubate at 30°C, 200rpm for 30min. Incubate at 42°C for 30min (heat shock). Transfer to an eppendorf tube and centrifuge for 5 seconds. Remove supernatant and dissolve in 3ml YPD. The cell suspension was incubated at 200rpm at 30°C for 45min. The suspension was poured into SC-glucose plates and incubated at 30°C for 3 days to generate colonies. Yeast total DNA was extracted by Robzyk and Kassir's method described in Nucleic Acids Research, Vol. 20, No. 14 (1992) 3790.

DNA sequencing

E. coli transformation was performed by electroporation (BIO-RAD Gene Pulser) for DNA sequencing. DNA plasmids were prepared by the alkaline method (Molecular Cloning, Cold Spring Harbor) or with the Qiagen ^(R) Plasmid kit. DNA fragments were recovered from agarose gels using a Qiagen gel extraction kit. PCR was performed with PTC-200 DNA Engine. ABI PRISM ^TM 310 Genetic Analyzer was used for all DNA sequence determinations.

Table 2

Amino acid (AA) and DNA sequence numbering of the catalytic domain (CD), linker, carbohydrate binding module (CBM), plasmid, and primers used. AA refers to alpha-amylase and GA refers to glucoamylase. type code source of sequence SEQ ID CD C001   Aspergillus niger α-amylase SEQ ID NO: 1 dna CD C001   Aspergillus niger α-amylase SEQ ID NO: 2 aa CD C002  Aspergillus oryzae α-amylase Fungamyl SEQ ID NO: 3 dna CD C002  Aspergillus oryzae α-amylase Fungamyl SEQ ID NO: 4 Aa CD C003 Aspergillus oryzae α-amylase Fungamyl variant SEQ ID NO: 5 DNA CD C003 Aspergillus oryzae α-amylase Fungamyl variant SEQ ID NO: 6 Aa CD C004 Trichophaea saccata α-amylase SEQ ID NO: 7 DNA CD C004 Trichophaea saccata α-amylase SEQ ID NO: 8 Aa CD C005 Subulispora provurvata alpha-amylase SEQ ID NO: 9 DNA CD C005 Subulispora procurvata alpha-amylase SEQ ID NO: 10 Aa CD C006 Valsaria rubricosa alpha-amylase SEQ ID NO: 11 DNA CD C006 Valsaria rubricosa alpha-amylase SEQ ID NO: 12 Aa CD C007   Thermomyces lanuginosa α-amylase SEQ ID NO: 13 DNA CD C007   Thermomyces lanuginosa α-amylase SEQ ID NO: 14 Aa CD C008 Acremonium α-amylase SEQ ID NO: 15 DNA CD C008 Acremonium α-amylase SEQ ID NO: 16 Aa CD C009   α-amylase from species of the genus Malbranchea SEQ ID NO: 17 dna CD C009   α-amylase from species of the genus Malbranchea SEQ ID NO: 18 Aa CD C010   Rhizomucor pumila α-amylase SEQ ID NO: 19 DNA CD C010   Rhizomucor pumila α-amylase SEQ ID NO: 20 Aa CD C011   Dichotomocladium hesseltinei α-amylase SEQ ID NO: 21 dna CD C011   Dichotomocladium hesseltinei α-amylase SEQ ID NO: 22 Aa CD C012   α-amylase from the genus Macroporus SEQ ID NO: 23 dna CD C012   α-amylase from the genus Macroporus SEQ ID NO: 24 Aa CD C013   Stereus α-amylase SEQ ID NO: 25 dna

CD C013   Stereus α-amylase SEQ ID NO: 26 aa CD C014 Trametes species SEQ ID NO: 27 dna CD C014 Trametes species SEQ ID NO: 28 aa CD C015 Coriolus salmon alpha-amylase SEQ ID NO: 29 dna CD C015 Coriolus salmon alpha-amylase SEQ ID NO: 30 aa CD C016   Alpha-amylase from the genus Bichaete SEQ ID NO: 31 dna CD C016   Alpha-amylase from the genus Bichaete SEQ ID NO: 32 aa CD C017 Cryptosporiopsis species α-amylase SEQ ID NO: 33 dna CD C017 Cryptosporiopsis species α-amylase SEQ ID NO: 34 aa CD C018   Alpha-amylase from Chaetomium species SEQ ID NO: 35 dna CD C018   Alpha-amylase from Chaetomium species SEQ ID NO: 36 aa CD C020 Chrodispora species α-amylase SEQ ID NO: 37 DNA CD C020 Chrodispora species α-amylase SEQ ID NO: 38 Aa CD C021   Alpha-amylase SEQ ID NO: 39 DNA CD C021   Alpha-amylase SEQ ID NO: 40 Aa CD C022   α-amylase from Gliocladium sp. SEQ ID NO: 41 DNA CD C022   α-amylase from Gliocladium sp. SEQ ID NO: 42 Aa CD C023 Streptomyces thermocyaneoviolaceus alpha-amylase SEQ ID NO: 43 DNA CD C023 Streptomyces thermocyaneoviolaceus alpha-amylase SEQ ID NO: 44 Aa connector C024   Glucoamylase SEQ ID NO: 45 DNA connector C024   Glucoamylase SEQ ID NO: 46 Aa connector C025 Trametes valvularis glucoamylase SEQ ID NO: 47 DNA connector C025 Trametes valvularis glucoamylase SEQ ID NO: 48 Aa connector C026   Glucoamylase from Pleurotus chinensis SEQ ID NO: 49 DNA connector C026   Glucoamylase from Pleurotus chinensis SEQ ID NO: 50 Aa Connector+CBM C027 Trichophaea saccata α-amylase SEQ ID NO: 51 DNA Connector+CBM C027 Trichophaea saccata α-amylase SEQ ID NO: 52 Aa connector C028 Sublispora provurvata alpha-amylase SEQ ID NO: 53 dna connector C028 Sublispora provurvata alpha-amylase SEQ ID NO: 54 aa connector C029 Valsaria rubricosa alpha-amylase SEQ ID NO: 55 dna connector C029 Valsaria rubricosa alpha-amylase SEQ ID NO: 56 aa connector C030 Acremonium α-amylase SEQ ID NO: 57 dna connector C030 Acremonium α-amylase SEQ ID NO: 58 aa connector C031   Meripilus giganteus α-amylase SEQ ID NO: 59 dna connector C031   Macroporus α-amylase SEQ ID NO: 60 aa connector C032 Bacillus flavothermus α-amylase short linker SEQ ID NO: 61 dna connector C032 Bacillus flavothermus α-amylase short linker SEQ ID NO: 62 aa connector C033 Bacillus flavothermus α-amylase long linker SEQ ID NO: 63 dna connector C033 Bacillus flavothermus α-amylase long linker SEQ ID NO: 64 aa connector C034 Bacillus flavothermus α-amylase SEQ ID NO: 65 dna connector C034 Bacillus flavothermus α-amylase SEQ ID NO: 66 aa connector C035 Athelia rolfsii glucoamylase SEQ ID NO: 67 dna connector C035   Glucoamylase from Athena SEQ ID NO: 68 aa connector C036   Aspergillus kawachii glucoamylase SEQ ID NO: 69 DNA connector C036   Aspergillus kawachii glucoamylase SEQ ID NO: 70 Aa connector C037  Aspergillus niger Glucoamylase SEQ ID NO: 71 dna connector C037   Aspergillus niger glucoamylase SEQ ID NO: 72 aa connector C038 Coniochaeta species α-amylase SEQ ID NO: 73 dna connector C038 Coniochaeta species α-amylase SEQ ID NO: 74 aa CBM C039  Pachykytospora papayracea glucoamylase SEQ ID NO: 75 dna

CBM C039 Pachykytospora papayracea glucoamylase SEQ ID NO: 76 aa CBM C040 Trametes cingulata glucoamylase SEQ ID NO: 77 dna CBM C040 Trametes cingulata glucoamylase SEQ ID NO: 78 aa CBM C041 Glucoamylase from Leucopaxillus gigauntes SEQ ID NO: 79 dna CBM C041 Glucoamylase from Leucopaxillus gigantus SEQ ID NO: 80 aa CBM C042 Subulispora provurvata alpha-amylase SEQ ID NO: 81 dna CBM C042 Subulispora provurvata alpha-amylase SE0 ID NO: 82 aa CBM C043 Valsaria rubricosa alpha-amylase SEQ ID NO: 83 dna CBM C043 Valsaria rubricosa alpha-amylase SEQ ID NO: 84 aa CBM C044 Acremonium sp. alpha-amylase SEQ ID NO: 85 dna CBM C044 Acremontum sp. alpha-amylase SEQ ID NO: 86 aa CBM C045 Meripilus giganteus α-amylase SEQ ID NO: 87 dna CBM C045 Meripilus giganteus α-amylase SEQ ID NO: 88 aa CBM C046 Bacillus flavothermus α-amylase SEQ ID NO: 89 dna CBM C046 Bacillus flavothermus α-amylase SEQ ID NO: 90 aa CBM C047 Athelia rolfsii glucoamylase SEQ ID NO: 91 dna CBM C047 Athelia rolfsii glucoamylase SEQ ID NO: 92 aa CBM C048 Aspergillus kawachii glucoamylase SEQ ID NO: 93 dna CBM C048 Aspergillus kawachii glucoamylase SEQ ID NO: 94 aa CBM C049 Aspergillus niger glucoamylase SEQ ID NO: 95 dna CBM C049 Aspergillus niger glucoamylase SEQ ID NO: 96 aa CBM C050 Coniochaeta sp. SEQ ID NO: 97 dna CBM C050 Coniochaeta sp. SEQ ID NO: 98 aa hybrid V051 Hybrid of Fungamyl Variant CD and A. raciferum Glucoamylase CBM SEQ ID NO: 99 dna hybrid V051 Hybrid of Fungamyl Variant CD and A. raciferum Glucoamylase CBM SEQ ID NO: 100 aa hybrid V019 A hybrid of Rhizomucor pumila α-amylase CD and Athelia raciferum glucoamylase CBM SEQ ID NO: 101 aa hybrid V022 Hybrid of α-amylase from Macroporus and glucoamylase CBM from Athena rotundum SEO ID NO: 102 aa plasmid pLA1 plasmid SEQ ID NO: 103 dna Primer P001 Primer SEQ ID NO: 104 dna Primer P002 Primer SEQ ID NO: 105 dna Primer P003 Primer SEQ ID NO: 106 dna Primer P004 Primer SEQ ID NO: 107 dna CBM corn SEQ ID NO: 108 dna CBM corn SEQ ID NO: 109 aa CD C051 Thermoascus sp. II SEQ ID NO: 110 dna CD C051 Thermoascus species II α-amylase SEQ ID NO: 111 aa CD C055 Coniochaeta sp. II α-amylase SEQ ID NO: 112 dna CD C055 Coniochaeta sp. II α-amylase SEQ ID NO: 113 aa CD C052 Nectria sp. α-amylase SEQ ID NO: 114 dna CD C052 Nectria sp. α-amylase SEQ ID NO: 115 aa CD C054 Fusarium α-amylase SEQ ID NO: 116 dna CD C054 Fusarium α-amylase SEQ ID NO: 117 aa CD C057 Trametes corrugate α-amylase SEQ ID NO: 118 dna CD C057 Trametes corrugata alpha-amylase SEQ ID NO: 119 aa CD C059 Penicillium α-amylase SEQ ID NO: 120 dna CD C059 Penicillium α-amylase SEQ ID NO: 121 aa CD C060 Valsaria spartii alpha-amylase SEQ ID NO: 122 dna CD C060 Valsaria spartii alpha-amylase SEQ ID NO: 123 aa CD C061 Thermoascus aurantiacus α-amylase SEQ ID NO: 124 dna

CD C061 Thermoascus aurantiacus α-amylase SEQ ID NO: 125 aa CD C062 Phanerochaete chrysosporium α-amylase SEQ ID NO: 126 dna CD C062 Phanerochaete chrysosporium α-amylase SEQ ID NO: 127 aa CD C063 Rhizopus oryzae α-amylase SEQ ID NO: 128 dna CD C063 Rhizopus oryzae α-amylase SEQ ID NO: 129 aa CD C064 Thaminidium elegans alpha-amylase SEQ ID NO: 130 dna CD C064 Thaminidium elegans alpha-amylase SEQ ID NO: 131 aa CD C065 Absidia cristata α-amylase SEQ ID NO: 132 dna CD C065 Absidia crescens α-amylase SEQ ID NO: 133 aa CD C066 Syncephalastrum racemosum α-amylase SEQ ID NO: 134 dna CD C066 Syncephalastrum racemosum α-amylase SEQ ID NO: 135 aa CBM C067 Coniochaeta sp. α-amylase SEQ ID NO: 136 dna CBM C067 Coniochaeta sp. α-amylase SEQ ID NO: 137 aa CBM C068 Trametes corrugata alpha-amylase SEQ ID NO: 138 dna CBM C068 Trametes corrugata alpha-amylase SEQ ID NO: 139 aa CBM C069 Valsario spartii α-amylase SEQ ID NO: 140 dna CBM C069 Valsario spartii α-amylase SEQ ID NO: 141 aa CBM C070 Penicillium α-amylase SEQ ID NO: 142 dna CBM C070 Penicillium α-amylase SEQ ID NO: 143 aa Connector C072 Coniochaeta sp. α-amylase SEQ ID NO: 144 dna Connector C072 Coniochaeta sp. α-amylase SEQ ID NO: 145 aa Connector C073 Trametes corrugata alpha-amylase SEQ ID NO: 146 dna Connector C073 Trametes corrugata alpha-amylase SEQ ID NO: 147 aa Connector C074 Valsario spartii α-amylase SEQ ID NO: 148 na Connector C074 Valsario spartii α-amylase SEQ ID NO: 149 aa Connector C075 Penicillium α-amylase SEQ ID NO: 150 dna Connector C075 Penicillium α-amylase SEQ ID NO: 151 aa CD C077 Streptomyces limosus α-amylase SEQ ID NO: 154 dna CD C077 Streptomyces limosus α-amylase SEQ ID NO: 155 aa

Embodiment 1: the construction of the nucleic acid sequence V019 of coding Rhizomucor pusillus (Rhizomucor pusillus) alpha-amylase and Athelia rolfsii (Athelia rolfsii) glucoamylase CBM

Vector pLA1 was digested with appropriate restriction endonucleases to excise the region encoding the catalytic domain of the A. niger alpha-amylase. Use primers P001 (SEQ ID NO: 104) and P002 (SEQ ID NO: 105) to amplify the Rhizomucor microbes α-amylase gene by PCR, and the amplified fragment is shown in SEQ ID NO: 19.

PCR reaction system: condition: 38.9μL5μL1μL4μL0.3μL X 20.5μL H ₂ O10X reaction buffer Klen Taq LA (CLONTECH)10mM dNTPs100pmole/μL primer template DNA 121-23 98℃68℃ 10 seconds 90 seconds 30 cycles 68°C 10 minutes

DNA fragments were recovered from agarose gels using a Qiagen gel extraction kit. The resulting purified fragments were mixed with the vector digest. The mixed solution was introduced into Saccharomyces cerevisiae to construct expression plasmid pLAV019 by in vivo recombination.

Embodiment 2: the construction of the nucleic acid sequence V022 of encoding giant polyporus (Meripilus giganteus) α-amylase and Athena glucoamylase CBM

Use primers P003 (SEQ ID NO: 106) and P004 (SEQ ID NO: 107) to PCR amplify polyporus macroporus α-amylase gene.

DNA fragments were recovered from agarose gels using a Qiagen gel extraction kit. The resulting purified fragment was mixed with the vector pLA1 in which the catalytic domain encoding the A. niger α-amylase was excised by digestion with an appropriate restriction endonuclease. The mixed solution was introduced into Saccharomyces cerevisiae to construct expression plasmid pLAV022 by in vivo recombination.

Example 3. Expression of amylase with CBM in Aspergillus oryzae

The constructs described in Examples 1 and 2 containing the α-amylase gene with CBM were used to construct expression vectors pAspV019 and pAspV022, respectively. The two plasmids, pAspV019 and pAspV022, consist of an expression cassette based on the Aspergillus niger neutral amylase II promoter and the Aspergillus niger amyloglycosidase terminator (Tamg), the neutral amylase II promoter Fused to the untranslated leader sequence (Pna2/tpi) of Aspergillus nidulans triose phosphate isomerase. Also present on the plasmid is the Aspergillus selectable marker amdS from A. nidulans, which allows growth on acetamide as the sole nitrogen source. Expression plasmids pAspV019 and pAspV022 were transformed into Aspergillus as described in Lassen et al. (2001), Applied and Environmental Micorbiology, 67, 4701-4707. Transformants expressing V019 and V022 were isolated, purified and cultured in shake flasks. The broth obtained from the fermentation of Aspergillus oryzae expressing the amylase with CBM was purified by affinity purification (Biochem. J. (2003) 372, 905-910).

Example 4. Amylases with CBM

Polypeptides of the present invention were produced; the selected catalytic domain was fused to the linker-CBM region of A. roxarii glucoamylase and the selected CBM region was attached to the C003 Aspergillus oryzae catalytic domain (Fungamyl PE variant).

Since the CBM+ linker from Trichophaea saccata α-amylase is located at the N-terminus, it was inserted between the SP288 signal and the A. oryzae catalytic domain. The other CBMs are placed at the C-terminus.

Variant V008 contains both the A. raciferae glucoamylase linker and the CBM region placed at the C-terminus, and the linker+CBM from Trichophaea saccata α-amylase placed at the N-terminus.

The CBM variants of the Aspergillus oryzae alpha-amylase and the catalytic domain variants of the A. oryzae glucoamylase CBM are listed in Tables 3 and 4, respectively. Other polypeptides produced by the present invention are listed in Tables 5 and 6.

The variants have improved activity towards starch, especially granular starch.

table 3

Have the polypeptide of aspergillus oryzae α-amylase Fungamyl variant catalytic domain (SEQ ID NO: 6) Code Joints and CBMs from CBM Connector V001 Sublispora provurvata alpha-amylase SEQ ID NO: 82 SEQ ID NO: 54 V002 Valsaria rubricosa SEQ ID NO: 84 SEQ ID NO: 56 V003 Alpha-amylases from Acremonium sp. SEQ ID NO: 86 SEQ ID NO: 58 V004 glucoamylase SEQ ID NO: 76 SEQ ID NO: 46 V005 Trametes cingulata glucoamylase SEQ ID NO: 78 SEQ ID NO: 48 V006 Pleurotus glucoamylase SEQ ID NO: 80 SEQ ID NO: 50 V007 Macroporus α-amylase SEQ ID NO: 88 SEQ ID NO: 60 V008 Trichophaea saccata α-amylase (CBM21-N-terminal including linker) SEQ ID NO: 52 +A. roerii glucoamylase (C-terminal) SEQ ID NO: 92 SEQ ID NO: 68 V009 Trichophaea saccata α-amylase (CBM21-N-terminal including linker) SEQ ID NO: 52

V010 Bacillus flavothermus alpha-amylase with a short linker SEQ ID NO: 90 SEQ ID NO: 62 V011   Bacillus flavora alpha-amylase with long linker SEQ ID NO: 90 SEQ ID NO: 64 V012 Bacillus flavus α-amylase SEQ ID NO: 90 SEQ ID NO: 66

Table 4

Polypeptides with A. raciferae glucoamylase linker (SEQ ID NO: 68) and CBM (SEQ ID NO: 92) Code Catalyst module from: Catalytic Domain SEQ ID V013 Trichophaea saccata alpha-amylase SEQ ID NO: 8 V014 Subulispora provurvata alpha-amylase SEQ ID NO: 10 V015 Valsaria rubricosa alpha-amylase SEQ ID NO: 12 V016 Thermomyces lanuginosa α-amylase SEQ ID NO: 14 V017 Acremonium α-amylase SEQ ID NO: 16 V018 Malbranchea species α-amylase SEQ ID NO: 18 V019 Rhizomucor microbes α-amylase SEQ ID NO: 20 V021 Dichotomocladium hesseltinei alpha-amylase SEQ ID NO: 22 V022 Macroporus α-amylase SEQ ID NO: 24 V023 Bacteria of the genus Resus SEQ ID NO: 26 V024 Streptomyces limosus α-amylase SEQ ID NO: 155 V025 Coriolus censors SEQ ID NO: 30 V026 Dinemasporium sp. α-amylase SEQ ID NO: 32 V027 Cryptosporiopsis species α-amylase SEQ ID NO: 34 V028 Coniochaeta sp. α-amylase SEQ ID NO: 36 V029 Diplodia sp. α-amylase SEQ ID NO: 38

V030 Nectria sp. α-amylase SEQ ID NO: 40 V031 Gliocladium sp. α-amylase SEQ ID NO: 42 V032 Streptomyces thermocyaneoviolaceus α-amylase SEQ ID NO: 44 V047 Thermoascus sp. II SEQ ID NO: 111 V048 Species of Conechaeta 2 SEQ ID NO: 113 V049 α-amylase SEQ ID NO: 115 V050 Fusarium sp. SEQ ID NO: 117 V051 Trametes corrugata SEQ ID NO: 119 V052 Valsaria spartii SEQ ID NO: 123 V054 Thermoascus aurantiacus SEQ ID NO: 125 V055 Penicillum sp. SEQ ID NO: 121 V057 Phanerochaetechrysosporium SEQ ID NO: 127 V059 Rhizopus oryzae SEQ ID NO: 129 V060 Thaminidium elegans SEQ ID NO: 131 V061 Absidia cristata SEQ ID NO: 133 V063 Syncephalastrum racemosum SEQ ID NO: 135

table 5

Polypeptides with other catalytic domains/CBMs with linkers. The CBM and linker in V069 have different origins. Code domain from: CDSEQ IDNO CBM and connectors from: Connector SEQ IDNO CBMSEQ IDNO V033 Acremonium α-amylase SEQ ID NO: 16 glucoamylase SEQ ID NO: 46 SEQ ID NO: 145 V034 Rhizomucor microbes α-amylase SEQ ID NO: 20 glucoamylase SEQ ID NO: 46 SEQ ID NO: 145 V035 Macroporus α-amylase SEQ ID NO: 24 glucoamylase SEQ ID NO: 46 SEQ ID NO: 145 V036 Macroporus α-amylase SEQ ID NO: 24 Valsaria rubricosa SEQ ID NO: 56 SEQ ID NO: 84 V037 Macroporus α-amylase SEQ ID NO: 24 Macroporus α-amylase SEQ ID NO: 60 SEQ ID NO: 88 V038 Rhizomucor microbes α-amylase SEQ ID NO: 20 Aspergillus basilica glucoamylase SEQ ID NO: 70 SEQ ID NO: 94 V039 Rhizomucor microbes α-amylase SEQ ID NO: 20 Aspergillus niger glucoamylase SEQ ID NO: 72 SEQ ID NO: 96 V040 Aspergillus oryzae Fungamyl variant SEQ ID NO: 06 Conechaeta sp. AM603 SEQ ID NO: 74 SEQ ID NO: 98 V069 Macroporus α-amylase SEQ ID NO: 24 Corn CBM Athena glucoamylase linker SEQ ID NO: 68 SEQ ID NO: 109

Table 6

Polypeptide with Rhizomucor pumila alpha-amylase catalytic domain (SEQ ID NO: 20), and CBM and linker from: Code CBM from CBM SEQ IDNO Connectors from Connector SEQ IDNO V041 Athena glucoamylase SEQ ID NO: 92 Aspergillus basilica α-amylase SEQ ID NO: 70 V042 Athena glucoamylase SEQ ID NO: 92 Aspergillus niger glucoamylase SEQ ID NO: 72 V043 corn SEQ ID NO: 109 Athena glucoamylase SEQ ID NO: 68 V064 Species of the genus Conechaeta SEQ ID NO: 113 Species of the genus Conechaeta SEQ ID NO: 145 V065 Trametes rugosa SEQ ID NO: 119 Trametes rugosa SEQ ID NO: 147 V066 Valsaria spartii SEQ ID NO: 123 Valsaria spartii SEQ ID NO: 149 V067 Penicillium species SEQ ID NO: 121 Penicillium species SEQ ID NO: 151 V068 giant polypore SEQ ID NO: 88 giant polypore SEQ ID NO: 60

Example 5

The performance of polypeptide V019 was evaluated in small scale fermentations with different doses of Talaromyces emersonii glucoamylase. The starch substrate, 583.3 g of ground corn, was added to 912.2 g of tap water. To this mixture was supplemented 4.5 ml of 1 g/L penicillin solution. The pH of the slurry was adjusted to _5.0 with 40% _H2SO4 . The DS level was determined in duplicate to be 34.2 ± 0.8%. Approximately 5 g of this slurry was added to a 20 ml vial. Each vial was dosed with the appropriate amount of enzyme, followed by the addition of 200 [mu]L yeast propagation/5 g slurry. Actual dosage is based on the exact weight of corn syrup in each vial. The vial was incubated at 32°C. Weight loss was measured over time after fermentation. Fermentation was terminated at 70 hours and HPLC analysis was prepared. Preparation for HPLC included stopping the reaction by adding 50 μL of 40% _H2SO4 , centrifugation, and filtration through _a 0.45 micron filter. Samples pending HPLC analysis were stored at 4°C.

Table 7

Performance of polypeptide V019 in small-scale fermentation. Relative to 70 hours ethanol at 0.14 AGU/DS and no alpha-amylase. Amylase dosage (mg protein/gDS) Dosage of T. emersonii glucoamylase (AGU/g DS) 70 hours ethanol 0 0.14 1.00 0 0.50 1.35 0 0.86 1.73 0.05 none 3.69 0.05 0.14 3.69 0.05 0.50 3.73 0.05 0.86 3.73

Example 6

DE 11 maltodextrin prepared by dissolving corn starch liquefied with thermostable bacterial α-amylase (LIQUOZYME X ^TM , Novozymes A/S) in Milli-Q ^TM water and adjusting the dry solids content (DS) to 30%, while preparing the substrate for saccharification. Saccharification experiments were performed in sealed 2 ml glass vials at 60°C, initial pH 4.3, with constant agitation. Two different doses of CBM alpha-amylase V019 or V022 were applied immediately after standard treatment with 0.35 AGU/g DS T. emersonii glucoamylase and 0.04 AFAU/g DS Aspergillus niger acid alpha-amylase .

Samples were taken at regular intervals and heated in boiling water for 15 minutes to inactivate the enzyme. After cooling, samples were diluted to 5% DS and filtered (Sartorius MINISART ^™ NML 0.2 micron) before HPLC analysis. Glucose levels expressed as a percentage of total soluble carbohydrates are provided in Table 8 below.

Table 8

All were treated with 0.35 AGU/g DS T. emersonii glucoamylase and 0.04 AFAU/g DS A. niger acid alpha-amylase. Next, acid alpha-amylase variants V019 and V022 were dosed according to the table.

DPI extra enzyme Acid alpha-amylase variant AFAU/g DS 24h 48h 70h Control V019V022 00.08750.17500.08750.1750 81.595.792.193.892.9 90.296.296.295.695.9 93.195.696.295.596.0

Example 7

Evaluation of raw starch SSF treatment in small-scale fermentations. A granular starch slurry of 35% DS was obtained by mixing 410 g of finely ground corn, 590 ml of tap water, 3.0 ml of 1 g/L penicillin and 1 g of urea. The pH of the slurry was adjusted to 4.5 with 5N NaOH and 5 g of sample was dispensed into 20 ml vials. Add the appropriate amount of enzyme quantitatively and inoculate the vial with yeast. The vial was incubated at 32°C. Nine replicate fermentations were performed for each treatment. Triplicates were selected for analysis at the 24 hr, 48 hr and 70 hr time points. Vials were vortexed at 24, 48 and 70 hours. Time point analysis included weighing vials and preparing samples for HPLC. For HPLC, the reaction was stopped by adding 50 μL of 40% _H2SO4 , centrifuged, and filtered through _a 0.45 μm filter. Samples were stored at 4°C pending HPLC analysis.

Example 7a

Enzymes and amounts used are shown in the table below. A-AMG is an Aspergillus niger glucoamylase composition.

Table 9

Raw starch SSF with Aspergillus niger glucoamylase and V019, enzyme dosage test number % dose mg/gDS AGU/gDS AFAU/gDS A-AMG V019 A-AMG V019 A-AMG V019 2 100% 0% 0.5 0 0.95 0 3 90% 10% 0.45 0.01 0.855 0.01 4 80% 20% 0.4 0.02 0.76 0.02 5 70% 30% 0.35 0.03 0.665 0.03 6 60% 40% 0.3 0.04 0.57 0.04 7 45% 55% 0.225 0.055 0.4275 0.055 8 30% 70% 0.15 0.07 0.285 0.07 9 15% 85% 0.075 0.085 0.1425 0.085 10 0% 100% 0 0.1 0 0.1

In the ratio range of A. niger AMG to V019 of 1.7-85.5 AGU/AFAU, very good ethanol yields after 70 hours of fermentation were observed, showing the excellent performance of the mixture of A. niger AMG and V019 over a wide range of activity ratios .

Table 10

Raw starch SSF with Aspergillus niger glucoamylase and V019, results test number AGU/gDS AFAU/gDS Ethanol production (g/l) AGU/AFAU ratio A-AMG V019 24hrs 48hr 70hrs 2345678910 0.9500.8550.7600.6650.5700.4280.2850.1430.000 0.0000.0100.0200.0300.0400.0550.0700.0850.100 77.792.993.192.691.690.187.1184.380.8 119.46134.6133.7134.3132.8130.8127.7120.9114.55 139.2144.3145.4147.5145.7146.2144.8143.4134.0 N/A85.538.022.214.37.84.11.70.0

Example 7b

Enzymes and amounts used are shown in the table below. A-AMG is T. emersonii glucoamylase composition.

Table 11

Raw starch SSF with T. emersonii glucoamylase and V019, enzyme dosage test number % dose mg/gDS AGU/gDS AFAU/gDS T-AMG V019 T-AMG V019 T-AMG V019 2345678910 100% 90% 80% 70% 60% 45% 30% 15% 0% 0% 10% 20% 30% 40% 55% 70% 85% 100% 0.30.270.240.210.180.1350.090.0450 00.010.020.030.040.0550.070.0850.1 2.42.161.921.681.441.080.720.360 00.010.020.030.040.0550.070.0850.1

Over the range of T. emersonii AMG to V019 ratios of 10-216 AGU/AFAU, very good ethanol production after 70 hours of fermentation was observed, showing a broad range of activity ratios for mixtures of T. emersonii AMG to V019 scope.

Table 12

Raw starch SSF with T. emersonii glucoamylase and V019, results test number AGU/g DS AFAU/gDS Ethanol production (g/l) AGU/AFAU ratio Sp Fuel V019 24hrs 48hrs 70hrs 2345678910 2.42.161.921.681.441.080.720.360 00.010.020.030.040.0550.070.0850.1 60.0789.0091.0293.3193.7192.8391.2586.1480.63 91.77129.36132.07133.75134.16131.53125.48124.22115.00 113.17142.91147.18148.19146.84141.80139.25137.38132.08 N/A216.096.056.036.019.610.34.20.0

biological material deposit

The following biological material has been deposited with the Deutsche Sammmlung von Microorganismen und Zellkulturen GmbH (DSMZ), Mascheroder Weg 1b, D-38124 Braunschweig DE under the Budapest Treaty and has been assigned the following accession number:

Deposit Deposit No. Deposit Date

Escherichia coli NN049798 DSM17106 February 2, 2005

Escherichia coli NN049797 DSM17105 February 2, 2005

Said strains have been deposited under conditions ensuring that those persons whom the Board of Patents and Trademarks determine to be entitled under 37 C.F.R. §1.14 and 35 U.S.C. §122 have access to the culture during the pendency of this patent application. The deposits are substantially pure cultures of the deposited strains. In foreign countries where counterparts of said applications, or sub-applications thereof, are filed, the deposits are available as required by the patent laws of those countries. It should be understood, however, that the availability of this deposit does not constitute a license to practice the invention in infringement of patents granted by action of the government.

sequence listing

<110> Novozymes (NOVOZYMES A/S)

Novozymes North America Inc. (NOVOZYMES NORTH AMERICA, INC.)

Fukuyama, Shiro

Matsui, Tomoko

Soong, Chee Leong

Allain, Eric

Nielsen, Anders Vikso

Udagawa, Hiroaki

Liu, Ye

Duan, Junxin

Wu, Wenping

Andersen, Lene Nonboe

<120> Enzymes for starch processing

<130>10729.500-US

<160>179

<170>PatentIn version 3.3

<210>1

<211>1533

<212>DNA

<213> Aspergillus niger

<220>

<221> CDS

<222>(1)..(1533)

<400>1

atg aga tta tcg act tcg agt ctc ttc ctt tcc gtg tct ctg ctg ggg 48

Met Arg Leu Ser Thr Ser Ser Ser Leu Phe Leu Ser Val Ser Leu Leu Gly

1 5 10 15

aag ctg gcc ctc ggg ctg tcg gct gca gaa tgg cgc act cag tcg att 96

Lys Leu Ala Leu Gly Leu Ser Ala Ala Glu Trp Arg Thr Gln Ser Ile

20 25 30

tac ttc cta ttg acg gat cgg ttc ggt agg acg gac aat tcg acg aca 144

Tyr Phe Leu Leu Thr Asp Arg Phe Gly Arg Thr Asp Asn Ser Thr Thr

35 40 45

gct aca tgc gat acg ggt gac caa atc tat tgt ggt ggc agt tgg caa 192

Ala Thr Cys Asp Thr Gly Asp Gln Ile Tyr Cys Gly Gly Ser Trp Gln

50 55 60

gga atc atc aac cat ctg gat tat atc cag ggc atg gga ttc acg gcc 240

Gly Ile Ile Asn His Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala

65 70 75 80

atc tgg atc tcg cct atc act gaa cag ctg ccc cag gat act gct gat 288

Ile Trp Ile Ser Pro Ile Thr Glu Gln Leu Pro Gln Asp Thr Ala Asp

85 90 95

ggt gaa gct tac cat gga tat tgg cag cag aag ata tac gac gtg aac 336

Gly Glu Ala Tyr His Gly Tyr Trp Gln Gln Lys Ile Tyr Asp Val Asn

100 105 110

tcc aac ttc ggc act gca gat gac ctc aag tcc ctc tca gat gcg ctt 384

Ser Asn Phe Gly Thr Ala Asp Asp Leu Lys Ser Leu Ser Asp Ala Leu

115 120 125

cat gcc cgc gga atg tac ctc atg gtg gac gtc gtc cct aac cac atg 432

His Ala Arg Gly Met Tyr Leu Met Val Asp Val Val Pro Asn His Met

130 135 140

ggc tac gcc ggc aac ggc aac gat gta gac tac agc gtc ttc gac ccc 480

Gly Tyr Ala Gly Asn Gly Asn Asp Val Asp Tyr Ser Val Phe Asp Pro

145 150 155 160

ttc gat tcc tcc tcc tac ttc cac cca tac tgc ctg atc aca gat tgg 528

Phe Asp Ser Ser Ser Tyr Phe His Pro Tyr Cys Leu Ile Thr Asp Trp

165 170 175

gac aac ttg acc atg gtc caa gat tgt tgg gag ggt gac acc atc gta 576

Asp Asn Leu Thr Met Val Gln Asp Cys Trp Glu Gly Asp Thr Ile Val

180 185 190

tct ctg cca gac cta aac acc acc gaa act gcc gtg aga aca atc tgg 624

Ser Leu Pro Asp Leu Asn Thr Thr Glu Thr Ala Val Arg Thr Ile Trp

195 200 205

tat gac tgg gta gcc gac ctg gta tcc aat tat tca gtc gac gga ctc 672

Tyr Asp Trp Val Ala Asp Leu Val Ser Asn Tyr Ser Val Asp Gly Leu

210 215 220

cgc atc gac agt gtc ctc gaa gtc gaa cca gac ttc ttc ccg ggc tac 720

Arg Ile Asp Ser Val Leu Glu Val Glu Pro Asp Phe Phe Pro Gly Tyr

225 230 235 240

cag gaa gca gca ggt gtc tac tgc gtc ggc gaa gtc gac aac ggc aac 768

Gln Glu Ala Ala Gly Val Tyr Cys Val Gly Glu Val Asp Asn Gly Asn

245 250 255

cct gcc ctc gac tgc cca tac cag aag gtc ctg gac ggc gtc ctc aac 816

Pro Ala Leu Asp Cys Pro Tyr Gln Lys Val Leu Asp Gly Val Leu Asn

260 265 270

tat ccg atc tac tgg caa ctc ctc tac gcc ttc gaa tcc tcc agc ggc 864

Tyr Pro Ile Tyr Trp Gln Leu Leu Tyr Ala Phe Glu Ser Ser Ser Ser Gly

275 280 285

agc atc agc aat ctc tac aac atg atc aaa tcc gtc gca agc gac tgc 912

Ser Ile Ser Asn Leu Tyr Asn Met Ile Lys Ser Val Ala Ser Asp Cys

290 295 300

tcc gat ccg aca cta ctc ggc aac ttc atc gaa aac cac gac aat ccc 960

Ser Asp Pro Thr Leu Leu Gly Asn Phe Ile Glu Asn His Asp Asn Pro

305 310 315 320

cgt ttc gcc tcc tac acc tcc gac tac tcg caa gcc aaa aac gtc ctc 1008

Arg Phe Ala Ser Tyr Thr Ser Asp Tyr Ser Gln Ala Lys Asn Val Leu

325 330 335

agc tac atc ttc ctc tcc gac ggc atc ccc atc gtc tac gcc ggc gaa 1056

Ser Tyr Ile Phe Leu Ser Asp Gly Ile Pro Ile Val Tyr Ala Gly Glu

340 345 350

gaa cag cac tac tcc ggc ggc aag gtg ccc tac aac cgc gaa gcg acc 1104

Glu Gln His Tyr Ser Gly Gly Lys Val Pro Tyr Asn Arg Glu Ala Thr

355 360 365

tgg ctt tca ggc tac gac acc tcc gca gag ctg tac acc tgg ata gcc 1152

Trp Leu Ser Gly Tyr Asp Thr Ser Ala Glu Leu Tyr Thr Trp Ile Ala

370 375 380

acc acg aac gcg atc cgc aaa cta gcc atc tca gct gac tcg gcc tac 1200

Thr Thr Asn Ala Ile Arg Lys Leu Ala Ile Ser Ala Asp Ser Ala Tyr

385 390 395 400

att acc tac gcg aat gat gca ttc tac act gac agc aac acc atc gca 1248

Ile Thr Tyr Ala Asn Asp Ala Phe Tyr Thr Asp Ser Asn Thr Ile Ala

405 410 415

atg cgc aaa ggc acc tca ggg agc caa gtc atc acc gtc ctc tcc aac 1296

Met Arg Lys Gly Thr Ser Gly Ser Gln Val Ile Thr Val Leu Ser Asn

420 425 430

aaa ggc tcc tca gga agc agc tac acc ctg acc ctc agc gga agc ggc 1344

Lys Gly Ser Ser Ser Gly Ser Ser Tyr Thr Leu Thr Leu Ser Gly Ser Gly

435 440 445

tac aca tcc ggc acg aag ctg atc gaa gcg tac aca tgc aca tcc gtg 1392

Tyr Thr Ser Gly Thr Lys Leu Ile Glu Ala Tyr Thr Cys Thr Ser Val

450 455 460

acc gtg gac tcg agc ggc gat att ccc gtg ccg atg gcg tcg gga tta 1440

Thr Val Asp Ser Ser Gly Asp Ile Pro Val Pro Met Ala Ser Gly Leu

465 470 475 480

ccg aga gtt ctt ctg ccc gcg tcc gtc gtc gat agc tct tcg ctc tgt 1488

Pro Arg Val Leu Leu Pro Ala Ser Val Val Asp Ser Ser Ser Leu Cys

485 490 495

ggc ggg agc gga aga aca acc acg acc aca act gct gct act agt 1533

Gly Gly Ser Gly Arg Thr Thr Thr Thr Thr Thr Thr Ala Ala Thr Ser

500 505 510

<210>2

<211>511

<212>PRT

<213> Aspergillus niger

<400>2

Met Arg Leu Ser Thr Ser Ser Ser Leu Phe Leu Ser Val Ser Leu Leu Gly

1 5 10 15

Lys Leu Ala Leu Gly Leu Ser Ala Ala Glu Trp Arg Thr Gln Ser Ile

20 25 30

Tyr Phe Leu Leu Thr Asp Arg Phe Gly Arg Thr Asp Asn Ser Thr Thr

35 40 45

Ala Thr Cys Asp Thr Gly Asp Gln Ile Tyr Cys Gly Gly Ser Trp Gln

50 55 60

Gly Ile Ile Asn His Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala

65 70 75 80

Ile Trp Ile Ser Pro Ile Thr Glu Gln Leu Pro Gln Asp Thr Ala Asp

85 90 95

Gly Glu Ala Tyr His Gly Tyr Trp Gln Gln Lys Ile Tyr Asp Val Asn

100 105 110

Ser Asn Phe Gly Thr Ala Asp Asp Leu Lys Ser Leu Ser Asp Ala Leu

115 120 125

His Ala Arg Gly Met Tyr Leu Met Val Asp Val Val Pro Asn His Met

130 135 140

Gly Tyr Ala Gly Asn Gly Asn Asp Val Asp Tyr Ser Val Phe Asp Pro

145 150 155 160

Phe Asp Ser Ser Ser Tyr Phe His Pro Tyr Cys Leu Ile Thr Asp Trp

165 170 175

Asp Asn Leu Thr Met Val Gln Asp Cys Trp Glu Gly Asp Thr Ile Val

180 185 190

Ser Leu Pro Asp Leu Asn Thr Thr Glu Thr Ala Val Arg Thr Ile Trp

195 200 205

Tyr Asp Trp Val Ala Asp Leu Val Ser Asn Tyr Ser Val Asp Gly Leu

210 215 220

Arg Ile Asp Ser Val Leu Glu Val Glu Pro Asp Phe Phe Pro Gly Tyr

225 230 235 240

Gln Glu Ala Ala Gly Val Tyr Cys Val Gly Glu Val Asp Asn Gly Asn

245 250 255

Pro Ala Leu Asp Cys Pro Tyr Gln Lys Val Leu Asp Gly Val Leu Asn

260 265 270

Tyr Pro Ile Tyr Trp Gln Leu Leu Tyr Ala Phe Glu Ser Ser Ser Ser Gly

275 280 285

Ser Ile Ser Asn Leu Tyr Asn Met Ile Lys Ser Val Ala Ser Asp Cys

290 295 300

Ser Asp Pro Thr Leu Leu Gly Asn Phe Ile Glu Asn His Asp Asn Pro

305 310 315 320

Arg Phe Ala Ser Tyr Thr Ser Asp Tyr Ser Gln Ala Lys Asn Val Leu

325 330 335

Ser Tyr Ile Phe Leu Ser Asp Gly Ile Pro Ile Val Tyr Ala Gly Glu

340 345 350

Glu Gln His Tyr Ser Gly Gly Lys Val Pro Tyr Asn Arg Glu Ala Thr

355 360 365

Trp Leu Ser Gly Tyr Asp Thr Ser Ala Glu Leu Tyr Thr Trp Ile Ala

370 375 380

Thr Thr Asn Ala Ile Arg Lys Leu Ala Ile Ser Ala Asp Ser Ala Tyr

385 390 395 400

Ile Thr Tyr Ala Asn Asp Ala Phe Tyr Thr Asp Ser Asn Thr Ile Ala

405 410 415

Met Arg Lys Gly Thr Ser Gly Ser Gln Val Ile Thr Val Leu Ser Asn

420 425 430

Lys Gly Ser Ser Ser Gly Ser Ser Tyr Thr Leu Thr Leu Ser Gly Ser Gly

435 440 445

Tyr Thr Ser Gly Thr Lys Leu Ile Glu Ala Tyr Thr Cys Thr Ser Val

450 455 460

Thr Val Asp Ser Ser Gly Asp Ile Pro Val Pro Met Ala Ser Gly Leu

465 470 475 480

Pro Arg Val Leu Leu Pro Ala Ser Val Val Asp Ser Ser Ser Leu Cys

485 490 495

Gly Gly Ser Gly Arg Thr Thr Thr Thr Thr Thr Thr Ala Ala Thr Ser

500 505 510

<210>3

<211>1440

<212>DNA

<213> Aspergillus oryzae

<220>

<221> CDS

<222>(1)..(1440)

<400>3

gca acg cct gcg gac tgg cga tcg caa tcc att tat ttc ctt ctc acg 48

Ala Thr Pro Ala Asp Trp Arg Ser Gln Ser Ile Tyr Phe Leu Leu Thr

1 5 10 15

gat cga ttt gca agg acg gat ggg tcg acg act gcg act tgt aat act 96

Asp Arg Phe Ala Arg Thr Asp Gly Ser Thr Thr Ala Thr Cys Asn Thr

20 25 30

gcg gat cag aaa tac tgt ggt gga aca tgg cag ggc atc atc gac aag 144

Ala Asp Gln Lys Tyr Cys Gly Gly Thr Trp Gln Gly Ile Ile Asp Lys

35 40 45

ttg gac tat atc cag gga atg ggc ttc aca gcc atc tgg atc acc ccc 192

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Thr Pro

50 55 60

gtt aca gcc cag ctg ccc cag acc acc gca tat gga gat gcc tac cat 240

Val Thr Ala Gln Leu Pro Gln Thr Thr Ala Tyr Gly Asp Ala Tyr His

65 70 75 80

ggc tac tgg cag cag gat ata tac tct ctg aac gaa aac tac ggc act 288

Gly Tyr Trp Gln Gln Asp Ile Tyr Ser Leu Asn Glu Asn Tyr Gly Thr

85 90 95

gca gat gac ttg aag gcg ctc tct tcg gcc ctt cat gag agg ggg atg 336

Ala Asp Asp Leu Lys Ala Leu Ser Ser Ala Leu His Glu Arg Gly Met

100 105 110

tat ctt atg gtc gat gtg gtt gct aac cat atg ggc tat gat gga gcg 384

Tyr Leu Met Val Asp Val Val Ala Asn His Met Gly Tyr Asp Gly Ala

115 120 125

ggt agc tca gtc gat tac agt gtg ttt aaa ccg ttc agt tcc caa gac 432

Gly Ser Ser Val Asp Tyr Ser Val Phe Lys Pro Phe Ser Ser Gln Asp

130 135 140

tac ttc cac ccg ttc tgt ttc att caa aac tat gaa gat cag act cag 480

Tyr Phe His Pro Phe Cys Phe Ile Gln Asn Tyr Glu Asp Gln Thr Gln

145 150 155 160

gtt gag gat tgc tgg cta gga gat aac act gtc tcc ttg cct gat ctc 528

Val Glu Asp Cys Trp Leu Gly Asp Asn Thr Val Ser Leu Pro Asp Leu

165 170 175

gat acc acc aag gat gtg gtc aag aat gaa tgg tac gac tgg gtg gga 576

Asp Thr Thr Lys Asp Val Val Lys Asn Glu Trp Tyr Asp Trp Val Gly

180 185 190

tca ttg gta tcg aac tac tcc att gac ggc ctc cgt atc gac aca gta 624

Ser Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Val

195 200 205

aaa cac gtc cag aag gac ttc tgg ccc ggg tac aac aaa gcc gca ggc 672

Lys His Val Gln Lys Asp Phe Trp Pro Gly Tyr Asn Lys Ala Ala Gly

210 215 220

gtg tac tgt atc ggc gag gtg ctc gac ggt gat ccg gcc tac act tgt 720

Val Tyr Cys Ile Gly Glu Val Leu Asp Gly Asp Pro Ala Tyr Thr Cys

225 230 235 240

ccc tac cag aac gtc atg gac ggc gta ctg aac tat ccc att tac tat 768

Pro Tyr Gln Asn Val Met Asp Gly Val Leu Asn Tyr Pro Ile Tyr Tyr

245 250 255

cca ctc ctc aac gcc ttc aag tca acc tcc ggc agc atg gac gac ctc 816

Pro Leu Leu Asn Ala Phe Lys Ser Thr Ser Gly Ser Met Asp Asp Leu

260 265 270

tac aac atg atc aac acc gtc aaa tcc gac tgt cca gac tca aca ctc 864

Tyr Asn Met Ile Asn Thr Val Lys Ser Asp Cys Pro Asp Ser Thr Leu

275 280 285

ctg ggc aca ttc gtc gag aac cac gac aac cca cgg ttc gct tct tac 912

Leu Gly Thr Phe Val Glu Asn His Asp Asn Pro Arg Phe Ala Ser Tyr

290 295 300

acc aac gac ata gcc ctc gcc aag aac gtc gca gca ttc atc atc ctc 960

Thr Asn Asp Ile Ala Leu Ala Lys Asn Val Ala Ala Phe Ile Ile Leu

305 310 315 320

aac gac gga atc ccc atc atc tac gcc ggc caa gaa cag cac tac gcc 1008

Asn Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ala

325 330 335

ggc gga aac gac ccc gcg aac cgc gaa gca acc tgg ctc tcg ggc tac 1056

Gly Gly Asn Asp Pro Ala Asn Arg Glu Ala Thr Trp Leu Ser Gly Tyr

340 345 350

ccg acc gac agc gag ctg tac aag tta att gcc tcc gcg aac gca atc 1104

Pro Thr Asp Ser Glu Leu Tyr Lys Leu Ile Ala Ser Ala Asn Ala Ile

355 360 365

cgg aac tat gcc att agc aaa gat aca gga ttc gtg acc tac aag aac 1152

Arg Asn Tyr Ala Ile Ser Lys Asp Thr Gly Phe Val Thr Tyr Lys Asn

370 375 380

tgg ccc atc tac aaa gac gac aca acg atc gcc atg cgc aag ggc aca 1200

Trp Pro Ile Tyr Lys Asp Asp Thr Thr Ile Ala Met Arg Lys Gly Thr

385 390 395 400

gat ggg tcg cag atc gtg act atc ttg tcc aac aag ggt gct tcg ggt 1248

Asp Gly Ser Gln Ile Val Thr Ile Leu Ser Asn Lys Gly Ala Ser Gly

405 410 415

gat tcg tat acc ctc tcc ttg agt ggt gcg ggt tac aca gcc ggc cag 1296

Asp Ser Tyr Thr Leu Ser Leu Ser Gly Ala Gly Tyr Thr Ala Gly Gln

420 425 430

caa ttg acg gag gtc att ggc tgc acg acc gtg acg gtt ggt tcg gat 1344

Gln Leu Thr Glu Val Ile Gly Cys Thr Thr Val Thr Val Gly Ser Asp

435 440 445

gga aat gtg cct gtt cct atg gca ggt ggg cta cct agg gta ttg tat 1392

Gly Asn Val Pro Val Pro Met Ala Gly Gly Leu Pro Arg Val Leu Tyr

450 455 460

ccg act gag aag ttg gca ggt agc aag atc tgt agt agc tcg gga aga 1440

Pro Thr Glu Lys Leu Ala Gly Ser Lys Ile Cys Ser Ser Ser Ser Gly Arg

465 470 475 480

<210>4

<211>480

<212>PRT

<213> Aspergillus oryzae

<400>4

Ala Thr Pro Ala Asp Trp Arg Ser Gln Ser Ile Tyr Phe Leu Leu Thr

1 5 10 15

Asp Arg Phe Ala Arg Thr Asp Gly Ser Thr Thr Ala Thr Cys Asn Thr

20 25 30

Ala Asp Gln Lys Tyr Cys Gly Gly Thr Trp Gln Gly Ile Ile Asp Lys

35 40 45

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Thr Pro

50 55 60

Val Thr Ala Gln Leu Pro Gln Thr Thr Ala Tyr Gly Asp Ala Tyr His

65 70 75 80

Gly Tyr Trp Gln Gln Asp Ile Tyr Ser Leu Asn Glu Asn Tyr Gly Thr

85 90 95

Ala Asp Asp Leu Lys Ala Leu Ser Ser Ala Leu His Glu Arg Gly Met

100 105 110

Tyr Leu Met Val Asp Val Val Ala Asn His Met Gly Tyr Asp Gly Ala

115 120 125

Gly Ser Ser Val Asp Tyr Ser Val Phe Lys Pro Phe Ser Ser Gln Asp

130 135 140

Tyr Phe His Pro Phe Cys Phe Ile Gln Asn Tyr Glu Asp Gln Thr Gln

145 150 155 160

Val Glu Asp Cys Trp Leu Gly Asp Asn Thr Val Ser Leu Pro Asp Leu

165 170 175

Asp Thr Thr Lys Asp Val Val Lys Asn Glu Trp Tyr Asp Trp Val Gly

180 185 190

Ser Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Val

195 200 205

Lys His Val Gln Lys Asp Phe Trp Pro Gly Tyr Asn Lys Ala Ala Gly

210 215 220

Val Tyr Cys Ile Gly Glu Val Leu Asp Gly Asp Pro Ala Tyr Thr Cys

225 230 235 240

Pro Tyr Gln Asn Val Met Asp Gly Val Leu Asn Tyr Pro Ile Tyr Tyr

245 250 255

Pro Leu Leu Asn Ala Phe Lys Ser Thr Ser Gly Ser Met Asp Asp Leu

260 265 270

Tyr Asn Met Ile Asn Thr Val Lys Ser Asp Cys Pro Asp Ser Thr Leu

275 280 285

Leu Gly Thr Phe Val Glu Asn His Asp Asn Pro Arg Phe Ala Ser Tyr

290 295 300

Thr Asn Asp Ile Ala Leu Ala Lys Asn Val Ala Ala Phe Ile Ile Leu

305 310 315 320

Asn Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ala

325 330 335

Gly Gly Asn Asp Pro Ala Asn Arg Glu Ala Thr Trp Leu Ser Gly Tyr

340 345 350

Pro Thr Asp Ser Glu Leu Tyr Lys Leu Ile Ala Ser Ala Asn Ala Ile

355 360 365

Arg Asn Tyr Ala Ile Ser Lys Asp Thr Gly Phe Val Thr Tyr Lys Asn

370 375 380

Trp Pro Ile Tyr Lys Asp Asp Thr Thr Ile Ala Met Arg Lys Gly Thr

385 390 395 400

Asp Gly Ser Gln Ile Val Thr Ile Leu Ser Asn Lys Gly Ala Ser Gly

405 410 415

Asp Ser Tyr Thr Leu Ser Leu Ser Gly Ala Gly Tyr Thr Ala Gly Gln

420 425 430

Gln Leu Thr Glu Val Ile Gly Cys Thr Thr Val Thr Val Gly Ser Asp

435 440 445

Gly Asn Val Pro Val Pro Met Ala Gly Gly Leu Pro Arg Val Leu Tyr

450 455 460

Pro Thr Glu Lys Leu Ala Gly Ser Lys Ile Cys Ser Ser Ser Ser Gly Arg

465 470 475 480

<210>5

<211>1434

<212>DNA

<213> Aspergillus oryzae

<220>

<221> CDS

<222>(1)..(1434)

<400>5

gca acg cct gcg gac tgg cga tcg caa tcc att tat ttc ctt ctc acg 48

Ala Thr Pro Ala Asp Trp Arg Ser Gln Ser Ile Tyr Phe Leu Leu Thr

1 5 10 15

gat cga ttt gca agg acg gat ggg tcg acg act gcg act tgt aat act 96

Asp Arg Phe Ala Arg Thr Asp Gly Ser Thr Thr Ala Thr Cys Asn Thr

20 25 30

gcg gat cag aaa tac tgt ggt gga aca tgg cag ggc atc atc gac aag 144

Ala Asp Gln Lys Tyr Cys Gly Gly Thr Trp Gln Gly Ile Ile Asp Lys

35 40 45

ttg gac tat atc cag gga atg ggc ttc aca gcc atc tgg atc acc ccc 192

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Thr Pro

50 55 60

gtt aca gcc cag ctg ccc cag acc acc gca tat gga gat gcc tac cat 240

Val Thr Ala Gln Leu Pro Gln Thr Thr Ala Tyr Gly Asp Ala Tyr His

65 70 75 80

ggc tac tgg cag cag gat ata tac tct ctg aac gaa aac tac ggc act 288

Gly Tyr Trp Gln Gln Asp Ile Tyr Ser Leu Asn Glu Asn Tyr Gly Thr

85 90 95

gca gat gac ttg aag gcg ctc tct tcg gcc ctt cat gag agg ggg atg 336

Ala Asp Asp Leu Lys Ala Leu Ser Ser Ala Leu His Glu Arg Gly Met

100 105 110

tat ctt atg gtc gat gtg gtt gct aac cat atg ggc tat gat gga ccg 384

Tyr Leu Met Val Asp Val Val Ala Asn His Met Gly Tyr Asp Gly Pro

115 120 125

ggt agc tca gtc gat tac agt gtg ttt gtt ccg ttc aat tcc gct agc 432

Gly Ser Ser Val Asp Tyr Ser Val Phe Val Pro Phe Asn Ser Ala Ser

130 135 140

tac ttc cac ccg ttc tgt ttc att caa aac tgg aat gat cag act cag 480

Tyr Phe His Pro Phe Cys Phe Ile Gln Asn Trp Asn Asp Gln Thr Gln

145 150 155 160

gtt gag gat tgc tgg cta gga gat aac act gtc tcc ttg cct gat ctc 528

Val Glu Asp Cys Trp Leu Gly Asp Asn Thr Val Ser Leu Pro Asp Leu

165 170 175

gat acc acc aag gat gtg gtc aag aat gaa tgg tac gac tgg gtg gga 576

Asp Thr Thr Lys Asp Val Val Lys Asn Glu Trp Tyr Asp Trp Val Gly

180 185 190

tca ttg gta tcg aac tac tcc att gac ggc ctc cgt atc gac aca gta 624

Ser Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Val

195 200 205

aaa cac gtc cag aag gac ttc tgg ccc ggg tac aac aaa gcc gca ggc 672

Lys His Val Gln Lys Asp Phe Trp Pro Gly Tyr Asn Lys Ala Ala Gly

210 215 220

gtg tac tgt atc ggc gag gtg ctc gac ggt gat ccg gcc tac act tgt 720

Val Tyr Cys Ile Gly Glu Val Leu Asp Gly Asp Pro Ala Tyr Thr Cys

225 230 235 240

ccc tac cag gaa gtc ctg gac ggc gta ctg aac tac ccc att tac tat 768

Pro Tyr Gln Glu Val Leu Asp Gly Val Leu Asn Tyr Pro Ile Tyr Tyr

245 250 255

cca ctc ctc aac gcc ttc aag tca acc tcc ggc agc atg gac gac ctc 816

Pro Leu Leu Asn Ala Phe Lys Ser Thr Ser Gly Ser Met Asp Asp Leu

260 265 270

tac aac atg atc aac acc gtc aaa tcc gac tgt cca gac tca aca ctc 864

Tyr Asn Met Ile Asn Thr Val Lys Ser Asp Cys Pro Asp Ser Thr Leu

275 280 285

ctg ggc aca ttc gtc gag aac cac gac aac cca cgg ttc gct tct tac 912

Leu Gly Thr Phe Val Glu Asn His Asp Asn Pro Arg Phe Ala Ser Tyr

290 295 300

acc aac gac ata gcc ctc gcc aag aac gtc gca gca ttc atc atc ctc 960

Thr Asn Asp Ile Ala Leu Ala Lys Asn Val Ala Ala Phe Ile Ile Leu

305 310 315 320

aac gac gga atc ccc atc atc tac gcc ggc caa gaa cag cac tac gcc 1008

Asn Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ala

325 330 335

ggc gga aac gac ccc gcg aac cgc gaa gca acc tgg ctc tcg ggc tac 1056

Gly Gly Asn Asp Pro Ala Asn Arg Glu Ala Thr Trp Leu Ser Gly Tyr

340 345 350

ccg acc gac agc gag ctg tac aag tta att gcc tcc gcg aac gca atc 1104

Pro Thr Asp Ser Glu Leu Tyr Lys Leu Ile Ala Ser Ala Asn Ala Ile

355 360 365

cgg aac tat gcc att agc aaa gat aca gga ttc gtg acc tac aag aac 1152

Arg Asn Tyr Ala Ile Ser Lys Asp Thr Gly Phe Val Thr Tyr Lys Asn

370 375 380

tgg ccc atc tac aaa gac gac aca acg atc gcc atg cgc aag ggc aca 1200

Trp Pro Ile Tyr Lys Asp Asp Thr Thr Ile Ala Met Arg Lys Gly Thr

385 390 395 400

gat ggg tcg cag atc gtg act atc ttg tcc aac aag ggt gct tcg ggt 1248

Asp Gly Ser Gln Ile Val Thr Ile Leu Ser Asn Lys Gly Ala Ser Gly

405 410 415

gat tcg tat acc ctc tcc ttg agt ggt gcg ggt tac aca gcc ggc cag 1296

Asp Ser Tyr Thr Leu Ser Leu Ser Gly Ala Gly Tyr Thr Ala Gly Gln

420 425 430

caa ttg acg gag gtc att ggc tgc acg acc gtg acg gtt gat tcg tcg 1344

Gln Leu Thr Glu Val Ile Gly Cys Thr Thr Val Thr Val Asp Ser Ser

435 440 445

gga gat gtg cct gtt cct atg gcg ggt ggg cta cct agg gta ttg tat 1392

Gly Asp Val Pro Val Pro Met Ala Gly Gly Leu Pro Arg Val Leu Tyr

450 455 460

ccg act gag aag ttg gca ggt agc aag atc tgt agt agc tcg 1434

Pro Thr Glu Lys Leu Ala Gly Ser Lys Ile Cys Ser Ser Ser

465 470 475

<210>6

<211>478

<212>PRT

<213> Aspergillus oryzae

<400>6

Ala Thr Pro Ala Asp Trp Arg Ser Gln Ser Ile Tyr Phe Leu Leu Thr

1 5 10 15

Asp Arg Phe Ala Arg Thr Asp Gly Ser Thr Thr Ala Thr Cys Asn Thr

20 25 30

Ala Asp Gln Lys Tyr Cys Gly Gly Thr Trp Gln Gly Ile Ile Asp Lys

35 40 45

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Thr Pro

50 55 60

Val Thr Ala Gln Leu Pro Gln Thr Thr Ala Tyr Gly Asp Ala Tyr His

65 70 75 80

Gly Tyr Trp Gln Gln Asp Ile Tyr Ser Leu Asn Glu Asn Tyr Gly Thr

85 90 95

Ala Asp Asp Leu Lys Ala Leu Ser Ser Ala Leu His Glu Arg Gly Met

100 105 110

Tyr Leu Met Val Asp Val Val Ala Asn His Met Gly Tyr Asp Gly Pro

115 120 125

Gly Ser Ser Val Asp Tyr Ser Val Phe Val Pro Phe Asn Ser Ala Ser

130 135 140

Tyr Phe His Pro Phe Cys Phe Ile Gln Asn Trp Asn Asp Gln Thr Gln

145 150 155 160

Val Glu Asp Cys Trp Leu Gly Asp Asn Thr Val Ser Leu Pro Asp Leu

165 170 175

Asp Thr Thr Lys Asp Val Val Lys Asn Glu Trp Tyr Asp Trp Val Gly

180 185 190

Ser Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Val

195 200 205

Lys His Val Gln Lys Asp Phe Trp Pro Gly Tyr Asn Lys Ala Ala Gly

210 215 220

Val Tyr Cys Ile Gly Glu Val Leu Asp Gly Asp Pro Ala Tyr Thr Cys

225 230 235 240

Pro Tyr Gln Glu Val Leu Asp Gly Val Leu Asn Tyr Pro Ile Tyr Tyr

245 250 255

Pro Leu Leu Asn Ala Phe Lys Ser Thr Ser Gly Ser Met Asp Asp Leu

260 265 270

Tyr Asn Met Ile Asn Thr Val Lys Ser Asp Cys Pro Asp Ser Thr Leu

275 280 285

Leu Gly Thr Phe Val Glu Asn His Asp Asn Pro Arg Phe Ala Ser Tyr

290 295 300

Thr Asn Asp Ile Ala Leu Ala Lys Asn Val Ala Ala Phe Ile Ile Leu

305 310 315 320

Asn Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ala

325 330 335

Gly Gly Asn Asp Pro Ala Asn Arg Glu Ala Thr Trp Leu Ser Gly Tyr

340 345 350

Pro Thr Asp Ser Glu Leu Tyr Lys Leu Ile Ala Ser Ala Asn Ala Ile

355 360 365

Arg Asn Tyr Ala Ile Ser Lys Asp Thr Gly Phe Val Thr Tyr Lys Asn

370 375 380

Trp Pro Ile Tyr Lys Asp Asp Thr Thr Ile Ala Met Arg Lys Gly Thr

385 390 395 400

Asp Gly Ser Gln Ile Val Thr Ile Leu Ser Asn Lys Gly Ala Ser Gly

405 410 415

Asp Ser Tyr Thr Leu Ser Leu Ser Gly Ala Gly Tyr Thr Ala Gly Gln

420 425 430

Gln Leu Thr Glu Val Ile Gly Cys Thr Thr Val Thr Val Asp Ser Ser

435 440 445

Gly Asp Val Pro Val Pro Met Ala Gly Gly Leu Pro Arg Val Leu Tyr

450 455 460

Pro Thr Glu Lys Leu Ala Gly Ser Lys Ile Cys Ser Ser Ser

465 470 475

<210>7

<211>1461

<212>DNA

<213> Trichophaea saccata

<220>

<221> CDS

<222>(1)..(1461)

<400>7

tca tcc ggc aag aaa tta gag ctg gag gcc ctc aac ttt gtt tgg cag 48

Ser Ser Gly Lys Lys Leu Glu Leu Glu Ala Leu Asn Phe Val Trp Gln

1 5 10 15

aat gca gtt ctt act ggc gct cag agc act ttc aac aat ggg cag aag 96

Asn Ala Val Leu Thr Gly Ala Gln Ser Thr Phe Asn Asn Asn Gly Gln Lys

20 25 30

ggc gct att gtg gag ctt ttt ggg tgg ccg tat gca gat att gca aag 144

Gly Ala Ile Val Glu Leu Phe Gly Trp Pro Tyr Ala Asp Ile Ala Lys

35 40 45

gag tgc gct ttc ctt gga aaa gcc gga tac atg gga gtc aag gtt tgg 192

Glu Cys Ala Phe Leu Gly Lys Ala Gly Tyr Met Gly Val Lys Val Trp

50 55 60

cct cca aac gag cac atc tgg gga tcg gac tac tac gaa acc gac aat 240

Pro Pro Asn Glu His Ile Trp Gly Ser Asp Tyr Tyr Glu Thr Asp Asn

65 70 75 80

atg ttc cgt ccg tgg tat ctg gtg tac cag ccg gtc agt tac aag ctt 288

Met Phe Arg Pro Trp Tyr Leu Val Tyr Gln Pro Val Ser Tyr Lys Leu

85 90 95

gtg agc cgt caa gga acc cgt gag gag ctt cga gct atg ata act gct 336

Val Ser Arg Gln Gly Thr Arg Glu Glu Leu Arg Ala Met Ile Thr Ala

100 105 110

tgc cgg agt gct gga gtg cgc gtc tat gcc gac gcc gtc att aat cac 384

Cys Arg Ser Ala Gly Val Arg Val Tyr Ala Asp Ala Val Ile Asn His

115 120 125

atg tct gga aac gga aac gat atc caa aac cat cgt aat acc gcc tgc 432

Met Ser Gly Asn Gly Asn Asp Ile Gln Asn His Arg Asn Thr Ala Cys

130 135 140

gcc tac tgg aca ggc cac aac gca acc gcg aat tcg cct tac ttc acc 480

Ala Tyr Trp Thr Gly His Asn Ala Thr Ala Asn Ser Pro Tyr Phe Thr

145 150 155 160

tcc ggt tac acc tat ctt att aat ccc ttc acg aac aca cgc ccc acc 528

Ser Gly Tyr Thr Tyr Leu Ile Asn Pro Phe Thr Asn Thr Arg Pro Thr

165 170 175

ttc gag tac cca gcg gta cca tgg ggc cca act gat ttc cat tgc gtt 576

Phe Glu Tyr Pro Ala Val Pro Trp Gly Pro Thr Asp Phe His Cys Val

180 185 190

tcc tct atc aca gat tgg acc aac ggc caa atc gtc aca aag ggc tat 624

Ser Ser Ile Thr Asp Trp Thr Asn Gly Gln Ile Val Thr Lys Gly Tyr

195 200 205

ctc gtg gga ctc tcc gat ctc aac aca gag aag gat tac gtc cag gac 672

Leu Val Gly Leu Ser Asp Leu Asn Thr Glu Lys Asp Tyr Val Gln Asp

210 215 220

cgc atc gcc act tat ctt gtg gat ctc ttg tca atc ggc ttc tcc ggc 720

Arg Ile Ala Thr Tyr Leu Val Asp Leu Leu Ser Ile Gly Phe Ser Gly

225 230 235 240

ttc cgt gtt gat gcg gca aaa cat att ggc ccc acc tcc atg gca cag 768

Phe Arg Val Asp Ala Ala Lys His Ile Gly Pro Thr Ser Met Ala Gln

245 250 255

atc ttc gga agg gtt gca aag aag atg ggc gga agt ctt cca gat gat 816

Ile Phe Gly Arg Val Ala Lys Lys Met Gly Gly Ser Leu Pro Asp Asp

260 265 270

ttt atc act tgg ctt gaa gtg ttg atg ggt ggt gag aag gag cag tat 864

Phe Ile Thr Trp Leu Glu Val Leu Met Gly Gly Glu Lys Glu Gln Tyr

275 280 285

gct tgc ggc ggc ggt gaa tgg agt tgg tac acc aac ttc aat acc cag 912

Ala Cys Gly Gly Gly Glu Trp Ser Trp Tyr Thr Asn Phe Asn Thr Gln

290 295 300

ctt tcc aat gcg gga att agt gac act gat atc aat aag atc aag att 960

Leu Ser Asn Ala Gly Ile Ser Asp Thr Asp Ile Asn Lys Ile Lys Ile

305 310 315 320

tgg agc tcc gac tat ccc aag gag ttc ccg atc tgc ggt tct tgg atc 1008

Trp Ser Ser Asp Tyr Pro Lys Glu Phe Pro Ile Cys Gly Ser Trp Ile

325 330 335

atc cca tcc act cgc ttt gtc atc caa aat gac gac cat gac cag cag 1056

Ile Pro Ser Thr Arg Phe Val Ile Gln Asn Asp Asp His Asp Gln Gln

340 345 350

aac ccg ggc tct tcc tcc aga gat atg ggt gac caa ggc tcc gta ctc 1104

Asn Pro Gly Ser Ser Ser Arg Asp Met Gly Asp Gln Gly Ser Val Leu

355 360 365

atc aaa gat caa gat gta gcc aag cac cgg gca ttt gag gtc aag ctc 1152

Ile Lys Asp Gln Asp Val Ala Lys His Arg Ala Phe Glu Val Lys Leu

370 375 380

ttc acc cgt acc gac ggt gac tgg caa atc agg aat atc ctc tcc tct 1200

Phe Thr Arg Thr Asp Gly Asp Trp Gln Ile Arg Asn Ile Leu Ser Ser

385 390 395 400

tat atg ttt gcc tcc aac gga gca aat ggc ttc ccc gat ggt ctt tcg 1248

Tyr Met Phe Ala Ser Asn Gly Ala Asn Gly Phe Pro Asp Gly Leu Ser

405 410 415

gat tgt tcc ctt tat act ggc tca cag agt gcg agt ggt tgt ttg ggt 1296

Asp Cys Ser Leu Tyr Thr Gly Ser Gln Ser Ala Ser Gly Cys Leu Gly

420 425 430

atc gcg aag gat acc gct tat gta gaa ggt atc tgt ggg tat act atg 1344

Ile Ala Lys Asp Thr Ala Tyr Val Glu Gly Ile Cys Gly Tyr Thr Met

435 440 445

gtt gct gga agg tac acc agg ccg cat agg gat ctg agc atc att aat 1392

Val Ala Gly Arg Tyr Thr Arg Pro His Arg Asp Leu Ser Ile Ile Asn

450 455 460

gct atg agg agt tgg gtc ggg ttg tcg agt acc aca gcg gat gct ctt 1440

Ala Met Arg Ser Trp Val Gly Leu Ser Ser Thr Thr Ala Asp Ala Leu

465 470 475 480

gga atc ccc ggt tgt agc tga 1461

Gly Ile Pro Gly Cys Ser

485

<210>8

<211>486

<212>PRT

<213> Trichophaea saccata

<400>8

Ser Ser Gly Lys Lys Leu Glu Leu Glu Ala Leu Asn Phe Val Trp Gln

1 5 10 15

Asn Ala Val Leu Thr Gly Ala Gln Ser Thr Phe Asn Asn Asn Gly Gln Lys

20 25 30

Gly Ala Ile Val Glu Leu Phe Gly Trp Pro Tyr Ala Asp Ile Ala Lys

35 40 45

Glu Cys Ala Phe Leu Gly Lys Ala Gly Tyr Met Gly Val Lys Val Trp

50 55 60

Pro Pro Asn Glu His Ile Trp Gly Ser Asp Tyr Tyr Glu Thr Asp Asn

65 70 75 80

Met Phe Arg Pro Trp Tyr Leu Val Tyr Gln Pro Val Ser Tyr Lys Leu

85 90 95

Val Ser Arg Gln Gly Thr Arg Glu Glu Leu Arg Ala Met Ile Thr Ala

100 105 110

Cys Arg Ser Ala Gly Val Arg Val Tyr Ala Asp Ala Val Ile Asn His

115 120 125

Met Ser Gly Asn Gly Asn Asp Ile Gln Asn His Arg Asn Thr Ala Cys

130 135 140

Ala Tyr Trp Thr Gly His Asn Ala Thr Ala Asn Ser Pro Tyr Phe Thr

145 150 155 160

Ser Gly Tyr Thr Tyr Leu Ile Asn Pro Phe Thr Asn Thr Arg Pro Thr

165 170 175

Phe Glu Tyr Pro Ala Val Pro Trp Gly Pro Thr Asp Phe His Cys Val

180 185 190

Ser Ser Ile Thr Asp Trp Thr Asn Gly Gln Ile Val Thr Lys Gly Tyr

195 200 205

Leu Val Gly Leu Ser Asp Leu Asn Thr Glu Lys Asp Tyr Val Gln Asp

210 215 220

Arg Ile Ala Thr Tyr Leu Val Asp Leu Leu Ser Ile Gly Phe Ser Gly

225 230 235 240

Phe Arg Val Asp Ala Ala Lys His Ile Gly Pro Thr Ser Met Ala Gln

245 250 255

Ile Phe Gly Arg Val Ala Lys Lys Met Gly Gly Ser Leu Pro Asp Asp

260 265 270

Phe Ile Thr Trp Leu Glu Val Leu Met Gly Gly Glu Lys Glu Gln Tyr

275 280 285

Ala Cys Gly Gly Gly Glu Trp Ser Trp Tyr Thr Asn Phe Asn Thr Gln

290 295 300

Leu Ser Asn Ala Gly Ile Ser Asp Thr Asp Ile Asn Lys Ile Lys Ile

305 310 315 320

Trp Ser Ser Asp Tyr Pro Lys Glu Phe Pro Ile Cys Gly Ser Trp Ile

325 330 335

Ile Pro Ser Thr Arg Phe Val Ile Gln Asn Asp Asp His Asp Gln Gln

340 345 350

Asn Pro Gly Ser Ser Ser Arg Asp Met Gly Asp Gln Gly Ser Val Leu

355 360 365

Ile Lys Asp Gln Asp Val Ala Lys His Arg Ala Phe Glu Val Lys Leu

370 375 380

Phe Thr Arg Thr Asp Gly Asp Trp Gln Ile Arg Asn Ile Leu Ser Ser

385 390 395 400

Tyr Met Phe Ala Ser Asn Gly Ala Asn Gly Phe Pro Asp Gly Leu Ser

405 410 415

Asp Cys Ser Leu Tyr Thr Gly Ser Gln Ser Ala Ser Gly Cys Leu Gly

420 425 430

Ile Ala Lys Asp Thr Ala Tyr Val Glu Gly Ile Cys Gly Tyr Thr Met

435 440 445

Val Ala Gly Arg Tyr Thr Arg Pro His Arg Asp Leu Ser Ile Ile Asn

450 455 460

Ala Met Arg Ser Trp Val Gly Leu Ser Ser Thr Thr Ala Asp Ala Leu

465 470 475 480

Gly Ile Pro Gly Cys Ser

485

<210>9

<211>1398

<212>DNA

<213>Subulispora provurvata

<220>

<221> CDS

<222>(1)..(1398)

<400>9

acc gaa tgg ggg agt cag tcc atc tac cag gta ttg acg gat cgc ttt 48

Thr Glu Trp Gly Ser Gln Ser Ile Tyr Gln Val Leu Thr Asp Arg Phe

1 5 10 15

gcc cgc act gat ggg tct act acc gcc tcc tgt gat gtg aac aag tac 96

Ala Arg Thr Asp Gly Ser Thr Thr Ala Ser Cys Asp Val Asn Lys Tyr

20 25 30

tgc ggc ggc acc tgg cag ggc ata atc gac aag ctg gac tac atc cag 144

Cys Gly Gly Thr Trp Gln Gly Ile Ile Asp Lys Leu Asp Tyr Ile Gln

35 40 45

ggc atg ggt ttc act gcg atc tgg att tcg cct atc gtc gac aac atc 192

Gly Met Gly Phe Thr Ala Ile Trp Ile Ser Pro Ile Val Asp Asn Ile

50 55 60

gac gcc gat act gtt gat ggc acc tct tat cac ggt tac tgg gcc cag 240

Asp Ala Asp Thr Val Asp Gly Thr Ser Tyr His Gly Tyr Trp Ala Gln

65 70 75 80

gac atc acc tca gtg aac tcg gcg ttc ggc acg gag cag gac ctc atc 288

Asp Ile Thr Ser Val Asn Ser Ala Phe Gly Thr Glu Gln Asp Leu Ile

85 90 95

aac ctc tca gca gct ctg cac gac agg ggc atg tat ctg atg gta gac 336

Asn Leu Ser Ala Ala Leu His Asp Arg Gly Met Tyr Leu Met Val Asp

100 105 110

gtg gta aac aac cac atg gga tac aac ggc tgc ggc gat tgt gtt gac 384

Val Val Asn Asn His Met Gly Tyr Asn Gly Cys Gly Asp Cys Val Asp

115 120 125

tac agc ata tac acg cca ttc aac cag cag tcc tac tac cac ccg tac 432

Tyr Ser Ile Tyr Thr Pro Phe Asn Gln Gln Ser Tyr Tyr His Pro Tyr

130 135 140

tgc gcc act gat tac agc aac ctg acc tcc atc cag gtg tgc tgg gag 480

Cys Ala Thr Asp Tyr Ser Asn Leu Thr Ser Ile Gln Val Cys Trp Glu

145 150 155 160

ggt gac aac att gtc agt ctc ccc gac ctg agg aca gag gat gac gat 528

Gly Asp Asn Ile Val Ser Leu Pro Asp Leu Arg Thr Glu Asp Asp Asp

165 170 175

gtc cgc acc atg tgg tac gac tgg atc acg ccg ttg gta acc aag tac 576

Val Arg Thr Met Trp Tyr Asp Trp Ile Thr Pro Leu Val Thr Lys Tyr

180 185 190

tcg atc gat gga ctg cgc atg gac agc gcc gag cat gtc gag aag agc 624

Ser Ile Asp Gly Leu Arg Met Asp Ser Ala Glu His Val Glu Lys Ser

195 200 205

ttc tgg cct ggt tgg gta tcc gcc tcg gga gta tac aac ata gga gag 672

Phe Trp Pro Gly Trp Val Ser Ala Ser Gly Val Tyr Asn Ile Gly Glu

210 215 220

gtt gat gag ggc gac ccc acc atc ttc cca gac tgg ctg aac tac atc 720

Val Asp Glu Gly Asp Pro Thr Ile Phe Pro Asp Trp Leu Asn Tyr Ile

225 230 235 240

gac gga acc ttg aac tat cca gct tac tac tgg atc act caa gct ttc 768

Asp Gly Thr Leu Asn Tyr Pro Ala Tyr Tyr Trp Ile Thr Gln Ala Phe

245 250 255

cag tca act tct ggt tct atc agc aac ctg gtt aat gga atc aac caa 816

Gln Ser Thr Ser Gly Ser Ile Ser Asn Leu Val Asn Gly Ile Asn Gln

260 265 270

atg aag ggc tca atg aaa acc agc acc ctc ggg tcg ttc ctt gag aat 864

Met Lys Gly Ser Met Lys Thr Ser Thr Leu Gly Ser Phe Leu Glu Asn

275 280 285

cac gac cag cca cga ttc cct tct ctg act agt gat gcg gat ttg gcg 912

His Asp Gln Pro Arg Phe Pro Ser Leu Thr Ser Asp Ala Asp Leu Ala

290 295 300

aag aac gct atc gct ttt gct atg ctt gct gat ggc gtc cca atc gtc 960

Lys Asn Ala Ile Ala Phe Ala Met Leu Ala Asp Gly Val Pro Ile Val

305 310 315 320

tac tat ggt caa gag cag gcc tac tcg ggt ggt ggc gtg cct aat gac 1008

Tyr Tyr Gly Gln Glu Gln Ala Tyr Ser Gly Gly Gly Val Pro Asn Asp

325 330 335

cgt gag cca ctg tgg aca tcg gga tac agc acc aca tcg gca ggt tac 1056

Arg Glu Pro Leu Trp Thr Ser Gly Tyr Ser Thr Thr Ser Ala Gly Tyr

340 345 350

acg ttc atc acg acc atc aac aaa atc cgc cgc ctg gct ctc acc cag 1104

Thr Phe Ile Thr Thr Ile Asn Lys Ile Arg Arg Leu Ala Leu Thr Gln

355 360 365

gac agt gcc tac gta gca tac cag acc tac ccg atc tat tcg gat tct 1152

Asp Ser Ala Tyr Val Ala Tyr Gln Thr Tyr Pro Ile Tyr Ser Asp Ser

370 375 380

cac gtc atc gcc atg aag aag agc agc gtc gtc tcc gtc tat agc aac 1200

His Val Ile Ala Met Lys Lys Ser Ser Val Val Ser Val Tyr Ser Asn

385 390 395 400

att ggc tcc agc ggc agc acc tat tcg atc acc cta cct gcc ggc aca 1248

Ile Gly Ser Ser Ser Gly Ser Thr Tyr Ser Ile Thr Leu Pro Ala Gly Thr

405 410 415

ttc act ggg agt gta gcg ctc aca gac gtg gtg agc tgc cag acg tac 1296

Phe Thr Gly Ser Val Ala Leu Thr Asp Val Val Ser Cys Gln Thr Tyr

420 425 430

acg gcg agc tct act ggc agc ctc acc ttc acc ttc gga caa gtt ccc 1344

Thr Ala Ser Ser Thr Gly Ser Leu Thr Phe Thr Phe Gly Gln Val Pro

435 440 445

tcc gtc ttc tac ccg acg gca agc ctg tcc ggc agc ggg ctc tgc tct 1392

Ser Val Phe Tyr Pro Thr Ala Ser Leu Ser Gly Ser Gly Leu Cys Ser

450 455 460

agc tcc 1398

Ser Ser

465

<210>10

<211>466

<212>PRT

<213>Subulispora provurvata

<400>10

Thr Glu Trp Gly Ser Gln Ser Ile Tyr Gln Val Leu Thr Asp Arg Phe

1 5 10 15

Ala Arg Thr Asp Gly Ser Thr Thr Ala Ser Cys Asp Val Asn Lys Tyr

20 25 30

Cys Gly Gly Thr Trp Gln Gly Ile Ile Asp Lys Leu Asp Tyr Ile Gln

35 40 45

Gly Met Gly Phe Thr Ala Ile Trp Ile Ser Pro Ile Val Asp Asn Ile

50 55 60

Asp Ala Asp Thr Val Asp Gly Thr Ser Tyr His Gly Tyr Trp Ala Gln

65 70 75 80

Asp Ile ThrSer Val Asn Ser Ala Phe Gly Thr Glu Gln Asp Leu Ile

85 90 95

Asn Leu Ser Ala Ala Leu His Asp Arg Gly Met Tyr Leu Met Val Asp

100 105 110

Val Val Asn Asn His Met Gly Tyr Asn Gly Cys Gly Asp Cys Val Asp

115 120 125

Tyr Ser Ile Tyr Thr Pro Phe Asn Gln Gln Ser Tyr Tyr His Pro Tyr

130 135 140

Cys Ala Thr Asp Tyr Ser Asn Leu Thr Ser Ile Gln Val Cys Trp Glu

145 150 155 160

Gly Asp Asn Ile Val Ser Leu Pro Asp Leu Arg Thr Glu Asp Asp Asp

165 170 175

Val Arg Thr Met Trp Tyr Asp Trp Ile Thr Pro Leu Val Thr Lys Tyr

180 185 190

Ser Ile Asp Gly Leu Arg Met Asp Ser Ala Glu His Val Glu Lys Ser

195 200 205

Phe Trp Pro Gly Trp Val Ser Ala Ser Gly Val Tyr Asn Ile Gly Glu

210 215 220

Val Asp Glu Gly Asp Pro Thr Ile Phe Pro Asp Trp Leu Asn Tyr Ile

225 230 235 240

Asp Gly Thr Leu Asn Tyr Pro Ala Tyr Tyr Trp Ile Thr Gln Ala Phe

245 250 255

Gln Ser Thr Ser Gly Ser Ile Ser Asn Leu Val Asn Gly Ile Asn Gln

260 265 270

Met Lys Gly Ser Met Lys Thr Ser Thr Leu Gly Ser Phe Leu Glu Asn

275 280 285

His Asp Gln Pro Arg Phe Pro Ser Leu Thr Ser Asp Ala Asp Leu Ala

290 295 300

Lys Asn Ala Ile Ala Phe Ala Met Leu Ala Asp Gly Val Pro Ile Val

305 310 315 320

Tyr Tyr Gly Gln Glu Gln Ala Tyr Ser Gly Gly Gly Val Pro Asn Asp

325 330 335

Arg Glu Pro Leu Trp Thr Ser Gly Tyr Ser Thr Thr Ser Ala Gly Tyr

340 345 350

Thr Phe Ile Thr Thr Ile Asn Lys Ile Arg Arg Leu Ala Leu Thr Gln

355 360 365

Asp Ser Ala Tyr Val Ala Tyr Gln Thr Tyr Pro Ile Tyr Ser Asp Ser

370 375 380

His Val Ile Ala Met Lys Lys Ser Ser Val Val Ser Val Tyr Ser Asn

385 390 395 400

Ile Gly Ser Ser Ser Gly Ser Thr Tyr Ser Ile Thr Leu Pro Ala Gly Thr

405 410 415

Phe Thr Gly Ser Val Ala Leu Thr Asp Val Val Ser Cys Gln Thr Tyr

420 425 430

Thr Ala Ser Ser Thr Gly Ser Leu Thr Phe Thr Phe Gly Gln Val Pro

435 440 445

Ser Val Phe Tyr Pro Thr Ala Ser Leu Ser Gly Ser Gly Leu Cys Ser

450 455 460

Ser Ser

465

<210>11

<211>1350

<212>DNA

<213>Valsaria rubricosa

<220>

<221> CDS

<222>(1)..(1350)

<400>11

agc aac tcc gac tgg agg tcc cgc aat atc tac ttt gcc ttg acc gac 48

Ser Asn Ser Asp Trp Arg Ser Arg Asn Ile Tyr Phe Ala Leu Thr Asp

1 5 10 15

cgc gtc gcc aat ccg tcc acc acg acc gca tgt agt agt gac ctg aac aac 96

Arg Val Ala Asn Pro Ser Thr Thr Thr Ala Cys Ser Asp Leu Ser Asn

20 25 30

tac tgc ggc ggc acg tgg agc ggc ctg tcg aag ctg gac tac atc 144

Tyr Cys Gly Gly Thr Trp Ser Gly Leu Ser Ser Lys Leu Asp Tyr Ile

35 40 45

caa ggg atg ggc ttc gat tcc atc tgg att acc ccc gtg gtc gag aac 192

Gln Gly Met Gly Phe Asp Ser Ile Trp Ile Thr Pro Val Val Glu Asn

50 55 60

tgc gac ggt ggc tac cac ggc tac tgg gcc aag gcg ctc tac aac gtc 240

Cys Asp Gly Gly Tyr His Gly Tyr Trp Ala Lys Ala Leu Tyr Asn Val

65 70 75 80

aac acg aac tac ggc agt gcg gat gat ctg aag aac ttc gtt gcg gcc 288

Asn Thr Asn Tyr Gly Ser Ala Asp Asp Leu Lys Asn Phe Val Ala Ala

85 90 95

gcc cat gcg aag ggc atg tac gtg atg gtg gac gtc gtc gcg aat cac 336

Ala His Ala Lys Gly Met Tyr Val Met Val Asp Val Val Ala Asn His

100 105 110

atg ggt tcc tgc ggc atc gcc aac ctc tcc cca cct ccc ctg aac gag 384

Met Gly Ser Cys Gly Ile Ala Asn Leu Ser Pro Pro Pro Leu Asn Glu

115 120 125

cag agc tct tat cac acc cag tgc gac att gac tac agc agt cag tcc 432

Gln Ser Ser Tyr His Thr Gln Cys Asp Ile Asp Tyr Ser Ser Gln Ser

130 135 140

agc att gag acg tgc tgg ata tcc ggc ctc cct gac ctg gac acc acc 480

Ser Ile Glu Thr Cys Trp Ile Ser Gly Leu Pro Asp Leu Asp Thr Thr

145 150 155 160

gat agc act atc cga tcc ctc ttc cag acc tgg gtc cac ggc ctg gtc 528

Asp Ser Thr Ile Arg Ser Leu Phe Gln Thr Trp Val His Gly Leu Val

165 170 175

agc aac tac agc ttc gac ggt ctc cgc gtc gac acc gtc aag cac gtg 576

Ser Asn Tyr Ser Phe Asp Gly Leu Arg Val Asp Thr Val Lys His Val

180 185 190

gag aag gat tac tgg ccc ggc ttc gtg tcg gcg gcg ggc acc tac gcc 624

Glu Lys Asp Tyr Trp Pro Gly Phe Val Ser Ala Ala Gly Thr Tyr Ala

195 200 205

atc ggc gaa gtc ttc tcc ggc gac acc tcc tac gtg gcc ggc tat caa 672

Ile Gly Glu Val Phe Ser Gly Asp Thr Ser Tyr Val Ala Gly Tyr Gln

210 215 220

tcg gtg atg ccg ggc ttg ctc aac tat ccc atc tac tat ccg ctc atc 720

Ser Val Met Pro Gly Leu Leu Asn Tyr Pro Ile Tyr Tyr Pro Leu Ile

225 230 235 240

cgc gtc ttc gcg cag ggt gcg tcc ttc acc gat ctc gtc aac aac cac 768

Arg Val Phe Ala Gln Gly Ala Ser Phe Thr Asp Leu Val Asn Asn His

245 250 255

gat acc gtc ggc tcg acc ttc tcc gac ccg acg ctg ctg ggt aac ttt 816

Asp Thr Val Gly Ser Thr Phe Ser Asp Pro Thr Leu Leu Gly Asn Phe

260 265 270

atc gac aac cac gac aac cca cgt ttc ctg agc tac acc agc gac cac 864

Ile Asp Asn His Asp Asn Pro Arg Phe Leu Ser Tyr Thr Ser Asp His

275 280 285

gcc ctc ctc aag aac gct ctg gcc tac gtc atc ctg gcc aga ggc atc 912

Ala Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile Leu Ala Arg Gly Ile

290 295 300

ccc atc gtc tac tac ggc acc gag caa ggc tac tcg ggt tcg tcc gac 960

Pro Ile Val Tyr Tyr Gly Thr Glu Gln Gly Tyr Ser Gly Ser Ser Asp

305 310 315 320

ccg gcg aac cgc gag gat ctc tgg cgt agc gga tac agc act acg gga 1008

Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Gly Tyr Ser Thr Thr Gly

325 330 335

gac atc tac acc acc acc atc gcc gcg ctc tcc gcc gcg cgc acc gcg gcc 1056

Asp Ile Tyr Thr Thr Ile Ala Ala Leu Ser Ala Ala Arg Thr Ala Ala

340 345 350

ggt ggc ctc gcc ggt aac gac cac gtc cac ctg tac acg acc gac aac 1104

Gly Gly Leu Ala Gly Asn Asp His Val His Leu Tyr Thr Thr Asp Asn

355 360 365

gcg tac gcc tgg tcc cgg gcg agc ggc aag ctc atc gtc gtc acg tcc 1152

Ala Tyr Ala Trp Ser Arg Ala Ser Gly Lys Leu Ile Val Val Thr Ser

370 375 380

aac cgc ggc agc tcc gac agc agc acc atc tgc ttc agc acc cag cag 1200

Asn Arg Gly Ser Ser Asp Ser Ser Thr Ile Cys Phe Ser Thr Gln Gln

385 390 395 400

gcc agc ggc acc acc tgg acc agc acg atc acc ggc aac tcg tac acc 1248

Ala Ser Gly Thr Thr Trp Thr Ser Thr Ile Thr Gly Asn Ser Tyr Thr

405 410 415

gcc gac agc aac ggc cag atc tgc gtg cag ctg tcc agc ggc gga ccc 1296

Ala Asp Ser Asn Gly Gly Gln Ile Cys Val Gln Leu Ser Ser Gly Gly Pro

420 425 430

gag gcg ctc gtc gtc tcc acc gcg acc ggc acc gcc acc gcg acg act 1344

Glu Ala Leu Val Val Ser Thr Ala Thr Gly Thr Ala Thr Ala Thr Thr

435 440 445

ctg tcc 1350

Leu Ser

450

<210>12

<211>450

<212>PRT

<213>Valsaria rubricosa

<400>12

Ser Asn Ser Asp Trp Arg Ser Arg Asn Ile Tyr Phe Ala Leu Thr Asp

1 5 10 15

Arg Val Ala Asn Pro Ser Thr Thr Thr Ala Cys Ser Asp Leu Ser Asn

20 25 30

Tyr Cys Gly Gly Thr Trp Ser Gly Leu Ser Ser Lys Leu Asp Tyr Ile

35 40 45

Gln Gly Met Gly Phe Asp Ser Ile Trp Ile Thr Pro Val Val Glu Asn

50 55 60

Cys Asp Gly Gly Tyr His Gly Tyr Trp Ala Lys Ala Leu Tyr Asn Val

65 70 75 80

Asn Thr Asn Tyr Gly Ser Ala Asp Asp Leu Lys Asn Phe Val Ala Ala

85 90 95

Ala His Ala Lys Gly Met Tyr Val Met Val Asp Val Val Ala Asn His

100 105 110

Met Gly Ser Cys Gly Ile Ala Asn Leu Ser Pro Pro Pro Leu Asn Glu

115 120 125

Gln Ser Ser Tyr His Thr Gln Cys Asp Ile Asp Tyr Ser Ser Gln Ser

130 135 140

Ser Ile Glu Thr Cys Trp Ile Ser Gly Leu Pro Asp Leu Asp Thr Thr

145 150 155 160

Asp Ser Thr Ile Arg Ser Leu Phe Gln Thr Trp Val His Gly Leu Val

165 170 175

Ser Asn Tyr Ser Phe Asp Gly Leu Arg Val Asp Thr Val Lys His Val

180 185 190

Glu Lys Asp Tyr Trp Pro Gly Phe Val Ser Ala Ala Gly Thr Tyr Ala

195 200 205

Ile Gly Glu Val Phe Ser Gly Asp Thr Ser Tyr Val Ala Gly Tyr Gln

210 215 220

Ser Val Met Pro Gly Leu Leu Asn Tyr Pro Ile Tyr Tyr Pro Leu Ile

225 230 235 240

Arg Val Phe Ala Gln Gly Ala Ser Phe Thr Asp Leu Val Asn Asn His

245 250 255

Asp Thr Val Gly Ser Thr Phe Ser Asp Pro Thr Leu Leu Gly Asn Phe

260 265 270

Ile Asp Asn His Asp Asn Pro Arg Phe Leu Ser Tyr Thr Ser Asp His

275 280 285

Ala Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile Leu Ala Arg Gly Ile

290 295 300

Pro Ile Val Tyr Tyr Gly Thr Glu Gln Gly Tyr Ser Gly Ser Ser Asp

305 310 315 320

Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Gly Tyr Ser Thr Thr Gly

325 330 335

Asp Ile Tyr Thr Thr Ile Ala Ala Leu Ser Ala Ala Arg Thr Ala Ala

340 345 350

Gly Gly Leu Ala Gly Asn Asp His Val His Leu Tyr Thr Thr Asp Asn

355 360 365

Ala Tyr Ala Trp Ser Arg Ala Ser Gly Lys Leu Ile Val Val Thr Ser

370 375 380

Asn Arg Gly Ser Ser Asp Ser Ser Thr Ile Cys Phe Ser Thr Gln Gln

385 390 395 400

Ala Ser Gly Thr Thr Trp Thr Ser Thr Ile Thr Gly Asn Ser Tyr Thr

405 410 415

Ala Asp Ser Asn Gly Gly Gln Ile Cys Val Gln Leu Ser Ser Gly Gly Pro

420 425 430

Glu Ala Leu Val Val Ser Thr Ala Thr Gly Thr Ala Thr Ala Thr Thr

435 440 445

Leu Ser

450

<210>13

<211>1326

<212>DNA

<213> Thermomyces lanuginosus

<220>

<221> CDS

<222>(1)..(1326)

<400>13

aaa tat tgc ggg gga aca tgg cga ggt atc atc aac aac ctg gat tac 48

Lys Tyr Cys Gly Gly Thr Trp Arg Gly Ile Ile Asn Asn Leu Asp Tyr

1 5 10 15

atc cag gat atg ggc ttc aca gct atc tgg att act cca gtg aca gcc 96

Ile Gln Asp Met Gly Phe Thr Ala Ile Trp Ile Thr Pro Val Thr Ala

20 25 30

cag tgg gac gac gat gtg gat gcg gca gat gca acg tcg tat cac ggt 144

Gln Trp Asp Asp Asp Val Asp Ala Ala Asp Ala Thr Ser Tyr His Gly

35 40 45

tat tgg cag aaa gac cta tac tct ctg aat tcg aaa ttc ggc act gcc 192

Tyr Trp Gln Lys Asp Leu Tyr Ser Leu Asn Ser Lys Phe Gly Thr Ala

50 55 60

gat gac ttg aaa gcc ctg gct gat acc ctt cac gcc cgt ggg atg ctt 240

Asp Asp Leu Lys Ala Leu Ala Asp Thr Leu His Ala Arg Gly Met Leu

65 70 75 80

ctc atg gtc gac gtc gtg gct aat cac ttt ggc tac ggc ggt tct cat 288

Leu Met Val Asp Val Val Ala Asn His Phe Gly Tyr Gly Gly Ser His

85 90 95

agc gag gtg gat tac tcg atc ttc aat cct ctg aac agc cag gat tac 336

Ser Glu Val Asp Tyr Ser Ile Phe Asn Pro Leu Asn Ser Gln Asp Tyr

100 105 110

ttc cac ccg ttc tgt ctc att gag gac tac gac aac cag gaa gaa gtc 384

Phe His Pro Phe Cys Leu Ile Glu Asp Tyr Asp Asn Gln Glu Glu Val

115 120 125

gaa caa tgc tgg ctg gcc gat act ccg acg aca ttg ccc gac gtg gac 432

Glu Gln Cys Trp Leu Ala Asp Thr Pro Thr Thr Leu Pro Asp Val Asp

130 135 140

acc acc aat cct cag gtt cgg acg ttt ttc aac gac tgg atc aag agc 480

Thr Thr Asn Pro Gln Val Arg Thr Phe Phe Asn Asp Trp Ile Lys Ser

145 150 155 160

ctg gtg gcg aac tac tcc atc gat ggt ctg cgc gtc gac acc gtt aag 528

Leu Val Ala Asn Tyr Ser Ile Asp Gly Leu Arg Val Asp Thr Val Lys

165 170 175

cac gtg gag aaa gat ttc tgg ccc gac ttc aac gaa gct gct ggc gtg 576

His Val Glu Lys Asp Phe Trp Pro Asp Phe Asn Glu Ala Ala Gly Val

180 185 190

tac gcc gtc ggc gag gtg ttc aac ggt gac cca gcg tac acc tgc cca 624

Tyr Ala Val Gly Glu Val Phe Asn Gly Asp Pro Ala Tyr Thr Cys Pro

195 200 205

tac cag gaa gtg ctg gat ggc gtt ctg aac tat ccg atc tac tat cct 672

Tyr Gln Glu Val Leu Asp Gly Val Leu Asn Tyr Pro Ile Tyr Tyr Pro

210 215 220

gcg ctt gat gca ttc aag tct gtc ggc ggc aat ctc ggc ggc ttg gct 720

Ala Leu Asp Ala Phe Lys Ser Val Gly Gly Asn Leu Gly Gly Leu Ala

225 230 235 240

cag gcc atc acc acc gtg cag gag agc tgc aag gat tcc aat ctg ctc 768

Gln Ala Ile Thr Thr Val Gln Glu Ser Cys Lys Asp Ser Asn Leu Leu

245 250 255

ggc aat ttc ctt gag aat cac gac att gct cgc ttt gct tcg tac acg 816

Gly Asn Phe Leu Glu Asn His Asp Ile Ala Arg Phe Ala Ser Tyr Thr

260 265 270

gat gac ctt gct ctc gcc aag aat ggt ctc gct ttc atc atc ctc tcg 864

Asp Asp Leu Ala Leu Ala Lys Asn Gly Leu Ala Phe Ile Ile Leu Ser

275 280 285

gat ggt att ccg atc atc tac gcg ggc cag gag cag cac tac gcc ggt 912

Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ala Gly

290 295 300

gat cac gat ccc aca aat cgt gag gcc gtc tgg ctg tct ggc tac aat 960

Asp His Asp Pro Thr Asn Arg Glu Ala Val Trp Leu Ser Gly Tyr Asn

305 310 315 320

acc gac gcc gag ctg tac cag ttc atc aag aag gcc aat ggc atc cgc 1008

Thr Asp Ala Glu Leu Tyr Gln Phe Ile Lys Lys Ala Asn Gly Ile Arg

325 330 335

aac ttg gct atc agc cag aac ccg gaa ttc acc tcc tcc aag acc aag 1056

Asn Leu Ala Ile Ser Gln Asn Pro Glu Phe Thr Ser Ser Lys Thr Lys

340 345 350

gtc atc tac caa gac gat tcg acc ctt gcc att aac cgg ggc ggc gtc 1104

Val Ile Tyr Gln Asp Asp Ser Thr Leu Ala Ile Asn Arg Gly Gly Val

355 360 365

gtt act gtc ctg agc aat gaa ggc gcc tcc ggc gga gac cgg act gtc 1152

Val Thr Val Leu Ser Asn Glu Gly Ala Ser Gly Gly Asp Arg Thr Val

370 375 380

tcc att ccg gga act ggc ttc gag gcc ggc acg gaa ttg act gat gtc 1200

Ser Ile Pro Gly Thr Gly Phe Glu Ala Gly Thr Glu Leu Thr Asp Val

385 390 395 400

atc tcc tgc aag acc gtg act gcg ggg gac agc ggg gcg gtc gac gtg 1248

Ile Ser Cys Lys Thr Val Thr Ala Gly Asp Ser Gly Ala Val Asp Val

405 410 415

ccc ttg tcg ggc gga ctg cca agc gtg ctc tat ccc agc tcc cag ctg 1296

Pro Leu Ser Gly Gly Leu Pro Ser Val Leu Tyr Pro Ser Ser Gln Leu

420 425 430

gcc aag agt ggt ctg tgt gcg tcg gcg tga 1326

Ala Lys Ser Gly Leu Cys Ala Ser Ala

435 440

<210>14

<211>441

<212>PRT

<213> Thermomyces lanuginosus

<400>14

Lys Tyr Cys Gly Gly Thr Trp Arg Gly Ile Ile Asn Asn Leu Asp Tyr

1 5 10 15

Ile Gln Asp Met Gly Phe Thr Ala Ile Trp Ile Thr Pro Val Thr Ala

20 25 30

Gln Trp Asp Asp Asp Val Asp Ala Ala Asp Ala Thr Ser Tyr His Gly

35 40 45

Tyr Trp Gln Lys Asp Leu Tyr Ser Leu Asn Ser Lys Phe Gly Thr Ala

50 55 60

Asp Asp Leu Lys Ala Leu Ala Asp Thr Leu His Ala Arg Gly Met Leu

65 70 75 80

Leu Met Val Asp Val Val Ala Asn His Phe Gly Tyr Gly Gly Ser His

85 90 95

Ser Glu Val Asp Tyr Ser Ile Phe Asn Pro Leu Asn Ser Gln Asp Tyr

100 105 110

Phe His Pro Phe Cys Leu Ile Glu Asp Tyr Asp Asn Gln Glu Glu Val

115 120 125

Glu Gln Cys Trp Leu Ala Asp Thr Pro Thr Thr Leu Pro Asp Val Asp

130 135 140

Thr Thr Asn Pro Gln Val Arg Thr Phe Phe Asn Asp Trp Ile Lys Ser

145 150 155 160

Leu Val Ala Asn Tyr Ser Ile Asp Gly Leu Arg Val Asp Thr Val Lys

165 170 175

His Val Glu Lys Asp Phe Trp Pro Asp Phe Asn Glu Ala Ala Gly Val

180 185 190

Tyr Ala Val Gly Glu Val Phe Asn Gly Asp Pro Ala Tyr Thr Cys Pro

195 200 205

Tyr Gln Glu Val Leu Asp Gly Val Leu Asn Tyr Pro Ile Tyr Tyr Pro

210 215 220

Ala Leu Asp Ala Phe Lys Ser Val Gly Gly Asn Leu Gly Gly Leu Ala

225 230 235 240

Gln Ala Ile Thr Thr Val Gln Glu Ser Cys Lys Asp Ser Asn Leu Leu

245 250 255

Gly Asn Phe Leu Glu Asn His Asp Ile Ala Arg Phe Ala Ser Tyr Thr

260 265 270

Asp Asp Leu Ala Leu Ala Lys Asn Gly Leu Ala Phe Ile Ile Leu Ser

275 280 285

Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ala Gly

290 295 300

Asp His Asp Pro Thr Asn Arg Glu Ala Val Trp Leu Ser Gly Tyr Asn

305 310 315 320

Thr Asp Ala Glu Leu Tyr Gln Phe Ile Lys Lys Ala Asn Gly Ile Arg

325 330 335

Asn Leu Ala Ile Ser Gln Asn Pro Glu Phe Thr Ser Ser Lys Thr Lys

340 345 350

Val Ile Tyr Gln Asp Asp Ser Thr Leu Ala Ile Asn Arg Gly Gly Val

355 360 365

Val Thr Val Leu Ser Asn Glu Gly Ala Ser Gly Gly Asp Arg Thr Val

370 375 380

Ser Ile Pro Gly Thr Gly Phe Glu Ala Gly Thr Glu Leu Thr Asp Val

385 390 395 400

Ile Ser Cys Lys Thr Val Thr Ala Gly Asp Ser Gly Ala Val Asp Val

405 410 415

Pro Leu Ser Gly Gly Leu Pro Ser Val Leu Tyr Pro Ser Ser Gln Leu

420 425 430

Ala Lys Ser Gly Leu Cys Ala Ser Ala

435 440

<210>15

<211>1443

<212>DNA

<213>Acremonium sp.

<220>

<221> CDS

<222>(1)..(1443)

<400>15

gct gcc ggg ctc tcg gct gcc gag tgg cgg agc cag tcc atc tac cag 48

Ala Ala Gly Leu Ser Ala Ala Glu Trp Arg Ser Gln Ser Ile Tyr Gln

1 5 10 15

gtt gtc acc gac agg ttc gcc cgg acc gac ctg tcg acc acg gcg tcg 96

Val Val Thr Asp Arg Phe Ala Arg Thr Asp Leu Ser Thr Thr Ala Ser

20 25 30

tgc aac acg gca gac caa gtc tac tgc gga ggg aca tgg cag ggg ctc 144

Cys Asn Thr Ala Asp Gln Val Tyr Cys Gly Gly Thr Trp Gln Gly Leu

35 40 45

atc tcc aag ctg gac tac atc cag ggc atg ggt ttc acc gcc gta tgg 192

Ile Ser Lys Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Val Trp

50 55 60

atc tca cca gtg gtc aag cag gtg gaa ggc aat tcc cag gac ggg tcg 240

Ile Ser Pro Val Val Lys Gln Val Glu Gly Asn Ser Gln Asp Gly Ser

65 70 75 80

gcc tat cac gga tac tgg gcg cag gat atc tgg gcc ttg aat ccg gct 288

Ala Tyr His Gly Tyr Trp Ala Gln Asp Ile Trp Ala Leu Asn Pro Ala

85 90 95

ttt ggg acc gag gag gat ctc gct gcg ctt gcc gcg gcg ctg cat gcc 336

Phe Gly Thr Glu Glu Asp Leu Ala Ala Leu Ala Ala Ala Leu His Ala

100 105 110

cga ggc atg tac ctc atg gtt gac att gtc acc aac cac atg gca tac 384

Arg Gly Met Tyr Leu Met Val Asp Ile Val Thr Asn His Met Ala Tyr

115 120 125

atg ggc tgc ggc acc tgt gta gac tac agc ctg ttc aac ccc ttc tca 432

Met Gly Cys Gly Thr Cys Val Asp Tyr Ser Leu Phe Asn Pro Phe Ser

130 135 140

tcg tca tcg tac ttc cac cca tat tgc gcc atc gac tac agc aac cag 480

Ser Ser Ser Tyr Phe His Pro Tyr Cys Ala Ile Asp Tyr Ser Asn Gln

145 150 155 160

acg tcg gtc gag gtt tgc tgg caa ggg gat aac att gtc agt ctg cct 528

Thr Ser Val Glu Val Cys Trp Gln Gly Asp Asn Ile Val Ser Leu Pro

165 170 175

gac ctg cgc acc gag gat gac acg gtg cgc agc atc tgg aac cgc tgg 576

Asp Leu Arg Thr Glu Asp Asp Thr Val Arg Ser Ile Trp Asn Arg Trp

180 185 190

gtt agc cag ctc gtg tcc aac tac tcc atc gac ggc ttc cga gtc gac 624

Val Ser Gln Leu Val Ser Asn Tyr Ser Ile Asp Gly Phe Arg Val Asp

195 200 205

agc gca aaa cac gtc gag acg tcc ttt tgg caa gac ttc tcg aca gcg 672

Ser Ala Lys His Val Glu Thr Ser Phe Trp Gln Asp Phe Ser Thr Ala

210 215 220

gcg ggc gtg tac ctg ctg ggc gag gtc ttt gac ggg gac ccg tcg tac 720

Ala Gly Val Tyr Leu Leu Gly Glu Val Phe Asp Gly Asp Pro Ser Tyr

225 230 235 240

gtg gcg cct tac cag aac tac ctc aac ggg gtt ctg gat tat ccc agc 768

Val Ala Pro Tyr Gln Asn Tyr Leu Asn Gly Val Leu Asp Tyr Pro Ser

245 250 255

tac tac tgg atc ctc cgg gct ttc cag tca tcc agc ggc agc atc agc 816

Tyr Tyr Trp Ile Leu Arg Ala Phe Gln Ser Ser Ser Gly Ser Ile Ser

260 265 270

gac ctc gtc tcc ggg ctc aac acg ctc cat ggc gtt gct ctg gac ctg 864

Asp Leu Val Ser Gly Leu Asn Thr Leu His Gly Val Ala Leu Asp Leu

275 280 285

agt cta tat ggg tcc ttc ctc gag aac cac gat gtg gcg cgg ttt gcg 912

Ser Leu Tyr Gly Ser Phe Leu Glu Asn His Asp Val Ala Arg Phe Ala

290 295 300

tcc ttc acg cag gac atg tcc cta gcg aag aat gcc atc gca ttc aca 960

Ser Phe Thr Gln Asp Met Ser Leu Ala Lys Asn Ala Ile Ala Phe Thr

305 310 315 320

atg ctg aaa gac ggc atc ccc atc ata tac cag gga caa gag caa cat 1008

Met Leu Lys Asp Gly Ile Pro Ile Ile Tyr Gln Gly Gln Glu Gln His

325 330 335

tac gct ggc gga acg acg ccc aac aac cgc gag gcg ctc tgg ctc tcg 1056

Tyr Ala Gly Gly Thr Thr Pro Asn Asn Arg Glu Ala Leu Trp Leu Ser

340 345 350

ggc tac tcg act agc tcc gag ctc tac aag tgg att gcc gcc ttg aac 1104

Gly Tyr Ser Thr Ser Ser Glu Leu Tyr Lys Trp Ile Ala Ala Leu Asn

355 360 365

cag atc cgg gcc cga gct att gct caa gat agc ggc tac ctc tcc tac 1152

Gln Ile Arg Ala Arg Ala Ile Ala Gln Asp Ser Gly Tyr Leu Ser Tyr

370 375 380

agc agc caa gcc atc tac tcg gac agc cat acc att gcc atg cgc aaa 1200

Ser Ser Gln Ala Ile Tyr Ser Asp Ser His Thr Ile Ala Met Arg Lys

385 390 395 400

ggt acc tcg gga tac cag atc gtg ggc gtg ttc acc aat gtc ggg gcc 1248

Gly Thr Ser Gly Tyr Gln Ile Val Gly Val Phe Thr Asn Val Gly Ala

405 410 415

tcg tcg tcg gct acg gtc acc cta acc tct tcc gca acg ggc ttc ggg 1296

Ser Ser Ser Ala Thr Val Thr Leu Thr Ser Ser Ala Thr Gly Phe Gly

420 425 430

gcg aac caa gca ctc gtc gac gtg atg agc tgc acc gct tac acc aca 1344

Ala Asn Gln Ala Leu Val Asp Val Met Ser Cys Thr Ala Tyr Thr Thr

435 440 445

gat tcg acg gga gcc ctc acg gta acc ctg aac gac ggc ctg ccc aag 1392

Asp Ser Thr Gly Ala Leu Thr Val Thr Leu Asn Asp Gly Leu Pro Lys

450 455 460

gtg ctt tat ccg att gcg cgg ctc tcg ggc agc ggt atc tgc cca ggg 1440

Val Leu Tyr Pro Ile Ala Arg Leu Ser Gly Ser Gly Ile Cys Pro Gly

465 470 475 480

cag 1443

Gln

<210>16

<211>481

<212>PRT

<213>Acremonium sp.

<400>16

Ala Ala Gly Leu Ser Ala Ala Glu Trp Arg Ser Gln Ser Ile Tyr Gln

1 5 10 15

Val Val Thr Asp Arg Phe Ala Arg Thr Asp Leu Ser Thr Thr Ala Ser

20 25 30

Cys Asn Thr Ala Asp Gln Val Tyr Cys Gly Gly Thr Trp Gln Gly Leu

35 40 45

Ile Ser Lys Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Val Trp

50 55 60

Ile Ser Pro Val Val Lys Gln Val Glu Gly Asn Ser Gln Asp Gly Ser

65 70 75 80

Ala Tyr His Gly Tyr Trp Ala Gln Asp Ile Trp Ala Leu Asn Pro Ala

85 90 95

Phe Gly Thr Glu Glu Asp Leu Ala Ala Leu Ala Ala Ala Leu His Ala

100 105 110

Arg Gly Met Tyr Leu Met Val Asp Ile Val Thr Asn His Met Ala Tyr

115 120 125

Met Gly Cys Gly Thr Cys Val Asp Tyr Ser Leu Phe Asn Pro Phe Ser

130 135 140

Ser Ser Ser Tyr Phe His Pro Tyr Cys Ala Ile Asp Tyr Ser Asn Gln

145 150 155 160

Thr Ser Val Glu Val Cys Trp Gln Gly Asp Asn Ile Val Ser Leu Pro

165 170 175

Asp Leu Arg Thr Glu Asp Asp Thr Val Arg Ser Ile Trp Asn Arg Trp

180 185 190

Val Ser Gln Leu Val Ser Asn Tyr Ser Ile Asp Gly Phe Arg Val Asp

195 200 205

Ser Ala Lys His Val Glu Thr Ser Phe Trp Gln Asp Phe Ser Thr Ala

210 215 220

Ala Gly Val Tyr Leu Leu Gly Glu Val Phe Asp Gly Asp Pro Ser Tyr

225 230 235 240

Val Ala Pro Tyr Gln Asn Tyr Leu Asn Gly Val Leu Asp Tyr Pro Ser

245 250 255

Tyr Tyr Trp Ile Leu Arg Ala Phe Gln Ser Ser Ser Gly Ser Ile Ser

260 265 270

Asp Leu Val Ser Gly Leu Asn Thr Leu His Gly Val Ala Leu Asp Leu

275 280 285

Ser Leu Tyr Gly Ser Phe Leu Glu Asn His Asp Val Ala Arg Phe Ala

290 295 300

Ser Phe Thr Gln Asp Met Ser Leu Ala Lys Asn Ala Ile Ala Phe Thr

305 310 315 320

Met Leu Lys Asp Gly Ile Pro Ile Ile Tyr Gln Gly Gln Glu Gln His

325 330 335

Tyr Ala Gly Gly Thr Thr Pro Asn Asn Arg Glu Ala Leu Trp Leu Ser

340 345 350

Gly Tyr Ser Thr Ser Ser Glu Leu Tyr Lys Trp Ile Ala Ala Leu Asn

355 360 365

Gln Ile Arg Ala Arg Ala Ile Ala Gln Asp Ser Gly Tyr Leu Ser Tyr

370 375 380

Ser Ser Gln Ala Ile Tyr Ser Asp Ser His Thr Ile Ala Met Arg Lys

385 390 395 400

Gly Thr Ser Gly Tyr Gln Ile Val Gly Val Phe Thr Asn Val Gly Ala

405 410 415

Ser Ser Ser Ala Thr Val Thr Leu Thr Ser Ser Ala Thr Gly Phe Gly

420 425 430

Ala Asn Gln Ala Leu Val Asp Val Met Ser Cys Thr Ala Tyr Thr Thr

435 440 445

Asp Ser Thr Gly Ala Leu Thr Val Thr Leu Asn Asp Gly Leu Pro Lys

450 455 460

Val Leu Tyr Pro Ile Ala Arg Leu Ser Gly Ser Gly Ile Cys Pro Gly

465 470 475 480

Gln

<210>17

<211>1413

<212>DNA

<213>Malbranchea sp.

<220>

<221> CDS

<222>(1)..(1413)

<400>17

gcc acg cct gat gag tgg cgc tca agg tcc atc tat cag gtc ctg acc 48

Ala Thr Pro Asp Glu Trp Arg Ser Arg Ser Ile Tyr Gln Val Leu Thr

1 5 10 15

gac cgg ttc gcc cgc ggg gat ggc tcg acc gat gcc ccg tgc gat acg 96

Asp Arg Phe Ala Arg Gly Asp Gly Ser Thr Asp Ala Pro Cys Asp Thr

20 25 30

ggt gcc agg aag tat tgc gga gga aac tat cgg gga ctc atc agc cag 144

Gly Ala Arg Lys Tyr Cys Gly Gly Asn Tyr Arg Gly Leu Ile Ser Gln

35 40 45

ctc gac tat atc cag ggc atg gga ttc gac agc gtc tgg ata tcc ccc 192

Leu Asp Tyr Ile Gln Gly Met Gly Phe Asp Ser Val Trp Ile Ser Pro

50 55 60

atc acc aag cag ttt gag gat gac tgg aac ggt gcc ccg tac cac ggg 240

Ile Thr Lys Gln Phe Glu Asp Asp Trp Asn Gly Ala Pro Tyr His Gly

65 70 75 80

tac tgg cag acg gac ctc tat gcg ctg aac gag cac ttt ggt acc gag 288

Tyr Trp Gln Thr Asp Leu Tyr Ala Leu Asn Glu His Phe Gly Thr Glu

85 90 95

gag gat ctc cga gct ctc gcc gat gag ctc cac gcc cgt ggc atg ttc 336

Glu Asp Leu Arg Ala Leu Ala Asp Glu Leu His Ala Arg Gly Met Phe

100 105 110

ctc atg gtc gac gtc gtc atc aac cac aac ggc tgg ccc ggc gac gca 384

Leu Met Val Asp Val Val Ile Asn His Asn Gly Trp Pro Gly Asp Ala

115 120 125

gcg tcc atc gac tac tcg cag ttc aac ccg ttc aac agc tcc gac tat 432

Ala Ser Ile Asp Tyr Ser Gln Phe Asn Pro Phe Asn Ser Ser Asp Tyr

130 135 140

tac cat cca ccc tgt gag atc aac tat gac gac cag act tcg gtc gag 480

Tyr His Pro Pro Cys Glu Ile Asn Tyr Asp Asp Gln Thr Ser Val Glu

145 150 155 160

cag tgc tgg ctc tac acc ggg gcc aat gcg ctg cct gat ctc aag acg 528

Gln Cys Trp Leu Tyr Thr Gly Ala Asn Ala Leu Pro Asp Leu Lys Thr

165 170 175

gag gac ccc cat gtc tcg cag gtg cac aac gac tgg atc gcc gac ctc 576

Glu Asp Pro His Val Ser Gln Val His Asn Asp Trp Ile Ala Asp Leu

180 185 190

gtc tcc aag tat tcc atc gac ggc ttg cgc att gac acc aca aag cat 624

Val Ser Lys Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Thr Lys His

195 200 205

gtg gac aaa ccc gct atc ggt tcc ttc aat gac gcc gct ggc gtg tac 672

Val Asp Lys Pro Ala Ile Gly Ser Phe Asn Asp Ala Ala Gly Val Tyr

210 215 220

gcc gtc gga gag gtt tac cac ggt gat cct gca tac act tgt ccc tac 720

Ala Val Gly Glu Val Tyr His Gly Asp Pro Ala Tyr Thr Cys Pro Tyr

225 230 235 240

cag gac tgg gtc gac ggg gtc ctc aac ttc cct gtc tac tac ccg cta 768

Gln Asp Trp Val Asp Gly Val Leu Asn Phe Pro Val Tyr Tyr Pro Leu

245 250 255

atc gac gcg ttc aag tcg cct tcg ggc acc atg tgg tct ctt gtc gac 816

Ile Asp Ala Phe Lys Ser Pro Ser Gly Thr Met Trp Ser Leu Val Asp

260 265 270

aac atc aac aaa gtc ttc caa acc tgc aat gac ccg cgg ctc ctg ggg 864

Asn Ile Asn Lys Val Phe Gln Thr Cys Asn Asp Pro Arg Leu Leu Gly

275 280 285

acc ttc tcg gag aac cat gac atc ccc cgc ttc gcc tcg tac acg caa 912

Thr Phe Ser Glu Asn His Asp Ile Pro Arg Phe Ala Ser Tyr Thr Gln

290 295 300

gac ctc gcc ctc gcg aag aac gtg ctg gcc ttc acg atc ctg ttc gac 960

Asp Leu Ala Leu Ala Lys Asn Val Leu Ala Phe Thr Ile Leu Phe Asp

305 310 315 320

ggc atc cca atc gtc tac gcg ggc cag gag caa cag tac tct gga gac 1008

Gly Ile Pro Ile Val Tyr Ala Gly Gln Glu Gln Gln Tyr Ser Gly Asp

325 330 335

tcg gac ccg tat aat cga gag gcc ctc tgg ctc tcc gga ttc aac acc 1056

Ser Asp Pro Tyr Asn Arg Glu Ala Leu Trp Leu Ser Gly Phe Asn Thr

340 345 350

gac gct cct cta tac aag cac att gca gct tgc aac aga ata cgg tcg 1104

Asp Ala Pro Leu Tyr Lys His Ile Ala Ala Cys Asn Arg Ile Arg Ser

355 360 365

cac gca gtg tcc aac gac gac gcg tac atc acc act ccg acg gac atc 1152

His Ala Val Ser Asn Asp Asp Ala Tyr Ile Thr Thr Pro Thr Asp Ile

370 375 380

aag tac agc gat gac cac acc ctg gcg ctg gtc aag ggt gcg gtg acg 1200

Lys Tyr Ser Asp Asp His Thr Leu Ala Leu Val Lys Gly Ala Val Thr

385 390 395 400

acc gtg ctg acc aac gcc ggc gcc aac gcc ggc gag acc acc gta acg 1248

Thr Val Leu Thr Asn Ala Gly Ala Asn Ala Gly Glu Thr Thr Val Thr

405 410 415

gtg gaa gca acc ggc tat gcc agt gga gag cag gtt act gat gtg ctg 1296

Val Glu Ala Thr Gly Tyr Ala Ser Gly Glu Gln Val Thr Asp Val Leu

420 425 430

agc tgc gag tcg atc gct gcg tcg gat ggc gga cgt ctc agt gta aca 1344

Ser Cys Glu Ser Ile Ala Ala Ser Asp Gly Gly Arg Leu Ser Val Thr

435 440 445

ctg aac cag ggc ctt cca cgt gtg ttc ttc ccg act gat gcc ctt gcg 1392

Leu Asn Gln Gly Leu Pro Arg Val Phe Phe Pro Thr Asp Ala Leu Ala

450 455 460

ggc tcc ggg ctc tgc gag aac 1413

Gly Ser Gly Leu Cys Glu Asn

465 470

<210>18

<211>471

<212>PRT

<213>Malbranchea sp.

<400>18

Ala Thr Pro Asp Glu Trp Arg Ser Arg Ser Ile Tyr Gln Val Leu Thr

1 5 10 15

Asp Arg Phe Ala Arg Gly Asp Gly Ser Thr Asp Ala Pro Cys Asp Thr

20 25 30

Gly Ala Arg Lys Tyr Cys Gly Gly Asn Tyr Arg Gly Leu Ile Ser Gln

35 40 45

Leu Asp Tyr Ile Gln Gly Met Gly Phe Asp Ser Val Trp Ile Ser Pro

50 55 60

Ile Thr Lys Gln Phe Glu Asp Asp Trp Asn Gly Ala Pro Tyr His Gly

65 70 75 80

Tyr Trp Gln Thr Asp Leu Tyr Ala Leu Asn Glu His Phe Gly Thr Glu

85 90 95

Glu Asp Leu Arg Ala Leu Ala Asp Glu Leu His Ala Arg Gly Met Phe

100 105 110

Leu Met Val Asp Val Val Ile Asn His Asn Gly Trp Pro Gly Asp Ala

115 120 125

Ala Ser Ile Asp Tyr Ser Gln Phe Asn Pro Phe Asn Ser Ser Asp Tyr

130 135 140

Tyr His Pro Pro Cys Glu Ile Asn Tyr Asp Asp Gln Thr Ser Val Glu

145 150 155 160

Gln Cys Trp Leu Tyr Thr Gly Ala Asn Ala Leu Pro Asp Leu Lys Thr

165 170 175

Glu Asp Pro His Val Ser Gln Val His Asn Asp Trp Ile Ala Asp Leu

180 185 190

Val Ser Lys Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Thr Lys His

195 200 205

Val Asp Lys Pro Ala Ile Gly Ser Phe Asn Asp Ala Ala Gly Val Tyr

210 215 220

Ala Val Gly Glu Val Tyr His Gly Asp Pro Ala Tyr Thr Cys Pro Tyr

225 230 235 240

Gln Asp Trp Val Asp Gly Val Leu Asn Phe Pro Val Tyr Tyr Pro Leu

245 250 255

Ile Asp Ala Phe Lys Ser Pro Ser Gly Thr Met Trp Ser Leu Val Asp

260 265 270

Asn Ile Asn Lys Val Phe Gln Thr Cys Asn Asp Pro Arg Leu Leu Gly

275 280 285

Thr Phe Ser Glu Asn His Asp Ile Pro Arg Phe Ala Ser Tyr Thr Gln

290 295 300

Asp Leu Ala Leu Ala Lys Asn Val Leu Ala Phe Thr Ile Leu Phe Asp

305 310 315 320

Gly Ile Pro Ile Val Tyr Ala Gly Gln Glu Gln Gln Tyr Ser Gly Asp

325 330 335

Ser Asp Pro Tyr Asn Arg Glu Ala Leu Trp Leu Ser Gly Phe Asn Thr

340 345 350

Asp Ala Pro Leu Tyr Lys His Ile Ala Ala Cys Asn Arg Ile Arg Ser

355 360 365

His Ala Val Ser Asn Asp Asp Ala Tyr Ile Thr Thr Pro Thr Asp Ile

370 375 380

Lys Tyr Ser Asp Asp His Thr Leu Ala Leu Val Lys Gly Ala Val Thr

385 390 395 400

Thr Val Leu Thr Asn Ala Gly Ala Asn Ala Gly Glu Thr Thr Val Thr

405 410 415

Val Glu Ala Thr Gly Tyr Ala Ser Gly Glu Gln Val Thr Asp Val Leu

420 425 430

Ser Cys Glu Ser Ile Ala Ala Ser Asp Gly Gly Arg Leu Ser Val Thr

435 440 445

Leu Asn Gln Gly Leu Pro Arg Val Phe Phe Pro Thr Asp Ala Leu Ala

450 455 460

Gly Ser Gly Leu Cys Glu Asn

465 470

<210>19

<211>1350

<212>DNA

<213>Rhizomucor pusillus

<220>

<221> CDS

<222>(1)..(1350)

<400>19

agc cct ttg ccc caa cag cag cga tat ggc aaa aga gca act tcg gat 48

Ser Pro Leu Pro Gln Gln Gln Arg Tyr Gly Lys Arg Ala Thr Ser Asp

1 5 10 15

gac tgg aaa ggc aag gcc att tat cag ctg ctt aca gat cga ttt ggc 96

Asp Trp Lys Gly Lys Ala Ile Tyr Gln Leu Leu Thr Asp Arg Phe Gly

20 25 30

cgc gcc gat gac tca aca agc aac tgc tct aat tta tcc aac tac tgt 144

Arg Ala Asp Asp Ser Thr Ser Asn Cys Ser Asn Leu Ser Asn Tyr Cys

35 40 45

ggt ggt acc tac gaa ggc att acg aag cat ctt gac tac att tcc ggt 192

Gly Gly Thr Tyr Glu Gly Ile Thr Lys His Leu Asp Tyr Ile Ser Gly

50 55 60

atg ggc ttt gat gct atc tgg ata tcg cca att ccc aag aac tcg gat 240

Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro Lys Asn Ser Asp

65 70 75 80

gga ggc tac cac ggc tac tgg gct aca gat ttc tac caa cta aac agc 288

Gly Gly Tyr His Gly Tyr Trp Ala Thr Asp Phe Tyr Gln Leu Asn Ser

85 90 95

aac ttt ggt gat gaa tcc cag ctc aaa gcg ctc atc cag gct gcc cat 336

Asn Phe Gly Asp Glu Ser Gln Leu Lys Ala Leu Ile Gln Ala Ala His

100 105 110

gaa cgt gac atg tat gtt atg ctt gat gtc gta gcc aat cat gca ggt 384

Glu Arg Asp Met Tyr Val Met Leu Asp Val Val Ala Asn His Ala Gly

115 120 125

ccc acc agc aat ggc tac tcg ggt tac aca ttc ggc gat gca agt tta 432

Pro Thr Ser Asn Gly Tyr Ser Gly Tyr Thr Phe Gly Asp Ala Ser Leu

130 135 140

tat cat cct aaa tgc acc ata gat tac aat gat cag acg tct att gag 480

Tyr His Pro Lys Cys Thr Ile Asp Tyr Asn Asp Gln Thr Ser Ile Glu

145 150 155 160

caa tgc tgg gtt gct gac gag ttg cct gat att gac act gaa aat tct 528

Gln Cys Trp Val Ala Asp Glu Leu Pro Asp Ile Asp Thr Glu Asn Ser

165 170 175

gac aac gtg gcc att ctc aac gac atc gtc tcc ggc tgg gtg ggt aac 576

Asp Asn Val Ala Ile Leu Asn Asp Ile Val Ser Gly Trp Val Gly Asn

180 185 190

tat agc ttt gac ggc atc cgc att gat act gtc aag cat att cgc aag 624

Tyr Ser Phe Asp Gly Ile Arg Ile Asp Thr Val Lys His Ile Arg Lys

195 200 205

gac ttt tgg aca ggc tac gca gaa gct gcc ggc gta ttc gca act gga 672

Asp Phe Trp Thr Gly Tyr Ala Glu Ala Ala Gly Val Phe Ala Thr Gly

210 215 220

gag gtc ttc aat ggt gat ccg gcc tac gtt gga cct tat caa aag tac 720

Glu Val Phe Asn Gly Asp Pro Ala Tyr Val Gly Pro Tyr Gln Lys Tyr

225 230 235 240

ctg cca tct ctc atc aat tac cca atg tat tac gct ttg aac gac gtc 768

Leu Pro Ser Leu Ile Asn Tyr Pro Met Tyr Tyr Ala Leu Asn Asp Val

245 250 255

ttt gta tcc aaa agc aaa gga ttc agc cgc atc agc gaa atg cta gga 816

Phe Val Ser Lys Ser Lys Gly Phe Ser Arg Ile Ser Glu Met Leu Gly

260 265 270

tca aat cgc aat gcg ttt gag gat acc agc gta ctt aca acg ttt gta 864

Ser Asn Arg Asn Ala Phe Glu Asp Thr Ser Val Leu Thr Thr Phe Val

275 280 285

gac aac cat gac aat ccg cgc ttc ttg aac agt caa agc gac aag gct 912

Asp Asn His Asp Asn Pro Arg Phe Leu Asn Ser Gln Ser Asp Lys Ala

290 295 300

ctc ttc aag aac gct ctc aca tac gta ctg cta ggt gaa ggc atc cca 960

Leu Phe Lys Asn Ala Leu Thr Tyr Val Leu Leu Gly Glu Gly Ile Pro

305 310 315 320

att gtg tat tat ggt tct gag caa ggt ttc agc gga gga gcg gat cct 1008

Ile Val Tyr Tyr Gly Ser Glu Gln Gly Phe Ser Gly Gly Ala Asp Pro

325 330 335

gct aac cgt gaa gtg ctg tgg acc acc aat tat gat aca tcc agc gat 1056

Ala Asn Arg Glu Val Leu Trp Thr Thr Asn Tyr Asp Thr Ser Ser Ser Asp

340 345 350

ctc tac caa ttt atc aag aca gtc aac agt gtc cgc atg aaa agc aac 1104

Leu Tyr Gln Phe Ile Lys Thr Val Asn Ser Val Arg Met Lys Ser Asn

355 360 365

aag gcc gtc tac atg gat att tat gtt ggc gac aat gct tac gcc ttc 1152

Lys Ala Val Tyr Met Asp Ile Tyr Val Gly Asp Asn Ala Tyr Ala Phe

370 375 380

aag cac ggc gat gct ttg gtt gtt ctc aat aac tat gga tca ggt tcc 1200

Lys His Gly Asp Ala Leu Val Val Leu Asn Asn Tyr Gly Ser Gly Ser

385 390 395 400

aca aac caa gtc agc ttc agc gtt agt ggc aag ttc gat agc ggc gca 1248

Thr Asn Gln Val Ser Phe Ser Val Ser Gly Lys Phe Asp Ser Gly Ala

405 410 415

agc ctc atg gat att gtc agt aac att acc acc acg gtg tcc tcg gat 1296

Ser Leu Met Asp Ile Val Ser Asn Ile Thr Thr Thr Val Ser Ser Asp

420 425 430

gga aca gtc act ttc aac ctt aaa gat gga ctt ccg gct atc ttc acc 1344

Gly Thr Val Thr Phe Asn Leu Lys Asp Gly Leu Pro Ala Ile Phe Thr

435 440 445

tct gct 1350

Ser Ala

450

<210>20

<211>450

<212>PRT

<213>Rhizomucor pusillus

<400>20

Ser Pro Leu Pro Gln Gln Gln Arg Tyr Gly Lys Arg Ala Thr Ser Asp

1 5 10 15

Asp Trp Lys Gly Lys Ala Ile Tyr Gln Leu Leu Thr Asp Arg Phe Gly

20 25 30

Arg Ala Asp Asp Ser Thr Ser Asn Cys Ser Asn Leu Ser Asn Tyr Cys

35 40 45

Gly Gly Thr Tyr Glu Gly Ile Thr Lys His Leu Asp Tyr Ile Ser Gly

50 55 60

Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro Lys Asn Ser Asp

65 70 75 80

Gly Gly Tyr His Gly Tyr Trp Ala Thr Asp Phe Tyr Gln Leu Asn Ser

85 90 95

Asn Phe Gly Asp Glu Ser Gln Leu Lys Ala Leu Ile Gln Ala Ala His

100 105 110

Glu Arg Asp Met Tyr Val Met Leu Asp Val Val Ala Asn His Ala Gly

115 120 125

Pro Thr Ser Asn Gly Tyr Ser Gly Tyr Thr Phe Gly Asp Ala Ser Leu

130 135 140

Tyr His Pro Lys Cys Thr Ile Asp Tyr Asn Asp Gln Thr Ser Ile Glu

145 150 155 160

Gln Cys Trp Val Ala Asp Glu Leu Pro Asp Ile Asp Thr Glu Asn Ser

165 170 175

Asp Asn Val Ala Ile Leu Asn Asp Ile Val Ser Gly Trp Val Gly Asn

180 185 190

Tyr Ser Phe Asp Gly Ile Arg Ile Asp Thr Val Lys His Ile Arg Lys

195 200 205

Asp Phe Trp Thr Gly Tyr Ala Glu Ala Ala Gly Val Phe Ala Thr Gly

210 215 220

Glu Val Phe Asn Gly Asp Pro Ala Tyr Val Gly Pro Tyr Gln Lys Tyr

225 230 235 240

Leu Pro Ser Leu Ile Asn Tyr Pro Met Tyr Tyr Ala Leu Asn Asp Val

245 250 255

Phe Val Ser Lys Ser Lys Gly Phe Ser Arg Ile Ser Glu Met Leu Gly

260 265 270

Ser Asn Arg Asn Ala Phe Glu Asp Thr Ser Val Leu Thr Thr Phe Val

275 280 285

Asp Asn His Asp Asn Pro Arg Phe Leu Asn Ser Gln Ser Asp Lys Ala

290 295 300

Leu Phe Lys Asn Ala Leu Thr Tyr Val Leu Leu Gly Glu Gly Ile Pro

305 310 315 320

Ile Val Tyr Tyr Gly Ser Glu Gln Gly Phe Ser Gly Gly Ala Asp Pro

325 330 335

Ala Asn Arg Glu Val Leu Trp Thr Thr Asn Tyr Asp Thr Ser Ser Ser Asp

340 345 350

Leu Tyr Gln Phe Ile Lys Thr Val Asn Ser Val Arg Met Lys Ser Asn

355 360 365

Lys Ala Val Tyr Met Asp Ile Tyr Val Gly Asp Asn Ala Tyr Ala Phe

370 375 380

Lys His Gly Asp Ala Leu Val Val Leu Asn Asn Tyr Gly Ser Gly Ser

385 390 395 400

Thr Asn Gln Val Ser Phe Ser Val Ser Gly Lys Phe Asp Ser Gly Ala

405 410 415

Ser Leu Met Asp Ile Val Ser Asn Ile Thr Thr Thr Val Ser Ser Asp

420 425 430

Gly Thr Val Thr Phe Asn Leu Lys Asp Gly Leu Pro Ala Ile Phe Thr

435 440 445

Ser Ala

450

<210>21

<211>1338

<212>DNA

<213>Dichotomocladium hesseltinei

<220>

<221> CDS

<222>(1)..(1338)

<400>21

caa ccg gtg aac atc acg aag cga gct tct gct gct gac tgg cgc tcg 48

Gln Pro Val Asn Ile Thr Lys Arg Ala Ser Ala Ala Asp Trp Arg Ser

1 5 10 15

cgt gcc atc tac caa gtc ctg acc gac cgc ttt gcg cgt acc gat ggg 96

Arg Ala Ile Tyr Gln Val Leu Thr Asp Arg Phe Ala Arg Thr Asp Gly

20 25 30

tcc aca agc gga tgc tca aac ttg tca aat tat tgc ggt ggc acg ttc 144

Ser Thr Ser Gly Cys Ser Asn Leu Ser Asn Tyr Cys Gly Gly Thr Phe

35 40 45

aaa ggc att acc aac aag ctt gac tac att gcc aac ctg ggc ttt gac 192

Lys Gly Ile Thr Asn Lys Leu Asp Tyr Ile Ala Asn Leu Gly Phe Asp

50 55 60

gct atc tgg atc tca ccc atc cca aca aac tcg ccc ggc ggc tac cat 240

Ala Ile Trp Ile Ser Pro Ile Pro Thr Asn Ser Pro Gly Gly Tyr His

65 70 75 80

ggc tac tgg gcc acc gac ttt tat ggt atc aat agc aac ttt gga tcc 288

Gly Tyr Trp Ala Thr Asp Phe Tyr Gly Ile Asn Ser Asn Phe Gly Ser

85 90 95

tcg aac gat ctc aag gag ctt gtc aat gct gct cac gcc aag ggt atg 336

Ser Asn Asp Leu Lys Glu Leu Val Asn Ala Ala His Ala Lys Gly Met

100 105 110

tac gtc atg ctc gat gtc gtg gca aac cac gct ggt cca acc tcg aac 384

Tyr Val Met Leu Asp Val Val Ala Asn His Ala Gly Pro Thr Ser Asn

115 120 125

ggc gac tac tct ggc tac acg ttc ggt tcc tct ggc ctc tac cat aac 432

Gly Asp Tyr Ser Gly Tyr Thr Phe Gly Ser Ser Gly Leu Tyr His Asn

130 135 140

cgg tgc tcg atc aac tac aac gac cag aga tcc att gag cag tgc tgg 480

Arg Cys Ser Ile Asn Tyr Asn Asp Gln Arg Ser Ile Glu Gln Cys Trp

145 150 155 160

gtg gcc gac gat ctc cct gat att aac acc gag aac aac gac aac gtc 528

Val Ala Asp Asp Leu Pro Asp Ile Asn Thr Glu Asn Asn Asp Asn Val

165 170 175

aac aag ccc aat aac att gtg tcc acc tgg gtc aag aca tat ggc ttt 576

Asn Lys Pro Asn Asn Ile Val Ser Thr Trp Val Lys Thr Tyr Gly Phe

180 185 190

gat gct atc cgc att gac acc gtc aag cat gtc cgc aag gat ttc tgg 624

Asp Ala Ile Arg Ile Asp Thr Val Lys His Val Arg Lys Asp Phe Trp

195 200 205

cct ggt tat aca tct gct gca ggc gtg ttc gcc act ggc gag gtc ttt 672

Pro Gly Tyr Thr Ser Ala Ala Gly Val Phe Ala Thr Gly Glu Val Phe

210 215 220

gat ggt aac ccg agt tat gtg gcc gat tat caa aac tac atg gag tcg 720

Asp Gly Asn Pro Ser Tyr Val Ala Asp Tyr Gln Asn Tyr Met Glu Ser

225 230 235 240

ctc atc aac tac ccg ctc tac tac gcg ctc aat gac gtc ttt gcg tcg 768

Leu Ile Asn Tyr Pro Leu Tyr Tyr Ala Leu Asn Asp Val Phe Ala Ser

245 250 255

ggt tat agc ttc agc cgg ctg agc aac cag cgt gtc gca aac tac cac 816

Gly Tyr Ser Phe Ser Arg Leu Ser Asn Gln Arg Val Ala Asn Tyr His

260 265 270

gcc ttc aaa gac gtg agc gtc ctt ccc att ttt atc gac aac cac gac 864

Ala Phe Lys Asp Val Ser Val Leu Pro Ile Phe Ile Asp Asn His Asp

275 280 285

aac ccc cgc ttc ctc aac aaa aag aat gac atc gcc cag ttc aag aac 912

Asn Pro Arg Phe Leu Asn Lys Lys Asn Asp Ile Ala Gln Phe Lys Asn

290 295 300

gct ctg acc tac gtg ctt ctc ggt gag ggc atc cct gtc gtc tac tac 960

Ala Leu Thr Tyr Val Leu Leu Gly Glu Gly Ile Pro Val Val Tyr Tyr

305 310 315 320

ggc tcc gag caa gct tac gcg ggt ggt gcc gac ccg gcc aac cgc gag 1008

Gly Ser Glu Gln Ala Tyr Ala Gly Gly Ala Asp Pro Ala Asn Arg Glu

325 330 335

gcc ctc tgg tcg agc ggg ttc tcg acc aac tcg gac atg tac cag ttc 1056

Ala Leu Trp Ser Ser Gly Phe Ser Thr Asn Ser Asp Met Tyr Gln Phe

340 345 350

att gcc aaa ctc aat cgc gtc cgt caa aag agc aac aag agc gtg tac 1104

Ile Ala Lys Leu Asn Arg Val Arg Gln Lys Ser Asn Lys Ser Val Tyr

355 360 365

atg gac ctg gac gtc cag aac aat gtg tac gcc ttc atg cac ggc aaa 1152

Met Asp Leu Asp Val Gln Asn Asn Val Tyr Ala Phe Met His Gly Lys

370 375 380

tcg ctc gtt gtg ctc aac aac ttt ggt aac ggt gcc tcg aga cag gtt 1200

Ser Leu Val Val Leu Asn Asn Phe Gly Asn Gly Ala Ser Arg Gln Val

385 390 395 400

act gtc aat gtc gga gct cag gtg gcc agc aac acc cga ttg acg gat 1248

Thr Val Asn Val Gly Ala Gln Val Ala Ser Asn Thr Arg Leu Thr Asp

405 410 415

gtt gtc agc ggc aca tcg gtc acg gtt tcg ggc agc tct gtc acc ttc 1296

Val Val Ser Gly Thr Ser Val Thr Val Ser Gly Ser Ser Val Thr Phe

420 425 430

act atc aac aac ggt ttg ccc gca gtc ttc act gtt tct tag 1338

Thr Ile Asn Asn Gly Leu Pro Ala Val Phe Thr Val Ser

435 440 445

<210>22

<211>445

<212>PRT

<213>Dichotomocladium hesseltinei

<400>22

Gln Pro Val Asn Ile Thr Lys Arg Ala Ser Ala Ala Asp Trp Arg Ser

1 5 10 15

Arg Ala Ile Tyr Gln Val Leu Thr Asp Arg Phe Ala Arg Thr Asp Gly

20 25 30

Ser Thr Ser Gly Cys Ser Asn Leu Ser Asn Tyr Cys Gly Gly Thr Phe

35 40 45

Lys Gly Ile Thr Asn Lys Leu Asp Tyr Ile Ala Asn Leu Gly Phe Asp

50 55 60

Ala Ile Trp Ile Ser Pro Ile Pro Thr Asn Ser Pro Gly Gly Tyr His

65 70 75 80

Gly Tyr Trp Ala Thr Asp Phe Tyr Gly Ile Asn Ser Asn Phe Gly Ser

85 90 95

Ser Asn Asp Leu Lys Glu Leu Val Asn Ala Ala His Ala Lys Gly Met

100 105 110

Tyr Val Met Leu Asp Val Val Ala Asn His Ala Gly Pro Thr Ser Asn

115 120 125

Gly Asp Tyr Ser Gly Tyr Thr Phe Gly Ser Ser Gly Leu Tyr His Asn

130 135 140

Arg Cys Ser Ile Asn Tyr Asn Asp Gln Arg Ser Ile Glu Gln Cys Trp

145 150 155 160

Val Ala Asp Asp Leu Pro Asp Ile Asn Thr Glu Asn Asn Asp Asn Val

165 170 175

Asn Lys Pro Asn Asn Ile Val Ser Thr Trp Val Lys Thr Tyr Gly Phe

180 185 190

Asp Ala Ile Arg Ile Asp Thr Val Lys His Val Arg Lys Asp Phe Trp

195 200 205

Pro Gly Tyr Thr Ser Ala Ala Gly Val Phe Ala Thr Gly Glu Val Phe

210 215 220

Asp Gly Asn Pro Ser Tyr Val Ala Asp Tyr Gln Asn Tyr Met Glu Scr

225 230 235 240

Leu Ile Asn Tyr Pro Leu Tyr Tyr Ala Leu Asn Asp Val Phe Ala Ser

245 250 255

Gly Tyr Ser Phe Ser Arg Leu Ser Asn Gln Arg Val Ala Asn Tyr His

260 265 270

Ala Phe Lys Asp Val Ser Val Leu Pro Ile Phe Ile Asp Asn His Asp

275 280 285

Asn Pro Arg Phe Leu Asn Lys Lys Asn Asp Ile Ala Gln Phe Lys Asn

290 295 300

Ala Leu Thr Tyr Val Leu Leu Gly Glu Gly Ile Pro Val Val Tyr Tyr

305 310 315 320

Gly Ser Glu Gln Ala Tyr Ala Gly Gly Ala Asp Pro Ala Asn Arg Glu

325 330 335

Ala Leu Trp Ser Ser Gly Phe Ser Thr Asn Ser Asp Met Tyr Gln Phe

340 345 350

Ile Ala Lys Leu Asn Arg Val Arg Gln Lys Ser Asn Lys Ser Val Tyr

355 360 365

Met Asp Leu Asp Val Gln Asn Asn Val Tyr Ala Phe Met His Gly Lys

370 375 380

Ser Leu Val Val Leu Asn Asn Phe Gly Asn Gly Ala Ser Arg Gln Val

385 390 395 400

Thr Val Asn Val Gly Ala Gln Val Ala Ser Asn Thr Arg Leu Thr Asp

405 410 415

Val Val Ser Gly Thr Ser Val Thr Val Ser Gly Ser Ser Val Thr Phe

420 425 430

Thr Ile Asn Asn Gly Leu Pro Ala Val Phe Thr Val Ser

435 440 445

<210>23

<211>1398

<212>DNA

<213>Meripilus giganteus

<220>

<221> CDS

<222>(1)..(1398)

<400>23

cgc cct act gtc ttt gac gcc ggc gcg gac gca cac tcg ctg cat gcc 48

Arg Pro Thr Val Phe Asp Ala Gly Ala Asp Ala His Ser Leu His Ala

1 5 10 15

cgg gcc ccc tcc ggc agc aag gat gtc atc atc cag atg ttt gag tgg 96

Arg Ala Pro Ser Gly Ser Lys Asp Val Ile Ile Gln Met Phe Glu Trp

20 25 30

aac tgg gac agc gtc gct gcc gag tgc act aac ttc atc ggc ccc gcc 144

Asn Trp Asp Ser Val Ala Ala Glu Cys Thr Asn Phe Ile Gly Pro Ala

35 40 45

ggg tac ggc ttc gtg caa gtg agc ccg ccc cag gag acc atc cag ggc 192

Gly Tyr Gly Phe Val Gln Val Ser Pro Pro Gln Glu Thr Ile Gln Gly

50 55 60

gcg cag tgg tgg acc gac tac cag ccg gtg tcg tac acg ctc act ggg 240

Ala Gln Trp Trp Thr Asp Tyr Gln Pro Val Ser Tyr Thr Leu Thr Gly

65 70 75 80

aag cgg ggc gac cgc tcc cag ttt gcg aac atg att act acg tgc cac 288

Lys Arg Gly Asp Arg Ser Gln Phe Ala Asn Met Ile Thr Thr Cys His

85 90 95

gcc gcg ggc gtc ggc gtg atc gtt gac acc atc tgg aac cac atg gcg 336

Ala Ala Gly Val Gly Val Ile Val Asp Thr Ile Trp Asn His Met Ala

100 105 110

ggc gtc gac tcc ggc acg ggt acc gcc ggc tcg tcc ttc acg cac tac 384

Gly Val Asp Ser Gly Thr Gly Thr Ala Gly Ser Ser Phe Thr His Tyr

115 120 125

aac tac ccc ggc atc tac caa aac cag gac ttt cac cac tgc ggc ctc 432

Asn Tyr Pro Gly Ile Tyr Gln Asn Gln Asp Phe His His Cys Gly Leu

130 135 140

gag ccg ggc gat gac atc gtc aac tac gac aac gcg gtt gag gtc cag 480

Glu Pro Gly Asp Asp Ile Val Asn Tyr Asp Asn Ala Val Glu Val Gln

145 150 155 160

acc tgc gag ctt gtc aac ctc gct gac ctc gcc acc gac acg gag tat 528

Thr Cys Glu Leu Val Asn Leu Ala Asp Leu Ala Thr Asp Thr Glu Tyr

165 170 175

gtg cgc ggt cgc ctt gcc cag tac gga aac gac ctg ctc tcg ctc ggt 576

Val Arg Gly Arg Leu Ala Gln Tyr Gly Asn Asp Leu Leu Ser Leu Gly

180 185 190

gcc gat ggc ctg cgt ctt gac gct tcc aaa cac att cct gtg ggc gac 624

Ala Asp Gly Leu Arg Leu Asp Ala Ser Lys His Ile Pro Val Gly Asp

195 200 205

atc gcg aac atc ctg tct cgc ctc agt cgc tct gtc tac atc acc cag 672

Ile Ala Asn Ile Leu Ser Arg Leu Ser Arg Ser Va1 Tyr Ile Thr Gln

210 215 220

gaa gtc atc ttt ggg gcc ggc gag ccc atc acg ccg aac cag tac acc 720

Glu Val Ile Phe Gly Ala Gly Glu Pro Ile Thr Pro Asn Gln Tyr Thr

225 230 235 240

ggg aac ggc gac gtt cag gag ttc cgc tac acc tct gcg cta aag gac 768

Gly Asn Gly Asp Val Gln Glu Phe Arg Tyr Thr Ser Ala Leu Lys Asp

245 250 255

gcc ttc ttg agc tcg ggc ata tcc aac ctg cag gac ttc gaa aac cgt 816

Ala Phe Leu Ser Ser Ser Gly Ile Ser Asn Leu Gln Asp Phe Glu Asn Arg

260 265 270

gga tgg gta cct ggc tcg ggc gcc aac gtg ttc gtc gtc aac cat gac 864

Gly Trp Val Pro Gly Ser Gly Ala Asn Val Phe Val Val Asn His Asp

275 280 285

acc gag cgg aac ggc gcg tcg ctg aac aac aac tcg cct tcg aac acc 912

Thr Glu Arg Asn Gly Ala Ser Leu Asn Asn Asn Ser Pro Ser Asn Thr

290 295 300

tac gtc acc gcg acg atc ttc tcg ctc gca cac ccg tac ggc acg ccc 960

Tyr Val Thr Ala Thr Ile Phe Ser Leu Ala His Pro Tyr Gly Thr Pro

305 310 315 320

acg atc ctc tcc tcg tat gat ggc ttc acg aac acc gac gcc ggt gcg 1008

Thr Ile Leu Ser Ser Tyr Asp Gly Phe Thr Asn Thr Asp Ala Gly Ala

325 330 335

ccg aac aac aac gtc ggc aca tgc tcg acc agc ggt ggt gcg aac ggg 1056

Pro Asn Asn Asn Val Gly Thr Cys Ser Thr Ser Ser Gly Gly Ala Asn Gly

340 345 350

tgg ctc tgc cag cac cgc tgg acc gcg atc gcc ggc atg gtc ggc ttc 1104

Trp Leu Cys Gln His Arg Trp Thr Ala Ile Ala Gly Met Val Gly Phe

355 360 365

cgc aac aac gtc ggc agc gct gca ctc aac aac tgg cag gcc ccg cag 1152

Arg Asn Asn Val Gly Ser Ala Ala Leu Asn Asn Trp Gln Ala Pro Gln

370 375 380

tcg cag cag att gcg ttc ggt cgc ggc gca ctt ggc ttc gtc gcg atc 1200

Ser Gln Gln Ile Ala Phe Gly Arg Gly Ala Leu Gly Phe Val Ala Ile

385 390 395 400

aac aac gcc gac tcg gcc tgg tct acg acg ttc acc act tcc ctc ccc 1248

Asn Asn Ala Asp Ser Ala Trp Ser Thr Thr Phe Thr Thr Ser Leu Pro

405 410 415

gat ggt tcc tac tgc gat gtc atc agc ggc aag gcc tcc ggc agt agc 1296

Asp Gly Ser Tyr Cys Asp Val Ile Ser Gly Lys Ala Ser Gly Ser Ser

420 425 430

tgc acc ggt tct tcg ttc acc acc gtc tcc ggc ggg aag ctg acc gcc acg 1344

Cys Thr Gly Ser Ser Phe Thr Val Ser Gly Gly Lys Leu Thr Ala Thr

435 440 445

gtg ccg gcg cgt agc gcc atc gcc gtg cac acc ggt cag aaa ggt tct 1392

Val Pro Ala Arg Ser Ala Ile Ala Val His Thr Gly Gln Lys Gly Ser

450 455 460

ggt ggt 1398

Gly Gly

465

<210>24

<211>466

<212>PRT

<213>Meripilus giganteus

<400>24

Arg Pro Thr Val Phe Asp Ala Gly Ala Asp Ala His Ser Leu His Ala

1 5 10 15

Arg Ala Pro Ser Gly Ser Lys Asp Val Ile Ile Gln Met Phe Glu Trp

20 25 30

Asn Trp Asp Ser Val Ala Ala Glu Cys Thr Asn Phe Ile Gly Pro Ala

35 40 45

Gly Tyr Gly Phe Val Gln Val Ser Pro Pro Gln Glu Thr Ile Gln Gly

50 55 60

Ala Gln Trp Trp Thr Asp Tyr Gln Pro Val Ser Tyr Thr Leu Thr Gly

65 70 75 80

Lys Arg Gly Asp Arg Ser Gln Phe Ala Asn Met Ile Thr Thr Cys His

85 90 95

Ala Ala Gly Val Gly Val Ile Val Asp Thr Ile Trp Asn His Met Ala

100 105 110

Gly Val Asp Ser Gly Thr Gly Thr Ala Gly Ser Ser Phe Thr His Tyr

115 120 125

Asn Tyr Pro Gly Ile Tyr Gln Asn Gln Asp Phe His His Cys Gly Leu

130 135 140

Glu Pro Gly Asp Asp Ile Val Asn Tyr Asp Asn Ala Val Glu Val Gln

145 150 155 160

Thr Cys Glu Leu Val Asn Leu Ala Asp Leu Ala Thr Asp Thr Glu Tyr

165 170 175

Val Arg Gly Arg Leu Ala Gln Tyr Gly Asn Asp Leu Leu Ser Leu Gly

180 185 190

Ala Asp Gly Leu Arg Leu Asp Ala Ser Lys His Ile Pro Val Gly Asp

195 200 205

Ile Ala Asn Ile Leu Ser Arg Leu Ser Arg Ser Val Tyr Ile Thr Gln

210 215 220

Glu Val Ile Phe Gly Ala Gly Glu Pro Ile Thr Pro Asn Gln Tyr Thr

225 230 235 240

Gly Asn Gly Asp Val Gln Glu Phe Arg Tyr Thr Ser Ala Leu Lys Asp

245 250 255

Ala Phe Leu Ser Ser Ser Gly Ile Ser Asn Leu Gln Asp Phe Glu Asn Arg

260 265 270

Gly Trp Val Pro Gly Ser Gly Ala Asn Val Phe Val Val Asn His Asp

275 280 285

Thr Glu Arg Asn Gly Ala Ser Leu Asn Asn Asn Ser Pro Ser Asn Thr

290 295 300

Tyr Val Thr Ala Thr Ile Phe Ser Leu Ala His Pro Tyr Gly Thr Pro

305 310 315 320

Thr Ile Leu Ser Ser Tyr Asp Gly Phe Thr Asn Thr Asp Ala Gly Ala

325 330 335

Pro Asn Asn Asn Val Gly Thr Cys Ser Thr Ser Ser Gly Gly Ala Asn Gly

340 345 350

Trp Leu Cys Gln His Arg Trp Thr Ala Ile Ala Gly Met Val Gly Phe

355 360 365

Arg Asn Asn Val Gly Ser Ala Ala Leu Asn Asn Trp Gln Ala Pro Gln

370 375 380

Ser Gln Gln Ile Ala Phe Gly Arg Gly Ala Leu Gly Phe Val Ala Ile

385 390 395 400

Asn Asn Ala Asp Ser Ala Trp Ser Thr Thr Phe Thr Thr Ser Leu Pro

405 410 415

Asp Gly Ser Tyr Cys Asp Val Ile Ser Gly Lys Ala Ser Gly Ser Ser

420 425 430

Cys Thr Gly Ser Ser Phe Thr Val Ser Gly Gly Lys Leu Thr Ala Thr

435 440 445

Val Pro Ala Arg Ser Ala Ile Ala Val His Thr Gly Gln Lys Gly Ser

450 455 460

Gly Gly

465

<210>25

<211>1494

<212>DNA

<213> Stereum sp.

<220>

<221> CDS

<222>(1)..(1494)

<400>25

gat gat tgg aag aac cgt act atc tat cag ctc gtg acg gac cgc ttc 48

Asp Asp Trp Lys Asn Arg Thr Ile Tyr Gln Leu Val Thr Asp Arg Phe

1 5 10 15

gcg cta gcc aat gat tcc agc ggt tca tgc gac act tca gac cgt gtt 96

Ala Leu Ala Asn Asp Ser Ser Gly Ser Cys Asp Thr Ser Asp Arg Val

20 25 30

tac tgt gga gga tca tgg caa ggt gtt atc aac cac ctc gat tac atc 144

Tyr Cys Gly Gly Ser Trp Gln Gly Val Ile Asn His Leu Asp Tyr Ile

35 40 45

caa aac atg ggc ttc gac gcc gtc tgg att tct ccc gtc agc acc aac 192

Gln Asn Met Gly Phe Asp Ala Val Trp Ile Ser Pro Val Ser Thr Asn

50 55 60

ttt gaa ggc tcg agt gct tat ggc gag gcc ttc cat ggt tac tgg ccc 240

Phe Glu Gly Ser Ser Ala Tyr Gly Glu Ala Phe His Gly Tyr Trp Pro

65 70 75 80

tct gac ctt tca tct gtc aac tct cac ttc ggt tct gat gac gac ctc 288

Ser Asp Leu Ser Ser Val Asn Ser His Phe Gly Ser Asp Asp Asp Leu

85 90 95

aag agc ctt gca tca gcc ctt cat gat cgc tca atg tac ctc atg att 336

Lys Ser Leu Ala Ser Ala Leu His Asp Arg Ser Met Tyr Leu Met Ile

100 105 110

gat gtc gtc gtc aat cac ctc gtc tac ccc tcc aac cct ccc acc ttc 384

Asp Val Val Val Asn His Leu Val Tyr Pro Ser Asn Pro Pro Thr Phe

115 120 125

agt gac ttc aac cct ttc aac acc gag tcc gac ttc cat ccc gag tgc 432

Ser Asp Phe Asn Pro Phe Asn Thr Glu Ser Asp Phe His Pro Glu Cys

130 135 140

ttc atc acc gac tat aat aac caa act gat gtt gag cag tgc tgg ctc 480

Phe Ile Thr Asp Tyr Asn Asn Gln Thr Asp Val Glu Gln Cys Trp Leu

145 150 155 160

ggt gat tca aac ttg cct ctg gca gat acc aac acg gag gat gat gat 528

Gly Asp Ser Asn Leu Pro Leu Ala Asp Thr Asn Thr Glu Asp Asp Asp

165 170 175

aac gtc tcg agc ttg tac agc tgg att aag aac ctt gtc agc acg tac 576

Asn Val Ser Ser Leu Tyr Ser Trp Ile Lys Asn Leu Val Ser Thr Tyr

180 185 190

agc gct gac ggt atc cgt atc gac acc gtg aag cac atc cgt cag gac 624

Ser Ala Asp Gly Ile Arg Ile Asp Thr Val Lys His Ile Arg Gln Asp

195 200 205

ttc tgg ccc gac ttt gct agc tct gct gga gtc tac acc att gga gag 672

Phe Trp Pro Asp Phe Ala Ser Ser Ser Ala Gly Val Tyr Thr Ile Gly Glu

210 215 220

gtt ctg agc aac gac acc gcc tac atc gcc aac tac acg caa gtc ctt 720

Val Leu Ser Asn Asp Thr Ala Tyr Ile Ala Asn Tyr Thr Gln Val Leu

225 230 235 240

gac ggt gtt ctc gat tac tct acc tgg tat cct ctc gtg gct ggc ttc 768

Asp Gly Val Leu Asp Tyr Ser Thr Trp Tyr Pro Leu Val Ala Gly Phe

245 250 255

cag tcg acc tcc gga aac ctt tcc gct atc aag gcc acc tat agc caa 816

Gln Ser Thr Ser Gly Asn Leu Ser Ala Ile Lys Ala Thr Tyr Ser Gln

260 265 270

gtc tcc agc tcg ttc aag aac ggc ggg ttc caa tca ggc tct ttc ctc 864

Val Ser Ser Ser Phe Lys Asn Gly Gly Phe Gln Ser Gly Ser Phe Leu

275 280 285

gaa aac cat gac cag ccc cgt ttc cag agc atg acc acg gat cag tct 912

Glu Asn His Asp Gln Pro Arg Phe Gln Ser Met Thr Thr Asp Gln Ser

290 295 300

ctc gtc aag aac gcg atg acc tgg ccc ttc atc aac gat ggt att ccc 960

Leu Val Lys Asn Ala Met Thr Trp Pro Phe Ile Asn Asp Gly Ile Pro

305 310 315 320

att ctg tac tac gga caa gag caa ggc tac tct ggt ggc gct gac ccc 1008

Ile Leu Tyr Tyr Gly Gln Glu Gln Gly Tyr Ser Gly Gly Ala Asp Pro

325 330 335

gct aac cgt gag gcc ctt tgg tcg tcc ggc tac gaa gag gat aag gat 1056

Ala Asn Arg Glu Ala Leu Trp Ser Ser Gly Tyr Glu Glu Asp Lys Asp

340 345 350

ctc gtt acc cac gtg aag ag ag ctc gtt gcc gcc cgc aag ctc gct gct 1104

Leu Val Thr His Val Lys Thr Leu Val Ala Ala Arg Lys Leu Ala Ala

355 360 365

gcc gct aac agc aac ttc cac agt acc gct gcc acg ttc ccc acg act 1152

Ala Ala Asn Ser Asn Phe His Ser Thr Ala Ala Thr Phe Pro Thr Thr

370 375 380

agc gac gaa tcc acc ctg gcc gtc ctc aaa acc cca atg ctt gcc ctc 1200

Ser Asp Glu Ser Thr Leu Ala Val Leu Lys Thr Pro Met Leu Ala Leu

385 390 395 400

ctc act aac acc ggc tca tcc ggc tct gca tcc ttc tcg act tca ggc 1248

Leu Thr Asn Thr Gly Ser Ser Ser Gly Ser Ala Ser Phe Ser Thr Ser Gly

405 410 415

gcc ggc ttt tcc gct aac gag gcg ctc gtt gat gtc ctc act tgc aac 1296

Ala Gly Phe Ser Ala Asn Glu Ala Leu Val Asp Val Leu Thr Cys Asn

420 425 430

acc gtc acc gct gac tcg tcc ggt gag gtc ggg ctc gcg tct aag tcg 1344

Thr Val Thr Ala Asp Ser Ser Gly Glu Val Gly Leu Ala Ser Lys Ser

435 440 445

ggc ctg ccg cag gtg tta ttg ccc gtc agt gcg ctg acg tcg gcc ggt 1392

Gly Leu Pro Gln Val Leu Leu Pro Val Ser Ala Leu Thr Ser Ala Gly

450 455 460

ggc gtg tgc acg aac ttg gtg agc gcg gcg cat gtc agc gcg aga gtg 1440

Gly Val Cys Thr Asn Leu Val Ser Ala Ala His Val Ser Ala Arg Val

465 470 475 480

ccg agt gcg atg gtg gcg acg acg gtg ttg ttt gcg ctc ttc cga ttc 1488

Pro Ser Ala Met Val Ala Thr Thr Val Leu Phe Ala Leu Phe Arg Phe

485 490 495

ctg gcg 1494

Leu Ala

<210>26

<211>498

<212>PRT

<213> Stereum sp.

<400>26

Asp Asp Trp Lys Asn Arg Thr Ile Tyr Gln Leu Val Thr Asp Arg Phe

1 5 10 15

Ala Leu Ala Asn Asp Ser Ser Gly Ser Cys Asp Thr Ser Asp Arg Val

20 25 30

Tyr Cys Gly Gly Ser Trp Gln Gly Val Ile Asn His Leu Asp Tyr Ile

35 40 45

Gln Asn Met Gly Phe Asp Ala Val Trp Ile Ser Pro Val Ser Thr Asn

50 55 60

Phe Glu Gly Ser Ser Ala Tyr Gly Glu Ala Phe His Gly Tyr Trp Pro

65 70 75 80

Ser Asp Leu Ser Ser Val Asn Ser His Phe Gly Ser Asp Asp Asp Leu

85 90 95

Lys Ser Leu Ala Ser Ala Leu His Asp Arg Ser Met Tyr Leu Met Ile

100 105 110

Asp Val Val Val Asn His Leu Val Tyr Pro Ser Asn Pro Pro Thr Phe

115 120 125

Ser Asp Phe Asn Pro Phe Asn Thr Glu Ser Asp Phe His Pro Glu Cys

130 135 140

Phe Ile Thr Asp Tyr Asn Asn Gln Thr Asp Val Glu Gln Cys Trp Leu

145 150 155 160

Gly Asp Ser Asn Leu Pro Leu Ala Asp Thr Asn Thr Glu Asp Asp Asp

165 170 175

Asn Val Ser Ser Leu Tyr Ser Trp Ile Lys Asn Leu Val Ser Thr Tyr

180 185 190

Ser Ala Asp Gly Ile Arg Ile Asp Thr Val Lys His Ile Arg Gln Asp

195 200 205

Phe Trp Pro Asp Phe Ala Ser Ser Ser Ala Gly Val Tyr Thr Ile Gly Glu

210 215 220

Val Leu Ser Asn Asp Thr Ala Tyr Ile Ala Asn Tyr Thr Gln Val Leu

225 230 235 240

Asp Gly Val Leu Asp Tyr Ser Thr Trp Tyr Pro Leu Val Ala Gly Phe

245 250 255

Gln Ser Thr Ser Gly Asn Leu Ser Ala Ile Lys Ala Thr Tyr Ser Gln

260 265 270

Val Ser Ser Ser Phe Lys Asn Gly Gly Phe Gln Ser Gly Ser Phe Leu

275 280 285

Glu Asn His Asp Gln Pro Arg Phe Gln Ser Met Thr Thr Asp Gln Ser

290 295 300

Leu Val Lys Asn Ala Met Thr Trp Pro Phe Ile Asn Asp Gly Ile Pro

305 310 315 320

Ile Leu Tyr Tyr Gly Gln Glu Gln Gly Tyr Ser Gly Gly Ala Asp Pro

325 330 335

Ala Asn Arg Glu Ala Leu Trp Ser Ser Gly Tyr Glu Glu Asp Lys Asp

340 345 350

Leu Val Thr His Val Lys Thr Leu Val Ala Ala Arg Lys Leu Ala Ala

355 360 365

Ala Ala Asn Ser Asn Phe His Ser Thr Ala Ala Thr Phe Pro Thr Thr

370 375 380

Ser Asp Glu Ser Thr Leu Ala Val Leu Lys Thr Pro Met Leu Ala Leu

385 390 395 400

Leu Thr Asn Thr Gly Ser Ser Ser Gly Ser Ala Ser Phe Ser Thr Ser Gly

405 410 415

Ala Gly Phe Ser Ala Asn Glu Ala Leu Val Asp Val Leu Thr Cys Asn

420 425 430

Thr Val Thr Ala Asp Ser Ser Gly Glu Val Gly Leu Ala Ser Lys Ser

435 440 445

Gly Leu Pro Gln Val Leu Leu Pro Val Ser Ala Leu Thr Ser Ala Gly

450 455 460

Gly Val Cys Thr Asn Leu Val Ser Ala Ala His Val Ser Ala Arg Val

465 470 475 480

Pro Ser Ala Met Val Ala Thr Thr Val Leu Phe Ala Leu Phe Arg Phe

485 490 495

Leu Ala

<210>27

<211>1539

<212>DNA

<213> Trametes sp.

<220>

<221> CDS

<222>(1)..(1539)

<400>27

gcg agc gca gac cag tgg cag aac cgg tct atc tac cag ttg gta aca 48

Ala Ser Ala Asp Gln Trp Gln Asn Arg Ser Ile Tyr Gln Leu Val Thr

1 5 10 15

gat cgt ttt gca acc cct gac ggc tct agc ccg tca tgc gac act tcg 96

Asp Arg Phe Ala Thr Pro Asp Gly Ser Ser Pro Ser Cys Asp Thr Ser

20 25 30

caa cgc cag tat tgt ggt ggc acc tgg aaa ggc gtg gca aac aaa ctc 144

Gln Arg Gln Tyr Cys Gly Gly Thr Trp Lys Gly Val Ala Asn Lys Leu

35 40 45

gac tac att cag aac atg ggc ttt gac gcg atc tgg atc tcc ccg atc 192

Asp Tyr Ile Gln Asn Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile

50 55 60

gtc gca aac gtc gag ggg aac acc tca tat ggc gaa gca ttc cat gga 240

Val Ala Asn Val Glu Gly Asn Thr Ser Tyr Gly Glu Ala Phe His Gly

65 70 75 80

tac tgg aca caa gac atc aac tcg ctc aac tct cat ttc ggt tcc gcc 288

Tyr Trp Thr Gln Asp Ile Asn Ser Leu Asn Ser His Phe Gly Ser Ala

85 90 95

gac gat ctc aaa gcc ctc agc tca gcc ttg cat gat cga ggc atg tac 336

Asp Asp Leu Lys Ala Leu Ser Ser Ser Ala Leu His Asp Arg Gly Met Tyr

100 105 110

ctc atg gtc gac gtc gtt gta aac cac atg gtt ggc acc tcc gac ccg 384

Leu Met Val Asp Val Val Val Asn His Met Val Gly Thr Ser Asp Pro

115 120 125

ccc aac ttc tct tcc ttc cag ccg ttc tcg tca cag tcc gac ttc cac 432

Pro Asn Phe Ser Ser Phe Gln Pro Phe Ser Ser Gln Ser Asp Phe His

130 135 140

tcc gag tgc ttt gtg tcg aac tac gac aac cag acc gaa gtc gaa cag 480

Ser Glu Cys Phe Val Ser Asn Tyr Asp Asn Gln Thr Glu Val Glu Gln

145 150 155 160

tgc tgg cta ggc gac aag aac gtc ccc ttg gta gac ttg aac acc gag 528

Cys Trp Leu Gly Asp Lys Asn Val Pro Leu Val Asp Leu Asn Thr Glu

165 170 175

gat gcg gac atc gta aag acc atg aac aca tgg atc tct acg ctc gtt 576

Asp Ala Asp Ile Val Lys Thr Met Asn Thr Trp Ile Ser Thr Leu Val

180 185 190

ggt aac tac agc gtc gac ggt gtc cgt atc gac act gtc aag cac gtc 624

Gly Asn Tyr Ser Val Asp Gly Val Arg Ile Asp Thr Val Lys His Val

195 200 205

cgg aaa gac ttc tgg ccc gac ttc gcc aag tct gct ggc gtc ttc acc 672

Arg Lys Asp Phe Trp Pro Asp Phe Ala Lys Ser Ala Gly Val Phe Thr

210 215 220

att ggc gag gtc ctc cac aat gag acg gat tac gtc tcg gca tac act 720

Ile Gly Glu Val Leu His Asn Glu Thr Asp Tyr Val Ser Ala Tyr Thr

225 230 235 240

cag gtc ctc gac agc gtc ctc gac tac ccc acc tgg ttc ccg ctt gtg 768

Gln Val Leu Asp Ser Val Leu Asp Tyr Pro Thr Trp Phe Pro Leu Val

245 250 255

gct gct ttc cag act acg ggt ggc aat ctg tca gct ctt gct gcg acc 816

Ala Ala Phe Gln Thr Thr Gly Gly Asn Leu Ser Ala Leu Ala Ala Thr

260 265 270

gtt caa cag gcg caa ggc tct tat aag aag ggc gag ttc atg acg ggt 864

Val Gln Gln Ala Gln Gly Ser Tyr Lys Lys Gly Glu Phe Met Thr Gly

275 280 285

tcc ttc ctt gag aac cac gat cag cct cga ttc caa tcc ctc acg caa 912

Ser Phe Leu Glu Asn His Asp Gln Pro Arg Phe Gln Ser Leu Thr Gln

290 295 300

gat cag gcg ttg gta aag aac gcc atg act tgg cca ttc gtt caa gat 960

Asp Gln Ala Leu Val Lys Asn Ala Met Thr Trp Pro Phe Val Gln Asp

305 310 315 320

ggt gtc ccg att atg tac tac ggc caa gaa cag tcc tac gct gga gga 1008

Gly Val Pro Ile Met Tyr Tyr Gly Gln Glu Gln Ser Tyr Ala Gly Gly

325 330 335

cct gac ccg gcc aac cgt gaa gct ttg tgg ctc tcc ggc tat gtc gaa 1056

Pro Asp Pro Ala Asn Arg Glu Ala Leu Trp Leu Ser Gly Tyr Val Glu

340 345 350

gat aag ccc ctg gtc aag cat gtt agg gca cta aac gca gcc cgc aaa 1104

Asp Lys Pro Leu Val Lys His Val Arg Ala Leu Asn Ala Ala Arg Lys

355 360 365

gct gcg atc tcg gcg aac agt aac tat ctg aac acc ggc gtc aaa ttt 1152

Ala Ala Ile Ser Ala Asn Ser Asn Tyr Leu Asn Thr Gly Val Lys Phe

370 375 380

ttg tcc acc gga tcc gaa tcc tcc atg gcc gtg tct aag ccg ccc atg 1200

Leu Ser Thr Gly Ser Glu Ser Ser Met Ala Val Ser Lys Pro Pro Met

385 390 395 400

ctg gct ctc ctc acg aac ggc ggc agc tcg tca acg cct tcg tgg acc 1248

Leu Ala Leu Leu Thr Asn Gly Gly Ser Ser Ser Thr Pro Ser Trp Thr

405 410 415

gtc tca gat gct ggg tac caa gcc aac gag gag ctg atc gac gtg ctc 1296

Val Ser Asp Ala Gly Tyr Gln Ala Asn Glu Glu Leu Ile Asp Val Leu

420 425 430

agt tgc cag aag gtc acc gcc gac gga aac ggc ggg gtg agc gtg cag 1344

Ser Cys Gln Lys Val Thr Ala Asp Gly Asn Gly Gly Val Ser Val Gln

435 440 445

gga tcc agc ggc agc cct caa gtc ctc atg ccg acg tct gcg ctc aac 1392

Gly Ser Ser Gly Ser Pro Gln Val Leu Met Pro Thr Ser Ala Leu Asn

450 455 460

aag tct gga agc atc tgt gca gaa gac gcg acg gga ggc caa gcc tcg 1440

Lys Ser Gly Ser Ile Cys Ala Glu Asp Ala Thr Gly Gly Gln Ala Ser

465 470 475 480

gct gcg caa ggc tgg atc gaa cgt gcg gca gag tct ctg cca atc gct 1488

Ala Ala Gln Gly Trp Ile Glu Arg Ala Ala Glu Ser Leu Pro Ile Ala

485 490 495

gct gcg ctg ttg ctc gcg gga tgg gct gcg cag tcc agc ctt gtt atc 1536

Ala Ala Leu Leu Leu Ala Gly Trp Ala Ala Gln Ser Ser Leu Val Ile

500 505 510

ctg 1539

Leu

<210>28

<211>513

<212>PRT

<213> Trametes sp.

<400>28

Ala Ser Ala Asp Gln Trp Gln Asn Arg Ser Ile Tyr Gln Leu Val Thr

1 5 10 15

Asp Arg Phe Ala Thr Pro Asp Gly Ser Ser Pro Ser Cys Asp Thr Ser

20 25 30

Gln Arg Gln Tyr Cys Gly Gly Thr Trp Lys Gly Val Ala Asn Lys Leu

35 40 45

Asp Tyr Ile Gln Asn Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile

50 55 60

Val Ala Asn Val Glu Gly Asn Thr Ser Tyr Gly Glu Ala Phe His Gly

65 70 75 80

Tyr Trp Thr Gln Asp Ile Asn Ser Leu Asn Ser His Phe Gly Ser Ala

85 90 95

Asp Asp Leu Lys Ala Leu Ser Ser Ser Ala Leu His Asp Arg Gly Met Tyr

100 105 110

Leu Met Val Asp Val Val Val Asn His Met Val Gly Thr Ser Asp Pro

115 120 125

Pro Asn Phe Ser Ser Phe Gln Pro Phe Ser Ser Gln Ser Asp Phe His

130 135 140

Ser Glu Cys Phe Val Ser Asn Tyr Asp Asn Gln Thr Glu Val Glu Gln

145 150 155 160

Cys Trp Leu Gly Asp Lys Asn Val Pro Leu Val Asp Leu Asn Thr Glu

165 170 175

Asp Ala Asp Ile Val Lys Thr Met Asn Thr Trp Ile Ser Thr Leu Val

180 185 190

Gly Asn Tyr Ser Val Asp Gly Val Arg Ile Asp Thr Val Lys His Val

195 200 205

Arg Lys Asp Phe Trp Pro Asp Phe Ala Lys Ser Ala Gly Val Phe Thr

210 215 220

Ile Gly Glu Val Leu His Asn Glu Thr Asp Tyr Val Ser Ala Tyr Thr

225 230 235 240

Gln Val Leu Asp Ser Val Leu Asp Tyr Pro Thr Trp Phe Pro Leu Val

245 250 255

Ala Ala Phe Gln Thr Thr Gly Gly Asn Leu Ser Ala Leu Ala Ala Thr

260 265 270

Val Gln Gln Ala Gln Gly Ser Tyr Lys Lys Gly Glu Phe Met Thr Gly

275 280 285

Ser Phe Leu Glu Asn His Asp Gln Pro Arg Phe Gln Ser Leu Thr Gln

290 295 300

Asp Gln Ala Leu Val Lys Asn Ala Met Thr Trp Pro Phe Val Gln Asp

305 310 315 320

Gly Val Pro Ile Met Tyr Tyr Gly Gln Glu Gln Ser Tyr Ala Gly Gly

325 330 335

Pro Asp Pro Ala Asn Arg Glu Ala Leu Trp Leu Ser Gly Tyr Val Glu

340 345 350

Asp Lys Pro Leu Val Lys His Val Arg Ala Leu Asn Ala Ala Arg Lys

355 360 365

Ala Ala Ile Ser Ala Asn Ser Asn Tyr Leu Asn Thr Gly Val Lys Phe

370 375 380

Leu Ser Thr Gly Ser Glu Ser Ser Met Ala Val Ser Lys Pro Pro Met

385 390 395 400

Leu Ala Leu Leu Thr Asn Gly Gly Ser Ser Ser Thr Pro Ser Trp Thr

405 410 415

Val Ser Asp Ala Gly Tyr Gln Ala Asn Glu Glu Leu Ile Asp Val Leu

420 425 430

Ser Cys Gln Lys Val Thr Ala Asp Gly Asn Gly Gly Val Ser Val Gln

435 440 445

Gly Ser Ser Gly Ser Pro Gln Val Leu Met Pro Thr Ser Ala Leu Asn

450 455 460

Lys Ser Gly Ser Ile Cys Ala Glu Asp Ala Thr Gly Gly Gln Ala Ser

465 470 475 480

Ala Ala Gln Gly Trp Ile Glu Arg Ala Ala Glu Ser Leu Pro Ile Ala

485 490 495

Ala Ala Leu Leu Leu Ala Gly Trp Ala Ala Gln Ser Ser Leu Val Ile

500 505 510

Leu

<210>29

<211>1521

<212>DNA

<213> Coriolus censor

<220>

<221> CDS

<222>(1)..(1521)

<400>29

gcc tct cct gac gac tgg cgt act agg tcg atc tac cag ctt gtg acc 48

Ala Ser Pro Asp Asp Trp Arg Thr Arg Ser Ile Tyr Gln Leu Val Thr

1 5 10 15

gac aga ttt gca acc cct gat ggc tca agc cca aca tgt aac acc gag 96

Asp Arg Phe Ala Thr Pro Asp Gly Ser Ser Pro Thr Cys Asn Thr Glu

20 25 30

gac cga agg tac tgc ggt ggt aac tac aag ggt atc atc aac aag ctc 144

Asp Arg Arg Tyr Cys Gly Gly Asn Tyr Lys Gly Ile Ile Asn Lys Leu

35 40 45

gac tac att caa aac atg ggg ttt gac gcc atc tgg atc tca cct gtg 192

Asp Tyr Ile Gln Asn Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Val

50 55 60

gtc gcg aat gta gag gga aat acc agt ctc ggt gaa gcc ttc cat ggc 240

Val Ala Asn Val Glu Gly Asn Thr Ser Leu Gly Glu Ala Phe His Gly

65 70 75 80

tac tgg act caa gat atc aac aaa ttg aac gat cat ttc ggg tct act 288

Tyr Trp Thr Gln Asp Ile Asn Lys Leu Asn Asp His Phe Gly Ser Thr

85 90 95

gac gat ttg aag tcg ctt tcg gat gcc ctg cac aag cgt aac atg tat 336

Asp Asp Leu Lys Ser Leu Ser Asp Ala Leu His Lys Arg Asn Met Tyr

100 105 110

ctg atg gtc gat gtg gtt gtc aac cat atg gcg gca acg tca aac cca 384

Leu Met Val Asp Val Val Val Asn His Met Ala Ala Thr Ser Asn Pro

115 120 125

ccg aac ttt ggc agt ttc gcg ccc ttc aat caa cag tcc aac ttc cac 432

Pro Asn Phe Gly Ser Phe Ala Pro Phe Asn Gln Gln Ser Asn Phe His

130 135 140

ccg gaa tgt ttt atc caa gcc tcg gac tac gac aac aat cag acc gct 480

Pro Glu Cys Phe Ile Gln Ala Ser Asp Tyr Asp Asn Asn Gln Thr Ala

145 150 155 160

gtc gaa caa tgc tgg ctt ggc gac gaa aat ctc cca ctc gcg gat atg 528

Val Glu Gln Cys Trp Leu Gly Asp Glu Asn Leu Pro Leu Ala Asp Met

165 170 175

aat acc gag gac caa aac gtg atc agc aca tgg aac aca tgg atc ggc 576

Asn Thr Glu Asp Gln Asn Val Ile Ser Thr Trp Asn Thr Trp Ile Gly

180 185 190

gac ttg gtc aag aac tat act atc gat ggt gtc cgc att gat act gtc 624

Asp Leu Val Lys Asn Tyr Thr Ile Asp Gly Val Arg Ile Asp Thr Val

195 200 205

aag cat gtg cga aag gac ttc tgg ccc gac ttt gcc aag gcc gct ggc 672

Lys His Val Arg Lys Asp Phe Trp Pro Asp Phe Ala Lys Ala Ala Gly

210 215 220

gta tac act att ggt gaa gtt ttg cac aac gat acc aac tat gtt gca 720

Val Tyr Thr Ile Gly Glu Val Leu His Asn Asp Thr Asn Tyr Val Ala

225 230 235 240

ccc tac acg cag gcg ctt tct gct gca cta gac tat cct gcc tac ttc 768

Pro Tyr Thr Gln Ala Leu Ser Ala Ala Leu Asp Tyr Pro Ala Tyr Phe

245 250 255

ttc ttg act gct ggt ttc caa acc tcc aac ggc aac tta tcg aat ttt 816

Phe Leu Thr Ala Gly Phe Gln Thr Ser Asn Gly Asn Leu Ser Asn Phe

260 265 270

gct tcg gtt atc cag gcc ggg cag ggt gca tac aac aat ggc gag cac 864

Ala Ser Val Ile Gln Ala Gly Gln Gly Ala Tyr Asn Asn Gly Glu His

275 280 285

tac atg ggc tcc ttc ctt gag aat cac gac aac cct cgt ttc caa tcc 912

Tyr Met Gly Ser Phe Leu Glu Asn His Asp Asn Pro Arg Phe Gln Ser

290 295 300

ctc act caa gat caa gca ttg gta aag aat gcg atg act tgg cca ttt 960

Leu Thr Gln Asp Gln Ala Leu Val Lys Asn Ala Met Thr Trp Pro Phe

305 310 315 320

atc caa gac ggt atc ccg atc ctt tac tac ggt cag gaa caa ggc tac 1008

Ile Gln Asp Gly Ile Pro Ile Leu Tyr Tyr Gly Gln Glu Gln Gly Tyr

325 330 335

gcc ggt gga aat gat cct gct aac cgt gaa gca ctc tgg ctg tcc ggg 1056

Ala Gly Gly Asn Asp Pro Ala Asn Arg Glu Ala Leu Trp Leu Ser Gly

340 345 350

tac ggc gaa gac aaa ccc ctg gtt cag cat gtc aag acg ttg aac gcc 1104

Tyr Gly Glu Asp Lys Pro Leu Val Gln His Val Lys Thr Leu Asn Ala

355 360 365

gcg cgt aag gcc gct gcc gct gcc aaa agc gac ttc cac acc agc agc 1152

Ala Arg Lys Ala Ala Ala Ala Ala Lys Ser Asp Phe His Thr Ser Ser

370 375 380

ctc caa ttc ctt gtc agc aca cag aac aat ctg gcc att tcg aag ccc 1200

Leu Gln Phe Leu Val Ser Thr Gln Asn Asn Leu Ala Ile Ser Lys Pro

385 390 395 400

cct atg ctt acg ctg ctc act aat gaa ggt agc act tct acg cca caa 1248

Pro Met Leu Thr Leu Leu Thr Asn Glu Gly Ser Thr Ser Thr Pro Gln

405 410 415

tgg agc gtc cca aac gct ggg ttc agc gca aac gag gaa gtc gtc gat 1296

Trp Ser Val Pro Asn Ala Gly Phe Ser Ala Asn Glu Glu Val Val Asp

420 425 430

gtg ttg act tgc aag aag ata aac gct gac gct aac gga ggt gtc act 1344

Val Leu Thr Cys Thr Lys Ile Asn Ala Asp Ala Asn Gly Gly Val Thr

435 440 445

gtc aaa ggc tcg gga ggt aat ccc caa gtc ctg atg cct act tct gcc 1392

Val Lys Gly Ser Gly Gly Asn Pro Gln Val Leu Met Pro Thr Ser Ala

450 455 460

ctt cca aaa ggc ggg acc gta tgt ccc gac tta gca acg gga gca cag 1440

Leu Pro Lys Gly Gly Thr Val Cys Pro Asp Leu Ala Thr Gly Ala Gln

465 470 475 480

tct tcc tct gct cgt tca ctc gcg gtg cag gtg ctt ggg act tct ctc 1488

Ser Ser Ser Ala Arg Ser Leu Ala Val Gln Val Leu Gly Thr Ser Leu

485 490 495

gct gcc gtt ctc act ctc gcc att gca ttc tcg 1521

Ala Ala Val Leu Thr Leu Ala Ile Ala Phe Ser

500 505

<210>30

<211>507

<212>PRT

<213> Coriolus censor

<400>30

Ala Ser Pro Asp Asp Trp Arg Thr Arg Ser Ile Tyr Gln Leu Val Thr

1 5 10 15

Asp Arg Phe Ala Thr Pro Asp Gly Ser Ser Pro Thr Cys Asn Thr Glu

20 25 30

Asp Arg Arg Tyr Cys Gly Gly Asn Tyr Lys Gly Ile Ile Asn Lys Leu

35 40 45

Asp Tyr Ile Gln Asn Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Val

50 55 60

Val Ala Asn Val Glu Gly Asn Thr Ser Leu Gly Glu Ala Phe His Gly

65 70 75 80

Tyr Trp Thr Gln Asp Ile Asn Lys Leu Asn Asp His Phe Gly Ser Thr

85 90 95

Asp Asp Leu Lys Ser Leu Ser Asp Ala Leu His Lys Arg Asn Met Tyr

100 105 110

Leu Met Val Asp Val Val Val Asn His Met Ala Ala Thr Ser Asn Pro

115 120 125

Pro Asn Phe Gly Ser Phe Ala Pro Phe Asn Gln Gln Ser Asn Phe His

130 135 140

Pro Glu Cys Phe Ile Gln Ala Ser Asp Tyr Asp Asn Asn Gln Thr Ala

145 150 155 160

Val Glu Gln Cys Trp Leu Gly Asp Glu Asn Leu Pro Leu Ala Asp Met

165 170 175

Asn Thr Glu Asp Gln Asn Val Ile Ser Thr Trp Asn Thr Trp Ile Gly

180 185 190

Asp Leu Val Lys Asn Tyr Thr Ile Asp Gly Val Arg Ile Asp Thr Val

195 200 205

Lys His Val Arg Lys Asp Phe Trp Pro Asp Phe Ala Lys Ala Ala Gly

210 215 220

Val Tyr Thr Ile Gly Glu Val Leu His Asn Asp Thr Asn Tyr Val Ala

225 230 235 240

Pro Tyr Thr Gln Ala Leu Ser Ala Ala Leu Asp Tyr Pro Ala Tyr Phe

245 250 255

Phe Leu Thr Ala Gly Phe Gln Thr Ser Asn Gly Asn Leu Ser Asn Phe

260 265 270

Ala Ser Val Ile Gln Ala Gly Gln Gly Ala Tyr Asn Asn Gly Glu His

275 280 285

Tyr Met Gly Ser Phe Leu Glu Asn His Asp Asn Pro Arg Phe Gln Ser

290 295 300

Leu Thr Gln Asp Gln Ala Leu Val Lys Asn Ala Met Thr Trp Pro Phe

305 310 315 320

Ile Gln Asp Gly Ile Pro Ile Leu Tyr Tyr Gly Gln Glu Gln Gly Tyr

325 330 335

Ala Gly Gly Asn Asp Pro Ala Asn Arg Glu Ala Leu Trp Leu Ser Gly

340 345 350

Tyr Gly Glu Asp Lys Pro Leu Val Gln His Val Lys Thr Leu Asn Ala

355 360 365

Ala Arg Lys Ala Ala Ala Ala Ala Lys Ser Asp Phe His Thr Ser Ser

370 375 380

Leu Gln Phe Leu Val Ser Thr Gln Asn Asn Leu Ala Ile Ser Lys Pro

385 390 395 400

Pro Met Leu Thr Leu Leu Thr Asn Glu Gly Ser Thr Ser Thr Pro Gln

405 410 415

Trp Ser Val Pro Asn Ala Gly Phe Ser Ala Asn Glu Glu Val Val Asp

420 425 430

Val Leu Thr Cys Thr Lys Ile Asn Ala Asp Ala Asn Gly Gly Val Thr

435 440 445

Val Lys Gly Ser Gly Gly Asn Pro Gln Val Leu Met Pro Thr Ser Ala

450 455 460

Leu Pro Lys Gly Gly Thr Val Cys Pro Asp Leu Ala Thr Gly Ala Gln

465 470 475 480

Ser Ser Ser Ala Arg Ser Leu Ala Val Gln Val Leu Gly Thr Ser Leu

485 490 495

Ala Ala Val Leu Thr Leu Ala Ile Ala Phe Ser

500 505

<210>31

<211>1443

<212>DNA

<213>Dinemasporium sp.

<220>

<221> CDS

<222>(1)..(1443)

<400>31

gcc acg gca gag caa tgg agg tcg cgg gcg ata tat cag ctt ctc act 48

Ala Thr Ala Glu Gln Trp Arg Ser Arg Ala Ile Tyr Gln Leu Leu Thr

1 5 10 15

gat cga ttc gca aga cca gat aat agc acg aca gca aca tgt tat aca 96

Asp Arg Phe Ala Arg Pro Asp Asn Ser Thr Thr Ala Thr Cys Tyr Thr

20 25 30

cca gat aga aac tac tgt gga gga act tgg agt ggc atc atc agc caa 144

Pro Asp Arg Asn Tyr Cys Gly Gly Thr Trp Ser Gly Ile Ile Ser Gln

35 40 45

tta gat tac atc cag gac atg ggc ttc acc gcg ata tgg ata tct ccc 192

Leu Asp Tyr Ile Gln Asp Met Gly Phe Thr Ala Ile Trp Ile Ser Pro

50 55 60

gta act tcg aac att cct aat ata act tct tac ggc tac gct tat cac 240

Val Thr Ser Asn Ile Pro Asn Ile Thr Ser Tyr Gly Tyr Ala Tyr His

65 70 75 80

gga tac tgg caa caa gac ctt tat aag ttg aat gat cat ttt ggc act 288

Gly Tyr Trp Gln Gln Asp Leu Tyr Lys Leu Asn Asp His Phe Gly Thr

85 90 95

gcc gaa gat ttg aaa gca ctc agc cag gca ttg cat gac aga gac atg 336

Ala Glu Asp Leu Lys Ala Leu Ser Gln Ala Leu His Asp Arg Asp Met

100 105 110

tat ctg atg gta gat gta gtc gca aac cat aac ggc tgg ccc ggc gat 384

Tyr Leu Met Val Asp Val Val Ala Asn His Asn Gly Trp Pro Gly Asp

115 120 125

tct gcc tca gta aat tac tcc gcg ttc tac ccg ttc gac aat gca tca 432

Ser Ala Ser Val Asn Tyr Ser Ala Phe Tyr Pro Phe Asp Asn Ala Ser

130 135 140

cac tat cat ttg ttc tgc gtc gtc gac gat tat agc aat cag acc gac 480

His Tyr His Leu Phe Cys Val Val Asp Asp Tyr Ser Asn Gln Thr Asp

145 150 155 160

gtc gag gac tgt tgg ctc ggg gat acg aat gtc gag ctg gtg gat tta 528

Val Glu Asp Cys Trp Leu Gly Asp Thr Asn Val Glu Leu Val Asp Leu

165 170 175

gac acg aac agt caa gat gtt gtt gat ggg tac tct aaa tgg att ggt 576

Asp Thr Asn Ser Gln Asp Val Val Asp Gly Tyr Ser Lys Trp Ile Gly

180 185 190

gaa ttg gtc tcg aac tac tcc atc gac ggt ctc cgc atc gac acg gta 624

Glu Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Val

195 200 205

aag cac gtc gac aag ccc ttc tgg act tct ttc caa caa gca gcc ggc 672

Lys His Val Asp Lys Pro Phe Trp Thr Ser Phe Gln Gln Ala Ala Gly

210 215 220

gtc ttc acg aca ggg gaa ata ctc tcg ggt gat cct tcc tat act tgc 720

Val Phe Thr Thr Gly Glu Ile Leu Ser Gly Asp Pro Ser Tyr Thr Cys

225 230 235 240

gac tac cag aat tat ctt gat agt aca ttg aac tac ccg tta tgg tgg 768

Asp Tyr Gln Asn Tyr Leu Asp Ser Thr Leu Asn Tyr Pro Leu Trp Trp

245 250 255

cca gca atg gcg ttc ctc aac tca aca tct ggc tcc tcc gcc aac ctc 816

Pro Ala Met Ala Phe Leu Asn Ser Thr Ser Gly Ser Ser Ala Asn Leu

260 265 270

ctc aac cta ctg agc tcc cta cgg tct act tgc aaa gac gtc tcc gtc 864

Leu Asn Leu Leu Ser Ser Leu Arg Ser Thr Cys Lys Asp Val Ser Val

275 280 285

ctc ggt gta ttc acc gag aac cac gac ctc cct cgc ttc gcc tcg caa 912

Leu Gly Val Phe Thr Glu Asn His Asp Leu Pro Arg Phe Ala Ser Gln

290 295 300

act caa gac atg gct tta gcc aag aac gct ctc gcc ctc acg atc ttg 960

Thr Gln Asp Met Ala Leu Ala Lys Asn Ala Leu Ala Leu Thr Ile Leu

305 310 315 320

tct gac ggc ata ccc ata gtc tac gca gga caa gaa caa cac tac gac 1008

Ser Asp Gly Ile Pro Ile Val Tyr Ala Gly Gln Glu Gln His Tyr Asp

325 330 335

gga tcg ggc gat ccc tac aac aga gag gca aat tgg ctc tcg ggc tac 1056

Gly Ser Gly Asp Pro Tyr Asn Arg Glu Ala Asn Trp Leu Ser Gly Tyr

340 345 350

tcg cgc tcg aac gaa ctg tac ctc ctc gtc gcc gcc gtc aac caa gtc 1104

Ser Arg Ser Asn Glu Leu Tyr Leu Leu Val Ala Ala Val Asn Gln Val

355 360 365

cgc aac aga gcc ttg tat cga gat gca aac tac gcg act tat aat gct 1152

Arg Asn Arg Ala Leu Tyr Arg Asp Ala Asn Tyr Ala Thr Tyr Asn Ala

370 375 380

acc tct atc tat agt gat caa cat act gtt gcg ttc cgc aaa ggg tac 1200

Thr Ser Ile Tyr Ser Asp Gln His Thr Val Ala Phe Arg Lys Gly Tyr

385 390 395 400

gat gga cac cag atc atc tcc gtc atc acc aat acc ggg acc tct act 1248

Asp Gly His Gln Ile Ile Ser Val Ile Thr Asn Thr Gly Thr Ser Thr

405 410 415

cct cta tgg aac ctc acg gtg ccg gac aca ggt ctg gca tct ggc act 1296

Pro Leu Trp Asn Leu Thr Val Pro Asp Thr Gly Leu Ala Ser Gly Thr

420 425 430

gct gtt gta gag att ata acg tgc gat cag tct gtc att gcg agt gat 1344

Ala Val Val Glu Ile Ile Thr Cys Asp Gln Ser Val Ile Ala Ser Asp

435 440 445

ggg agt cta gct gtg ccg atg gaa gga ggg atg ccg agg ata tat tat 1392

Gly Ser Leu Ala Val Pro Met Glu Gly Gly Met Pro Arg Ile Tyr Tyr

450 455 460

ccg gtg gat gag gcg gtt ggt agt ggg att tgt aat ctt acg agt agc 1440

Pro Val Asp Glu Ala Val Gly Ser Gly Ile Cys Asn Leu Thr Ser Ser

465 470 475 480

tat 1443

Tyr

<210>32

<211>481

<212>PRT

<213>Dinemasporium sp.

<400>32

Ala Thr Ala Glu Gln Trp Arg Ser Arg Ala Ile Tyr Gln Leu Leu Thr

1 5 10 15

Asp Arg Phe Ala Arg Pro Asp Asn Ser Thr Thr Ala Thr Cys Tyr Thr

20 25 30

Pro Asp Arg Asn Tyr Cys Gly Gly Thr Trp Ser Gly Ile Ile Ser Gln

35 40 45

Leu Asp Tyr Ile Gln Asp Met Gly Phe Thr Ala Ile Trp Ile Ser Pro

50 55 60

Val Thr Ser Asn Ile Pro Asn Ile Thr Ser Tyr Gly Tyr Ala Tyr His

65 70 75 80

Gly Tyr Trp Gln Gln Asp Leu Tyr Lys Leu Asn Asp His Phe Gly Thr

85 90 95

Ala Glu Asp Leu Lys Ala Leu Ser Gln Ala Leu His Asp Arg Asp Met

100 105 110

Tyr Leu Met Val Asp Val Val Ala Asn His Asn Gly Trp Pro Gly Asp

115 120 125

Ser Ala Ser Val Asn Tyr Ser Ala Phe Tyr Pro Phe Asp Asn Ala Ser

130 135 140

His Tyr His Leu Phe Cys Val Val Asp Asp Tyr Ser Asn Gln Thr Asp

145 150 155 160

Val Glu Asp Cys Trp Leu Gly Asp Thr Asn Val Glu Leu Val Asp Leu

165 170 175

Asp Thr Asn Ser Gln Asp Val Val Asp Gly Tyr Ser Lys Trp Ile Gly

180 185 190

Glu Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Val

195 200 205

Lys His Val Asp Lys Pro Phe Trp Thr Ser Phe Gln Gln Ala Ala Gly

210 215 220

Val Phe Thr Thr Gly Glu Ile Leu Ser Gly Asp Pro Ser Tyr Thr Cys

225 230 235 240

Asp Tyr Gln Asn Tyr Leu Asp Ser Thr Leu Asn Tyr Pro Leu Trp Trp

245 250 255

Pro Ala Met Ala Phe Leu Asn Ser Thr Ser Gly Ser Ser Ala Asn Leu

260 265 270

Leu Asn Leu Leu Ser Ser Leu Arg Ser Thr Cys Lys Asp Val Ser Val

275 280 285

Leu Gly Val Phe Thr Glu Asn His Asp Leu Pro Arg Phe Ala Ser Gln

290 295 300

Thr Gln Asp Met Ala Leu Ala Lys Asn Ala Leu Ala Leu Thr Ile Leu

305 310 315 320

Ser Asp Gly Ile Pro Ile Val Tyr Ala Gly Gln Glu Gln His Tyr Asp

325 330 335

Gly Ser Gly Asp Pro Tyr Asn Arg Glu Ala Asn Trp Leu Ser Gly Tyr

340 345 350

Ser Arg Ser Asn Glu Leu Tyr Leu Leu Val Ala Ala Val Asn Gln Val

355 360 365

Arg Asn Arg Ala Leu Tyr Arg Asp Ala Asn Tyr Ala Thr Tyr Asn Ala

370 375 380

Thr Ser Ile Tyr Ser Asp Gln His Thr Val Ala Phe Arg Lys Gly Tyr

385 390 395 400

Asp Gly His Gln Ile Ile Ser Val Ile Thr Asn Thr Gly Thr Ser Thr

405 410 415

Pro Leu Trp Asn Leu Thr Val Pro Asp Thr Gly Leu Ala Ser Gly Thr

420 425 430

Ala Val Val Glu Ile Ile Thr Cys Asp Gln Ser Val Ile Ala Ser Asp

435 440 445

Gly Ser Leu Ala Val Pro Met Glu Gly Gly Met Pro Arg Ile Tyr Tyr

450 455 460

Pro Val Asp Glu Ala Val Gly Ser Gly Ile Cys Asn Leu Thr Ser Ser

465 470 475 480

Tyr

<210>33

<211>1485

<212>DNA

<213>Cryptosporiopsis sp.

<220>

<221> CDS

<222>(1)..(1485)

<400>33

ttg gac gca gca gga tgg cga aac cag agc atc tac cag gtc ctg acg 48

Leu Asp Ala Ala Gly Trp Arg Asn Gln Ser Ile Tyr Gln Val Leu Thr

1 5 10 15

gac cgc ttc gcc atg gcc gac ggc tcg aca ccc gca tgc gac gca tcc 96

Asp Arg Phe Ala Met Ala Asp Gly Ser Thr Pro Ala Cys Asp Ala Ser

20 25 30

caa ggc ctc tac tgc ggt ggc acc tgg cag ggc atc acc aac cag ttg 144

Gln Gly Leu Tyr Cys Gly Gly Thr Trp Gln Gly Ile Thr Asn Gln Leu

35 40 45

gat tac atc cag aac ctg ggt gcc acc gcc gtc tgg atc tcc cct gtc 192

Asp Tyr Ile Gln Asn Leu Gly Ala Thr Ala Val Trp Ile Ser Pro Val

50 55 60

atc aag aac gtc gag ggc aac ttt gcc gat tcc ggc gag gcc tac cac 240

Ile Lys Asn Val Glu Gly Asn Phe Ala Asp Ser Gly Glu Ala Tyr His

65 70 75 80

ggc ttc tgg gcg caa gac ctc tac tcg ctc aac tcg cat ttc ggt acc 288

Gly Phe Trp Ala Gln Asp Leu Tyr Ser Leu Asn Ser His Phe Gly Thr

85 90 95

gag gcc gac ctc aag gcc ctc gcc gac gcg ctc cac gcc cgg ggc atg 336

Glu Ala Asp Leu Lys Ala Leu Ala Asp Ala Leu His Ala Arg Gly Met

100 105 110

tac ctg atg gtc gac atc gcc ccg aac cac gtg ggc ctg aat acg gat 384

Tyr Leu Met Val Asp Ile Ala Pro Asn His Val Gly Leu Asn Thr Asp

115 120 125

gcc aac aac tat acc ggt tac act ccc ttc aac gag acc gaa tac tac 432

Ala Asn Asn Tyr Thr Gly Tyr Thr Pro Phe Asn Glu Thr Glu Tyr Tyr

130 135 140

cac gac gag tgc agc atc gtc tgg aac gtc cct acg tcc gag agg ctc 480

His Asp Glu Cys Ser Ile Val Trp Asn Val Pro Thr Ser Ser Glu Arg Leu

145 150 155 160

tgc tgg ctc gag ggt ctg ccc gac ctg cgt acc gaa gat gcc ggc gta 528

Cys Trp Leu Glu Gly Leu Pro Asp Leu Arg Thr Glu Asp Ala Gly Val

165 170 175

cgc cag gtg tat gcg gaa tgg atc aag gac ctg gtt gcc aat tac tcc 576

Arg Gln Val Tyr Ala Glu Trp Ile Lys Asp Leu Val Ala Asn Tyr Ser

180 185 190

atc gac ggt ctc cgt atc gat acc gcc ctg gag atc gag ccg gag ttc 624

Ile Asp Gly Leu Arg Ile Asp Thr Ala Leu Glu Ile Glu Pro Glu Phe

195 200 205

tgg acc gac ggt ggt gtc cgc gag gcc gcc ggc gtc ttc ctc ctg gcc 672

Trp Thr Asp Gly Gly Val Arg Glu Ala Ala Gly Val Phe Leu Leu Ala

210 215 220

gag att aac cac agc aac ccg gag acc ctg gcg ccc tac cag cag tac 720

Glu Ile Asn His Ser Asn Pro Glu Thr Leu Ala Pro Tyr Gln Gln Tyr

225 230 235 240

ctc gac ggg tac atg gac tac agc agc tgg aac tgg atc acg gat tcg 768

Leu Asp Gly Tyr Met Asp Tyr Ser Ser Trp Asn Trp Ile Thr Asp Ser

245 250 255

ttc cag gcc gtc gac gcc agc atg acc gac ctc tac gag ggg acc aac 816

Phe Gln Ala Val Asp Ala Ser Met Thr Asp Leu Tyr Glu Gly Thr Asn

260 265 270

cag ctg gcg gcc atg acc gac atc gac ccg tcg ctc ttc ggc tcc ttt 864

Gln Leu Ala Ala Met Thr Asp Ile Asp Pro Ser Leu Phe Gly Ser Phe

275 280 285

gtc gag aac cac gac cag gtc cgg ttc ccc tac cgc aac gcc gac atg 912

Val Glu Asn His Asp Gln Val Arg Phe Pro Tyr Arg Asn Ala Asp Met

290 295 300

gcc ctg gcc aag aac ctg tac acc ctc gcc ctg ctc cgg gac ggg atc 960

Ala Leu Ala Lys Asn Leu Tyr Thr Leu Ala Leu Leu Arg Asp Gly Ile

305 310 315 320

ccc atc gtc tac tac gga cag gag cag cac ttt gac ggc ggc atc gtg 1008

Pro Ile Val Tyr Tyr Gly Gln Glu Gln His Phe Asp Gly Gly Ile Val

325 330 335

ccc agc aac cgg gag gcg ctc tgg ctc ggc acc tac gac atc tac gcc 1056

Pro Ser Asn Arg Glu Ala Leu Trp Leu Gly Thr Tyr Asp Ile Tyr Ala

340 345 350

gag ctg tac ggc tgg atc cag cag acc atc aag gcg cgc gcg cac gcc 1104

Glu Leu Tyr Gly Trp Ile Gln Gln Thr Ile Lys Ala Arg Ala His Ala

355 360 365

gcg gcg gcg gac gcc acc ttc ctc acg acg cag agg aca cag gcc atc 1152

Ala Ala Ala Asp Ala Thr Phe Leu Thr Thr Gln Arg Thr Gln Ala Ile

370 375 380

ttc tac cag aac gcc acc gac atc aac agc agc gtc atc ggc ttc cgc 1200

Phe Tyr Gln Asn Ala Thr Asp Ile Asn Ser Ser Val Ile Gly Phe Arg

385 390 395 400

aag ggc cag atg ctc acc atg tac acc aac ggt ggc gcc gat gcc ctc 1248

Lys Gly Gln Met Leu Thr Met Tyr Thr Asn Gly Gly Ala Asp Ala Leu

405 410 415

aac ggt gcc tac ttt gcc att gcc cgc aac gtg cac ggc tac gcc atc 1296

Asn Gly Ala Tyr Phe Ala Ile Ala Arg Asn Val His Gly Tyr Ala Ile

420 425 430

ggt gag gac ctg gtc gac gtg gtg aac tgc gaa tcg ttc cag gtc gcc 1344

Gly Glu Asp Leu Val Asp Val Val Asn Cys Glu Ser Phe Gln Val Ala

435 440 445

ccc cac gga cgg ctc tgg gtc cag atg ccc aac ggt ggt ctg ccg cgt 1392

Pro His Gly Arg Leu Trp Val Gln Met Pro Asn Gly Gly Leu Pro Arg

450 455 460

gtg ttt tta ccg gtg aat cag acc gag ggg ctc tgc aac aac gtc ggc 1440

Val Phe Leu Pro Val Asn Gln Thr Glu Gly Leu Cys Asn Asn Val Gly

465 470 475 480

acg cct ttg tct aac tct acc atc act gtt gcg att gac aag gca 1485

Thr Pro Leu Ser Asn Ser Thr Ile Thr Val Ala Ile Asp Lys Ala

485 490 495

<210>34

<211>495

<212>PRT

<213>Cryptosporiopsis sp.

<400>34

Leu Asp Ala Ala Gly Trp Arg Asn Gln Ser Ile Tyr Gln Val Leu Thr

1 5 10 15

Asp Arg Phe Ala Met Ala Asp Gly Ser Thr Pro Ala Cys Asp Ala Ser

20 25 30

Gln Gly Leu Tyr Cys Gly Gly Thr Trp Gln Gly Ile Thr Asn Gln Leu

35 40 45

Asp Tyr Ile Gln Asn Leu Gly Ala Thr Ala Val Trp Ile Ser Pro Val

50 55 60

Ile Lys Asn Val Glu Gly Asn Phe Ala Asp Ser Gly Glu Ala Tyr His

65 70 75 80

Gly Phe Trp Ala Gln Asp Leu Tyr Ser Leu Asn Ser His Phe Gly Thr

85 90 95

Glu Ala Asp Leu Lys Ala Leu Ala Asp Ala Leu His Ala Arg Gly Met

100 105 110

Tyr Leu Met Val Asp Ile Ala Pro Asn His Val Gly Leu Asn Thr Asp

115 120 125

Ala Asn Asn Tyr Thr Gly Tyr Thr Pro Phe Asn Glu Thr Glu Tyr Tyr

130 135 140

His Asp Glu Cys Ser Ile Val Trp Asn Val Pro Thr Ser Ser Glu Arg Leu

145 150 155 160

Cys Trp Leu Glu Gly Leu Pro Asp Leu Arg Thr Glu Asp Ala Gly Val

165 170 175

Arg Gln Val Tyr Ala Glu Trp Ile Lys Asp Leu Val Ala Asn Tyr Ser

180 185 190

Ile Asp Gly Leu Arg Ile Asp Thr Ala Leu Glu Ile Glu Pro Glu Phe

195 200 205

Trp Thr Asp Gly Gly Val Arg Glu Ala Ala Gly Val Phe Leu Leu Ala

210 215 220

Glu Ile Asn His Ser Asn Pro Glu Thr Leu Ala Pro Tyr Gln Gln Tyr

225 230 235 240

Leu Asp Gly Tyr Met Asp Tyr Ser Ser Trp Asn Trp Ile Thr Asp Ser

245 250 255

Phe Gln Ala Val Asp Ala Ser Met Thr Asp Leu Tyr Glu Gly Thr Asn

260 265 270

Gln Leu Ala Ala Met Thr Asp Ile Asp Pro Ser Leu Phe Gly Ser Phe

275 280 285

Val Glu Asn His Asp Gln Val Arg Phe Pro Tyr Arg Asn Ala Asp Met

290 295 300

Ala Leu Ala Lys Asn Leu Tyr Thr Leu Ala Leu Leu Arg Asp Gly Ile

305 310 315 320

Pro Ile Val Tyr Tyr Gly Gln Glu Gln His Phe Asp Gly Gly Ile Val

325 330 335

Pro Ser Asn Arg Glu Ala Leu Trp Leu Gly Thr Tyr Asp Ile Tyr Ala

340 345 350

Glu Leu Tyr Gly Trp Ile Gln Gln Thr Ile Lys Ala Arg Ala His Ala

355 360 365

Ala Ala Ala Asp Ala Thr Phe Leu Thr Thr Gln Arg Thr Gln Ala Ile

370 375 380

Phe Tyr Gln Asn Ala Thr Asp Ile Asn Ser Ser Val Ile Gly Phe Arg

385 390 395 400

Lys Gly Gln Met Leu Thr Met Tyr Thr Asn Gly Gly Ala Asp Ala Leu

405 410 415

Asn Gly Ala Tyr Phe Ala Ile Ala Arg Asn Val His Gly Tyr Ala Ile

420 425 430

Gly Glu Asp Leu Val Asp Val Val Asn Cys Glu Ser Phe Gln Val Ala

435 440 445

Pro His Gly Arg Leu Trp Val Gln Met Pro Asn Gly Gly Leu Pro Arg

450 455 460

Val Phe Leu Pro Val Asn Gln Thr Glu Gly Leu Cys Asn Asn Val Gly

465 470 475 480

Thr Pro Leu Ser Asn Ser Thr Ile Thr Val Ala Ile Asp Lys Ala

485 490 495

<210>35

<211>1428

<212>DNA

<213> Coniochaeta sp.

<220>

<221> CDS

<222>(1)..(1428)

<400>35

gca gac tgg cgt gag cag tcc atc tac cag gtc gtg acg gac cgc ttc 48

Ala Asp Trp Arg Glu Gln Ser Ile Tyr Gln Val Val Thr Asp Arg Phe

1 5 10 15

gcg cgg acg gac ctg tcc acc acg gcc acg tgc gac acc tcg gcg cag 96

Ala Arg Thr Asp Leu Ser Thr Thr Ala Thr Cys Asp Thr Ser Ala Gln

20 25 30

gtg tat tgc ggc ggc acg tac aag ggt ctg atc tcc aag ctg gat tac 144

Val Tyr Cys Gly Gly Thr Tyr Lys Gly Leu Ile Ser Lys Leu Asp Tyr

35 40 45

att cag ggc atg ggc ttc act gcc atc tgg ata tcg ccc atc gtc gag 192

Ile Gln Gly Met Gly Phe Thr Ala 1le Trp Ile Ser Pro Ile Val Glu

50 55 60

cag atg gac ggt aat act gcc gac ggc tcc tcg tat cac ggt tac tgg 240

Gln Met Asp Gly Asn Thr Ala Asp Gly Ser Ser Tyr His Gly Tyr Trp

65 70 75 80

gcg cag gat att tgg agt ctg aac ccg tcg ttc gga tcg gct ggc gac 288

Ala Gln Asp Ile Trp Ser Leu Asn Pro Ser Phe Gly Ser Ala Gly Asp

85 90 95

ctg atc gcg ctc tcc aac gcg ctg cac gcc cgg ggc atg tac ctc atg 336

Leu Ile Ala Leu Ser Asn Ala Leu His Ala Arg Gly Met Tyr Leu Met

100 105 110

ctg gac gtg gtg acc aac cac ttt gct tac aac ggc tgc ggc aac tgc 384

Leu Asp Val Val Thr Asn His Phe Ala Tyr Asn Gly Cys Gly Asn Cys

115 120 125

gtc gac tac agc atc ttc acc ccg ttc aac tcg tcg tcg tac ttc cac 432

Val Asp Tyr Ser Ile Phe Thr Pro Phe Asn Ser Ser Ser Tyr Phe His

130 135 140

ccc ttc tgc ttg atc gac tac aac aac cag acg tcg atc gag cag tgc 480

Pro Phe Cys Leu Ile Asp Tyr Asn Asn Gln Thr Ser Ile Glu Gln Cys

145 150 155 160

tgg gag gga gac aac acc gtc agc ctg ccg gac ctg cgg acg gag aac 528

Trp Glu Gly Asp Asn Thr Val Ser Leu Pro Asp Leu Arg Thr Glu Asn

165 170 175

tcc aac gta cgc gcg ata tgg aac gac tgg atc acg cag att gtg gcg 576

Ser Asn Val Arg Ala Ile Trp Asn Asp Trp Ile Thr Gln Ile Val Ala

180 185 190

gcg tac ggc atc gac ggt ctg cgc atc gac agc gtc aag cac cag gag 624

Ala Tyr Gly Ile Asp Gly Leu Arg Ile Asp Ser Val Lys His Gln Glu

195 200 205

acg tcg ttc tgg tcc ggt ttc ggg tcg gcc gcc ggc gtg ttc atg ctg 672

Thr Ser Phe Trp Ser Gly Phe Gly Ser Ala Ala Gly Val Phe Met Leu

210 215 220

ggc gag gtg tac aac ggc gat ccg acg cag ctg gcg ccg tac cag gat 720

Gly Glu Val Tyr Asn Gly Asp Pro Thr Gln Leu Ala Pro Tyr Gln Asp

225 230 235 240

tac atg ccc gga ctg ctg gac tac gcg agc tac tac tgg atc acg agg 768

Tyr Met Pro Gly Leu Leu Asp Tyr Ala Ser Tyr Tyr Trp Ile Thr Arg

245 250 255

gcg ttc cag tcg agc agc ggg agt atg agc gat ctg gcg tct ggt gtc 816

Ala Phe Gln Ser Ser Ser Gly Ser Met Ser Asp Leu Ala Ser Gly Val

260 265 270

aac aca ctc aag agc att gcc agg aac aca agc ctg tac gga tct ttc 864

Asn Thr Leu Lys Ser Ile Ala Arg Asn Thr Ser Leu Tyr Gly Ser Phe

275 280 285

ctg gag aac cac gac cag ccg cgg ttc gcg tcg ctt acc tcg gac gtc 912

Leu Glu Asn His Asp Gln Pro Arg Phe Ala Ser Leu Thr Ser Asp Val

290 295 300

gcc ttg gcg aag aat gcg ata gcg ttt act atg ctg aag gac ggt atc 960

Ala Leu Ala Lys Asn Ala Ile Ala Phe Thr Met Leu Lys Asp Gly Ile

305 310 315 320

ccg gtc gtt tac cag ggc caa gag cag cac tat gcg ggc gga aat gtc 1008

Pro Val Val Tyr Gln Gly Gln Glu Gln His Tyr Ala Gly Gly Asn Val

325 330 335

cca gct gac cgc gaa gcg atc tgg ttg tcg ggg tac tcc acg tct gcg 1056

Pro Ala Asp Arg Glu Ala Ile Trp Leu Ser Gly Tyr Ser Thr Ser Ala

340 345 350

acg ctg tac acc tgg atc gcc gcg ctg aac aag gtc cgt tcg agg gct 1104

Thr Leu Tyr Thr Trp Ile Ala Ala Leu Asn Lys Val Arg Ser Arg Ala

355 360 365

atc gcg caa gac agc agc tac ctg agc tat cag gcg tat cct gtc tat 1152

Ile Ala Gln Asp Ser Ser Tyr Leu Ser Tyr Gln Ala Tyr Pro Val Tyr

370 375 380

acg gac agc aac acc att gcc atg cgc aag gga cgg gac gga tac cag 1200

Thr Asp Ser Asn Thr Ile Ala Met Arg Lys Gly Arg Asp Gly Tyr Gln

385 390 395 400

gtc atc ggg gtg ttc acc aac aag gga tcg agc ggg ttg tcc agt ctc 1248

Val Ile Gly Val Phe Thr Asn Lys Gly Ser Ser Gly Leu Ser Ser Leu

405 410 415

acc ctc acg acg tcg atg acc gga ttc acg gcg ggc cag gcg gtc gtg 1296

Thr Leu Thr Thr Ser Met Thr Gly Phe Thr Ala Gly Gln Ala Val Val

420 425 430

gat gtc atg agc tgc acc act ttc acg acg gac tac agc ggt agc ctc 1344

Asp Val Met Ser Cys Thr Thr Phe Thr Thr Asp Tyr Ser Gly Ser Leu

435 440 445

gct gtc acc ctt tcg gga ggc att ccg cgg gtg ttc tat cca agc gcg 1392

Ala Val Thr Leu Ser Gly Gly Ile Pro Arg Val Phe Tyr Pro Ser Ala

450 455 460

agg ttg agt ggc tca gga ata tgt ggc tcc aat ggg 1428

Arg Leu Ser Gly Ser Gly Ile Cys Gly Ser Asn Gly

465 470 475

<210>36

<211>476

<212>PRT

<213> Coniochaeta sp.

<400>36

Ala Asp Trp Arg Glu Gln Ser Ile Tyr Gln Val Val Thr Asp Arg Phe

1 5 10 15

Ala Arg Thr Asp Leu Ser Thr Thr Ala Thr Cys Asp Thr Ser Ala Gln

20 25 30

Val Tyr Cys Gly Gly Thr Tyr Lys Gly Leu Ile Ser Lys Leu Asp Tyr

35 40 45

Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Ser Pro 1le Val Glu

50 55 60

Gln Met Asp Gly Asn Thr Ala Asp Gly Ser Ser Tyr His Gly Tyr Trp

65 70 75 80

Ala Gln Asp Ile Trp Ser Leu Asn Pro Ser Phe Gly Ser Ala Gly Asp

85 90 95

Leu Ile Ala Leu Ser Asn Ala Leu His Ala Arg Gly Met Tyr Leu Met

100 105 110

Leu Asp Val Val Thr Asn His Phe Ala Tyr Asn Gly Cys Gly Asn Cys

115 120 125

Val Asp Tyr Ser Ile Phe Thr Pro Phe Asn Ser Ser Ser Tyr Phe His

130 135 140

Pro Phe Cys Leu Ile Asp Tyr Asn Asn Gln Thr Ser Ile Glu Gln Cys

145 150 155 160

Trp Glu Gly Asp Asn Thr Val Ser Leu Pro Asp Leu Arg Thr Glu Asn

165 170 175

Ser Asn Val Arg Ala Ile Trp Asn Asp Trp Ile Thr Gln Ile Val Ala

180 185 190

Ala Tyr Gly Ile Asp Gly Leu Arg Ile Asp Ser Val Lys His Gln Glu

195 200 205

Thr Ser Phe Trp Ser Gly Phe Gly Ser Ala Ala Gly Val Phe Met Leu

210 215 220

Gly Glu Val Tyr Asn Gly Asp Pro Thr Gln Leu Ala Pro Tyr Gln Asp

225 230 235 240

Tyr Met Pro Gly Leu Leu Asp Tyr Ala Ser Tyr Tyr Trp Ile Thr Arg

245 250 255

Ala Phe Gln Ser Ser Ser Gly Ser Met Ser Asp Leu Ala Ser Gly Val

260 265 270

Asn Thr Leu Lys Ser Ile Ala Arg Asn Thr Ser Leu Tyr Gly Ser Phe

275 280 285

Leu Glu Asn His Asp Gln Pro Arg Phe Ala Ser Leu Thr Ser Asp Val

290 295 300

Ala Leu Ala Lys Asn Ala Ile Ala Phe Thr Met Leu Lys Asp Gly Ile

305 310 315 320

Pro Val Val Tyr Gln Gly Gln Glu Gln His Tyr Ala Gly Gly Asn Val

325 330 335

Pro Ala Asp Arg Glu Ala Ile Trp Leu Ser Gly Tyr Ser Thr Ser Ala

340 345 350

Thr Leu Tyr Thr Trp Ile Ala Ala Leu Asn Lys Val Arg Ser Arg Ala

355 360 365

Ile Ala Gln Asp Ser Ser Tyr Leu Ser Tyr Gln Ala Tyr Pro Val Tyr

370 375 380

Thr Asp Ser Asn Thr Ile Ala Met Arg Lys Gly Arg Asp Gly Tyr Gln

385 390 395 400

Val Ile Gly Val Phe Thr Asn Lys Gly Ser Ser Gly Leu Ser Ser Leu

405 410 415

Thr Leu Thr Thr Ser Met Thr Gly Phe Thr Ala Gly Gln Ala Val Val

420 425 430

Asp Val Met Ser Cys Thr Thr Phe Thr Thr Asp Tyr Ser Gly Ser Leu

435 440 445

Ala Val Thr Leu Ser Gly Gly Ile Pro Arg Val Phe Tyr Pro Ser Ala

450 455 460

Arg Leu Ser Gly Ser Gly Ile Cys Gly Ser Asn Gly

465 470 475

<210>37

<211>1431

<212>DNA

<213> Diplodia sp.

<220>

<221> CDS

<222>(1)..(1431)

<400>37

gct act ccc gcc caa tgg cgc tcc aag tcc atc tac cag gtc ctc act 48

Ala Thr Pro Ala Gln Trp Arg Ser Lys Ser Ile Tyr Gln Val Leu Thr

1 5 10 15

gat agg ttt gcc cgc acc gat ggc agc acc agc gca acg tgc aac acg 96

Asp Arg Phe Ala Arg Thr Asp Gly Ser Thr Ser Ala Thr Cys Asn Thr

20 25 30

cag gac aga aag tac tgc ggc gga acg tac cag gga atc atc aac caa 144

Gln Asp Arg Lys Tyr Cys Gly Gly Thr Tyr Gln Gly Ile Ile Asn Gln

35 40 45

ctg gac tac ata cag ggc atg ggc ttc act gcc att tgg atc tcc ccc 192

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Ser Pro

50 55 60

gtc gtc aag aat ctg ccc gag acc act ggc tat gga gag gcc tac cac 240

Val Val Lys Asn Leu Pro Glu Thr Thr Gly Tyr Gly Glu Ala Tyr His

65 70 75 80

ggc tac tgg cag cag gac ctg tac agc ctc aat gag aac ttt gga tct 288

Gly Tyr Trp Gln Gln Asp Leu Tyr Ser Leu Asn Glu Asn Phe Gly Ser

85 90 95

gca gct gat ctc cag gct ctc gct gcc gag ctg cat gac cgc gac atg 336

Ala Ala Asp Leu Gln Ala Leu Ala Ala Glu Leu His Asp Arg Asp Met

100 105 110

tac ttg atg gtg gat att gtc gtc aac cac aat ggc tgg gct ggc tcg 384

Tyr Leu Met Val Asp Ile Val Val Asn His Asn Gly Trp Ala Gly Ser

115 120 125

tca agc tct gtg gac tac agc agg ttc aac ccg ttc aac tcg cag gac 432

Ser Ser Ser Val Asp Tyr Ser Arg Phe Asn Pro Phe Asn Ser Gln Asp

130 135 140

tac tat cat tcg tac tgc acc gtc tcc gac tac aac aac cag gac ctc 480

Tyr Tyr His Ser Tyr Cys Thr Val Ser Asp Tyr Asn Asn Gln Asp Leu

145 150 155 160

gtc gag gat tgc tgg ctt ggt gac aac act gtc cag ctc gtc gac ctc 528

Val Glu Asp Cys Trp Leu Gly Asp Asn Thr Val Gln Leu Val Asp Leu

165 170 175

aag acc gaa gac tcg gcc gtt gcc gat ggc tac aac acc tgg atc tcc 576

Lys Thr Glu Asp Ser Ala Val Ala Asp Gly Tyr Asn Thr Trp Ile Ser

180 185 190

caa ctt gtt gca aac tac tcc att gac ggt ctg cgg atc gac acg gcc 624

Gln Leu Val Ala Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Ala

195 200 205

aag cac gtg gac aag gca ttc tac cct ccc ttt gag gct gcg gct ggt 672

Lys His Val Asp Lys Ala Phe Tyr Pro Pro Phe Glu Ala Ala Ala Gly

210 215 220

gtc ttc tcc acc ggc gaa gtc tac gat ggc aac cca tcc tac act tgt 720

Val Phe Ser Thr Gly Glu Val Tyr Asp Gly Asn Pro Ser Tyr Thr Cys

225 230 235 240

gac tac cag aac tat atg gac agc gtg ctc aac tat ccc gta tac tac 768

Asp Tyr Gln Asn Tyr Met Asp Ser Val Leu Asn Tyr Pro Val Tyr Tyr

245 250 255

ccg cta gtc cgg gcc ttc act tcg acc agt ggc tcc atc tcc gat ctt 816

Pro Leu Val Arg Ala Phe Thr Ser Thr Ser Gly Ser Ile Ser Asp Leu

260 265 270

gtg aac atg gtc agc acg ctc aag agc ggc tgc aag gac acc acg ctt 864

Val Asn Met Val Ser Thr Leu Lys Ser Gly Cys Lys Asp Thr Thr Leu

275 280 285

ctc ggc acc ttc tcc gag aac cac gac atc acg cgc ttc gcc gcc atc 912

Leu Gly Thr Phe Ser Glu Asn His Asp Ile Thr Arg Phe Ala Ala Ile

290 295 300

acg tcc gac ttc tcg cag gcc aag aac gtc atc gcc ttc aac atc ctc 960

Thr Ser Asp Phe Ser Gln Ala Lys Asn Val Ile Ala Phe Asn Ile Leu

305 310 315 320

gcc gac ggc atc cct atc atc tac cag ggc cag gag caa cac tac tcg 1008

Ala Asp Gly Ile Pro Ile Ile Tyr Gln Gly Gln Glu Gln His Tyr Ser

325 330 335

ggc gcc gag gac ccg gac aac cgc gag gcc gtc tgg ctc tcg ggc tac 1056

Gly Ala Glu Asp Pro Asp Asn Arg Glu Ala Val Trp Leu Ser Gly Tyr

340 345 350

aac acg ggc gcc gag ctg tac acc ttc acc gcc gcc gtc aac gcc atc 1104

Asn Thr Gly Ala Glu Leu Tyr Thr Phe Thr Ala Ala Val Asn Ala Ile

355 360 365

cgc aac cgc gcc atc gcc gac gac gcc gac tac ctg acg tac cag aac 1152

Arg Asn Arg Ala Ile Ala Asp Asp Ala Asp Tyr Leu Thr Tyr Gln Asn

370 375 380

tgg gtc atc tac agc gac acg acc acc atc gct atg cgc aag ggc ttc 1200

Trp Val Ile Tyr Ser Asp Thr Thr Thr Ile Ala Met Arg Lys Gly Phe

385 390 395 400

gac ggc tac cag atc atc acc gtc ttg agc aac aag ggc gcc aat ggc 1248

Asp Gly Tyr Gln Ile Ile Thr Val Leu Ser Asn Lys Gly Ala Asn Gly

405 410 415

gat gcg tac acg ctc aat ctg tcc aac acg ggc tgg acg agt gga acc 1296

Asp Ala Tyr Thr Leu Asn Leu Ser Asn Thr Gly Trp Thr Ser Gly Thr

420 425 430

gag gtc gtc gag gtg ctg acg tgc agc aga gtc acg gtg acg agc agc 1344

Glu Val Val Glu Val Leu Thr Cys Ser Arg Val Thr Val Thr Ser Ser

435 440 445

ggg acg gtg acg gta ccc atg tcg aat ggt ctg ccg agg agg gtc tac tac 1392

Gly Thr Val Thr Val Pro Met Ser Asn Gly Leu Pro Arg Val Tyr Tyr

450 455 460

ccg gct gcc cgg ctg agc ggg tcg ggc atc tgt gat cta 1431

Pro Ala Ala Arg Leu Ser Gly Ser Gly Ile Cys Asp Leu

465 470 475

<210>38

<211>477

<212>PRT

<213> Diplodia sp.

<400>38

Ala Thr Pro Ala Gln Trp Arg Ser Lys Ser Ile Tyr Gln Val Leu Thr

1 5 10 15

Asp Arg Phe Ala Arg Thr Asp Gly Ser Thr Ser Ala Thr Cys Asn Thr

20 25 30

Gln Asp Arg Lys Tyr Cys Gly Gly Thr Tyr Gln Gly Ile Ile Asn Gln

35 40 45

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Ser Pro

50 55 60

Val Val Lys Asn Leu Pro Glu Thr Thr Gly Tyr Gly Glu Ala Tyr His

65 70 75 80

Gly Tyr Trp Gln Gln Asp Leu Tyr Ser Leu Asn Glu Asn Phe Gly Ser

85 90 95

Ala Ala Asp Leu Gln Ala Leu Ala Ala Glu Leu His Asp Arg Asp Met

100 105 110

Tyr Leu Met Val Asp Ile Val Val Asn His Asn Gly Trp Ala Gly Ser

115 120 125

Ser Ser Ser Val Asp Tyr Ser Arg Phe Asn Pro Phe Asn Ser Gln Asp

130 135 140

Tyr Tyr His Ser Tyr Cys Thr Val Ser Asp Tyr Asn Asn Gln Asp Leu

145 150 155 160

Val Glu Asp Cys Trp Leu Gly Asp Asn Thr Val Gln Leu Val Asp Leu

165 170 175

Lys Thr Glu Asp Ser Ala Val Ala Asp Gly Tyr Asn Thr Trp Ile Ser

180 185 190

Gln Leu Val Ala Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Ala

195 200 205

Lys His Val Asp Lys Ala Phe Tyr Pro Pro Phe Glu Ala Ala Ala Gly

210 215 220

Val Phe Ser Thr Gly Glu Val Tyr Asp Gly Asn Pro Ser Tyr Thr Cys

225 230 235 240

Asp Tyr Gln Asn Tyr Met Asp Ser Val Leu Asn Tyr Pro Val Tyr Tyr

245 250 255

Pro Leu Val Arg Ala Phe Thr Ser Thr Ser Gly Ser Ile Ser Asp Leu

260 265 270

Val Asn Met Val Ser Thr Leu Lys Ser Gly Cys Lys Asp Thr Thr Leu

275 280 285

Leu Gly Thr Phe Ser Glu Asn His Asp Ile Thr Arg Phe Ala Ala Ile

290 295 300

Thr Ser Asp Phe Ser Gln Ala Lys Asn Val Ile Ala Phe Asn Ile Leu

305 310 315 320

Ala Asp Gly Ile Pro Ile Ile Tyr Gln Gly Gln Glu Gln His Tyr Ser

325 330 335

Gly Ala Glu Asp Pro Asp Asn Arg Glu Ala Val Trp Leu Ser Gly Tyr

340 345 350

Asn Thr Gly Ala Glu Leu Tyr Thr Phe Thr Ala Ala Val Asn Ala Ile

355 360 365

Arg Asn Arg Ala Ile Ala Asp Asp Ala Asp Tyr Leu Thr Tyr Gln Asn

370 375 380

Trp Val Ile Tyr Ser Asp Thr Thr Thr Ile Ala Met Arg Lys Gly Phe

385 390 395 400

Asp Gly Tyr Gln Ile Ile Thr Val Leu Ser Asn Lys Gly Ala Asn Gly

405 410 415

Asp Ala Tyr Thr Leu Asn Leu Ser Asn Thr Gly Trp Thr Ser Gly Thr

420 425 430

Glu Val Val Glu Val Leu Thr Cys Ser Arg Val Thr Val Thr Ser Ser

435 440 445

Gly Thr Val Thr Val Pro Met Ser Asn Gly Leu Pro Arg Val Tyr Tyr

450 455 460

Pro Ala Ala Arg Leu Ser Gly Ser Gly Ile Cys Asp Leu

465 470 475

<210>39

<211>1323

<212>DNA

<213> bacteria of the genus Nectria sp.

<220>

<221> CDS

<222>(1)..(1323)

<400>39

gcc gac acc cag tca tgg aag tct cgc aac atc tat ttt gcc ctg aca 48

Ala Asp Thr Gln Ser Trp Lys Ser Arg Asn Ile Tyr Phe Ala Leu Thr

1 5 10 15

gac cgc atc gcc aag agc agc tcg gac act ggc ggc agt gcc tgt ggc 96

Asp Arg Ile Ala Lys Ser Ser Ser Ser Asp Thr Gly Gly Ser Ala Cys Gly

20 25 30

aat ctt gga aac tac tgt ggt ggc acg ttc cag ggt ctg cag tcc aag 144

Asn Leu Gly Asn Tyr Cys Gly Gly Thr Phe Gln Gly Leu Gln Ser Lys

35 40 45

ctt gac tac atc aag ggc atg ggc ttt gac gcc atc tgg ata aca ccc 192

Leu Asp Tyr Ile Lys Gly Met Gly Phe Asp Ala Ile Trp Ile Thr Pro

50 55 60

gtc gtg gag aac act gat ggt ggc tac cat gga tac tgg gcc aag gac 240

Val Val Glu Asn Thr Asp Gly Gly Tyr His Gly Tyr Trp Ala Lys Asp

65 70 75 80

ctg tac tct gtc aat tcc aag tac gga act gcg gat gac ttg aag agc 288

Leu Tyr Ser Val Asn Ser Lys Tyr Gly Thr Ala Asp Asp Leu Lys Ser

85 90 95

ttg gtc agc gca gcg cat ggc aag ggc atc tac atg atg gtt gac gtt 336

Leu Val Ser Ala Ala His Gly Lys Gly Ile Tyr Met Met Val Asp Val

100 105 110

gtt gcc aac cac atg ggt agt ggc gac atc agc aca tac aac ccc ccg 384

Val Ala Asp His Met Gly Ser Gly Asp Ile Ser Thr Tyr Asn Pro Pro

115 120 125

ccg ctc aac caa gcg agc gcc tac cac ggc tcg tgt gat atc aac tac 432

Pro Leu Asn Gln Ala Ser Ala Tyr His Gly Ser Cys Asp Ile Asn Tyr

130 135 140

gac gac cag aac agc att gag cag tgc agg att tcc ggt ctt ccg gat 480

Asp Asp Gln Asn Ser Ile Glu Gln Cys Arg Ile Ser Gly Leu Pro Asp

145 150 155 160

atc aac acg gag gat aac tca gtg aaa gcg gcc ctg cac gaa tgg gtc 528

Ile Asn Thr Glu Asp Asn Ser Val Lys Ala Ala Leu His Glu Trp Val

165 170 175

gga tgg ctt gtc aag gag tac aac ttt gac ggt gtc cgc atc gac aca 576

Gly Trp Leu Val Lys Glu Tyr Asn Phe Asp Gly Val Arg Ile Asp Thr

180 185 190

gtc aag cat gtg tcg aag agt ttc tgg cct gat ttt gcc tgg tcc tct 624

Val Lys His Val Ser Lys Ser Phe Trp Pro Asp Phe Ala Trp Ser Ser

195 200 205

gga gta tac acc att ggc gag gtc ttc aat ggc gac ccc gat tac cta 672

Gly Val Tyr Thr Ile Gly Glu Val Phe Asn Gly Asp Pro Asp Tyr Leu

210 215 220

gcc gaa tat gac aac ctc atg gga ggt ctc ctc aac tat gcc gtc tac 720

Ala Glu Tyr Asp Asn Leu Met Gly Gly Leu Leu Asn Tyr Ala Val Tyr

225 230 235 240

tac ccc atg aac cgg ttc tac cag cag gag gga tcc tcg aag gac ctt 768

Tyr Pro Met Asn Arg Phe Tyr Gln Gln Glu Gly Ser Ser Lys Asp Leu

245 250 255

gcc agc atg atc gac acg gtt agt gcc aaa ttc tcc gat ccg acg acc 816

Ala Ser Met Ile Asp Thr Val Ser Ala Lys Phe Ser Asp Pro Thr Thr

260 265 270

ctg gga aca ttc ctc gac aac cat gac aac cct cga tgg ctc aac aag 864

Leu Gly Thr Phe Leu Asp Asn His Asp Asn Pro Arg Trp Leu Asn Lys

275 280 285

aag aac gac gtc act ctg ttc aag aac gcc ctg gct ttc gtc atc ctc 912

Lys Asn Asp Val Thr Leu Phe Lys Asn Ala Leu Ala Phe Val Ile Leu

290 295 300

gct cgt ggc att ccc atc gtc tac tac ggt agt gag cag ggc tac ggc 960

Ala Arg Gly Ile Pro Ile Val Tyr Tyr Gly Ser Glu Gln Gly Tyr Gly

305 310 315 320

ggt ggt gct gat ccg cag aac cgg gag gac ctt tgg cga agc ggc ttc 1008

Gly Gly Ala Asp Pro Gln Asn Arg Glu Asp Leu Trp Arg Ser Gly Phe

325 330 335

aac acc aac tct gac ctg tac ggt gcc atc tcg cgc ctc tct gct gcg 1056

Asn Thr Asn Ser Asp Leu Tyr Gly Ala Ile Ser Arg Leu Ser Ala Ala

340 345 350

cga tca gca cat ggt ggc ctc ccc aac aac gac cac gtc cac ctc aac 1104

Arg Ser Ala His Gly Gly Leu Pro Asn Asn Asp His Val His Leu Asn

355 360 365

acc gaa gac gga ata tac gcc tgg agc cga gcg ggc ggc gat ctc gtc 1152

Thr Glu Asp Gly Ile Tyr Ala Trp Ser Arg Ala Gly Gly Asp Leu Val

370 375 380

gtc ttc act tcc aac cgc ggc tcc agc ctc aac ggc gag tac tgc ttc 1200

Val Phe Thr Ser Asn Arg Gly Ser Ser Leu Asn Gly Glu Tyr Cys Phe

385 390 395 400

act act gat cgt tca aat gga tcg tgg aac gat gtt ttt ggc agc ggg 1248

Thr Thr Asp Arg Ser Asn Gly Ser Trp Asn Asp Val Phe Gly Ser Gly

405 410 415

tcc tat act tcg gat ggt aac ggc agg gtc tgt gtc aat gtg aac aat 1296

Ser Tyr Thr Ser Asp Gly Asn Gly Arg Val Cys Val Asn Val Asn Asn

420 425 430

ggc cag ccg gtg gtc ctg agt gct aaa 1323

Gly Gln Pro Val Val Leu Ser Ala Lys

435 440

<210>40

<211>441

<212>PRT

<213> bacteria of the genus Nectria sp.

<400>40

Ala Asp Thr Gln Ser Trp Lys Ser Arg Asn Ile Tyr Phe Ala Leu Thr

1 5 10 15

Asp Arg Ile Ala Lys Ser Ser Ser Ser Asp Thr Gly Gly Ser Ala Cys Gly

20 25 30

Asn Leu Gly Asn Tyr Cys Gly Gly Thr Phe Gln Gly Leu Gln Ser Lys

35 40 45

Leu Asp Tyr Ile Lys Gly Met Gly Phe Asp Ala Ile Trp Ile Thr Pro

50 55 60

Val Val Glu Asn Thr Asp Gly Gly Tyr His Gly Tyr Trp Ala Lys Asp

65 70 75 80

Leu Tyr Ser Val Asn Ser Lys Tyr Gly Thr Ala Asp Asp Leu Lys Ser

85 90 95

Leu Val Ser Ala Ala His Gly Lys Gly Ile Tyr Met Met Val Asp Val

100 105 110

Val Ala Asn His Met Gly Ser Gly Asp Ile Ser Thr Tyr Asn Pro Pro

115 120 125

Pro Leu Asn Gln Ala Ser Ala Tyr His Gly Ser Cys Asp Ile Asn Tyr

130 135 140

Asp Asp Gln Asn Ser Ile Glu Gln Cys Arg Ile Ser Gly Leu Pro Asp

145 150 155 160

Ile Asn Thr Glu Asp Asn Ser Val Lys Ala Ala Leu His Glu Trp Val

165 170 175

Gly Trp Leu Val Lys Glu Tyr Asn Phe Asp Gly Val Arg Ile Asp Thr

180 185 190

Val Lys His Val Ser Lys Ser Phe Trp Pro Asp Phe Ala Trp Ser Ser

195 200 205

Gly Val Tyr Thr Ile Gly Glu Val Phe Asn Gly Asp Pro Asp Tyr Leu

210 215 220

Ala Glu Tyr Asp Asn Leu Met Gly Gly Leu Leu Asn Tyr Ala Val Tyr

225 230 235 240

Tyr Pro Met Asn Arg Phe Tyr Gln Gln Glu Gly Ser Ser Lys Asp Leu

245 250 255

Ala Ser Met Ile Asp Thr Val Ser Ala Lys Phe Ser Asp Pro Thr Thr

260 265 270

Leu Gly Thr Phe Leu Asp Asn His Asp Asn Pro Arg Trp Leu Asn Lys

275 280 285

Lys Asn Asp Val Thr Leu Phe Lys Asn Ala Leu Ala Phe Val Ile Leu

290 295 300

Ala Arg Gly Ile Pro Ile Val Tyr Tyr Gly Ser Glu Gln Gly Tyr Gly

305 310 315 320

Gly Gly Ala Asp Pro Gln Asn Arg Glu Asp Leu Trp Arg Ser Gly Phe

325 330 335

Asn Thr Asn Ser Asp Leu Tyr Gly Ala Ile Ser Arg Leu Ser Ala Ala

340 345 350

Arg Ser Ala His Gly Gly Leu Pro Asn Asn Asp His Val His Leu Asn

355 360 365

Thr Glu Asp Gly Ile Tyr Ala Trp Ser Arg Ala Gly Gly Asp Leu Val

370 375 380

Val Phe Thr Ser Asn Arg Gly Ser Ser Leu Asn Gly Glu Tyr Cys Phe

385 390 395 400

Thr Thr Asp Arg Ser Asn Gly Ser Trp Asn Asp Val Phe Gly Ser Gly

405 410 415

Ser Tyr Thr Ser Asp Gly Asn Gly Arg Val Cys Val Asn Val Asn Asn

420 425 430

Gly Gln Pro Val Val Leu Ser Ala Lys

435 440

<210>41

<211>1347

<212>DNA

<213> Gliocladium sp.

<220>

<221> CDS

<222>(1)..(1347)

<400>41

gcc gac act gcc aca tgg aag tcc cgc aga att tac ttt gcg ctg acg 48

Ala Asp Thr Ala Thr Trp Lys Ser Arg Arg Ile Tyr Phe Ala Leu Thr

1 5 10 15

gac cgc att gcc cgg agc agc acc gac gcc ggt gga ggc tcg tgc agc 96

Asp Arg Ile Ala Arg Ser Ser Thr Asp Ala Gly Gly Gly Ser Cys Ser

20 25 30

gac ctt ggt agc tac tgc ggt ggc acg ttc cag ggc ctg cag gcc aag 144

Asp Leu Gly Ser Tyr Cys Gly Gly Thr Phe Gln Gly Leu Gln Ala Lys

35 40 45

ctc gac tac atc cag ggt ctg ggt ttt gac gct gtc tgg atc acg cca 192

Leu Asp Tyr Ile Gln Gly Leu Gly Phe Asp Ala Val Trp Ile Thr Pro

50 55 60

gtc gtc gcg aac agc gat ggc ggc tac cac ggc tac tgg gcc gag gac 240

Val Val Ala Asn Ser Asp Gly Gly Tyr His Gly Tyr Trp Ala Glu Asp

65 70 75 80

ctc ttc gcc att aac ccc aag tac gga tct gcc gac gac ctg aag agc 288

Leu Phe Ala Ile Asn Pro Lys Tyr Gly Ser Ala Asp Asp Leu Lys Ser

85 90 95

ctc gtc aat gcg agc cac gaa aaa ggc atg ttt gtt atg gtc gac gtc 336

Leu Val Asn Ala Ser His Glu Lys Gly Met Phe Val Met Val Asp Val

100 105 110

gtc gcc aac cat atg ggc cgc gcc aac atc gcc gac gac aag ccc tcg 384

Val Ala Asn His Met Gly Arg Ala Asn Ile Ala Asp Asp Lys Pro Ser

115 120 125

ccc ctc gat cag gag acg tcc tac cac gcg cca tgc acc atc gac tac 432

Pro Leu Asp Gln Glu Thr Ser Tyr His Ala Pro Cys Thr Ile Asp Tyr

130 135 140

tcc aac cag acg agt gtc gag aac tgc cgc atc gcc gcc gat ttg ccc 480

Ser Asn Gln Thr Ser Val Glu Asn Cys Arg Ile Ala Ala Asp Leu Pro

145 150 155 160

gat gtg gac acg cat gac ccg gcc att cgg cag ctc tat cag tcg tgg 528

Asp Val Asp Thr His Asp Pro Ala Ile Arg Gln Leu Tyr Gln Ser Trp

165 170 175

gtg cac tgg ctc gtg tct gag ttc agc ttc gac ggc gtg cgc att gac 576

Val His Trp Leu Val Ser Glu Phe Ser Phe Asp Gly Val Arg Ile Asp

180 185 190

acg gtc aag cac gtc gaa aag gac ttc tgg ccg ccg ttt gct acc gcc 624

Thr Val Lys His Val Glu Lys Asp Phe Trp Pro Pro Phe Ala Thr Ala

195 200 205

gcc ggt gtc tac acc atc ggc gag gtc ttc cat ggc gat ccg gcc tac 672

Ala Gly Val Tyr Thr Ile Gly Glu Val Phe His Gly Asp Pro Ala Tyr

210 215 220

gtc gct agc tac gcg gga ctc atg tcg ggg ctg ctc aac tat gct gtc 720

Val Ala Ser Tyr Ala Gly Leu Met Ser Gly Leu Leu Asn Tyr Ala Val

225 230 235 240

tac ttc ccg ctc acc cgt ttt tac cag cag cgc ggt tcg tct cag gat 768

Tyr Phe Pro Leu Thr Arg Phe Tyr Gln Gln Arg Gly Ser Ser Gln Asp

245 250 255

ctc gtc gat atg cac gat gca gtc agc tcc aag ttc ccc gac ccg gcc 816

Leu Val Asp Met His Asp Ala Val Ser Ser Lys Phe Pro Asp Pro Ala

260 265 270

gcc ctg ggc acc ttt ctc gac aac cac gac aat ccg cgg tgg cta ggc 864

Ala Leu Gly Thr Phe Leu Asp Asn His Asp Asn Pro Arg Trp Leu Gly

275 280 285

cag aac ggc gac acc gtc ctg cta cgc aac gct ttg acg tac gta ctg 912

Gln Asn Gly Asp Thr Val Leu Leu Arg Asn Ala Leu Thr Tyr Val Leu

290 295 300

ctt gcg cgg ggg gtc ccc atc ctg tac tac ggc acc gag cag ggg ttc 960

Leu Ala Arg Gly Val Pro Ile Leu Tyr Tyr Gly Thr Glu Gln Gly Phe

305 310 315 320

tca ggt ggt gcc gac ccg gcc aac cgg gag gac ctc tgg cgc agc ggc 1008

Ser Gly Gly Ala Asp Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Gly

325 330 335

ttc gcc act gac ggg cct ctc tac aag ttc ata gcc acc atg gcg ggt 1056

Phe Ala Thr Asp Gly Pro Leu Tyr Lys Phe Ile Ala Thr Met Ala Gly

340 345 350

gta cgc agg tct gct ggt ggg ctg ccg gat aac gac cat gtg cat ctt 1104

Val Arg Arg Ser Ala Gly Gly Leu Pro Asp Asn Asp His Val His Leu

355 360 365

tac gtt gcg ggt gat gcg tac gcg tgg agc cgc gcc ggc ggt aag gtc 1152

Tyr Val Ala Gly Asp Ala Tyr Ala Trp Ser Arg Ala Gly Gly Lys Val

370 375 380

atc gca ctg acg agc aac ggc ggg agc ggc aag tcg cag cgc tac tgc 1200

Ile Ala Leu Thr Ser Asn Gly Gly Ser Gly Lys Ser Gln Arg Tyr Cys

385 390 395 400

ttc aac tca cag agg cag aac gga gcg tgg aag ggg gcc tta gac ggc 1248

Phe Asn Ser Gln Arg Gln Asn Gly Ala Trp Lys Gly Ala Leu Asp Gly

405 410 415

aag acg tac gcg tcg gat gga aga ggg cag ctt tgt gcg gac gtg acc 1296

Lys Thr Tyr Ala Ser Asp Gly Arg Gly Gln Leu Cys Ala Asp Val Thr

420 425 430

aag ggg gag ccc gtc gtc ctt gtc gct tcc acc gcc atg cca ggg gaa 1344

Lys Gly Glu Pro Val Val Leu Val Ala Ser Thr Ala Met Pro Gly Glu

435 440 445

ttg 1347

Leu

<210>42

<211>449

<212>PRT

<213> Gliocladium sp.

<400>42

Ala Asp Thr Ala Thr Trp Lys Ser Arg Arg Ile Tyr Phe Ala Leu Thr

1 5 10 15

Asp Arg Ile Ala Arg Ser Ser Thr Asp Ala Gly Gly Gly Ser Cys Ser

20 25 30

Asp Leu Gly Ser Tyr Cys Gly Gly Thr Phe Gln Gly Leu Gln Ala Lys

35 40 45

Leu Asp Tyr Ile Gln Gly Leu Gly Phe Asp Ala Val Trp Ile Thr Pro

50 55 60

Val Val Ala Asn Ser Asp Gly Gly Tyr His Gly Tyr Trp Ala Glu Asp

65 70 75 80

Leu Phe Ala Ile Asn Pro Lys Tyr Gly Ser Ala Asp Asp Leu Lys Ser

85 90 95

Leu Val Asn Ala Ser His Glu Lys Gly Met Phe Val Met Val Asp Val

100 105 110

Val Ala Asn His Met Gly Arg Ala Asn Ile Ala Asp Asp Lys Pro Ser

115 120 125

Pro Leu Asp Gln Glu Thr Ser Tyr His Ala Pro Cys Thr Ile Asp Tyr

130 135 140

Ser Asn Gln Thr Ser Val Glu Asn Cys Arg Ile Ala Ala Asp Leu Pro

145 150 155 160

Asp Val Asp Thr His Asp Pro Ala Ile Arg Gln Leu Tyr Gln Ser Trp

165 170 175

Val His Trp Leu Val Ser Glu Phe Ser Phe Asp Gly Val Arg Ile Asp

180 185 190

Thr Val Lys His Val Glu Lys Asp Phe Trp Pro Pro Phe Ala Thr Ala

195 200 205

Ala Gly Val Tyr Thr Ile Gly Glu Val Phe His Gly Asp Pro Ala Tyr

210 215 220

Val Ala Ser Tyr Ala Gly Leu Met Ser Gly Leu Leu Asn Tyr Ala Val

225 230 235 240

Tyr Phe Pro Leu Thr Arg Phe Tyr Gln Gln Arg Gly Ser Ser Gln Asp

245 250 255

Leu Val Asp Met His Asp Ala Val Ser Ser Lys Phe Pro Asp Pro Ala

260 265 270

Ala Leu Gly Thr Phe Leu Asp Asn His Asp Asn Pro Arg Trp Leu Gly

275 280 285

Gln Asn Gly Asp Thr Val Leu Leu Arg Asn Ala Leu Thr Tyr Val Leu

290 295 300

Leu Ala Arg Gly Val Pro Ile Leu Tyr Tyr Gly Thr Glu Gln Gly Phe

305 310 315 320

Ser Gly Gly Ala Asp Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Gly

325 330 335

Phe Ala Thr Asp Gly Pro Leu Tyr Lys Phe Ile Ala Thr Met Ala Gly

340 345 350

Val Arg Arg Ser Ala Gly Gly Leu Pro Asp Asn Asp His Val His Leu

355 360 365

Tyr Val Ala Gly Asp Ala Tyr Ala Trp Ser Arg Ala Gly Gly Lys Val

370 375 380

Ile Ala Leu Thr Ser Asn Gly Gly Ser Gly Lys Ser Gln Arg Tyr Cys

385 390 395 400

Phe Asn Ser Gln Arg Gln Asn Gly Ala Trp Lys Gly Ala Leu Asp Gly

405 410 415

Lys Thr Tyr Ala Ser Asp Gly Arg Gly Gln Leu Cys Ala Asp Val Thr

420 425 430

Lys Gly Glu Pro Val Val Leu Val Ala Ser Thr Ala Met Pro Gly Glu

435 440 445

Leu

<210>43

<211>1317

<212>DNA

<213>Streptomyces thermocyaneoviolaceus

<220>

<221> CDS

<222>(1)..(1317)

<400>43

gct ccc gcc acc gtc gcc cac gcc tcc ccg ccc ggc acc aag gac gtc 48

Ala Pro Ala Thr Val Ala His Ala Ser Pro Pro Gly Thr Lys Asp Val

1 5 10 15

acc gcc gtc ctc ttc gag tgg gac tac gcc tcc gtg gcc aag gag tgc 96

Thr Ala Val Leu Phe Glu Trp Asp Tyr Ala Ser Val Ala Lys Glu Cys

20 25 30

acc agc acc ctc ggc ccg gcc ggc tac ggc tac gtg cag gtc tcc ccg 144

Thr Ser Thr Leu Gly Pro Ala Gly Tyr Gly Tyr Val Gln Val Ser Pro

35 40 45

ccc gcc gag cac atc cag ggc tcc cag tgg tgg acg tcg tac cag ccg 192

Pro Ala Glu His Ile Gln Gly Ser Gln Trp Trp Thr Ser Tyr Gln Pro

50 55 60

gtg agc tac aag atc gcc ggc cgg ctc ggc gac cgt gcc gcc ttc cga 240

Val Ser Tyr Lys Ile Ala Gly Arg Leu Gly Asp Arg Ala Ala Phe Arg

65 70 75 80

tcc atg gtg aac acc tgc cac gcc gcc ggg gtg aag gtg gtc gtc gac 288

Ser Met Val Asn Thr Cys His Ala Ala Gly Val Lys Val Val Val Asp

85 90 95

acg gtg atc aac cac atg tcg gcc ggc agc ggc acc ggc acc gga ggc 336

Thr Val Ile Asn His Met Ser Ala Gly Ser Gly Thr Gly Thr Gly Gly

100 105 110

tcg tcg tac acg aag tac gac tac ccg ggg ctg tac tcg gcc ccg gac 384

Ser Ser Tyr Thr Lys Tyr Asp Tyr Pro Gly Leu Tyr Ser Ala Pro Asp

115 120 125

ttc gac gac tgc acc gcg gag atc acc gac tac cag gac cgc tgg aac 432

Phe Asp Asp Cys Thr Ala Glu Ile Thr Asp Tyr Gln Asp Arg Trp Asn

130 135 140

gtc cag cac tgc gaa ctg gtg ggc ctc gcc gac ctc gac acc ggt gag 480

Val Gln His Cys Glu Leu Val Gly Leu Ala Asp Leu Asp Thr Gly Glu

145 150 155 160

gag tac gtg cga cag acg atc gcc ggc tac atg aac gac ctg ctc tcc 528

Glu Tyr Val Arg Gln Thr Ile Ala Gly Tyr Met Asn Asp Leu Leu Ser

165 170 175

ctc ggc gtc gac ggc ttc cgc atc gac gcg gcc aag cac atc ccc gcc 576

Leu Gly Val Asp Gly Phe Arg Ile Asp Ala Ala Lys His Ile Pro Ala

180 185 190

gag gac ctc gcg aac atc aag tcc cgc ctg agc aac ccg aac gcc tac 624

Glu Asp Leu Ala Asn Ile Lys Ser Arg Leu Ser Asn Pro Asn Ala Tyr

195 200 205

tgg aag cag gag gtc atc tac ggc gcc ggc gaa gcc gtc cag ccc ggc 672

Trp Lys Gln Glu Val Ile Tyr Gly Ala Gly Glu Ala Val Gln Pro Gly

210 215 220

gag tac acc ggc acc ggc gac gtc cag gag ttc cgc tac gcc tac gac 720

Glu Tyr Thr Gly Thr Gly Asp Val Gln Glu Phe Arg Tyr Ala Tyr Asp

225 230 235 240

ctc aag cgg gtc ttc acc cag gag cac ctc gcc tac ctg aag aac tac 768

Leu Lys Arg Val Phe Thr Gln Glu His Leu Ala Tyr Leu Lys Asn Tyr

245 250 255

ggc gag gac tgg ggc tac ctg agc agc acg acg gcc ggg gtc ttc gtc 816

Gly Glu Asp Trp Gly Tyr Leu Ser Ser Thr Thr Ala Gly Val Phe Val

260 265 270

gac aac cac gac acc gag cgc aac ggc tcc acg ctg aac tac aag aac 864

Asp Asn His Asp Thr Glu Arg Asn Gly Ser Thr Leu Asn Tyr Lys Asn

275 280 285

gac gcc acc tac acc ctg gcc aac gtc ttc atg ctg gcc tgg ccc tac 912

Asp Ala Thr Tyr Thr Leu Ala Asn Val Phe Met Leu Ala Trp Pro Tyr

290 295 300

ggc gcc ccc gac atc aat tcc ggc tac gag tgg tcc gac ccg gac gcc 960

Gly Ala Pro Asp Ile Asn Ser Gly Tyr Glu Trp Ser Asp Pro Asp Ala

305 310 315 320

ggc ccg ccc gac ggc ggc cac gtc gac gcc tgc tgg cag aac ggc tgg 1008

Gly Pro Pro Asp Gly Gly His Val Asp Ala Cys Trp Gln Asn Gly Trp

325 330 335

aag tgc cag cac aag tgg ccc gag atc gcc tcc atg gtc gcc ttc cgc 1056

Lys Cys Gln His Lys Trp Pro Glu Ile Ala Ser Met Val Ala Phe Arg

340 345 350

aac gcc acc cgc ggc gag ccg gtc acc gac tgg tgg gac gac ggc gcg 1104

Asn Ala Thr Arg Gly Glu Pro Val Thr Asp Trp Trp Asp Asp Gly Ala

355 360 365

gac gcc atc gcc ttc ggc cgg ggc aag aag ggc ttc gtg gcc atc aac 1152

Asp Ala Ile Ala Phe Gly Arg Gly Ser Lys Gly Phe Val Ala Ile Asn

370 375 380

cac gag tcc gcc acc gtc cag cgc acc tac cag acc tcc ctg ccc gcc 1200

His Glu Ser Ala Thr Val Gln Arg Thr Tyr Gln Thr Ser Leu Pro Ala

385 390 395 400

ggc acc tac tgc gac gtg cag agc aac acc acg gtg acg gtg gac tcc 1248

Gly Thr Tyr Cys Asp Val Gln Ser Asn Thr Thr Val Thr Val Asp Ser

405 410 415

gcc gga cgg ttc acc gcc gcg ctc ggc ccg gac acg gca ctg gcc ctg 1296

Ala Gly Arg Phe Thr Ala Ala Leu Gly Pro Asp Thr Ala Leu Ala Leu

420 425 430

cac acc ggc agg agg agc tgc 1317

His Thr Gly Arg Thr Ser Cys

435

<210>44

<211>439

<212>PRT

<213>Streptomyces thermocyaneoviolaceus

<400>44

Ala Pro Ala Thr Val Ala His Ala Ser Pro Pro Gly Thr Lys Asp Val

1 5 10 15

Thr Ala Val Leu Phe Glu Trp Asp Tyr Ala Ser Val Ala Lys Glu Cys

20 25 30

Thr Ser Thr Leu Gly Pro Ala Gly Tyr Gly Tyr Val Gln Val Ser Pro

35 40 45

Pro Ala Glu His Ile Gln Gly Ser Gln Trp Trp Thr Ser Tyr Gln Pro

50 55 60

Val Ser Tyr Lys Ile Ala Gly Arg Leu Gly Asp Arg Ala Ala Phe Arg

65 70 75 80

Ser Met Val Asn Thr Cys His Ala Ala Gly Val Lys Val Val Val Asp

85 90 95

Thr Val Ile Asn His Met Ser Ala Gly Ser Gly Thr Gly Thr Gly Gly

100 105 110

Ser Ser Tyr Thr Lys Tyr Asp Tyr Pro Gly Leu Tyr Ser Ala Pro Asp

115 120 125

Phe Asp Asp Cys Thr Ala Glu Ile Thr Asp Tyr Gln Asp Arg Trp Asn

130 135 140

Val Gln His Cys Glu Leu Val Gly Leu Ala Asp Leu Asp Thr Gly Glu

145 150 155 160

Glu Tyr Val Arg Gln Thr Ile Ala Gly Tyr Met Asn Asp Leu Leu Ser

165 170 175

Leu Gly Val Asp Gly Phe Arg Ile Asp Ala Ala Lys His Ile Pro Ala

180 185 190

Glu Asp Leu Ala Asn Ile Lys Ser Arg Leu Ser Asn Pro Asn Ala Tyr

195 200 205

Trp Lys Gln Glu Val Ile Tyr Gly Ala Gly Glu Ala Val Gln Pro Gly

210 215 220

Glu Tyr Thr Gly Thr Gly Asp Val Gln Glu Phe Arg Tyr Ala Tyr Asp

225 230 235 240

Leu Lys Arg Val Phe Thr Gln Glu His Leu Ala Tyr Leu Lys Asn Tyr

245 250 255

Gly Glu Asp Trp Gly Tyr Leu Ser Ser Thr Thr Ala Gly Val Phe Val

260 265 270

Asp Asn His Asp Thr Glu Arg Asn Gly Ser Thr Leu Asn Tyr Lys Asn

275 280 285

Asp Ala Thr Tyr Thr Leu Ala Asn Val Phe Met Leu Ala Trp Pro Tyr

290 295 300

Gly Ala Pro Asp Ile Asn Ser Gly Tyr Glu Trp Ser Asp Pro Asp Ala

305 310 315 320

Gly Pro Pro Asp Gly Gly His Val Asp Ala Cys Trp Gln Asn Gly Trp

325 330 335

Lys Cys Gln His Lys Trp Pro Glu Ile Ala Ser Met Val Ala Phe Arg

340 345 350

Asn Ala Thr Arg Gly Glu Pro Val Thr Asp Trp Trp Asp Asp Gly Ala

355 360 365

Asp Ala Ile Ala Phe Gly Arg Gly Ser Lys Gly Phe Val Ala Ile Asn

370 375 380

His Glu Ser Ala Thr Val Gln Arg Thr Tyr Gln Thr Ser Leu Pro Ala

385 390 395 400

Gly Thr Tyr Cys Asp Val Gln Ser Asn Thr Thr Val Thr Val Asp Ser

405 410 415

Ala Gly Arg Phe Thr Ala Ala Leu Gly Pro Asp Thr Ala Leu Ala Leu

420 425 430

His Thr Gly Arg Thr Ser Cys

435

<210>45

<211>18

<212>DNA

<213>Pachykytospora papayracea

<220>

<221> CDS

<222>(1)..(18)

<400>45

ggt aac gcg ggc ccc agc 18

Gly Asn Ala Gly Pro Ser

1 5

<210>46

<211>6

<212>PRT

<213>Pachykytospora papayracea

<400>46

Gly Asn Ala Gly Pro Ser

1 5

<210>47

<211>21

<212>DNA

<213> Trametes cingulata

<220>

<221> CDS

<222>(1)..(21)

<400>47

ggg agt ggc ggt gct ggg act 21

Gly Ser Gly Gly Ala Gly Thr

1 5

<210>48

<211>7

<212>PRT

<213> Trametes cingulata

<400>48

Gly Ser Gly Gly Ala Gly Thr

1 5

<210>49

<211>33

<212>DNA

<213> Leucopaxillus gigantus

<220>

<221> CDS

<222>(1)..(33)

<400>49

ggg ggt ggt tca aac cca ggt ggt gga ggg tcg 33

Gly Gly Gly Ser Asn Pro Gly Gly Gly Gly Ser

1 5 10

<210>50

<211>11

<212>PRT

<213> Leucopaxillus gigantus

<400>50

Gly Gly Gly Ser Asn Pro Gly Gly Gly Gly Ser

1 5 10

<210>51

<211>801

<212>DNA

<213> Trichophaea saccata

<220>

<221> CDS

<222>(1)..(801)

<400>51

tcg cca gtt cat cag aac acc aaa cga tct acc caa gtg tcg ttg atc 48

Ser Pro Val His Gln Asn Thr Lys Arg Ser Thr Gln Val Ser Leu Ile

1 5 10 15

agc tat acg ttt tct aac aat att ctc tct gga tcc atc agc att caa 96

Ser Tyr Thr Phe Ser Asn Asn Ile Leu Ser Gly Ser Ile Ser Ile Gln

20 25 30

aac att gct tac gcc aaa acg gtc agc gtt acc tat gcc att ggg agc 144

Asn Ile Ala Tyr Ala Lys Thr Val Ser Val Thr Tyr Ala Ile Gly Ser

35 40 45

tct tgg agc tcc tct cag gtg ata agc gct gcc tac tcc aca ggt cct 192

Ser Trp Ser Ser Set Gln Val Ile Ser Ala Ala Tyr Ser Thr Gly Pro

50 55 60

gat agc acc ggt tat gaa gtc tgg acg ttt agc ggc aca gca acg ggg 240

Asp Ser Thr Gly Tyr Glu Val Trp Thr Phe Ser Gly Thr Ala Thr Gly

65 70 75 80

gca act cag ttc tac att gcg tat act gtc tca ggg acc acc tac tac 288

Ala Thr Gln Phe Tyr Ile Ala Tyr Thr Val Ser Gly Thr Thr Tyr Tyr

85 90 95

gat cct gga aat ggc atc aat tac acg atc ggc acg ggt tcg tcc act 336

Asp Pro Gly Asn Gly Ile Asn Tyr Thr Ile Gly Thr Gly Ser Ser Thr

100 105 110

act tcc agc aca tct gcc act tcg aca acc aaa agt tcc acc act tcc 384

Thr Ser Ser Thr Ser Ala Thr Ser Thr Thr Lys Ser Ser Thr Thr Ser

115 120 125

acg agc act gcg act agc aca agc gtg gcg acc agc agt ctc cct gct 432

Thr Ser Thr Ala Thr Ser Thr Ser Val Ala Thr Ser Ser Leu Pro Ala

130 135 140

atc att tca tcc agt att cct tct gag gcg gca gcc acc gcg ctt tct 480

Ile Ile Ser Ser Ser Ile Pro Ser Glu Ala Ala Ala Thr Ala Leu Ser

145 150 155 160

gga tgc aat act tgg gat ggt ttt gac aac tgc caa act agt ggc gtg 528

Gly Cys Asn Thr Trp Asp Gly Phe Asp Asn Cys Gln Thr Ser Gly Val

165 170 175

tac gac ttt gtg gcc agt gcc gaa aac cgc aga tgg cag acg ccc ccg 576

Tyr Asp Phe Val Ala Ser Ala Glu Asn Arg Arg Trp Gln Thr Pro Pro

180 185 190

gac ggc gat cct gcc tat gtc aat acg ttc caa gac tac cga gat ctc 624

Asp Gly Asp Pro Ala Tyr Val Asn Thr Phe Gln Asp Tyr Arg Asp Leu

195 200 205

att ggc tac gcc gat atc cag tac agc cct tca cga acc tcc gcc gtt 672

Ile Gly Tyr Ala Asp Ile Gln Tyr Ser Pro Ser Arg Thr Ser Ala Val

210 215 220

gtg act gtc aat gct gct tcg cgg acc ggc gag act ttg acc tac aaa 720

Val Thr Val Asn Ala Ala Ser Arg Thr Gly Glu Thr Leu Thr Tyr Lys

225 230 235 240

ttt ggg gga att act cag acg tct aac gcg tac acc gtg agc agc tcg 768

Phe Gly Gly Ile Thr Gln Thr Ser Asn Ala Tyr Thr Val Ser Ser Ser

245 250 255

ttt atc gga acc ctg gca atc aca gtc acc agt 801

Phe Ile Gly Thr Leu Ala Ile Thr Val Thr Ser

260 265

<210>52

<211>267

<212>PRT

<213> Trichophaea saccata

<400>52

Ser Pro Val His Gln Asn Thr Lys Arg Ser Thr Gln Val Ser Leu Ile

1 5 10 15

Ser Tyr Thr Phe Ser Asn Asn Ile Leu Ser Gly Ser Ile Ser Ile Gln

20 25 30

Asn Ile Ala Tyr Ala Lys Thr Val Ser Val Thr Tyr Ala Ile Gly Ser

35 40 45

Ser Trp Ser Ser Ser Ser Gln Val Ile Ser Ala Ala Tyr Ser Thr Gly Pro

50 55 60

Asp Ser Thr Gly Tyr Glu Val Trp Thr Phe Ser Gly Thr Ala Thr Gly

65 70 75 80

Ala Thr Gln Phe Tyr Ile Ala Tyr Thr Val Ser Gly Thr Thr Tyr Tyr

85 90 95

Asp Pro Gly Asn Gly Ile Asn Tyr Thr Ile Gly Thr Gly Ser Ser Thr

100 105 110

Thr Ser Ser Thr Ser Ala Thr Ser Thr Thr Lys Ser Ser Thr Thr Ser

115 120 125

Thr Ser Thr Ala Thr Ser Thr Ser Val Ala Thr Ser Ser Leu Pro Ala

130 135 140

Ile Ile Ser Ser Ser Ile Pro Ser Glu Ala Ala Ala Thr Ala Leu Ser

145 150 155 160

Gly Cys Ash Thr Trp Asp Gly Phe Asp Asn Cys Gln Thr Ser Gly Val

165 170 175

Tyr Asp Phe Val Ala Ser Ala Glu Asn Arg Arg Trp Gln Thr Pro Pro

180 185 190

Asp Gly Asp Pro Ala Tyr Val Asn Thr Phe Gln Asp Tyr Arg Asp Leu

195 200 205

Ile Gly Tyr Ala Asp Ile Gln Tyr Ser Pro Ser Arg Thr Ser Ala Val

210 215 220

Val Thr Val Asn Ala Ala Ser Arg Thr Gly Glu Thr Leu Thr Tyr Lys

225 230 235 240

Phe Gly Gly Ile Thr Gln Thr Ser Asn Ala Tyr Thr Val Ser Ser Ser

245 250 255

Phe Ile Gly Thr Leu Ala Ile Thr Val Thr Ser

260 265

<210>53

<211>75

<212>DNA

<213> Subulispora provurvata

<220>

<221> CDS

<222>(1)..(75)

<400>53

gga ggc agc ggt acc act acc acg acc act acc agc act gca ggc aca 48

Gly Gly Ser Gly Thr Thr Thr Thr Thr Thr Thr Thr Thr Ser Thr Ala Gly Thr

1 5 10 15

tcg cca act tcg aca gcg tgc tcc tcg 75

Ser Pro Thr Ser Thr Ala Cys Ser Ser

20 25

<210>54

<211>25

<212>PRT

<213> Subulispora provurvata

<400>54

Gly Gly Ser Gly Thr Thr Thr Thr Thr Thr Thr Thr Thr Ser Thr Ala Gly Thr

1 5 10 15

Ser Pro Thr Ser Thr Ala Cys Ser Ser

20 25

<210>55

<211>45

<212>DNA

<213>Valsaria rubricosa

<220>

<221> CDS

<222>(1)..(45)

<400>55

acg acc acc aag ag acg tcc acc tcg acc gcc tcc tgc gcc gcc acc 45

Thr Thr Thr Lys Thr Ser Thr Ser Ser Thr Ala Ser Cys Ala Ala Thr

1 5 10 15

<210>56

<211>15

<212>PRT

<213>Valsaria rubricosa

<400>56

Thr Thr Thr Lys Thr Ser Thr Ser Ser Thr Ala Ser Cys Ala Ala Thr

1 5 10 15

<210>57

<211>78

<212>DNA

<213>Acremonium sp.

<220>

<221> CDS

<222>(1)..(78)

<400>57

acc agc aca gcg ctg ccg acg tca agc ttg act gca gca tca gcc acg 48

Thr Ser Thr Ala Leu Pro Thr Ser Ser Leu Thr Ala Ala Ser Ala Thr

1 5 10 15

acg act gcc tca gcc tgc tcc ttg tcg gcg 78

Thr Thr Ala Ser Ala Cys Ser Leu Ser Ala

20 25

<210>58

<211>26

<212>PRT

<213>Acremonium sp.

<400>58

Thr Ser Thr Ala Leu Pro Thr Ser Ser Leu Thr Ala Ala Ser Ala Thr

1 5 10 15

Thr Thr Ala Ser Ala Cys Ser Leu Ser Ala

20 25

<210>59

<211>45

<212>DNA

<213>Meripilus giganteus

<220>

<221> CDS

<222>(1)..(45)

<400>59

gcc acg ccc acc tcc gcc cct agt act aca cca acc agc ggc act 45

Ala Thr Pro Thr Ser Ala Pro Ser Thr Thr Pro Thr Ser Gly Thr

1 5 10 15

<210>60

<211>15

<212>PRT

<213>Meripilus giganteus

<400>60

Ala Thr Pro Thr Ser Ala Pro Ser Thr Thr Pro Thr Ser Gly Thr

1 5 10 15

<210>61

<211>9

<212>DNA

<213>Bacillus flavothermus

<220>

<221> CDS

<222>(1)..(9)

<400>61

aac gcc aca 9

Asn Ala Thr

1

<210>62

<211>3

<212>PRT

<213>Bacillus flavothermus

<220>

<221> PEPTIDE

<222>(1)..(3)

<400>62

Asn Ala Thr

1

<210>63

<211>186

<212>DNA

<213>Bacillus flavothermus

<220>

<221> CDS

<222>(1)..(186)

<400>63

act gag aag ttg gca ggt agc aag atc tgt agt ggc agt gga aat acc 48

Thr Glu Lys Leu Ala Gly Ser Lys Ile Cys Ser Gly Ser Gly Asn Thr

1 5 10 15

aca aca acg act acc gcg gct act agc acc agt aaa gcc act aca tca 96

Thr Thr Thr Thr Thr Ala Ala Thr Ser Thr Ser Lys Ala Thr Thr Ser

20 25 30

agt tcc agc tct tcg gcg gct gca aca act agt tca tct tgt act gct 144

Ser Ser Ser Ser Ser Ser Ala Ala Ala Thr Thr Ser Ser Ser Cys Thr Ala

35 40 45

aca tct act acg ctg cct ata aca ttt gaa gag ctc gta acg 186

Thr Scr Thr Thr Leu Pro Ile Thr Phe Glu Glu Leu Val Thr

50 55 60

<210>64

<211>62

<212>PRT

<213>Bacillus flavothermus

<400>64

Thr Glu Lys Leu Ala Gly Ser Lys Ile Cys Ser Gly Ser Gly Asn Thr

1 5 10 15

Thr Thr Thr Thr Thr Ala Ala Thr Ser Thr Ser Lys Ala Thr Thr Ser

20 25 30

Ser Ser Ser Ser Ser Ser Ala Ala Ala Thr Thr Ser Ser Ser Cys Thr Ala

35 40 45

Thr Ser Thr Thr Leu Pro Ile Thr Phe Glu Glu Leu Val Thr

50 55 60

<210>65

<211>105

<212>DNA

<213>Bacillus flavothermus

<220>

<221> CDS

<222>(1)..(105)

<400>65

act gag aag ttg gca ggt agc aag atc tgt agt aca tac act acg gcc 48

Thr Glu Lys Leu Ala Gly Ser Lys Ile Cys Ser Thr Tyr Thr Thr Ala

1 5 10 15

tca cca cct ccg gga ggt tgt tct gcg gga act gta gtt ttc gat gtg 96

Ser Pro Pro Pro Gly Gly Cys Ser Ala Gly Thr Val Val Phe Asp Val

20 25 30

tat gtc caa 105

Tyr Val Gln

35

<210>66

<211>35

<212>PRT

<213>Bacillus flavothermus

<400>66

Thr Glu Lys Leu Ala Gly Ser Lys Ile Cys Ser Thr Tyr Thr Thr Ala

1 5 10 15

Ser Pro Pro Pro Gly Gly Cys Ser Ala Gly Thr Val Val Phe Asp Val

20 25 30

Tyr Val Gln

35

<210>67

<211>33

<212>DNA

<213> Athelia rolfsii

<220>

<221> CDS

<222>(1)..(33)

<400>67

ggt gct aca agc ccg ggt ggc tcc tcg ggt agt 33

Gly Ala Thr Ser Pro Gly Gly Ser Ser Gly Ser

1 5 10

<210>68

<211>11

<212>PRT

<213> Athelia rolfsii

<400>68

Gly Ala Thr Ser Pro Gly Gly Ser Ser Gly Ser

1 5 10

<210>69

<211>93

<212>DNA

<213>Aspergillus kawachii

<220>

<221> CDS

<222>(1)..(93)

<400>69

aca acc acg acc aca act gct gct gct act agt aca tcc aaa gcc acc 48

Thr Thr Thr Thr Thr Thr Ala Ala Ala Thr Ser Thr Ser Lys Ala Thr

1 5 10 15

acc tcc tct tct tct tct tct gct gct gct act act tct tca tca 93

Thr Ser Ser Ser Ser Ser Ser Ser Ala Ala Ala Thr Thr Ser Ser Ser Ser

20 25 30

<210>70

<211>31

<212>PRT

<213>Aspergillus kawachii

<400>70

Thr Thr Thr Thr Thr Thr Ala Ala Ala Thr Ser Thr Ser Lys Ala Thr

1 5 10 15

Thr Ser Ser Ser Ser Ser Ser Ser Ala Ala Ala Thr Thr Ser Ser Ser Ser

20 25 30

<210>71

<211>111

<212>DNA

<213> Aspergillus niger

<220>

<221> CDS

<222>(1)..(111)

<400>71

act ggc ggc acc act acg acg gct acc ccc act gga tcc ggc agc gtg 48

Thr Gly Gly Thr Thr Thr Thr Ala Thr Pro Thr Gly Ser Gly Ser Val

1 5 10 15

acc tcg acc agc aag acc acc gcg act gct ag aag acc agc acc agt 96

Thr Ser Thr Ser Lys Thr Thr Ala Thr Ala Ser Lys Thr Ser Thr Ser

20 25 30

acg tca tca acc tcc 111

Thr Ser Ser Thr Ser

35

<210>72

<211>37

<212>PRT

<213> Aspergillus niger

<400>72

Thr Gly Gly Thr Thr Thr Thr Ala Thr Pro Thr Gly Ser Gly Ser Val

1 5 10 15

Thr Ser Thr Ser Lys Thr Thr Ala Thr Ala Ser Lys Thr Ser Thr Ser

20 25 30

Thr Ser Ser Thr Ser

35

<210>73

<211>96

<212>DNA

<213> Coniochaeta sp.

<220>

<221> CDS

<222>(1)..(96)

<400>73

acc acg aca aca gct acg acg aag ag ag agc acg acg ctg acc acg tcg 48

Thr Thr Thr Thr Ala Thr Thr Lys Thr Ser Thr Thr Leu Thr Thr Ser

1 5 10 15

acg aca aca acc tcc aca aag aca agt agt tct tgc acc gcc acc gcg 96

Thr Thr Thr Thr Ser Thr Lys Thr Ser Ser Ser Ser Cys Thr Ala Thr Ala

20 25 30

<210>74

<211>32

<212>PRT

<213> Coniochaeta sp.

<400>74

Thr Thr Thr Thr Ala Thr Thr Lys Thr Ser Thr Thr Leu Thr Thr Ser

1 5 10 15

Thr Thr Thr Thr Ser Thr Lys Thr Ser Ser Ser Ser Cys Thr Ala Thr Ala

20 25 30

<210>75

<211>285

<212>DNA

<213>Pachykytospora papayracea

<220>

<221> CDS

<222>(1)..(285)

<400>75

gtg aag gtg acg ttc aac gtc cag gct acg act acc ttc ggc gag aac 48

Val Lys Val Thr Phe Asn Val Gln Ala Thr Thr Thr Phe Gly Glu Asn

1 5 10 15

atc tac atc acc ggt aac acc gct gcg ctc cag aac tgg tcg ccc gat 96

Ile Tyr Ile Thr Gly Asn Thr Ala Ala Leu Gln Asn Trp Ser Pro Asp

20 25 30

aac gcg ctc ctc ctc tct gct gac aag tac ccc acc tgg agc atc acg 144

Asn Ala Leu Leu Leu Ser Ala Asp Lys Tyr Pro Thr Trp Ser Ile Thr

35 40 45

ctc gac ctc ccc gcg aac acc gtc gtc gag tac aaa tac atc cgc aag 192

Leu Asp Leu Pro Ala Asn Thr Val Val Glu Tyr Lys Tyr Ile Arg Lys

50 55 60

ttc aac ggc cag gtc acc tgg gaa tcg gac ccc aac aac tcg atc acg 240

Phe Asn Gly Gln Val Thr Trp Glu Ser Asp Pro Asn Asn Ser Ile Thr

65 70 75 80

acg ccc gcc gac ggt acc ttc acc cag aac gac acc tgg cgg tga 285

Thr Pro Ala Asp Gly Thr Phe Thr Gln Asn Asp Thr Trp Arg

85 90

<210>76

<211>94

<212>PRT

<213>Pachykytospora papayracea

<400>76

Val Lys Val Thr Phe Asn Val Gln Ala Thr Thr Thr Phe Gly Glu Asn

1 5 10 15

Ile Tyr Ile Thr Gly Asn Thr Ala Ala Leu Gln Asn Trp Ser Pro Asp

20 25 30

Asn Ala Leu Leu Leu Ser Ala Asp Lys Tyr Pro Thr Trp Ser Ile Thr

35 40 45

Leu Asp Leu Pro Ala Asn Thr Val Val Glu Tyr Lys Tyr Ile Arg Lys

50 55 60

Phe Asn Gly Gln Val Thr Trp Glu Ser Asp Pro Asn Asn Ser Ile Thr

65 70 75 80

Thr Pro Ala Asp Gly Thr Phe Thr Gln Asn Asp Thr Trp Arg

85 90

<210>77

<211>285

<212>DNA

<213> Trametes cingulata

<220>

<221> CDS

<222>(1)..(285)

<400>77

gtg gcc gtc acc ttc aac gtg cag gcg acc acc gtg ttc ggc gag aac 48

Val Ala Val Thr Phe Asn Val Gln Ala Thr Thr Val Phe Gly Glu Asn

1 5 10 15

att tac atc aca ggc tcg gtc ccc gct ctc cag aac tgg tcg ccc gac 96

Ile Tyr Ile Thr Gly Ser Val Pro Ala Leu Gln Asn Trp Ser Pro Asp

20 25 30

aac gcg ctc atc ctc tca gcg gcc aac tac ccc act tgg agc atc acc 144

Asn Ala Leu Ile Leu Ser Ala Ala Asn Tyr Pro Thr Trp Ser Ile Thr

35 40 45

gtg aac ctg ccg gcg agc acg acg atc gag tac aag tac att cgc aag 192

Val Asn Leu Pro Ala Ser Thr Thr Ile Glu Tyr Lys Tyr Ile Arg Lys

50 55 60

ttc aac ggc gcg gtc acc tgg gag tcc gac ccg aac aac tcg atc acg 240

Phe Asn Gly Ala Val Thr Trp Glu Ser Asp Pro Asn Asn Ser Ile Thr

65 70 75 80

acg ccc gcg agc ggc acg ttc acc cag aac gac acc tgg cgg tag 285

Thr Pro Ala Ser Gly Thr Phe Thr Gln Asn Asp Thr Trp Arg

85 90

<210>78

<211>94

<212>PRT

<213> Trametes cingulata

<400>78

Val Ala Val Thr Phe Asn Val Gln Ala Thr Thr Val Phe Gly Glu Asn

1 5 10 15

Ile Tyr Ile Thr Gly Ser Val Pro Ala Leu Gln Asn Trp Ser Pro Asp

20 25 30

Asn Ala Leu Ile Leu Ser Ala Ala Asn Tyr Pro Thr Trp Ser Ile Thr

35 40 45

Val Asn Leu Pro Ala Ser Thr Thr Ile Glu Tyr Lys Tyr Ile Arg Lys

50 55 60

Phe Asn Gly Ala Val Thr Trp Glu Ser Asp Pro Asn Asn Ser Ile Thr

65 70 75 80

Thr Pro Ala Ser Gly Thr Phe Thr Gln Asn Asp Thr Trp Arg

85 90

<210>79

<211>285

<212>DNA

<213> Leucopaxillus gigantus

<220>

<221> CDS

<222>(1)..(285)

<400>79

gtc tct gtt acg ttc aat gtt caa gct aca acc acc ttt ggt gaa aac 48

Val Ser Val Thr Phe Asn Val Gln Ala Thr Thr Thr Phe Gly Glu Asn

1 5 10 15

att ttt ttg acc ggc tcg atc aac gag tta gct aac tgg tct cct gat 96

Ile Phe Leu Thr Gly Ser Ile Asn Glu Leu Ala Asn Trp Ser Pro Asp

20 25 30

aat gct ctc gcc ctc tct gcg gcc aat tat ccc acc tgg agc agt acc 144

Asn Ala Leu Ala Leu Ser Ala Ala Asn Tyr Pro Thr Trp Ser Ser Thr

35 40 45

gtc aac gtt ccc gca agc act acg atc caa tac aag ttt atc cgt aaa 192

Val Asn Val Pro Ala Ser Thr Thr Ile Gln Tyr Lys Phe Ile Arg Lys

50 55 60

ttc aac gga gcc atc acc tgg gag tcc gac ccg aat agg cag atc aca 240

Phe Asn Gly Ala Ile Thr Trp Glu Ser Asp Pro Asn Arg Gln Ile Thr

65 70 75 80

acg ccg tct tcg gga agt ttt gtc cag aat gac tcg tgg aag tag 285

Thr Pro Ser Ser Gly Ser Phe Val Gln Asn Asp Ser Trp Lys

85 90

<210>80

<211>94

<212>PRT

<213> Leucopaxillus gigantus

<400>80

Val Ser Val Thr Phe Asn Val Gln Ala Thr Thr Thr Phe Gly Glu Asn

1 5 10 15

Ile Phe Leu Thr Gly Ser Ile Asn Glu Leu Ala Asn Trp Ser Pro Asp

20 25 30

Asn Ala Leu Ala Leu Ser Ala Ala Asn Tyr Pro Thr Trp Ser Ser Thr

35 40 45

Val Asn Val Pro Ala Ser Thr Thr Ile Gln Tyr Lys Phe Ile Arg Lys

50 55 60

Phe Asn Gly Ala Ile Thr Trp Glu Ser Asp Pro Asn Arg Gln Ile Thr

65 70 75 80

Thr Pro Ser Ser Gly Ser Phe Val Gln Asn Asp Ser Trp Lys

85 90

<210>81

<211>306

<212>DNA

<213>Subulispora provurvata

<220>

<221> CDS

<222>(1)..(306)

<400>81

gtc ccc gta acg ttc cgc gaa acg gtc aca act acg gta gga cag aca 48

Val Pro Val Thr Phe Arg Glu Thr Val Thr Thr Thr Val Gly Gln Thr

1 5 10 15

atc aag ata tct ggc gac gtc tcc gcc ctt gga aac tgg gat acg gac 96

Ile Lys Ile Ser Gly Asp Val Ser Ala Leu Gly Asn Trp Asp Thr Asp

20 25 30

gac gcg gtg gcc ctg agc gcc gcg agc tac acg tcc agc aac ccc gtg 144

Asp Ala Val Ala Leu Ser Ala Ala Ser Tyr Thr Ser Ser Asn Pro Val

35 40 45

tgg gac gtg acc gtc agc ttc gcc ccc ggc acc gtc atc gag tac aag 192

Trp Asp Val Thr Val Ser Phe Ala Pro Gly Thr Val Ile Glu Tyr Lys

50 55 60

tac atc aac gtg gcg agc ggc ggc gcc gtg acc tgg gag gcc gac ccg 240

Tyr Ile Asn Val Ala Ser Gly Gly Ala Val Thr Trp Glu Ala Asp Pro

65 70 75 80

aac cac acc tac acg gtg cct tcg tcc tgc gcc acc gcc gtg gtc tcc 288

Asn His Thr Tyr Thr Val Pro Ser Ser Cys Ala Thr Ala Val Val Ser

85 90 95

aac acc tgg cag acg tga 306

Asn Thr Trp Gln Thr

100

<210>82

<211>101

<212>PRT

<213> Subulispora provurvata

<400>82

Val Pro Val Thr Phe Arg Glu Thr Val Thr Thr Thr Val Gly Gln Thr

1 5 10 15

Ile Lys Ile Ser Gly Asp Val Ser Ala Leu Gly Asn Trp Asp Thr Asp

20 25 30

Asp Ala Val Ala Leu Ser Ala Ala Ser Tyr Thr Ser Ser Asn Pro Val

35 40 45

Trp Asp Val Thr Val Ser Phe Ala Pro Gly Thr Val Ile Glu Tyr Lys

50 55 60

Tyr Ile Asn Val Ala Ser Gly Gly Ala Val Thr Trp Glu Ala Asp Pro

65 70 75 80

Asn His Thr Tyr Thr Val Pro Ser Ser Cys Ala Thr Ala Val Val Ser

85 90 95

Asn Thr Trp Gln Thr

100

<210>83

<211>303

<212>DNA

<213>Valsaria rubricosa

<220>

<221> CDS

<222>(1)..(303)

<400>83

gtc gcc gtc acc ttc aac gag ctc gtc acc acg aac tac ggc gac acc 48

Val Ala Val Thr Phe Asn Glu Leu Val Thr Thr Asn Tyr Gly Asp Thr

1 5 10 15

atc cgc ctg acg ggc tcc atc tcc cag ctc agc agc tgg agc gca acc 96

Ile Arg Leu Thr Gly Ser Ile Ser Gln Leu Ser Ser Trp Ser Ala Thr

20 25 30

tcc ggg ctg gcc ctg agc gcg tcc gcg tac acg tcc agc aac ccg ctc 144

Ser Gly Leu Ala Leu Ser Ala Ser Ala Tyr Thr Ser Ser Asn Pro Leu

35 40 45

tgg agc gtg acg gtc agc ctg ccg gcc ggc acg tcg ttc gag tac aag 192

Trp Ser Val Thr Val Ser Leu Pro Ala Gly Thr Ser Phe Glu Tyr Lys

50 55 60

ttc gtc cgc atc acg agc gac ggc acc gtg acc tgg gaa tcg gac ccg 240

Phe Val Arg Ile Thr Ser Asp Gly Thr Val Thr Trp Glu Ser Asp Pro

65 70 75 80

aac cgc agc tac acc gtc ccg acg tgc gcg agc acc gcg acg atc agc 288

Asn Arg Ser Tyr Thr Val Pro Thr Cys Ala Ser Thr Ala Thr Ile Ser

85 90 95

aat acc tgg cgg tga 303

Asn Thr Trp Arg

100

<210>84

<211>100

<212>PRT

<213>Valsaria rubricosa

<400>84

Val Ala Val Thr Phe Asn Glu Leu Val Thr Thr Asn Tyr Gly Asp Thr

1 5 10 15

Ile Arg Leu Thr Gly Ser Ile Ser Gln Leu Ser Ser Trp Ser Ala Thr

20 25 30

Ser Gly Leu Ala Leu Ser Ala Ser Ala Tyr Thr Ser Ser Asn Pro Leu

35 40 45

Trp Ser Val Thr Val Ser Leu Pro Ala Gly Thr Ser Phe Glu Tyr Lys

50 55 60

Phe Val Arg Ile Thr Ser Asp Gly Thr Val Thr Trp Glu Ser Asp Pro

65 70 75 80

Asn Arg Ser Tyr Thr Val Pro Thr Cys Ala Ser Thr Ala Thr Ile Ser

85 90 95

Asn Thr Trp Arg

100

<210>85

<211>294

<212>DNA

<213>Acremonium sp.

<220>

<221> CDS

<222>(1)..(294)

<400>85

gtg aac atc acc ttc aac gag ctc gtc acc acg gtg tgg ggg gac acg 48

Val Asn Ile Thr Phe Asn Glu Leu Val Thr Thr Val Trp Gly Asp Thr

1 5 10 15

atc aag ctg gcc ggc aac ata tcc gct ctc ggc agc tgg agc cca agc 96

Ile Lys Leu Ala Gly Asn Ile Ser Ala Leu Gly Ser Trp Ser Pro Ser

20 25 30

agc gcc ttg aca ctg agc gca tcg cag tat tca caa agc aat ccg ctc 144

Ser Ala Leu Thr Leu Ser Ala Ser Gln Tyr Ser Gln Ser Asn Pro Leu

35 40 45

tgg tcg gtc tca acc ctg ctc ggt cca gga acg gtg atc gag tac aag 192

Trp Ser Val Ser Thr Leu Leu Gly Pro Gly Thr Val Ile Glu Tyr Lys

50 55 60

ttt atc aag gtc agc gcc tcc ggg act gta acg tgg gag tca gac ccg 240

Phe Ile Lys Val Ser Ala Ser Gly Thr Val Thr Trp Glu Ser Asp Pro

65 70 75 80

aac cgc gtc tac act gtg ccc tgc gca act gcg acg gtc agt agc act 288

Asn Arg Val Tyr Thr Val Pro Cys Ala Thr Ala Thr Val Ser Ser Thr

85 90 95

tgg cga 294

Trp Arg

<210>86

<211>98

<212>PRT

<213>Acremonium sp.

<400>86

Val Ash Ile Thr Phe Asn Glu Leu Val Thr Thr Val Trp Gly Asp Thr

1 5 10 15

Ile Lys Leu Ala Gly Asn Ile Ser Ala Leu Gly Ser Trp Ser Pro Ser

20 25 30

Ser Ala Leu Thr Leu Ser Ala Ser Gln Tyr Ser Gln Ser Asn Pro Leu

35 40 45

Trp Ser Val Ser Thr Leu Leu Gly Pro Gly Thr Val Ile Glu Tyr Lys

50 55 60

Phe Ile Lys Val Ser Ala Ser Gly Thr Val Thr Trp Glu Ser Asp Pro

65 70 75 80

Asn Arg Val Tyr Thr Val Pro Cys Ala Thr Ala Thr Val Ser Ser Thr

85 90 95

Trp Arg

<210>87

<211>285

<212>DNA

<213>Meripilus giganteus

<220>

<221> CDS

<222>(1)..(285)

<400>87

gtc agc atg acc ttc gct gag cag gcg acg acc acc ttc ggc gag aac 48

Val Ser Met Thr Phe Ala Glu Gln Ala Thr Thr Thr Phe Gly Glu Asn

1 5 10 15

atc ttc ctc gtc ggc agt att tcg cag ctc ggg aac tgg aac cca gcc 96

Ile Phe Leu Val Gly Ser Ile Ser Gln Leu Gly Asn Trp Asn Pro Ala

20 25 30

agc gcg atc gcc ctg tcc tct gcg gcg tac cct acg tgg tct gtg tct 144

Ser Ala Ile Ala Leu Ser Ser Ala Ala Tyr Pro Thr Trp Ser Val Ser

35 40 45

gtg aac att ccc gct gga acg acc ttc cag tac aag ttc atc cgc aag 192

Val Asn Ile Pro Ala Gly Thr Thr Phe Gln Tyr Lys Phe Ile Arg Lys

50 55 60

gag acg gac ggt agc gtc gtc tgg gag tcg gac ccc aac cgc cag gct 240

Glu Thr Asp Gly Ser Val Val Trp Glu Ser Asp Pro Asn Arg Gln Ala

65 70 75 80

acc gcg ccc gcg tcc ggt acc acc acc acg ctc acg tcc agc tgg cgg 285

Thr Ala Pro Ala Ser Gly Thr Thr Thr Leu Thr Ser Ser Trp Arg

85 90 95

<210>88

<211>95

<212>PRT

<213>Meripilus giganteus

<400>88

Val Ser Met Thr Phe Ala Glu Gln Ala Thr Thr Thr Phe Gly Glu Asn

1 5 10 15

Ile Phe Leu Val Gly Ser Ile Ser Gln Leu Gly Asn Trp Asn Pro Ala

20 25 30

Ser Ala Ile Ala Leu Ser Ser Ala Ala Tyr Pro Thr Trp Ser Val Ser

35 40 45

Val Asn Ile Pro Ala Gly Thr Thr Phe Gln Tyr Lys Phe Ile Arg Lys

50 55 60

Glu Thr Asp Gly Ser Val Val Trp Glu Ser Asp Pro Asn Arg Gln Ala

65 70 75 80

Thr Ala Pro Ala Ser Gly Thr Thr Thr Leu Thr Ser Ser Trp Arg

85 90 95

<210>89

<211>261

<212>DNA

<213>Bacillus flavothermus

<220>

<221> CDS

<222>(1)..(261)

<400>89

acc gtt tgg gga caa aat gta tac gtt gtc ggg aat att tcg cag ctg 48

Thr Val Trp Gly Gly Gln Asn Val Tyr Val Val Gly Asn Ile Ser Gln Leu

1 5 10 15

ggg aac tgg gat cca gtc cac gca gtt caa atg acg ccg tct tct tat 96

Gly Asn Trp Asp Pro Val His Ala Val Gln Met Thr Pro Ser Ser Tyr

20 25 30

cca aca tgg act gta aca atc cct ctt ctt caa ggg caa aac ata caa 144

Pro Thr Trp Thr Val Thr Ile Pro Leu Leu Gln Gly Gln Asn Ile Gln

35 40 45

ttt aaa ttt atc aaa aaa gat tca gct gga aat gtc att tgg gaa gat 192

Phe Lys Phe Ile Lys Lys Asp Ser Ala Gly Asn Val Ile Trp Glu Asp

50 55 60

ata tcg aat cga aca tac acc gtc cca act gct gca tcc gga gca tat 240

Ile Ser Asn Arg Thr Tyr Thr Val Pro Thr Ala Ala Ser Gly Ala Tyr

65 70 75 80

aca gcc agc tgg aac gtg ccc 261

Thr Ala Ser Trp Asn Val Pro

85

<210>90

<211>87

<212>PRT

<213>Bacillus flavothermus

<400>90

Thr Val Trp Gly Gly Gln Asn Val Tyr Val Val Gly Asn Ile Ser Gln Leu

1 5 10 15

Gly Asn Trp Asp Pro Val His Ala Val Gln Met Thr Pro Ser Ser Tyr

20 25 30

Pro Thr Trp Thr Val Thr Ile Pro Leu Leu Gln Gly Gln Asn Ile Gln

35 40 45

Phe Lys Phe Ile Lys Lys Asp Ser Ala Gly Asn Val Ile Trp Glu Asp

50 55 60

Ile Ser Asn Arg Thr Tyr Thr Val Pro Thr Ala Ala Ser Gly Ala Tyr

65 70 75 80

Thr Ala Ser Trp Asn Val Pro

85

<210>91

<211>294

<212>DNA

<213> Athelia rolfsii

<220>

<221> CDS

<222>(1)..(294)

<400>91

gtc gag gtc act ttc gac gtt tac gct acc aca gta tat ggc cag aac 48

Val Glu Val Thr Phe Asp Val Tyr Ala Thr Thr Val Tyr Gly Gln Asn

1 5 10 15

atc tat atc acc ggt gat gtg agt gag ctc ggc aac tgg aca ccc gcc 96

Ile Tyr Ile Thr Gly Asp Val Ser Glu Leu Gly Asn Trp Thr Pro Ala

20 25 30

aat ggt gtt gca ctc tct tct gct aac tac ccc acc tgg agt gcc acg 144

Asn Gly Val Ala Leu Ser Ser Ala Asn Tyr Pro Thr Trp Ser Ala Thr

35 40 45

atc gct ctc ccc gct gac acg aca atc cag tac aag tat gtc aac att 192

Ile Ala Leu Pro Ala Asp Thr Thr Ile Gln Tyr Lys Tyr Val Asn Ile

50 55 60

gac ggc agc acc gtc atc tgg gag gat gct atc agc aat cgc gag atc 240

Asp Gly Ser Thr Val Ile Trp Glu Asp Ala Ile Ser Asn Arg Glu Ile

65 70 75 80

acg acg ccc gcc agc ggc aca tac acc gaa aaa gac act tgg gat gaa 288

Thr Thr Pro Ala Ser Gly Thr Tyr Thr Glu Lys Asp Thr Trp Asp Glu

85 90 95

tct tag 294

Ser

<210>92

<211>97

<212>PRT

<213> Athelia rolfsii

<400>92

Val Glu Val Thr Phe Asp Val Tyr Ala Thr Thr Val Tyr Gly Gln Asn

1 5 10 15

Ile Tyr Ile Thr Gly Asp Val Ser Glu Leu Gly Asn Trp Thr Pro Ala

20 25 30

Asn Gly Val Ala Leu Ser Ser Ala Asn Tyr Pro Thr Trp Ser Ala Thr

35 40 45

Ile Ala Leu Pro Ala Asp Thr Thr Ile Gln Tyr Lys Tyr Val Asn Ile

50 55 60

Asp Gly Ser Thr Val Ile Trp Glu Asp Ala Ile Ser Asn Arg Glu Ile

65 70 75 80

Thr Thr Pro Ala Ser Gly Thr Tyr Thr Glu Lys Asp Thr Trp Asp Glu

85 90 95

Ser

<210>93

<211>327

<212>DNA

<213> Aspergillus kawachii

<220>

<221> CDS

<222>(1)..(327)

<400>93

tgc acc gca aca agc acc acc ctc ccc atc acc ttc gaa gaa ctc gtc 48

Cys Thr Ala Thr Ser Thr Thr Leu Pro Ile Thr Phe Glu Glu Leu Val

1 5 10 15

acc act acc tac ggg gaa gaa gtc tac ctc agc gga tct atc tcc cag 96

Thr Thr Thr Tyr Gly Glu Glu Val Tyr Leu Ser Gly Ser Ile Ser Gln

20 25 30

ctc gga gag tgg gat acg agt gac gcg gtg aag ttg tcc gcg gat gat 144

Leu Gly Glu Trp Asp Thr Ser Asp Ala Val Lys Leu Ser Ala Asp Asp

35 40 45

tat acc tcg agt aac ccc gag tgg tct gtt act gtg tcg ttg ccg gtg 192

Tyr Thr Ser Ser Asn Pro Glu Trp Ser Val Thr Val Ser Leu Pro Val

50 55 60

ggg acg acc ttc gag tat aag ttt att aag gtc gat gag ggt gga agt 240

Gly T0r Thr Phe Glu Tyr Lys Phe Ile Lys Val Asp Glu Gly Gly Ser

65 70 75 80

gtg act tgg gaa agt gat ccg aat agg gag tat act gtg cct gaa tgt 288

Val Thr Trp Glu Ser Asp Pro Asn Arg Glu Tyr Thr Val Pro Glu Cys

85 90 95

ggg aat ggg agt ggg gag acg gtg gtt gat acg tgg agg 327

Gly Asn Gly Ser Gly Glu Thr Val Val Asp Thr Trp Arg

100 105

<210>94

<211>109

<212>PRT

<213>Aspergillus kawachii

<400>94

Cys Thr Ala Thr Ser Thr Thr Leu Pro Ile Thr Phe Glu Glu Leu Val

1 5 10 15

Thr Thr Thr Tyr Gly Glu Glu Val Tyr Leu Ser Gly Ser Ile Ser Gln

20 25 30

Leu Gly Glu Trp Asp Thr Ser Asp Ala Val Lys Leu Ser Ala Asp Asp

35 40 45

Tyr Thr Ser Ser Asn Pro Glu Trp Ser Val Thr Val Ser Leu Pro Val

50 55 60

Gly Thr Thr Phe Glu Tyr Lys Phe Ile Lys Val Asp Glu Gly Gly Ser

65 70 75 80

Val Thr Trp Glu Ser Asp Pro Asn Arg Glu Tyr Thr Val Pro Glu Cys

85 90 95

Gly Asn Gly Ser Gly Glu Thr Val Val Asp Thr Trp Arg

100 105

<210>95

<211>324

<212>DNA

<213> Aspergillus niger

<220>

<221> CDS

<222>(1)..(324)

<400>95

tgt acc act ccc acc gcc gtg gct gtg act ttc gat ctg aca gct acc 48

Cys Thr Thr Pro Thr Ala Val Ala Val Thr Phe Asp Leu Thr Ala Thr

1 5 10 15

acc acc tac ggc gag aac atc tac ctg gtc gga tcg atc tct cag ctg 96

Thr Thr Tyr Gly Gly Glu Asn Ile Tyr Leu Val Gly Ser Ile Ser Gln Leu

20 25 30

ggt gac tgg gaa acc agc gac ggc ata gct ctg agt gct gac aag tac 144

Gly Asp Trp Glu Thr Ser Asp Gly Ile Ala Leu Ser Ala Asp Lys Tyr

35 40 45

act tcc agc gac ccg ctc tgg tat gtc act gtg act ctg ccg gct ggt 192

Thr Ser Ser Asp Pro Leu Trp Tyr Val Thr Val Thr Leu Pro Ala Gly

50 55 60

gag rcg ttt gag tac aag ttt atc cgc att gag agc gat gac tcc gtg 240

Glu Ser Phe Glu Tyr Lys Phe Ile Arg Ile Glu Ser Asp Asp Ser Val

65 70 75 80

gag tgg gag agt gat ccc aac cga gaa tac acc gtt cct cag gcg tgc 288

Glu Trp Glu Ser Asp Pro Asn Arg Glu Tyr Thr Val Pro Gln Ala Cys

85 90 95

gga acg tcg acc gcg acg gtg act gac acc tgg cgg 324

Gly Thr Ser Thr Ala Thr Val Thr Asp Thr Trp Arg

100 105

<210>96

<211>108

<212>PRT

<213> Aspergillus niger

<400>96

Cys Thr Thr Pro Thr Ala Val Ala Val Thr Phe Asp Leu Thr Ala Thr

1 5 10 15

Thr Thr Tyr Gly Gly Glu Asn Ile Tyr Leu Val Gly Ser Ile Ser Gln Leu

20 25 30

Gly Asp Trp Glu Thr Ser Asp Gly Ile Ala Leu Ser Ala Asp Lys Tyr

35 40 45

Thr Ser Ser Asp Pro Leu Trp Tyr Val Thr Val Thr Leu Pro Ala Gly

50 55 60

Glu Ser Phe Glu Tyr Lys Phe Ile Arg Ile Glu Ser Asp Asp Ser Val

65 70 75 80

Glu Trp Glu Ser Asp Pro Asn Arg Glu Tyr Thr Val Pro Gln Ala Cys

85 90 95

Gly Thr Ser Thr Ala Thr Val Thr Asp Thr Trp Arg

100 105

<210>97

<211>300

<212>DNA

<213> Coniochaeta sp.

<220>

<221> CDS

<222>(1)..(300)

<400>97

gta gca atc acc ttc aac gag ctc gtg tcg acc tcc tac ggc gac aca 48

Val Ala Ile Thr Phe Asn Glu Leu Val Ser Thr Ser Tyr Gly Asp Thr

1 5 10 15

gtc aag ctc acg ggc aac ata aca gcc ctg ggc agc tgg aac acg gcc 96

Val Lys Leu Thr Gly Asn Ile Thr Ala Leu Gly Ser Trp Asn Thr Ala

20 25 30

aac gcc gtc agc ctc agc gca tcg cag tac aca tct ggt agc ccg ctc 144

Asn Ala Val Ser Leu Ser Ala Ser Gln Tyr Thr Ser Gly Ser Pro Leu

35 40 45

tgg tcg ggc acc gtg tct ctg cct ccg ggc gtc ggg gta cag tac aag 192

Trp Ser Gly Thr Val Ser Leu Pro Pro Gly Val Gly Val Gln Tyr Lys

50 55 60

ttc gtc agg gtc ggc agc tcg ggg agc gtg acg tgg gag gcg gac ccg 240

Phe Val Arg Val Gly Ser Ser Ser Gly Ser Val Thr Trp Glu Ala Asp Pro

65 70 75 80

aac cac act tat tct gtg ccg tgc gcg gct gct act gtc ggt ggg agt 288

Asn His Thr Tyr Ser Val Pro Cys Ala Ala Ala Thr Val Gly Gly Ser

85 90 95

tgg cag agc tga 300

Trp Gln Ser

<210>98

<211>99

<212>PRT

<213> Coniochaeta sp.

<400>98

Val Ala Ile Thr Phe Asn Glu Leu Val Ser Thr Ser Tyr Gly Asp Thr

1 5 10 15

Val Lys Leu Thr Gly Asn Ile Thr Ala Leu Gly Ser Trp Asn Thr Ala

20 25 30

Asn Ala Val Ser Leu Ser Ala Ser Gln Tyr Thr Ser Gly Ser Pro Leu

35 40 45

Trp Ser Gly Thr Val Ser Leu Pro Pro Gly Val Gly Val Gln Tyr Lys

50 55 60

Phe Val Arg Val Gly Ser Ser Ser Gly Ser Val Thr Trp Glu Ala Asp Pro

65 70 75 80

Asn His Thr Tyr Ser Val Pro Cys Ala Ala Ala Thr Val Gly Gly Ser

85 90 95

Trp Gln Ser

<210>99

<211>1761

<212>DNA

<213> Artificial

<220>

<223> Hybrid containing Fungamyl variant CD and A.rolfsii CBM

<220>

<221> CDS

<222>(1)..(1761)

<400>99

gca acg cct gcg gac tgg cga tcg caa tcc att tat ttc ctt ctc acg 48

Ala Thr Pro Ala Asp Trp Arg Ser Gln Ser Ile Tyr Phe Leu Leu Thr

1 5 10 15

gat cga ttt gca agg acg gat ggg tcg acg act gcg act tgt aat act 96

Asp Arg Phe Ala Arg Thr Asp Gly Ser Thr Thr Ala Thr Cys Asn Thr

20 25 30

gcg gat cag aaa tac tgt ggt gga aca tgg cag ggc atc atc gac aag 144

Ala Asp Gln Lys Tyr Cys Gly Gly Thr Trp Gln Gly Ile Ile Asp Lys

35 40 45

ttg gac tat atc cag gga atg ggc ttc aca gcc atc tgg atc acc ccc 192

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Thr Pro

50 55 60

gtt aca gcc cag ctg ccc cag acc acc gca tat gga gat gcc tac cat 240

Val Thr Ala Gln Leu Pro Gln Thr Thr Ala Tyr Gly Asp Ala Tyr His

65 70 75 80

ggc tac tgg cag cag gat ata tac tct ctg aac gaa aac tac ggc act 288

Gly Tyr Trp Gln Gln Asp Ile Tyr Ser Leu Asn Glu Asn Tyr Gly Thr

85 90 95

gca gat gac ttg aag gcg ctc tct tcg gcc ctt cat gag agg ggg atg 336

Ala Asp Asp Leu Lys Ala Leu Ser Ser Ala Leu His Glu Arg Gly Met

100 105 110

tat ctt atg gtc gat gtg gtt gct aac cat atg ggc tat gat gga ccg 384

Tyr Leu Met Val Asp Val Val Ala Asn His Met Gly Tyr Asp Gly Pro

115 120 125

ggt agc tca gtc gat tac agt gtg ttt gtt ccg ttc aat tcc gct agc 432

Gly Ser Ser Val Asp Tyr Ser Val Phe Val Pro Phe Asn Ser Ala Ser

130 135 140

tac ttc cac ccg ttc tgt ttc att caa aac tgg aat gat cag act cag 480

Tyr Phe His Pro Phe Cys Phe Ile Gln Asn Trp Asn Asp Gln Thr Gln

145 150 155 160

gtt gag gat tgc tgg cta gga gat aac act gtc tcc ttg cct gat ctc 528

Val Glu Asp Cys Trp Leu Gly Asp Asn Thr Val Ser Leu Pro Asp Leu

165 170 175

gat acc acc aag gat gtg gtc aag aat gaa tgg tac gac tgg gtg gga 576

Asp Thr Thr Lys Asp Val Val Lys Asn Glu Trp Tyr Asp Trp Val Gly

180 185 190

tca ttg gta tcg aac tac tcc att gac ggc ctc cgt atc gac aca gta 624

Ser Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Val

195 200 205

aaa cac gtc cag aag gac ttc tgg ccc ggg tac aac aaa gcc gca ggc 672

Lys His Val Gln Lys Asp Phe Trp Pro Gly Tyr Asn Lys Ala Ala Gly

210 215 220

gtg tac tgt atc ggc gag gtg ctc gac ggt gat ccg gcc tac act tgt 720

Val Tyr Cys Ile Gly Glu Val Leu Asp Gly Asp Pro Ala Tyr Thr Cys

225 230 235 240

ccc tac cag gaa gtc ctg gac ggc gta ctg aac tac ccc att tac tat 768

Pro Tyr Gln Glu Val Leu Asp Gly Val Leu Asn Tyr Pro Ile Tyr Tyr

245 250 255

cca ctc ctc aac gcc ttc aag tca acc tcc ggc agc atg gac gac ctc 816

Pro Leu Leu Asn Ala Phe Lys Ser Thr Ser Gly Ser Met Asp Asp Leu

260 265 270

tac aac atg atc aac acc gtc aaa tcc gac tgt cca gac tca aca ctc 864

Tyr Asn Met Ile Asn Thr Val Lys Ser Asp Cys Pro Asp Ser Thr Leu

275 280 285

ctg ggc aca ttc gtc gag aac cac gac aac cca cgg ttc gct tct tac 912

Leu Gly Thr Phe Val Glu Asn His Asp Asn Pro Arg Phe Ala Ser Tyr

290 295 300

acc aac gac ata gcc ctc gcc aag aac gtc gca gca ttc atc atc ctc 960

Thr Asn Asp Ile Ala Leu Ala Lys Asn Val Ala Ala Phe Ile Ile Leu

305 310 315 320

aac gac gga atc ccc atc atc tac gcc ggc caa gaa cag cac tac gcc 1008

Asn Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ala

325 330 335

ggc gga aac gac ccc gcg aac cgc gaa gca acc tgg ctc tcg ggc tac 1056

Gly Gly Asn Asp Pro Ala Asn Arg Glu Ala Thr Trp Leu Ser Gly Tyr

340 345 350

ccg acc gac agc gag ctg tac aag tta att gcc tcc gcg aac gca atc 1104

Pro Thr Asp Ser Glu Leu Tyr Lys Leu Ile Ala Ser Ala Asn Ala Ile

355 360 365

cgg aac tat gcc att agc aaa gat aca gga ttc gtg acc tac aag aac 1152

Arg Asn Tyr Ala IIe Ser Lys Asp Thr Gly Phe Val Thr Tyr Lys Asn

370 375 380

tgg ccc atc tac aaa gac gac aca acg atc gcc atg cgc aag ggc aca 1200

Trp Pro Ile Tyr Lys Asp Asp Thr Thr Ile Ala Met Arg Lys Gly Thr

385 390 395 400

gat ggg tcg cag atc gtg act atc ttg tcc aac aag ggt gct tcg ggt 1248

Asp Gly Ser Gln Ile Val Thr Ile Leu Ser Asn Lys Gly Ala Ser Gly

405 410 415

gat tcg tat acc ctc tcc ttg agt ggt gcg ggt tac aca gcc ggc cag 1296

Asp Set Tyr Thr Leu Ser Leu Ser Gly Ala Gly Tyr Thr Ala Gly Gln

420 425 430

caa ttg acg gag gtc att ggc tgc acg acc gtg acg gtt gat tcg tcg 1344

Gln Leu Thr Glu Val Ile Gly Cys Thr Thr Val Thr Val Asp Ser Ser

435 440 445

gga gat gtg cct gtt cct atg gcg ggt ggg cta cct agg gta ttg tat 1392

Gly Asp Val Pro Val Pro Met Ala Gly Gly Leu Pro Arg Val Leu Tyr

450 455 460

ccg act gag aag ttg gca ggt agc aag atc tgt agt agc tcg ggt gct 1440

Pro Thr Glu Lys Leu Ala Gly Ser Lys Ile Cys Ser Ser Ser Gly Ala

465 470 475 480

aca agc ccg ggt ggc tcc tcg ggt agt gtc gag gtc act ttc gac gtt 1488

Thr Ser Pro Gly Gly Ser Ser Ser Gly Ser Val Glu Val Thr Phe Asp Val

485 490 495

tac gct acc aca gta tat ggc cag aac atc tat atc acc ggt gat gtg 1536

Tyr Ala Thr Thr Val Tyr Gly Gln Asn Ile Tyr Ile Thr Gly Asp Val

500 505 510

agt gag ctc ggc aac tgg aca ccc gcc aat ggt gtt gca ctc tct tct 1584

Ser Glu Leu Gly Asn Trp Thr Pro Ala Asn Gly Val Ala Leu Ser Ser

515 520 525

gct aac tac ccc acc tgg agt gcc acg atc gct ctc ccc gct gac acg 1632

Ala Asn Tyr Pro Thr Trp Ser Ala Thr Ile Ala Leu Pro Ala Asp Thr

530 535 540

aca atc cag tac aag tat gtc aac att gac ggc agc acc gtc atc tgg 1680

Thr Ile Gln Tyr Lys Tyr Val Asn Ile Asp Gly Ser Thr Val Ile Trp

545 550 555 560

gag gat gct atc agc aat cgc gag atc acg acg ccc gcc agc ggc aca 1728

Glu Asp Ala Ile Ser Asn Arg Glu Ile Thr Thr Pro Ala Ser Gly Thr

565 570 575

tac acc gaa aaa gac act tgg gat gaa tct tag 1761

Tyr Thr Glu Lys Asp Thr Trp Asp Glu Ser

580 585

<210>100

<211>586

<212>PRT

<213> Artificial

<220>

<223> Synthetic constructs

<400>100

Ala Thr Pro Ala Asp Trp Arg Ser Gln Ser Ile Tyr Phe Leu Leu Thr

1 5 10 15

Asp Arg Phe Ala Arg Thr Asp Gly Ser Thr Thr Ala Thr Cys Asn Thr

20 25 30

Ala Asp Gln Lys Tyr Cys Gly Gly Thr Trp Gln Gly Ile Ile Asp Lys

35 40 45

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Thr Pro

50 55 60

Val Thr Ala Gln Leu Pro Gln Thr Thr Ala Tyr Gly Asp Ala Tyr His

65 70 75 80

Gly Tyr Trp Gln Gln Asp Ile Tyr Ser Leu Asn Glu Asn Tyr Gly Thr

85 90 95

Ala Asp Asp Leu Lys Ala Leu Ser Ser Ala Leu His Glu Arg Gly Met

100 105 110

Tyr Leu Met Val Asp Val Val Ala Asn His Met Gly Tyr Asp Gly Pro

115 120 125

Gly Ser Ser Val Asp Tyr Ser Val Phe Val Pro Phe Asn Ser Ala Ser

130 135 140

Tyr Phe His Pro Phe Cys Phe Ile Gln Asn Trp Asn Asp Gln Thr Gln

145 150 155 160

Val Glu Asp Cys Trp Leu Gly Asp Asn Thr Val Ser Leu Pro Asp Leu

165 170 175

Asp Thr Thr Lys Asp Val Val Lys Asn Glu Trp Tyr Asp Trp Val Gly

180 185 190

Ser Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Val

195 200 205

Lys His Val Gln Lys Asp Phe Trp Pro Gly Tyr Asn Lys Ala Ala Gly

210 215 220

Val Tyr Cys Ile Gly Glu Val Leu Asp Gly Asp Pro Ala Tyr Thr Cys

225 230 235 240

Pro Tyr Gln Glu Val Leu Asp Gly Val Leu Asn Tyr Pro Ile Tyr Tyr

245 250 255

Pro Leu Leu Asn Ala Phe Lys Ser Thr Ser Gly Ser Met Asp Asp Leu

260 265 270

Tyr Asn Met Ile Asn Thr Val Lys Ser Asp Cys Pro Asp Ser Thr Leu

275 280 285

Leu Gly Thr Phe Val Glu Asn His Asp Asn Pro Arg Phe Ala Ser Tyr

290 295 300

Thr Asn Asp Ile Ala Leu Ala Lys Asn Val Ala Ala Phe Ile Ile Leu

305 310 315 320

Asn Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ala

325 330 335

Gly Gly Asn Asp Pro Ala Asn Arg Glu Ala Thr Trp Leu Ser Gly Tyr

340 345 350

Pro Thr Asp Ser Glu Leu Tyr Lys Leu Ile Ala Ser Ala Asn Ala Ile

355 360 365

Arg Asn Tyr Ala Ile Ser Lys Asp Thr Gly Phe Val Thr Tyr Lys Asn

370 375 380

Trp Pro Ile Tyr Lys Asp Asp Thr Thr Ile Ala Met Arg Lys Gly Thr

385 390 395 400

Asp Gly Ser Gln Ile Val Thr Ile Leu Ser Asn Lys Gly Ala Ser Gly

405 410 415

Asp Ser Tyr Thr Leu Ser Leu Ser Gly Ala Gly Tyr Thr Ala Gly Gln

420 425 430

Gln Leu Thr Glu Val Ile Gly Cys Thr Thr Val Thr Val Asp Ser Ser

435 440 445

Gly Asp Val Pro Val Pro Met Ala Gly Gly Leu Pro Arg Val Leu Tyr

450 455 460

Pro Thr Glu Lys Leu Ala Gly Ser Lys Ile Cys Ser Ser Ser Gly Ala

465 470 475 480

Thr Ser Pro Gly Gly Ser Ser Ser Gly Ser Val Glu Val Thr Phe Asp Val

485 490 495

Tyr Ala Thr Thr Val Tyr Gly Gln Asn Ile Tyr Ile Thr Gly Asp Val

500 505 510

Ser Glu Leu Gly Asn Trp Thr Pro Ala Asn Gly Val Ala Leu Ser Ser

515 520 525

Ala Asn Tyr Pro Thr Trp Ser Ala Thr Ile Ala Leu Pro Ala Asp Thr

530 535 540

Thr Ile Gln Tyr Lys Tyr Val Asn Ile Asp Gly Ser Thr Val Ile Trp

545 550 555 560

Glu Asp Ala Ile Ser Asn Arg Glu Ile Thr Thr Pro Ala Ser Gly Thr

565 570 575

Tyr Thr Glu Lys Asp Thr Trp Asp Glu Ser

580 585

<210>101

<211>558

<212>PRT

<213> Artificial

<220>

<223> Rhizomucor pusillus amylase with linker and from A.rolfsii

SBD

<400>101

Ser Pro Leu Pro Gln Gln Gln Arg Tyr Gly Lys Arg Ala Thr Ser Asp

1 5 10 15

Asp Trp Lys Ser Lys Ala Ile Tyr Gln Leu Leu Thr Asp Arg Phe Gly

20 25 30

Arg Ala Asp Asp Ser Thr Ser Asn Cys Ser Asn Leu Ser Asn Tyr Cys

35 40 45

Gly Gly Thr Tyr Glu Gly Ile Thr Lys His Leu Asp Tyr Ile Ser Gly

50 55 60

Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro Lys Asn Ser Asp

65 70 75 80

Gly Gly Tyr His Gly Tyr Trp Ala Thr Asp Phe Tyr Gln Leu Asn Ser

85 90 95

Asn Phe Gly Asp Glu Ser Gln Leu Lys Ala Leu Ile Gln Ala Ala His

100 105 110

Glu Arg Asp Met Tyr Val Met Leu Asp Val Val Ala Asn His Ala Gly

115 120 125

Pro Thr Ser Asn Gly Tyr Ser Gly Tyr Thr Phe Gly Asp Ala Ser Leu

130 135 140

Tyr His Pro Lys Cys Thr Ile Asp Tyr Asn Asp Gln Thr Ser Ile Glu

145 150 155 160

Gln Cys Trp Val Ala Asp Glu Leu Pro Asp Ile Asp Thr Glu Asn Ser

165 170 175

Asp Asn Val Ala Ile Leu Asn Asp Ile Val Ser Gly Trp Val Gly Asn

180 185 190

Tyr Ser Phe Asp Gly Ile Arg Ile Asp Thr Val Lys His Ile Arg Lys

195 200 205

Asp Phe Trp Thr Gly Tyr Ala Glu Ala Ala Gly Val Phe Ala Thr Gly

210 215 220

Glu Val Phe Asn Gly Asp Pro Ala Tyr Val Gly Pro Tyr Gln Lys Tyr

225 230 235 240

Leu Pro Ser Leu Ile Asn Tyr Pro Met Tyr Tyr Ala Leu Asn Asp Val

245 250 255

Phe Val Ser Lys Ser Lys Gly Phe Ser Arg Ile Ser Glu Met Leu Gly

260 265 270

Ser Asn Arg Asn Ala Phe Glu Asp Thr Ser Val Leu Thr Thr Phe Val

275 280 285

Asp Asn His Asp Asn Pro Arg Phe Leu Asn Ser Gln Ser Asp Lys Ala

290 295 300

Leu Phe Lys Asn Ala Leu Thr Tyr Val Leu Leu Gly Glu Gly Ile Pro

305 310 315 320

Ile Val Tyr Tyr Gly Ser Glu Gln Gly Phe Ser Gly Gly Ala Asp Pro

325 330 335

Ala Asn Arg Glu Val Leu Trp Thr Thr Asn Tyr Asp Thr Ser Ser Ser Asp

340 345 350

Leu Tyr Gln Phe Ile Lys Thr Val Asn Ser Val Arg Met Lys Ser Asn

355 360 365

Lys Ala Val Tyr Met Asp Ile Tyr Val Gly Asp Asn Ala Tyr Ala Phe

370 375 380

Lys His Gly Asp Ala Leu Val Val Leu Asn Asn Tyr Gly Ser Gly Ser

385 390 395 400

Thr Asn Gln Val Ser Phe Ser Val Ser Gly Lys Phe Asp Ser Gly Ala

405 410 415

Ser Leu Met Asp Ile Val Ser Asn Ile Thr Thr Thr Val Ser Ser Asp

420 425 430

Gly Thr Val Thr Phe Asn Leu Lys Asp Gly Leu Pro Ala Ile Phe Thr

435 440 445

Ser Ala Gly Ala Thr Ser Pro Gly Gly Ser Ser Gly Ser Val Glu Val

450 455 460

Thr Phe Asp Val Tyr Ala Thr Thr Val Tyr Gly Gln Asn Ile Tyr Ile

465 470 475 480

Thr Gly Asp Val Ser Glu Leu Gly Asn Trp Thr Pro Ala Asn Gly Val

485 490 495

Ala Leu Ser Ser Ala Asn Tyr Pro Thr Trp Ser Ala Thr Ile Ala Leu

500 505 510

Pro Ala Asp Thr Thr Ile Gln Tyr Lys Tyr Val Asn Ile Asp Gly Ser

515 520 525

Thr Val Ile Trp Glu Asp Ala Ile Ser Asn Arg Glu Ile Thr Thr Pro

530 535 540

Ala Ser Gly Thr Tyr Thr Glu Lys Asp Thr Trp Asp Glu Ser

545 550 555

<210>102

<211>574

<212>PRT

<213> Artificial

<220>

<223> Hybrid of Meripilus giganteus amylase and A.rolfsii SBD

<400>102

Arg Pro Thr Val Phe Asp Ala Gly Ala Asp Ala His Ser Leu His Ala

1 5 10 15

Arg Ala Pro Ser Gly Ser Lys Asp Val Ile Ile Gln Met Phe Glu Trp

20 25 30

Asn Trp Asp Ser Val Ala Ala Glu Cys Thr Asn Phe Ile Gly Pro Ala

35 40 45

Gly Tyr Gly Phe Val Gln Val Ser Pro Pro Gln Glu Thr Ile Gln Gly

50 55 60

Ala Gln Trp Trp Thr Asp Tyr Gln Pro Val Ser Tyr Thr Leu Thr Gly

65 70 75 80

Lys Arg Gly Asp Arg Ser Gln Phe Ala Asn Met Ile Thr Thr Cys His

85 90 95

Ala Ala Gly Val Gly Val Ile Val Asp Thr Ile Trp Asn His Met Ala

100 105 110

Gly Val Asp Ser Gly Thr Gly Thr Ala Gly Ser Ser Phe Thr His Tyr

115 120 125

Asn Tyr Pro Gly Ile Tyr Gln Asn Gln Asp Phe His His Cys Gly Leu

130 135 140

Glu Pro Gly Asp Asp Ile Val Asn Tyr Asp Asn Ala Val Glu Val Gln

145 150 155 160

Thr Cys Glu Leu Val Asn Leu Ala Asp Leu Ala Thr Asp Thr Glu Tyr

165 170 175

Val Arg Gly Arg Leu Ala Gln Tyr Gly Asn Asp Leu Leu Ser Leu Gly

180 185 190

Ala Asp Gly Leu Arg Leu Asp Ala Ser Lys His Ile Pro Val Gly Asp

195 200 205

Ile Ala Asn Ile Leu Ser Arg Leu Ser Arg Ser Val Tyr Ile Thr Gln

210 215 220

Glu Val Ile Phe Gly Ala Gly Glu Pro Ile Thr Pro Asn Gln Tyr Thr

225 230 235 240

Gly Asn Gly Asp Val Gln Glu Phe Arg Tyr Thr Ser Ala Leu Lys Asp

245 250 255

Ala Phe Leu Ser Ser Ser Gly Ile Ser Asn Leu Gln Asp Phe Glu Asn Arg

260 265 270

Gly Trp Val Pro Gly Ser Gly Ala Asn Val Phe Val Val Asn His Asp

275 280 285

Thr Glu Arg Asn Gly Ala Ser Leu Asn Asn Asn Ser Pro Ser Asn Thr

290 295 300

Tyr Val Thr Ala Thr Ile Phe Ser Leu Ala His Pro Tyr Gly Thr Pro

305 310 315 320

Thr Ile Leu Ser Ser Tyr Asp Gly Phe Thr Asn Thr Asp Ala Gly Ala

325 330 335

Pro Asn Asn Asn Val Gly Thr Cys Ser Thr Ser Ser Gly Gly Ala Asn Gly

340 345 350

Trp Leu Cys Gln His Arg Trp Thr Ala Ile Ala Gly Met Val Gly Phe

355 360 365

Arg Asn Asn Val Gly Ser Ala Ala Leu Asn Asn Trp Gln Ala Pro Gln

370 375 380

Ser Gln Gln Ile Ala Phe Gly Arg Gly Ala Leu Gly Phe Val Ala Ile

385 390 395 400

Asn Asn Ala Asp Ser Ala Trp Ser Thr Thr Phe Thr Thr Ser Leu Pro

405 410 415

Asp Gly Ser Tyr Cys Asp Val Ile Ser Gly Lys Ala Ser Gly Ser Ser

420 425 430

Cys Thr Gly Ser Ser Phe Thr Val Ser Gly Gly Lys Leu Thr Ala Thr

435 440 445

Val Pro Ala Arg Ser Ala Ile Ala Val His Thr Gly Gln Lys Gly Ser

450 455 460

Gly Gly Gly Ala Thr Ser Pro Gly Gly Ser Ser Gly Ser Val Glu Val

465 470 475 480

Thr Phe Asp Val Tyr Ala Thr Thr Val Tyr Gly Gln Asn Ile Tyr Ile

485 490 495

Thr Gly Asp Val Ser Glu Leu Gly Asn Trp Thr Pro Ala Asn Gly Val

500 505 510

Ala Leu Ser Ser Ala Asn Tyr Pro Thr Trp Ser Ala Tnr Ile Ala Leu

515 520 525

Pro Ala Asp Thr Thr Ile Gln Tyr Lys Tyr Val Asn Ile Asp Gly Ser

530 535 540

Thr Val Ile Trp Glu Asp Ala Ile Ser Asn Arg Glu Ile Thr Thr Pro

545 550 555 560

Ala Ser Gly Thr Tyr Thr Glu Lys Asp Thr Trp Asp Glu Ser

565 570

<210>103

<211>7063

<212>DNA

<213> Artificial

<220>

<223> Plasmids for construction of hybrids

<220>

<221>misc_feature

<222>(1)..(7063)

<400>103

ctgcattaat gaatcggcca acgcgcgggg agaggcggtt tgcgtattgg gcgctcttcc 60

gcttcctcgc tcactgactc gctgcgctcg gtcgttcggc tgcggcgagc ggtatcagct 120

cactcaaagg cggtaatacg gttatccaca gaatcagggg ataacgcagg aaagaacatg 180

tgagcaaaag gccagcaaaa ggccaggaac cgtaaaaagg ccgcgttgct ggcgtttttc 240

cataggctcc gcccccctga cgagcatcac aaaaatcgac gctcaagtca gaggtggcga 300

aacccgacag gactataaag ataccaggcg tttccccctg gaagctccct cgtgcgctct 360

cctgttccga ccctgccgct taccggatac ctgtccgcct ttctcccttc gggaagcgtg 420

gcgctttctc atagctcacg ctgtaggtat ctcagttcgg tgtaggtcgt tcgctccaag 480

ctgggctgtg tgcacgaacc ccccgttcag cccgaccgct gcgccttatc cggtaactat 540

cgtcttgagt ccaacccggt aagacacgac ttatcgccac tggcagcagc cactggtaac 600

aggattagca gagcgaggta tgtaggcggt gctacagagt tcttgaagtg gtggcctaac 660

tacggctaca ctagaaggac agtatttggt atctgcgctc tgctgaagcc agttaccttc 720

ggaaaaagag ttggtagctc ttgatccggc aaacaaacca ccgctggtag cggtggtttt 780

tttgtttgca agcagcagat tacgcgcaga aaaaaaggat ctcaagaaga tcctttgatc 840

ttttctacgg ggtctgacgc tcagtggaac gaaaactcac gttaagggat tttggtcatg 900

agattatcaa aaaggatctt cacctagatc cttttaaatt aaaaatgaag ttttaaatca 960

atctaaagta tatatgagta aacttggtct gacagttacc aatgcttaat cagtgaggca 1020

cctatctcag cgatctgtct atttcgttca tccatagttg cctgactccc cgtcgtgtag 1080

ataactacga tacgggaggg cttaccatct ggccccagtg ctgcaatgat accgcgagac 1140

ccacgctcac cggctccaga tttatcagca ataaaccagc cagccggaag ggccgagcgc 1200

agaagtggtc ctgcaacttt atccgcctcc atccagtcta ttaattgttg ccgggaagct 1260

agagtaagta gttcgccagt taatagtttg cgcaacgttg ttgccattgc tacaggcatc 1320

gtggtgtcac gctcgtcgtt tggtatggct tcattcagct ccggttccca acgatcaagg 1380

cgagttacat gatcccccat gttgtgcaaa aaagcggtta gctccttcgg tcctccgatc 1440

gttgtcagaa gtaagttggc cgcagtgtta tcactcatgg ttatggcagc actgcataat 1500

tctcttactg tcatgccatc cgtaagatgc ttttctgtga ctggtgagta ctcaaccaag 1560

tcattctgag aatagtgtat gcggcgaccg agttgctctt gcccggcgtc aatacgggat 1620

aataccgcgc cacatagcag aactttaaaa gtgctcatca ttggaaaacg ttcttcgggg 1680

cgaaaactct caaggatctt accgctgttg agatccagtt cgatgtaacc cactcgtgca 1740

cccaactgat cttcagcatc ttttactttc accagcgttt ctgggtgagc aaaaacagga 1800

aggcaaaatg ccgcaaaaaa gggaataagg gcgacacgga aatgttgaat actcatactc 1860

ttcctttttc aatgggtaat aactgatata attaaattga agctctaatt tgtgagttta 1920

gtatacatgc atttacttat aatacagttt tttagttttg ctggccgcat cttctcaaat 1980

atgcttccca gcctgctttt ctgtaacgtt caccctctac cttagcatcc cttccctttg 2040

caaatagtcc tcttccaaca ataataatgt cagatcctgt agagaccaca tcatccacgg 2100

ttctatactg ttgacccaat gcgtctccct tgtcatctaa accccacaccg ggtgtcataa 2160

tcaaccaatc gtaaccttca tctcttccac ccatgtctct ttgagcaata aagccgataa 2220

caaaatcttt gtcgctcttc gcaatgtcaa cagtacccctt agtatattct ccagtagata 2280

gggagccctt gcatgacaat tctgctaaca tcaaaaggcc tctaggttcc tttgttactt 2340

cttctgccgc ctgcttcaaa ccgctaacaa tacctgggcc caccacaccg tgtgcattcg 2400

taatgtctgc ccattctgct attctgtata cacccgcaga gtactgcaat ttgactgtat 2460

taccaatgtc agcaaatttt ctgtcttcga agagtaaaaa attgtacttg gcggataatg 2520

cctttagcgg cttaactgtg ccctccatgg aaaaatcagt caagatatcc acatgtgttt 2580

ttagtaaaca aattttggga cctaatgctt caactaactc cagtaattcg ttggtggtac 2640

gaacatccaa tgaagcacac aagtttgttt gcttttcgtg catgatatta aatagcttgg 2700

cagcaacagg actaggatga gtagcagcac gttccttata tgtagctttc gacatgattt 2760

atcttcgttt cctgcagctt ctcaatgata ttcgaatacg ctttgaggag atacagccta 2820

atatccgaca aactgtttta cagattacg atcgtacttg ttacccatca ttgaattttg 2880

aacatccgaa cctgggagtt ttccctgaaa cagatagtat atttgaacct gtataataat 2940

atatagtcta gcgctttacg gaagacaatg tatgtatttc ggttcctgga gaaactattg 3000

catctattgc ataggtaatc ttgcacgtcg catccccggt tcattttctg cgtttccatc 3060

ttgcacttca atagcatatc tttgttaacg aagcatctgt gcttcatttt gtagaacaaa 3120

aatgcaacgc gagagcgcta atttttcaaa caaagaatct gagctgcatt tttacagaac 3180

agaaatgcaa cgcgaaagcg ctattttacc aacgaagaat ctgtgcttca tttttgtaaa 3240

acaaaaatgc aacgcgagag cgctaatttt tcaaacaaag aatctgagct gcatttttac 3300

agaacagaaa tgcaacgcga gagcgctatt ttaccaacaa agaatctata cttctttttt 3360

gttctacaaa aatgcatccc gagagcgcta tttttctaac aaagcatctt agattacttt 3420

ttttctcctt tgtgcgctct ataatgcagt ctcttgataa ctttttgcac tgtaggtccg 3480

ttaaggttag aagaaggcta ctttggtgtc tattttctct tccataaaaa aagcctgact 3540

ccacttcccg cgtttactga ttactagcga agctgcgggt gcattttttc aagataaagg 3600

catccccgat tatattctat accgatgtgg attgcgcata ctttgtgaag agaaagtgat 3660

agcgttgatg attcttcatt ggtcagaaaa ttatgaacgg tttcttctat tttgtctcta 3720

tatactacgt ataggaaatg tttacatttt cgtattgttt tcgattcact ctatgaatag 3780

ttcttactac aatttttttg tctaaagagt aatactagag ataaacataa aaaatgtaga 3840

ggtcgagttt agatgcaagt tcaaggagcg aaaggtggat gggtaggtta tatagggata 3900

tagcacagag atatatagca aagagatact tttgagcaat gtttgtggaa gcggtattcg 3960

caatgggaag ctcccaggcc ggttgataat cagaaaagcc ccaaaaaaca ggaagattgt 4020

ataagcaaat atttaaattg taaacgttaa tattttgtta aaattcgcgt taaatttttg 4080

ttaaatcagc tcatttttta acgaatagcc cgaaatcggc aaaatccctt ataaatcaaa 4140

agaatagacc gagatagggt tgagtgttgt tccagtttcc aacaagagtc cactattaaa 4200

gaacgtggac tccaacgtca aagggcgaaa aagggtctat cagggcgatg gcccactacg 4260

tgaaccatca ccctaatgaa gttttttggg gtcgaggtgc cgtaaagcag taaatcggaa 4320

gggtaaacgg atgcccccat ttagagcttg acggggaaag ccggcgaacg tggcgagaaa 4380

ggaagggaag aaagcgaaac cagcgggggc tagggcggtg ggaagtgtag gggtcacgct 4440

gggcgtaacc accacacccg ccgcgcttaa tggggcgcta cagggcgcgt ggggatatcc 4500

actagcatgc ctcagcttcc tctattgatg ttacacctgg acaccccttt tctggcatcc 4560

agtttttaat cttcagtggc atgtgagatt ctccgaaatt aattaaagca atcacacaat 4620

tctctcggat accacctcgg ttgaaactga caggtggttt gttacgctaa tgcaaaggag 4680

cctatatacc tttggctcgg ctgctgtaac agggaatata aagggcagca taatttagga 4740

gtttagtgaa cttgcaacat ttactatttt cccttcttac gtaaatattt ttctttttaa 4800

ttctaaatca atctttttca attttttgtt tgtattcttt tcttgcttaa atctataact 4860

acaaaaaaca catacagaaa ttcattcaag aatagttcaa acaagaagat tacaaactat 4920

caatttcata cacaatataa acgacgggac ccggggatcg aattcatgag attatcgact 4980

tcgagtctct tcctttccgt gtctctgctg gggaagctgg ccctcgggct gtcggctgca 5040

gaatggcgca ctcagtcgat ttacttccta ttgacggatc ggttcggtag gacggacaat 5100

tcgacgacag ctacatgcga tacgggtgac caaatctatt gtggtggcag ttggcaagga 5160

atcatcaacc atctggatta tatccagggc atgggattca cggccatctg gatctcgcct 5220

atcactgaac agctgcccca ggatactgct gatggtgaag cttaccatgg atattggcag 5280

cagaagatat acgacgtgaa ctccaacttc ggcactgcag atgacctcaa gtccctctca 5340

gatgcgcttc atgcccgcgg aatgtacctc atggtggacg tcgtccctaa ccacatgggc 5400

tacgccggca acggcaacga tgtagactac agcgtcttcg accccttcga ttcctcctcc 5460

tacttccacc catactgcct gatcacagat tgggacaact tgaccatggt ccaagattgt 5520

tgggagggtg acaccatcgt atctctgcca gacctaaaca ccaccgaaac tgccgtgaga 5580

acaatctggt atgactgggt agccgacctg gtatccaatt attcagtcga cggactccgc 5640

atcgacagtg tcctcgaagt cgaaccagac ttcttcccgg gctaccagga agcagcaggt 5700

gtctactgcg tcggcgaagt cgacaacggc aaccctgccc tcgactgccc ataccagaag 5760

gtcctggacg gcgtcctcaa ctatccgatc tactggcaac tcctctacgc cttcgaatcc 5820

tccagcggca gcatcagcaa tctctacaac atgatcaaat ccgtcgcaag cgactgctcc 5880

gatccgacac tactcggcaa cttcatcgaa aaccacgaca atccccgttt cgcctcctac 5940

acctccgact actcgcaagc caaaaacgtc ctcagctaca tcttcctctc cgacggcatc 6000

cccatcgtct acgccggcga agaacagcac tactccggcg gcaaggtgcc ctacaaccgc 6060

gaagcgacct ggctttcagg ctacgacacc tccgcagagc tgtacacctg gatagccacc 6120

acgaacgcga tccgcaaact agccatctca gctgactcgg cctacattac ctacgcgaat 6180

gatgcattct acactgacag caacaccatc gcaatgcgca aaggcacctc agggagccaa 6240

gtcatcaccg tcctctccaa caaaggctcc tcaggaagca gctacaccct gaccctcagc 6300

ggaagcggct acacatccgg cacgaagctg atcgaagcgt acacatgcac atccgtgacc 6360

gtggactcga gcggcgatat tcccgtgccg atggcgtcgg gattaccgag agttcttctg 6420

cccgcgtccg tcgtcgatag ctcttcgctc tgtggcggga gcggaagagg tgctacaagc 6480

ccgggtggct cctcgggtag tgtcgaggtc actttcgacg tttacgctac cacagtatat 6540

ggccagaaca tctatatcac cggtgatgtg agtgagctcg gcaactggac acccgccaat 6600

ggtgttgcac tctcttctgc taactaccccc acctggagtg ccacgatcgc tctccccgct 6660

gacacgacaa tccagtacaa gtatgtcaac attgacggca gcaccgtcat ctgggaggat 6720

gctatcagca atcgcgagat cacgacgccc gccagcggca catacaccga aaaagacact 6780

tgggatgaat cttaggcggc cgcgggccgc atcatgtaat tagttatgtc acgcttacat 6840

tcacgccctc cccccacatc cgctctaacc gaaaaggaag gagttagaca acctgaagtc 6900

taggtcccta tttatttttt tatagttatg ttagtattaa gaacgttatt tatatttcaa 6960

attttcttt tttttctgta cagacgcgtg tacgcatgta aattatact gaaaaccttg 7020

cttgagaagg ttttgggacg ctcgaaggct ttaatttgcg gcc 7063

<210>104

<211>41

<212>DNA

<213> Artificial

<220>

<223> Primer

<220>

<221>misc_feature

<222>(1)..(41)

<400>104

gctggggaag ctggccctcg ggagcccttt gccccaacagc 41

<210>105

<211>42

<212>DNA

<213>ja126r

<220>

<221>misc_feature

<222>(1)..(42)

<400>105

agccacccgg gcttgtagca ccagcagagg tgaagatagc cg 42

<210>106

<211>42

<212>DNA

<213> Artificial

<220>

<223> Primer

<400>106

gctggggaag ctggccctcg ggcgccctac tgtctttgac gc 42

<210>107

<211>42

<212>DNA

<213> Artificial

<220>

<223> Primer

<400>107

agccacccgg gcttgtagca ccaccaccag aacctttctg ac 42

<210>108

<211>387

<212>DNA

<213> Corn (Zea mays)

<220>

<221> CDS

<222>(1)..(387)

<400>108

gtg cgt gtt cga ttt gtg ctg aaa agg cag tgc acg ttc ggg cag agc 48

Val Arg Val Arg Phe Val Leu Lys Arg Gln Cys Thr Phe Gly Gln Ser

1 5 10 15

gtc tgc ctt gtc ggc gac gac cct gcg ctc ggc ctc tgg gat ctg tcg 96

Val Cys Leu Val Gly Asp Asp Pro Ala Leu Gly Leu Trp Asp Leu Ser

20 25 30

aac gcg ttt cct ttg aag tgg gcg gaa agc cac gac tgg acc tta gag 144

Asn Ala Phe Pro Leu Lys Trp Ala Glu Ser His Asp Trp Thr Leu Glu

35 40 45

aaa gat ttg ccg gcc aac aag ctg att gag ttc aag ttc ttg ctc caa 192

Lys Asp Leu Pro Ala Asn Lys Leu Ile Glu Phe Lys Phe Leu Leu Gln

50 55 60

gat tcc aca gga aag ttg cat tgg cag ggt ggg cca aac aga agc ttt 240

Asp Ser Thr Gly Lys Leu His Trp Gln Gly Gly Pro Asn Arg Ser Phe

65 70 75 80

cag aca ggt gaa acc gcc gca aac aca ttg gtt gtg ttt gaa gat tgg 288

Gln Thr Gly Glu Thr Ala Ala Asn Thr Leu Val Val Phe Glu Asp Trp

85 90 95

ggt gat gtg aag aat cag aaa ata gta gaa gag ggg gga gtg gcg tct 336

Gly Asp Val Lys Asn Gln Lys Ile Val Glu Glu Gly Gly Val Ala Ser

100 105 110

gct ggg ata gaa caa act gtt gtt tca aat gac agc gaa agc aga aag 384

Ala Gly Ile Glu Gln Thr Val Val Ser Asn Asp Ser Glu Ser Arg Lys

115 120 125

tag 387

<210>109

<211>128

<212>PRT

<213> Corn (Zea mays)

<400>109

Val Arg Val Arg Phe Val Leu Lys Arg Gln Cys Thr Phe Gly Gln Ser

1 5 10 15

Val Cys Leu Val Gly Asp Asp Pro Ala Leu Gly Leu Trp Asp Leu Ser

20 25 30

Asn Ala Phe Pro Leu Lys Trp Ala Glu Ser His Asp Trp Thr Leu Glu

35 40 45

Lys Asp Leu Pro Ala Asn Lys Leu Ile Glu Phe Lys Phe Leu Leu Gln

50 55 60

Asp Ser Thr Gly Lys Leu His Trp Gln Gly Gly Pro Asn Arg Ser Phe

65 70 75 80

Gln Thr Gly Glu Thr Ala Ala Asn Thr Leu Val Val Phe Glu Asp Trp

85 90 95

Gly Asp Val Lys Asn Gln Lys Ile Val Glu Glu Gly Gly Val Ala Ser

100 105 110

Ala Gly Ile Glu Gln Thr Val Val Ser Asn Asp Ser Glu Ser Arg Lys

115 120 125

<210>110

<211>1428

<212>DNA

<213> Species of the genus Thermoascus (Thermoascus sp.)

<220>

<221> CDS

<222>(1)..(1428)

<400>110

gcg acg cct gcc gaa tgg cgc tcg cag tca att tac ttt tta ctc acc 48

Ala Thr Pro Ala Glu Trp Arg Ser Gln Ser Ile Tyr Phe Leu Leu Thr

1 5 10 15

gat cgc ttt gcc cgc acc gac aac tcg aca acc gcc gaa tgt gat act 96

Asp Arg Phe Ala Arg Thr Asp Asn Ser Thr Thr Ala GIu Cys Asp Thr

20 25 30

agt gcg gtg aag tac tgt ggc ggg act tgg cag gga atc att aac cag 144

Ser Ala Val Lys Tyr Cys Gly Gly Thr Trp Gln Gly Ile Ile Asn Gln

35 40 45

ctg gac tac atc cag ggg atg ggc ttc aca gca acc tgg atc acc cca 192

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Thr Trp Ile Thr Pro

50 55 60

gtg acc gcc aat ctc gag gat ggg cag cat ggg gag gca tac cat ggg 240

Val Thr Ala Asn Leu Glu Asp Gly Gln His Gly Glu Ala Tyr His Gly

65 70 75 80

tac tgg cag cag gat ata tat gcg ttg aac ccg cac ttt ggc act caa 288

Tyr Trp Gln Gln Asp Ile Tyr Ala Leu Asn Pro His Phe Gly Thr Gln

85 90 95

gac gac ctc cga gca ctg tct gac gcg ctg cac gac cga gga atg tac 336

Asp Asp Leu Arg Ala Leu Ser Asp Ala Leu His Asp Arg Gly Met Tyr

100 105 110

ctt atg gtc gac gtg gtt gcc aat cat ttt ggc tac gac gcc ccc gcc 384

Leu Met Val Asp Val Val Ala Asn His Phe Gly Tyr Asp Ala Pro Ala

115 120 125

gcg tcg gtc gac tac agc gtc ttc aac ccg ttt aac tcg gca gac tac 432

Ala Ser Val Asp Tyr Ser Val Phe Asn Pro Phe Asn Ser Ala Asp Tyr

130 135 140

ttc cac act ccc tgc gat atc acg gac tac gac aac cag acc cag gtc 480

Phe His Thr Pro Cys Asp Ile Thr Asp Tyr Asp Asn Gln Thr Gln Val

145 150 155 160

gag gat tgc tgg ctg tac acc gac gcc gtc agt ctg cca gat gtc gat 528

Glu Asp Cys Trp Leu Tyr Thr Asp Ala Val Ser Leu Pro Asp Val Asp

165 170 175

acc acc aac gag gag gtc aag gag att tgg tac gac tgg gtg ggt gac 576

Thr Thr Asn Glu Glu Val Lys Glu Ile Trp Tyr Asp Trp Val Gly Asp

180 185 190

ctt gtg tct aac tac tct atc gac ggg ctt cgc atc gac acc gct cgg 624

Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Ala Arg

195 200 205

cac gta cag aag gac ttc tgg cgc gac tac aac gat gcc gcg ggc gtg 672

His Val Gln Lys Asp Phe Trp Arg Asp Tyr Asn Asp Ala Ala Gly Val

210 215 220

tac tgc gtc ggc gag gtc ttc cag ggc gat ccc gat tac aca tgc ggg 720

Tyr Cys Val Gly Glu Val Phe Gln Gly Asp Pro Asp Tyr Thr Cys Gly

225 230 235 240

tac cag gag gtt atg gac ggg gtg ctg aac tat ccc atc tac tac ccc 768

Tyr Gln Glu Val Met Asp Gly Val Leu Asn Tyr Pro Ile Tyr Tyr Pro

245 250 255

ctg ttg cgc gct ttc agc tcc aca tct ggc agt ctc agc gat cta gcc 816

Leu Leu Arg Ala Phe Ser Ser Thr Ser Gly Ser Leu Ser Asp Leu Ala

260 265 270

aac atg atc gaa acg gtc aag tac acc tgc tca gac gct acc ttg ctg 864

Asn Met Ile Glu Thr Val Lys Tyr Thr Cys Ser Asp Ala Thr Leu Leu

275 280 285

ggc aac ttc atc gag aac cac gat aac cca cgc ttt gcc tcg tac acc 912

Gly Asn Phe Ile Glu Asn His Asp Asn Pro Arg Phe Ala Ser Tyr Thr

290 295 300

gac gac atc tcc ctc gcc aag aac gtc gcc gcc ttc gtg atc ctc tcc 960

Asp Asp Ile Ser Leu Ala Lys Asn Val Ala Ala Phe Val Ile Leu Ser

305 310 315 320

gac ggg atc ccc ata atc tac gcc ggt caa gaa cag cac tac tcc ggc 1008

Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ser Gly

325 330 335

gca gga gac ccg gca aac cgc gag gca acc tgg cta tcc ggt tac gac 1056

Ala Gly Asp Pro Ala Asn Arg Glu Ala Thr Trp Leu Ser Gly Tyr Asp

340 345 350

aca acg agc gag ctg tac cag ttc att gcg aag acg aac cag atc cgg 1104

Thr Thr Ser Glu Leu Tyr Gln Phe Ile Ala Lys Thr Asn Gln Ile Arg

355 360 365

aat cat gct atc tgg cag aat gag acc tac ctt tct tac aaa aac tat 1152

Asn His Ala Ile Trp Gln Asn Glu Thr Tyr Leu Ser Tyr Lys Asn Tyr

370 375 380

gct atc tac aac gag aac aac gtc ctt gtc atg cgc aaa gga ttc gac 1200

Ala Ile Tyr Asn Glu Asn Asn Val Leu Val Met Arg Lys Gly Phe Asp

385 390 395 400

ggg tcg cag atc att aca atc ctc acg aac gct ggc gct gac gct ggt 1248

Gly Ser Gln Ile Ile Thr Ile Leu Thr Asn Ala Gly Ala Asp Ala Gly

405 410 415

tca tcg act gtc tcg gtt ccg aac acc ggg ttc acg gct ggt gcg gca 1296

Ser Ser Thr Val Ser Val Pro Asn Thr Gly Phe Thr Ala Gly Ala Ala

420 425 430

gtc act gag atc tat acc tgt gag gac att acg gtc tcg gac agc ggt 1344

Val Thr Glu Ile Tyr Thr Cys Glu Asp Ile Thr Val Ser Asp Ser Gly

435 440 445

gaa gtg tca gtg cct atg gag agc ggc ttg ccg agg gtt ctg tat ccg 1392

Glu Val Ser Val Pro Met Glu Ser Gly Leu Pro Arg Val Leu Tyr Pro

450 455 460

aag gcg aag ctg gaa ggg agc ggg att tgc gac ctg 1428

Lys Ala Lys Leu Glu Gly Ser Gly Ile Cys Asp Leu

465 470 475

<210>111

<211>476

<212>PRT

<213> Species of the genus Thermoascus (Thermoascus sp.)

<400>111

Ala Thr Pro Ala Glu Trp Arg Ser Gln Ser Ile Tyr Phe Leu Leu Thr

1 5 10 15

Asp Arg Phe Ala Arg Thr Asp Asn Ser Thr Thr Ala Glu Cys Asp Thr

20 25 30

Ser Ala Val Lys Tyr Cys Gly Gly Thr Trp Gln Gly Ile Ile Asn Gln

35 40 45

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Thr Trp Ile Thr Pro

50 55 60

Val Thr Ala Asn Leu Glu Asp Gly Gln His Gly Glu Ala Tyr His Gly

65 70 75 80

Tyr Trp Gln Gln Asp Ile Tyr Ala Leu Asn Pro His Phe Gly Thr Gln

85 90 95

Asp Asp Leu Arg Ala Leu Ser Asp Ala Leu His Asp Arg Gly Met Tyr

100 105 110

Leu Met Val Asp Val Val Ala Asn His Phe Gly Tyr Asp Ala Pro Ala

115 120 125

Ala Ser Val Asp Tyr Ser Val Phe Asn Pro Phe Asn Ser Ala Asp Tyr

130 135 140

Phe His Thr Pro Cys Asp Ile Thr Asp Tyr Asp Asn Gln Thr Gln Val

145 150 155 160

Glu Asp Cys Trp Leu Tyr Thr Asp Ala Val Ser Leu Pro Asp Val Asp

165 170 175

Thr Thr Asn Glu Glu Val Lys Glu Ile Trp Tyr Asp Trp Val Gly Asp

180 185 190

Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Ala Arg

195 200 205

His Val Gln Lys Asp Phe Trp Arg Asp Tyr Asn Asp Ala Ala Gly Val

210 215 220

Tyr Cys Val Gly Glu Val Phe Gln Gly Asp Pro Asp Tyr Thr Cys Gly

225 230 235 240

Tyr Gln Glu Val Met Asp Gly Val Leu Asn Tyr Pro Ile Tyr Tyr Pro

245 250 255

Leu Leu Arg Ala Phe Ser Ser Thr Ser Gly Ser Leu Ser Asp Leu Ala

260 265 270

Asn Met Ile Glu Thr Val Lys Tyr Thr Cys Ser Asp Ala Thr Leu Leu

275 280 285

Gly Asn Phe Ile Glu Asn His Asp Asn Pro Arg Phe Ala Ser Tyr Thr

290 295 300

Asp Asp Ile Ser Leu Ala Lys Asn Val Ala Ala Phe Val Ile Leu Ser

305 310 315 320

Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ser Gly

325 330 335

Ala Gly Asp Pro Ala Asn Arg Glu Ala Thr Trp Leu Ser Gly Tyr Asp

340 345 350

Thr Thr Ser Glu Leu Tyr Gln Phe Ile Ala Lys Thr Asn Gln Ile Arg

355 360 365

Asn His Ala Ile Trp Gln Asn Glu Thr Tyr Leu Ser Tyr Lys Asn Tyr

370 375 380

Ala Ile Tyr Asn Glu Asn Asn Val Leu Val Met Arg Lys Gly Phe Asp

385 390 395 400

Gly Ser Gln Ile Ile Thr Ile Leu Thr Asn Ala Gly Ala Asp Ala Gly

405 410 415

Ser Ser Thr Val Ser Val Pro Asn Thr Gly Phe Thr Ala Gly Ala Ala

420 425 430

Val Thr Glu Ile Tyr Thr Cys Glu Asp Ile Thr Val Ser Asp Ser Gly

435 440 445

Glu Val Ser Val Pro Met Glu Ser Gly Leu Pro Arg yal Leu Tyr Pro

450 455 460

Lys Ala Lys Leu Glu Gly Ser Gly Ile Cys Asp Leu

465 470 475

<210>112

<211>1440

<212>DNA

<213> Coniocheata sp.

<220>

<221> CDS

<222>(1)..(1440)

<400>112

ctc agc gcg gcc ggc tgg cgc cag cag tcc att tac cag gtc atg acg 48

Leu Ser Ala Ala Gly Trp Arg Gln Gln Ser Ile Tyr Gln Val Met Thr

1 5 10 15

gac cgc ttc gcg ccg acc gac ctg tcc acc acc gcc gca tgc gac acc 96

Asp Arg Phe Ala Pro Thr Asp Leu Ser Thr Thr Ala Ala Cys Asp Thr

20 25 30

tcg gcc cag gcg tac tgc ggc ggc acg tac cag ggc ctc atc tcc aag 144

Ser Ala Gln Ala Tyr Cys Gly Gly Thr Tyr Gln Gly Leu Ile Ser Lys

35 40 45

ctg gac tac atc cag ggc atg ggc ttc acc gcc gtg tgg ata tcg ccc 192

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Val Trp Ile Ser Pro

50 55 60

atc gtc aag cag atg gac ggc aac acc gcc gac ggg tcc tcg tac cac 240

Ile Val Lys Gln Met Asp Gly Ash Thr Ala Asp Gly Ser Ser Tyr His

65 70 75 80

ggg tac tgg gcg cag gac atc tgg agt ctg aac ccc tcc ttc ggc acg 288

Gly Tyr Trp Ala Gln Asp Ile Trp Ser Leu Asn Pro Ser Phe Gly Thr

85 90 95

gcg ggc gac ctg atc gcg ctc tcc aat gcg ctg cac gcc cgc ggg atg 336

Ala Gly Asp Leu Ile Ala Leu Ser Asn Ala Leu His Ala Arg Gly Met

100 105 110

tac ctg atg cta gac gtg gtg acg aac cac gtc gcc tac aag ggc tgc 384

Tyr Leu Met Leu Asp Val Val Thr Asn His Val Ala Tyr Lys Gly Cys

115 120 125

ggc gcc tgc gtc gac tac agc ctc ttc acg ccg ttc gac tcg gcg tcc 432

Gly Ala Cys Val Asp Tyr Ser Leu Phe Thr Pro Phe Asp Ser Ala Ser

130 135 140

tac ttc cac ccc ttc tgt ctg atc gac tac agc aac cag acc tcc atc 480

Tyr Phe His Pro Phe Cys Leu Ile Asp Tyr Ser Asn Gln Thr Ser Ile

145 150 155 160

gag cag tgc tgg gag ggc gac aac acc gtc agc ctg ccc gac ctg cgg 528

Glu Gln Cys Trp Glu Gly Asp Asn Thr Val Ser Leu Pro Asp Leu Arg

165 170 175

acc gag gac tcc tcc gtg cgc gcc atc tgg aac gac tgg att gcg cag 576

Thr Glu Asp Ser Ser Val Arg Ala Ile Trp Asn Asp Trp Ile Ala Gln

180 185 190

gtc gtg gag acg tac ggc atc gac ggc ctg cgc gtc gac agc gtc aag 624

Val Val Glu Thr Tyr Gly Ile Asp Gly Leu Arg Val Asp Ser Val Lys

195 200 205

cac cag gag acg tcg ttc tgg tcc ggc ttc ggg gcc gcc gcc ggc gtc 672

His Gln Glu Thr Ser Phe Trp Ser Gly Phe Gly Ala Ala Ala Gly Val

210 215 220

ttc atg ctg ggc gag gtg tac aac ggc gac ccg gcg cag ctg gcg ccc 720

Phe Met Leu Gly Glu Val Tyr Asn Gly Asp Pro Ala Gln Leu Ala Pro

225 230 235 240

tac cag gac tac atg ccg ggc ctg ctg gac tac gcg agc tac tac tgg 768

Tyr Gln Asp Tyr Met Pro Gly Leu Leu Asp Tyr Ala Ser Tyr Tyr Trp

245 250 255

atc acg cgc gcc ttc cag tcg agc tcg gga agc atc agc aac ctt gcc 816

Ile Thr Arg Ala Phe Gln Ser Ser Ser Ser Gly Ser Ile Ser Asn Leu Ala

260 265 270

tcc ggc atc aac acg ctc aag ggc gtc gcg agg aac acc agc ctg tac 864

Ser Gly Ile Asn Thr Leu Lys Gly Val Ala Arg Asn Thr Ser Leu Tyr

275 280 285

ggg agc ttc ctc gag aac cac gac cag ccg cgg ttc gcg tcg ctg act 912

Gly Ser Phe Leu Glu Asn His Asp Gln Pro Arg Phe Ala Ser Leu Thr

290 295 300

gcg gat ctc gcg ctg gcc aag aac gcg atc gcg ttc acg atg ctg aaa 960

Ala Asp Leu Ala Leu Ala Lys Asn Ala Ile Ala Phe Thr Met Leu Lys

305 310 315 320

gac ggc atc ccg gtc gtg tac cag ggc cag gag cag cac ttc gcc gga 1008

Asp Gly Ile Pro Val Val Tyr Gln Gly Gln Glu Gln His Phe Ala Gly

325 330 335

gga aac gtg ccg gcc gac cgc gag gcg ctc tgg tcg tcg ggg tac gac 1056

Gly Asn Val Pro Ala Asp Arg Glu Ala Leu Trp Ser Ser Gly Tyr Asp

340 345 350

acg tcc gcg acg ctg tac gcg tgg atc gca gcg ctg aat aag atc cgc 1104

Thr Ser Ala Thr Leu Tyr Ala Trp Ile Ala Ala Leu Asn Lys Ile Arg

355 360 365

gcg agg gcc atc gcg cag gac ggc gcg tac ctg agc tac cag gcg tat 1152

Ala Arg Ala Ile Ala Gln Asp Gly Ala Tyr Leu Ser Tyr Gln Ala Tyr

370 375 380

ccg gtg tac acg gac agc aac acc atc gcc atg cgc aaa gga cga gac 1200

Pro Val Tyr Thr Asp Ser Asn Thr Ile Ala Met Arg Lys Gly Arg Asp

385 390 395 400

ggg tac cag atc gtc ggg gtg ttc acc aac aag ggc tcc tcg gga ggg 1248

Gly Tyr Gln Ile Val Gly Val Phe Thr Asn Lys Gly Ser Ser Gly Gly

405 410 415

acg tcg agc gtc acg ctc acg acg tcg atg acg ggg ttt act gcc ggc 1296

Thr Ser Ser Val Thr Leu Thr Thr Ser Met Thr Gly Phe Thr Ala Gly

420 425 430

cag gcc gtg gtg gac gtc atg agc tgc acg acg ttc acg gcg gac tca 1344

Gln Ala Val Val Asp Val Met Ser Cys Thr Thr Phe Thr Ala Asp Ser

435 440 445

agc ggc agc ctg ggc atc acg ctc tcg ggg ggg att cca agg gtg ttc 1392

Ser Gly Ser Leu Gly Ile Thr Leu Ser Gly Gly Ile Pro Arg Val Phe

450 455 460

tac ccg agc gca agg ctg agc ggg tcc ggg ata tgc ggg tcc ggg agc 1440

Tyr Pro Ser Ala Arg Leu Ser Gly Ser Gly Ile Cys Gly Ser Gly Ser

465 470 475 480

<210>113

<211>480

<212>PRT

<213> Coniocheata sp.

<400>113

Leu Ser Ala Ala Gly Trp Arg Gln Gln Ser Ile Tyr Gln Val Met Thr

1 5 10 15

Asp Arg Phe Ala Pro Thr Asp Leu Ser Thr Thr Ala Ala Cys Asp Thr

20 25 30

Ser Ala Gln Ala Tyr Cys Gly Gly Thr Tyr Gln Gly Leu Ile Ser Lys

35 40 45

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Val Trp Ile Ser Pro

50 55 60

Ile Val Lys Gln Met Asp Gly Asn Thr Ala Asp Gly Ser Ser Tyr His

65 70 75 80

Gly Tyr Trp Ala Gln Asp Ile Trp Ser Leu Asn Pro Ser Phe Gly Thr

85 90 95

Ala Gly Asp Leu Ile Ala Leu Ser Asn Ala Leu His Ala Arg Gly Met

100 105 110

Tyr Leu Met Leu Asp Val Val Thr Asn His Val Ala Tyr Lys Gly Cys

115 120 125

Gly Ala Cys Val Asp Tyr Ser Leu Phe Thr Pro Phe Asp Ser Ala Ser

130 135 140

Tyr Phe His Pro Phe Cys Leu Ile Asp Tyr Ser Asn Gln Thr Ser Ile

145 150 155 160

Glu Gln Cys Trp Glu Gly Asp Asn Thr Val Ser Leu Pro Asp Leu Arg

165 170 175

Thr Glu Asp Ser Ser Val Arg Ala Ile Trp Asn Asp Trp Ile Ala Gln

180 185 190

Val Val Glu Thr Tyr Gly Ile Asp Gly Leu Arg Val Asp Ser Val Lys

195 200 205

His Gln Glu Thr Ser Phe Trp Ser Gly Phe Gly Ala Ala Ala Gly Val

210 215 220

Phe Met Leu Gly Glu Val Tyr Asn Gly Asp Pro Ala Gln Leu Ala Pro

225 230 235 240

Tyr Gln Asp Tyr Met Pro Gly Leu Leu Asp Tyr Ala Ser Tyr Tyr Trp

245 250 255

Ile Thr Arg Ala Phe Gln Ser Ser Ser Ser Gly Ser Ile Ser Asn Leu Ala

260 265 270

Ser Gly Ile Asn Thr Leu Lys Gly Val Ala Arg Asn Thr Ser Leu Tyr

275 280 285

Gly Ser Phe Leu Glu Asn His Asp Gln Pro Arg Phe Ala Ser Leu Thr

290 295 300

Ala Asp Leu Ala Leu Ala Lys Asn Ala Ile Ala Phe Thr Met Leu Lys

305 310 315 320

Asp Gly Ile Pro Val Val Tyr Gln Gly Gln Glu Gln His Phe Ala Gly

325 330 335

Gly Asn Val Pro Ala Asp Arg Glu Ala Leu Trp Ser Ser Gly Tyr Asp

340 345 350

Thr Ser Ala Thr Leu Tyr Ala Trp Ile Ala Ala Leu Asn Lys Ile Arg

355 360 365

Ala Arg Ala Ile Ala Gln Asp Gly Ala Tyr Leu Ser Tyr Gln Ala Tyr

370 375 380

Pro Val Tyr Thr Asp Ser Asn Thr Ile Ala Met Arg Lys Gly Arg Asp

385 390c 395 400

Gly Tyr Gln Ile Val Gly Val Phe Thr Asn Lys Gly Ser Ser Gly Gly

405 410 415

Thr Ser Ser Val Thr Leu Thr Thr Ser Met Thr Gly Phe Thr Ala Gly

420 425 430

Gln Ala Val Val Asp Val Met Ser Cys Thr Thr Phe Thr Ala Asp Ser

435 440 445

Ser Gly Ser Leu Gly Ile Thr Leu Ser Gly Gly Ile Pro Arg Val Phe

450 455 460

Tyr Pro Ser Ala Arg Leu Ser Gly Ser Gly Ile Cys Gly Ser Gly Ser

465 470 475 480

<210>114

<211>1326

<212>DNA

<213> Nectria sp.

<220>

<221> CDS

<222>(1)..(1326)

<400>114

gct gat acg gcg gcg tgg aag tcc cgc aac atc tac ttc gct ttg act 48

Ala Asp Thr Ala Ala Trp Lys Ser Arg Asn Ile Tyr Phe Ala Leu Thr

1 5 10 15

gac cgt att gcc cgc tct gct gat gac ggc ggc ggc gat gca tgc gga 96

Asp Arg Ile Ala Arg Ser Ala Asp Asp Gly Gly Gly Asp Ala Cys Gly

20 25 30

aac ttg ggt cag tat tgt ggt ggc acc ttt aag ggc ctc gag ggc aag 144

Asn Leu Gly Gln Tyr Cys Gly Gly Thr Phe Lys Gly Leu Glu Gly Lys

35 40 45

ctt gat tac atc aag gga atg ggg ttc gac gcc atc tgg att aca cca 192

Leu Asp Tyr Ile Lys Gly Met Gly Phe Asp Ala Ile Trp Ile Thr Pro

50 55 60

gtt gtt caa aac agt cct ggt ggt tac cac ggc tac tgg gca aca gac 240

Val Val Gln Asn Ser Pro Gly Gly Tyr His Gly Tyr Trp Ala Thr Asp

65 70 75 80

ctc tac tct gtc aac tcc gaa tat gga act gca gat gac ctg aag agc 288

Leu Tyr Ser Val Asn Ser Glu Tyr Gly Thr Ala Asp Asp Leu Lys Ser

85 90 95

ctc gta gct act gct cat gac aag ggc att tat atc atg gcc gat gtg 336

Leu Val Ala Thr Ala His Asp Lys Gly Ile Tyr Ile Met Ala Asp Val

100 105 110

gta gca aac cac atg ggc cct act gat att tca gca aac aag ccg gag 384

Val Ala Asn His Met Gly Pro Thr Asp Ile Ser Ala Asn Lys Pro Glu

115 120 125

cct ctc aac caa ggt tca tcc tat cat gac aac tgc gac atc aac tat 432

Pro Leu Asn Gln Gly Ser Ser Tyr His Asp Asn Cys Asp Ile Asn Tyr

130 135 140

aat gac caa aat agt atc gag acg tgc cgc att gcc ggt ctc cca gat 480

Asn Asp Gln Asn Ser Ile Glu Thr Cys Arg Ile Ala Gly Leu Pro Asp

145 150 155 160

gtc aag aca gag gat gag act atc cga acc ctc tat aaa gat tgg atc 528

Val Lys Thr Glu Asp Glu Thr Ile Arg Thr Leu Tyr Lys Asp Trp Ile

165 170 175

aag tgg ctt gtt gaa gag tac tct ttc gac ggc att cgc att gac act 576

Lys Trp Leu Val Glu Glu Tyr Ser Phe Asp Gly Ile Arg Ile Asp Thr

180 185 190

gtt aag cat gtt gaa aag agc ttc tgg cct gga ttc gcc gag gcc gca 624

Val Lys His Val Glu Lys Ser Phe Trp Pro Gly Phe Ala Glu Ala Ala

195 200 205

ggg gtc tac tcc atc ggc gaa gtc ttc gac gga ggc cca gac tac ctc 672

Gly Val Tyr Ser Ile Gly Glu Val Phe Asp Gly Gly Pro Asp Tyr Leu

210 215 220

gct ggc tac gcg agc gtt ttg cct ggt ctt ctt aac tat gcc atc tat 720

Ala Gly Tyr Ala Ser Val Leu Pro Gly Leu Leu Asn Tyr Ala Ile Tyr

225 230 235 240

tat ccc atg aac agg ttc tat cag cag gcg ggt tca tcg caa gac ctg 768

Tyr Pro Met Asn Arg Phe Tyr Gln Gln Ala Gly Ser Ser Gln Asp Leu

245 250 255

gct aat atg gtt gac gag gtc tcg tcc aag ttc ccc gac cct tcc gct 816

Ala Asn Met Val Asp Glu Val Ser Ser Lys Phe Pro Asp Pro Ser Ala

260 265 270

ctt ggt act ttc ctc gat aat cac gac aac gcg cgt tgg ctc aac acc 864

Leu Gly Thr Phe Leu Asp Asn His Asp Asn Ala Arg Trp Leu Asn Thr

275 280 285

aag aac gac aag act ctg ctc aag aac gcc ctg gct tat gtg atc ctc 912

Lys Asn Asp Lys Thr Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile Leu

290 295 300

gcc cga ggt atc ccc atc gtc tat tat gga acc gaa cag ggg tac gct 960

Ala Arg Gly Ile Pro Ile Val Tyr Tyr Gly Thr Glu Gln Gly Tyr Ala

305 310 315 320

ggc ggt aac gac cca gcc aac cgc gaa gat ctc tgg cgc agc agc ttc 1008

Gly Gly Asn Asp Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Ser Phe

325 330 335

agc act gat gcg gaa ctt tac caa gcc att aag cgt ctc tct gct gct 1056

Ser Thr Asp Ala Glu Leu Tyr Gln Ala Ile Lys Arg Leu Ser Ala Ala

340 345 350

aga tct gcc gtc ggt ggc cta gct gcg gac gat cat caa cat gtc ctt 1104

Arg Ser Ala Val Gly Gly Leu Ala Ala Asp Asp His Gln His Val Leu

355 360 365

gtg tct gac ggt gtt tac gct tgg aag cgc gct ggt gga gac ctc gtt 1152

Val Ser Asp Gly Val Tyr Ala Trp Lys Arg Ala Gly Gly Asp Leu Val

370 375 380

gtt ctc aca acc aac agt ggt agc agt ggt ggt ggt gag cgt tgc ctg 1200

Val Leu Thr Thr Asn Ser Gly Ser Ser Ser Gly Gly Gly Glu Arg Cys Leu

385 390 395 400

caa act gga cgg gct aac caa aaa tac gat gac gca ttc ggt gat ggc 1248

Gln Thr Gly Arg Ala Asn Gln Lys Tyr Asp Asp Ala Phe Gly Asp Gly

405 410 415

tct tat acc gct gat gga aat ggg cag gtc tgc gtt act atc tcc ggc 1296

Ser Tyr Thr Ala Asp Gly Asn Gly Gln Val Cys Val Thr Ile Ser Gly

420 425 430

ggt aac cct gtg gtg ctg gtg gct tcg gga 1326

Gly Asn Pro Val Val Leu Val Ala Ser Gly

435 440

<210>115

<211>442

<212>PRT

<213> Nectria sp.

<400>115

Ala Asp Thr Ala Ala Trp Lys Ser Arg Asn Ile Tyr Phe Ala Leu Thr

1 5 10 15

Asp Arg Ile Ala Arg Ser Ala Asp Asp Gly Gly Gly Asp Ala Cys Gly

20 25 30

Asn Leu Gly Gln Tyr Cys Gly Gly Thr Phe Lys Gly Leu Glu Gly Lys

35 40 45

Leu Asp Tyr Ile Lys Gly Met Gly Phe Asp Ala Ile Trp Ile Thr Pro

50 55 60

Val Val Gln Asn Ser Pro Gly Gly Tyr His Gly Tyr Trp Ala Thr Asp

65 70 75 80

Leu Tyr Ser Val Asn Ser Glu Tyr Gly Thr Ala Asp Asp Leu Lys Ser

85 90 95

Leu Val Ala Thr Ala His Asp Lys Gly Ile Tyr Ile Met Ala Asp Val

100 105 110

Val Ala Asn His Met Gly Pro Thr Asp Ile Ser Ala Asn Lys Pro Glu

115 120 125

Pro Leu Asn Gln Gly Ser Ser Tyr His Asp Asn Cys Asp Ile Asn Tyr

130 135 140

Asn Asp Gln Asn Ser Ile Glu Thr Cys Arg Ile Ala Gly Leu Pro Asp

145 150 155 160

Val Lys Thr Glu Asp Glu Thr Ile Arg Thr Leu Tyr Lys Asp Trp Ile

165 170 175

Lys Trp Leu Val Glu Glu Tyr Ser Phe Asp Gly Ile Arg Ile Asp Thr

180 185 190

Val Lys His Val Glu Lys Ser Phe Trp Pro Gly Phe Ala Glu Ala Ala

195 200 205

Gly Val Tyr Ser Ile Gly Glu Val Phe Asp Gly Gly Pro Asp Tyr Leu

210 215 220

Ala Gly Tyr Ala Ser Val Leu Pro Gly Leu Leu Asn Tyr Ala Ile Tyr

225 230 235 240

Tyr Pro Met Asn Arg Phe Tyr Gln Gln Ala Gly Ser Ser Gln Asp Leu

245 250 255

Ala Asn Met Val Asp Glu Val Ser Ser Lys Phe Pro Asp Pro Ser Ala

260 265 270

Leu Gly Thr Phe Leu Asp Asn His Asp Asn Ala Arg Trp Leu Asn Thr

275 280 285

Lys Asn Asp Lys Thr Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile Leu

290 295 300

Ala Arg Gly Ile Pro Ile Val Tyr Tyr Gly Thr Glu Gln Gly Tyr Ala

305 310 315 320

Gly Gly Asn Asp Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Ser Phe

325 330 335

Ser Thr Asp Ala Glu Leu Tyr Gln Ala Ile Lys Arg Leu Ser Ala Ala

340 345 350

Arg Ser Ala Val Gly Gly Leu Ala Ala Asp Asp His Gln His Val Leu

355 360 365

Val Ser Asp Gly Val Tyr Ala Trp Lys Arg Ala Gly Gly Asp Leu Val

370 375 380

Val Leu Thr Thr Asn Ser Gly Ser Ser Ser Gly Gly Gly Glu Arg Cys Leu

385 390 395 400

Gln Thr Gly Arg Ala Asn Gln Lys Tyr Asp Asp Ala Phe Gly Asp Gly

405 410 415

Ser Tyr Thr Ala Asp Gly Asn Gly Gln Val Cys Val Thr Ile Ser Gly

420 425 430

Gly Asn Pro Val Val Leu Val Ala Ser Gly

435 440

<210>116

<211>1323

<212>DNA

<213> Fusarium sp.

<220>

<221> CDS

<222>(1)..(1323)

<400>116

gcg gac gca aac gct tgg aag tcg cga aac atc tat ttc gca ctt act 48

Ala Asp Ala Asn Ala Trp Lys Ser Arg Asn Ile Tyr Phe Ala Leu Thr

1 5 10 15

gat cgt gtt gcg cga agc gct gac gat aat ggc ggt agt gca tgc gga 96

Asp Arg Val Ala Arg Ser Ala Asp Asp Asn Gly Gly Ser Ala Cys Gly

20 25 30

aac ctc gga aat tat tgt ggt gga act ttc aag ggt ctc gag tcg aag 144

Asn Leu Gly Asn Tyr Cys Gly Gly Thr Phe Lys Gly Leu Glu Ser Lys

35 40 45

ctt gat tat atc aag ggc atg gga ttt gat gct atc tgg att act ccc 192

Leu Asp Tyr Ile Lys Gly Met Gly Phe Asp Ala Ile Trp Ile Thr Pro

50 55 60

gtt gtt gac aat act gat gga gga tac cac gga tac tgg gcc aag gat 240

Val Val Asp Asn Thr Asp Gly Gly Tyr His Gly Tyr Trp Ala Lys Asp

65 70 75 80

ctt tat gcg gtc aac ccc aag tat ggt act gca gat gac ttg aag agt 288

Leu Tyr Ala Val Asn Pro Lys Tyr Gly Thr Ala Asp Asp Leu Lys Ser

85 90 95

ctt gtc aag tct gct cat gac aag aac atg tac gtc atg tgc gac gtg 336

Leu Val Lys Ser Ala His Asp Lys Asn Met Tyr Val Met Cys Asp Val

100 105 110

gtc gca aac cac atg ggc aaa gga atc tca gac cac aaa ccc tcg ccc 384

Val Ala Asn His Met Gly Lys Gly Ile Ser Asp His Lys Pro Ser Pro

115 120 125

ctc aac gaa caa agc tca tac cac act cct tgc gac atc gac tac agc 432

Leu Asn Glu Gln Ser Ser Tyr His Thr Pro Cys Asp Ile Asp Tyr Ser

130 135 140

aac cag aac agc att gaa cag tgc gaa atc gcc ggt ctt cca gat ctc 480

Asn Gln Asn Ser Ile Glu Gln Cys Glu Ile Ala Gly Leu Pro Asp Leu

145 150 155 160

aac acc ggc agc gac act gtc aag aag gtc ctc tac gac tgg atc aaa 528

Asn Thr Gly Ser Asp Thr Val Lys Lys Val Leu Tyr Asp Trp Ile Lys

165 170 175

tgg ctc gtc tct gag tac agc ttc gac ggt atc cgc atc gac act gtc 576

Trp Leu Val Ser Glu Tyr Ser Phe Asp Gly Ile Arg Ile Asp Thr Val

180 185 190

aag cat gtt gaa aag ccc ttc tgg cct ggt ttc caa gac gcc gct ggt 624

Lys His Val Glu Lys Pro Phe Trp Pro Gly Phe Gln Asp Ala Ala Gly

195 200 205

gtt tac gcc atc ggt gaa gtc tgg gac gga ggt cct gat tat ctc gct 672

Val Tyr Ala Ile Gly Glu Val Trp Asp Gly Gly Pro Asp Tyr Leu Ala

210 215 220

ggt tat gcc cag gtc atg cct ggt ctt ttg aac tac gct atg tac tac 720

Gly Tyr Ala Gln Val Met Pro Gly Leu Leu Asn Tyr Ala Met Tyr Tyr

225 230 235 240

ccc atg aac cgc ttt tac cag caa aag gga gat cct tca gat gtt gtc 768

Pro Met Asn Arg Phe Tyr Gln Gln Lys Gly Asp Pro Ser Asp Val Val

245 250 255

gcc atg cac gat gag att agc aac aaa ttc cct gat ccc act atc ctc 816

Ala Met His Asp Glu Ile Ser Asn Lys Phe Pro Asp Pro Thr Ile Leu

260 265 270

gga aca ttc atc gac aac cac gat aac cct cgt tgg ctc agc cag aag 864

Gly Thr Phe Ile Asp Asn His Asp Asn Pro Arg Trp Leu Ser Gln Lys

275 280 285

aat gac aaa gct ctt ctg aag aac gcc ctc gca tac gtt atc ctt gct 912

Asn Asp Lys Ala Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile Leu Ala

290 295 300

cga gga att ccc atc gtc tac tac gga aca gag caa ggt tac gct ggc 960

Arg Gly Ile Pro Ile Val Tyr Tyr Gly Thr Glu Gln Gly Tyr Ala Gly

305 310 315 320

ggc aat gac ccc gcc aac cgg gaa gat ctc tgg cga agc agt ttc agc 1008

Gly Asn Asp Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Ser Phe Ser

325 330 335

acc aac gca gat ctc tac caa cac atc tcg cgt ctc tct aag gct cgg 1056

Thr Asn Ala Asp Leu Tyr Gln His Ile Ser Arg Leu Ser Lys Ala Arg

340 345 350

tcg gca gtc ggt ggc ctc ggt gga aat gac cac aag cat ctt tac tct 1104

Ser Ala Val Gly Gly Leu Gly Gly Asn Asp His Lys His Leu Tyr Ser

355 360 365

cag aac agc gcc tac gcc tgg agt cgt gcg gac ggc gat ctt atc gtg 1152

Gln Asn Ser Ala Tyr Ala Trp Ser Arg Ala Asp Gly Asp Leu Ile Val

370 375 380

ctt acg ttg aac cgc ggt cag gga tac tca gga cag tac tgc ttc aac 1200

Leu Thr Leu Asn Arg Gly Gln Gly Tyr Ser Gly Gln Tyr Cys Phe Asn

385 390 395 400

act gga aag aac aac aag act tgg gac aag gta ttt gga agt ggc act 1248

Thr Gly Lys Asn Asn Lys Thr Trp Asp Lys Val Phe Gly Ser Gly Thr

405 410 415

gtt acc tct gat ggc aat gga cag gtt tgc gtt agc tac act aac ggt 1296

Val Thr Ser Asp Gly Asn Gly Gln Val Cys Val Ser Tyr Thr Asn Gly

420 425 430

gag cct gag gtc ttg gtt gcc tct agc 1323

Glu Pro Glu Val Leu Val Ala Ser Ser

435 440

<210>117

<211>441

<212>PRT

<213> Fusarium sp.

<400>117

Ala Asp Ala Asn Ala Trp Lys Ser Arg Asn Ile Tyr Phe Ala Leu Thr

1 5 10 15

Asp Arg Val Ala Arg Ser Ala Asp Asp Asn Gly Gly Ser Ala Cys Gly

20 25 30

Asn Leu Gly Asn Tyr Cys Gly Gly Thr Phe Lys Gly Leu Glu Ser Lys

35 40 45

Leu Asp Tyr Ile Lys Gly Met Gly Phe Asp Ala Ile Trp Ile Thr Pro

50 55 60

Val Val Asp Asn Thr Asp Gly Gly Tyr His Gly Tyr Trp Ala Lys Asp

65 70 75 80

Leu Tyr Ala Val Asn Pro Lys Tyr Gly Thr Ala Asp Asp Leu Lys Ser

85 90 95

Leu Val Lys Ser Ala His Asp Lys Asn Met Tyr Val Met Cys Asp Val

100 105 110

Val Ala Asn His Met Gly Lys Gly Ile Ser Asp His Lys Pro Ser Pro

115 120 125

Leu Asn Glu Gln Ser Ser Tyr His Thr Pro Cys Asp Ile Asp Tyr Ser

130 135 140

Asn Gln Asn Ser Ile Glu Gln Cys Glu Ile Ala Gly Leu Pro Asp Leu

145 150 155 160

Asn Thr Gly Ser Asp Thr Val Lys Lys Val Leu Tyr Asp Trp Ile Lys

165 170 175

Trp Leu Val Ser Glu Tyr Ser Phe Asp Gly Ile Arg Ile Asp Thr Val

180 185 190

Lys His Val Glu Lys Pro Phe Trp Pro Gly Phe Gln Asp Ala Ala Gly

195 200 205

Val Tyr Ala Ile Gly Glu Val Trp Asp Gly Gly Pro Asp Tyr Leu Ala

210 215 220

Gly Tyr Ala Gln Val Met Pro Gly Leu Leu Asn Tyr Ala Met Tyr Tyr

225 230 235 240

Pro Met Asn Arg Phe Tyr Gln Gln Lys Gly Asp Pro Ser Asp Val Val

245 250 255

Ala Met His Asp Glu Ile Ser Asn Lys Phe Pro Asp Pro Thr Ile Leu

260 265 270

Gly Thr Phe Ile Asp Asn His Asp Asn Pro Arg Trp Leu Ser Gln Lys

275 280 285

Asn Asp Lys Ala Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile Leu Ala

290 295 300

Arg Gly Ile Pro Ile Val Tyr Tyr Gly Thr Glu Gln Gly Tyr Ala Gly

305 310 315 320

Gly Asn Asp Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Ser Phe Ser

325 330 335

Thr Asn Ala Asp Leu Tyr Gln His Ile Ser Arg Leu Ser Lys Ala Arg

340 345 350

Ser Ala Val Gly Gly Leu Gly Gly Asn Asp His Lys His Leu Tyr Ser

355 360 365

Gln Asn Ser Ala Tyr Ala Trp Ser Arg Ala Asp Gly Asp Leu Ile Val

370 375 380

Leu Thr Leu Asn Arg Gly Gln Gly Tyr Ser Gly Gln Tyr Cys Phe Asn

385 390 395 400

Thr Gly Lys Asn Asn Lys Thr Trp Asp Lys Val Phe Gly Ser Gly Thr

405 410 415

Val Thr Ser Asp Gly Asn Gly Gln Val Cys Val Ser Tyr Thr Asn Gly

420 425 430

Glu Pro Glu Val Leu Val Ala Ser Ser

435 440

<210>118

<211>1371

<212>DNA

<213> Trametes currogata

<220>

<221> CDS

<222>(1)..(1371)

<400>118

gcg gat acg agt gca tgg aag tcc cgc agc atc tac ttc gtt ctg acc 48

Ala Asp Thr Ser Ala Trp Lys Ser Arg Ser Ile Tyr Phe Val Leu Thr

1 5 10 15

gat cgt gtt gct cga agc agc agc gac acc ggc ggt tcc tct tgc agc 96

Asp Arg Val Ala Arg Ser Ser Ser Asp Thr Gly Gly Ser Ser Cys Ser

20 25 30

aac ctg ggc aat tac tgt gga gga act ttc aaa ggt ctc gaa tct aag 144

Asn Leu Gly Asn Tyr Cys Gly Gly Thr Phe Lys Gly Leu Glu Ser Lys

35 40 45

ctg gat tac atc caa ggc ttg ggc ttt gac gct atc tgg atc acg cct 192

Leu Asp Tyr Ile Gln Gly Leu Gly Phe Asp Ala Ile Trp Ile Thr Pro

50 55 60

gtc gtt gct aac agt gct ggt ggc tac cat ggc tat tgg gca caa gac 240

Val Val Ala Asn Ser Ala Gly Gly Tyr His Gly Tyr Trp Ala Gln Asp

65 70 75 80

ttg tat tct gtc aac tcg aat tat ggt act gca gac gac cta aag agc 288

Leu Tyr Ser Val Asn Ser Asn Tyr Gly Thr Ala Asp Asp Leu Lys Ser

85 90 95

ctg gtc agc tct gct cat gcg aag ggca ata tat gtg atg gtc gat gtc 336

Leu Val Ser Ser Ala His Ala Lys Gly Ile Tyr Val Met Val Asp Val

100 105 110

gta gcc aat cat atg ggt aac ggt gca att gcc gat aac cgc cct gag 384

Val Ala Asn His Met Gly Asn Gly Ala Ile Ala Asp Asn Arg Pro Glu

115 120 125

cct ttg aac cag gct tca tcc tac cac cca gcc tgc gac atc aac tac 432

Pro Leu Asn Gln Ala Ser Ser Tyr His Pro Ala Cys Asp Ile Asn Tyr

130 135 140

gat aac cag acc agc atc gag cag tgc agc atc ggc ggt ctt gct gat 480

Asp Asn Gln Thr Ser Ile Glu Gln Cys Ser Ile Gly Gly Leu Ala Asp

145 150 155 160

ctt aac act gag agt acc gag gtt cgc act gtt ctc aac acc tgg gtt 528

Leu Asn Thr Glu Ser Thr Glu Val Arg Thr Val Leu Asn Thr Trp Val

165 170 175

tca tgg ctc gtc gac gag tac agc ttc gac gga gta cgt atc gac aca 576

Ser Trp Leu Val Asp Glu Tyr Ser Phe Asp Gly Val Arg Ile Asp Thr

180 185 190

gtc aag cac gtt caa aag gac ttc tgg cca gac ttc gtg tct tcc ata 624

Val Lys His Val Gln Lys Asp Phe Trp Pro Asp Phe Val Ser Ser Ile

195 200 205

ggc gaa tac agc atc ggt gag gtg ttt gac ggc aac cct cca tac ctc 672

Gly Glu Tyr Ser Ile Gly Glu Val Phe Asp Gly Asn Pro Pro Tyr Leu

210 215 220

gct gag tat gcc aag ctc atg cct ggg gtt cta aac tat gca gtc tac 720

Ala Glu Tyr Ala Lys Leu Met Pro Gly Val Leu Asn Tyr Ala Val Tyr

225 230 235 240

tac ccc atg aat gcc ttc tac cag caa acg ggc tca tct cag gca ctg 768

Tyr Pro Met Asn Ala Phe Tyr Gln Gln Thr Gly Ser Ser Gln Ala Leu

245 250 255

gtc gac atg atg aac acg att agc agc aca ttc cca gac ccc tca gca 816

Val Asp Met Met Asn Thr Ile Ser Ser Ser Thr Phe Pro Asp Pro Ser Ala

260 265 270

ctc ggc acg ttc ctc gac aac cac gac aac ccg cgc tgg cta aac gtg 864

Leu Gly Thr Phe Leu Asp Asn His Asp Asn Pro Arg Trp Leu Asn Val

275 280 285

aag aac gac cag aca ctc ctg aag aac gca cta gcc tac gtc att cta 912

Lys Asn Asp Gln Thr Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile Leu

290 295 300

gcc cga ggc att ccc atc cta tac tac ggc acc gag caa ggt tac tcc 960

Ala Arg Gly Ile Pro Ile Leu Tyr Tyr Gly Thr Glu Gln Gly Tyr Ser

305 310 315 320

gga ggc gcc gac cca gca aac cgc gaa gat ctt tgg cgc agc agc ttc 1008

Gly Gly Ala Asp Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Ser Phe

325 330 335

aat aca aac gcg gac ctc tac caa tcc atc aaa aag ctc acc gca gcc 1056

Asn Thr Asn Ala Asp Leu Tyr Gln Ser Ile Lys Lys Leu Thr Ala Ala

340 345 350

cga aaa gcc gcc ggc ggc ctc gcc ggc aac gac cac acg cat ctc tac 1104

Arg Lys Ala Ala Gly Gly Leu Ala Gly Asn Asp His Thr His Leu Tyr

355 360 365

gtc gcc gac acg gca tat gcc tgg agc cgg gca aac ggc gcc ctc atc 1152

Val Ala Asp Thr Ala Tyr Ala Trp Ser Arg Ala Asn Gly Ala Leu Ile

370 375 380

gtg ctc acc acc aac gcc ggc agc agc tcc aac gcg caa cac tgc ttc 1200

Val Leu Thr Thr Asn Ala Gly Ser Ser Ser Ser Asn Ala Gln His Cys Phe

385 390 395 400

aac acg cag atg gca aac ggg aaa tgg acg aac acg tat ggt gat ggc 1248

Asn Thr Gln Met Ala Asn Gly Lys Trp Thr Asn Thr Tyr Gly Asp Gly

405 410 415

gca acg gtg acc gcg gat tcc agc ggt aat atc tgc gtc acc gtt agc 1296

Ala Thr Val Thr Ala Asp Ser Ser Gly Asn Ile Cys Val Thr Val Ser

420 425 430

aac ggc gag cct gtt gtc ctc gtc gcc agc gca tca aca acg ggg gtt 1344

Asn Gly Glu Pro Val Val Leu Val Ala Ser Ala Ser Thr Thr Gly Val

435 440 445

acg ccc act aca gct aca acg ctg cgc 1371

Thr Pro Thr Thr Ala Thr Thr Leu Arg

450 455

<210>119

<211>457

<212>PRT

<213> Trametes currogata

<400>119

Ala Asp Thr Ser Ala Trp Lys Ser Arg Ser Ile Tyr Phe Val Leu Thr

1 5 10 15

Asp Arg Val Ala Arg Ser Ser Ser Asp Thr Gly Gly Ser Ser Cys Ser

20 25 30

Asn Leu Gly Asn Tyr Cys Gly Gly Thr Phe Lys Gly Leu Glu Ser Lys

35 40 45

Leu Asp Tyr Ile Gln Gly Leu Gly Phe Asp Ala Ile Trp Ile Thr Pro

50 55 60

Val Val Ala Asn Ser Ala Gly Gly Tyr His Gly Tyr Trp Ala Gln Asp

65 70 75 80

Leu Tyr Ser Val Asn Ser Asn Tyr Gly Thr Ala Asp Asp Leu Lys Ser

85 90 95

Leu Val Ser Ser Ala His Ala Lys Gly Ile Tyr Val Met Val Asp Val

100 105 110

Val Ala Asn His Met Gly Asn Gly Ala Ile Ala Asp Asn Arg Pro Glu

115 120 125

Pro Leu Asn Gln Ala Ser Ser Tyr His Pro Ala Cys Asp Ile Asn Tyr

130 135 140

Asp Asn Gln Thr Ser Ile Glu Gln Cys Ser Ile Gly Gly Leu Ala Asp

145 150 155 160

Leu Asn Thr Glu Ser Thr Glu Val Arg Thr Val Leu Asn Thr Trp Val

165 170 175

Ser Trp Leu Val Asp Glu Tyr Ser Phe Asp Gly Val Arg Ile Asp Thr

180 185 190

Val Lys His Val Gln Lys Asp Phe Trp Pro Asp Phe Val Ser Ser Ile

195 200 205

Gly Glu Tyr Ser Ile Gly Glu Val Phe Asp Gly Asn Pro Pro Tyr Leu

210 215 220

Ala Glu Tyr Ala Lys Leu Met Pro Gly Val Leu Asn Tyr Ala Val Tyr

225 230 235 240

Tyr Pro Met Asn Ala Phe Tyr Gln Gln Thr Gly Ser Ser Gln Ala Leu

245 250 255

Val Asp Met Met Asn Thr Ile Ser Ser Ser Thr Phe Pro Asp Pro Ser Ala

260 265 270

Leu Gly Thr Phe Leu Asp Asn His Asp Asn Pro Arg Trp Leu Asn Val

275 280 285

Lys Asn Asp Gln Thr Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile Leu

290 295 300

Ala Arg Gly Ile Pro Ile Leu Tyr Tyr Gly Thr Glu Gln Gly Tyr Ser

305 310 315 320

Gly Gly Ala Asp Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Ser Phe

325 330 335

Asn Thr Asn Ala Asp Leu Tyr Gln Ser Ile Lys Lys Leu Thr Ala Ala

340 345 350

Arg Lys Ala Ala Gly Gly Leu Ala Gly Asn Asp His Thr His Leu Tyr

355 360 365

Val Ala Asp Thr Ala Tyr Ala Trp Ser Arg Ala Asn Gly Ala Leu Ile

370 375 380

Val Leu Thr Thr Asn Ala Gly Ser Ser Ser Ser Asn Ala Gln His Cys Phe

385 390 395 400

Asn Thr Gln Met Ala Asn Gly Lys Trp Thr Asn Thr Tyr Gly Asp Gly

405 410 415

Ala Thr Val Thr Ala Asp Ser Ser Gly Asn Ile Cys Val Thr Val Ser

420 425 430

Asn Gly Glu Pro Val Val Leu Val Ala Ser Ala Ser Thr Thr Gly Val

435 440 445

Thr Pro Thr Thr Ala Thr Thr Leu Arg

450 455

<210>120

<211>1428

<212>DNA

<213> Penicillium sp.

<220>

<221> CDS

<222>(1)..(1428)

<400>120

gca gaa tgg cgc agt cag tcg atc tac ttt ctt cta act gat cgc ttt 48

Ala Glu Trp Arg Ser Gln Ser Ile Tyr Phe Leu Leu Thr Asp Arg Phe

1 5 10 15

ggc cga acg gac aat tcc acc acg gca gca tgc aat gtc agc gat cgg 96

Gly Arg Thr Asp Asn Ser Thr Thr Ala Ala Cys Asn Val Ser Asp Arg

20 25 30

gtc tac tgt ggt ggc agc tgg caa gga atc atc aat cac ttg gat tac 144

Val Tyr Cys Gly Gly Ser Trp Gln Gly Ile Ile Asn His Leu Asp Tyr

35 40 45

att cag ggc atg gga ttc acc gcg att tgg att acc cct gtc aca gaa 192

Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Thr Pro Val Thr Glu

50 55 60

cag ctc tct caa gac act gga gat ggc gag gca tac cac gga tac tgg 240

Gln Leu Ser Gln Asp Thr Gly Asp Gly Glu Ala Tyr His Gly Tyr Trp

65 70 75 80

caa caa gag ata tac aac gtc aac aca aac tat ggc act gct gct gac 288

Gln Gln Glu Ile Tyr Asn Val Asn Thr Asn Tyr Gly Thr Ala Ala Asp

85 90 95

ctt ttg gca ctt tct aaa gcc ctg cac agt cgt ggc atg tac ctc atg 336

Leu Leu Ala Leu Ser Lys Ala Leu His Ser Arg Gly Met Tyr Leu Met

100 105 110

gta gac gtg gtt gca aac cac atg ggc tat gat gga gct gga aat act 384

Val Asp Val Val Ala Asn His Met Gly Tyr Asp Gly Ala Gly Asn Thr

115 120 125

gtt gac tac agt gtc ttt aat cca ttc gac tct tcg tct tac ttc cac 432

Val Asp Tyr Ser Val Phe Asn Pro Phe Asp Ser Ser Ser Tyr Phe His

130 135 140

tcg tat tgt gag atc agc gat tac tct gat cag aca aac gtg gag gac 480

Ser Tyr Cys Glu Ile Ser Asp Tyr Ser Asp Gln Thr Asn Val Glu Asp

145 150 155 160

tgt tgg ctt gga gac act aca gtt tct ctt cca gat ctc gac acg acc 528

Cys Trp Leu Gly Asp Thr Thr Val Ser Leu Pro Asp Leu Asp Thr Thr

165 170 175

ctt act tct gtt cag acg atc tgg tat aac tgg gtc act gaa ttg gtg 576

Leu Thr Ser Val Gln Thr Ile Trp Tyr Asn Trp Val Thr Glu Leu Val

180 185 190

tcc aac tac tcc att gat ggt ttg cga att gat aca gtc aaa cac gtg 624

Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Val Lys His Val

195 200 205

cag aag tcg ttc tgg ccg ggc tac aac agt gct gca ggt gtc tac tgt 672

Gln Lys Ser Phe Trp Pro Gly Tyr Asn Ser Ala Ala Gly Val Tyr Cys

210 215 220

gtg gga gag gtg ttt gat ggg gac cca gca tac act tgc ccc tac cag 720

Val Gly Glu Val Phe Asp Gly Asp Pro Ala Tyr Thr Cys Pro Tyr Gln

225 230 235 240

agc tac ctc gat ggt gtt ctg aac tat ccg att tat tac caa ctg ctg 768

Ser Tyr Leu Asp Gly Val Leu Asn Tyr Pro Ile Tyr Tyr Gln Leu Leu

245 250 255

tac gca ttc gag tcg aca agt ggc agt atc agc ggt cta tat aat atg 816

Tyr Ala Phe Glu Ser Thr Ser Gly Ser Ile Ser Gly Leu Tyr Asn Met

260 265 270

atc aac tcc gtt gca tct gac tgt tcc gat cca acc ttg ctc gga aac 864

Ile Asn Ser Val Ala Ser Asp Cys Ser Asp Pro Thr Leu Leu Gly Asn

275 280 285

ttc atc gag aat cat gac aac cca cgc ttt gct tcc tac acg agc gat 912

Phe Ile Glu Asn His Asp Asn Pro Arg Phe Ala Ser Tyr Thr Ser Asp

290 295 300

tat tct caa gcg aag aat gtg att tct ttc atc ttc ttc tcg gat ggt 960

Tyr Ser Gln Ala Lys Asn Val Ile Ser Phe Ile Phe Phe Ser Asp Gly

305 310 315 320

att cca atc gtc tat gct ggc cag gaa caa cac tat agc ggt ggc agt 1008

Ile Pro Ile Val Tyr Ala Gly Gln Glu Gln His Tyr Ser Gly Gly Ser

325 330 335

gac cct gcc aat cgt gaa gca act tgg cta tcc gga tac gac aag aca 1056

Asp Pro Ala Asn Arg Glu Ala Thr Trp Leu Ser Gly Tyr Asp Lys Thr

340 345 350

gct cag ctt tac acc tac atc acc acc aca aac aag atc cgt gcc cta 1104

Ala Gln Leu Tyr Thr Tyr Ile Thr Thr Thr Asn Lys Ile Arg Ala Leu

355 360 365

gcc att tca aag gac agc gcc tac ata agt tcc aag aat aat gct ttc 1152

Ala Ile Ser Lys Asp Ser Ala Tyr Ile Ser Ser Lys Asn Asn Ala Phe

370 375 380

tac act gat agc aat act att gcc atg aag aaa gga tct agc ggc tcg 1200

Tyr Thr Asp Ser Asn Thr Ile Ala Met Lys Lys Gly Ser Ser Gly Ser

385 390 395 400

caa gtt ata act gtt ctt tca aac cgt ggc tca tcg ggt agc tcg tat 1248

Gln Val Ile Thr Val Leu Ser Asn Arg Gly Ser Ser Gly Ser Ser Tyr

405 410 415

acc ttg act ctt agc gga agc ggt tac tcg tct ggc acg aag ctc atg 1296

Thr Leu Thr Leu Ser Gly Ser Gly Tyr Ser Ser Gly Thr Lys Leu Met

420 425 430

gag atg tac acc tgc aca gcc gtg act gtg gac tct agt ggc aac atc 1344

Glu Met Tyr Thr Cys Thr Ala Val Thr Val Asp Ser Ser Gly Asn Ile

435 440 445

gcc gtg ccg atg gct tcc gga ctc cct cga gtc tac atg ctt gct tcc 1392

Ala Val Pro Met Ala Ser Gly Leu Pro Arg Val Tyr Met Leu Ala Ser

450 455 460

tcg gct tgc tct att tgc agt tct gcc tgt tca gca 1428

Ser Ala Cys Ser Ile Cys Ser Ser Ala Cys Ser Ala

465 470 475

<210>121

<211>476

<212>PRT

<213> Penicillium sp.

<400>121

Ala Glu Trp Arg Ser Gln Ser Ile Tyr Phe Leu Leu Thr Asp Arg Phe

1 5 10 15

Gly Arg Thr Asp Asn Ser Thr Thr Ala Ala Cys Asn Val Ser Asp Arg

20 25 30

Val Tyr Cys Gly Gly Ser Trp Gln Gly Ile Ile Asn His Leu Asp Tyr

35 40 45

Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Thr Pro Val Thr Glu

50 55 60

Gln Leu Ser Gln Asp Thr Gly Asp Gly Glu Ala Tyr His Gly Tyr Trp

65 70 75 80

Gln Gln Glu Ile Tyr Asn Val Asn Thr Asn Tyr Gly Thr Ala Ala Asp

85 90 95

Leu Leu Ala Leu Ser Lys Ala Leu His Ser Arg Gly Met Tyr Leu Met

100 105 110

Val Asp Val Val Ala Asn His Met Gly Tyr Asp Gly Ala Gly Asn Thr

115 120 125

Val Asp Tyr Ser Val Phe Asn Pro Phe Asp Ser Ser Ser Tyr Phe His

130 135 140

Ser Tyr Cys Glu Ile Ser Asp Tyr Ser Asp Gln Thr Asn Val Glu Asp

145 150 155 160

Cys Trp Leu Gly Asp Thr Thr Val Ser Leu Pro Asp Leu Asp Thr Thr

165 170 175

Leu Thr Ser Val Gln Thr Ile Trp Tyr Asn Trp Val Thr Glu Leu Val

180 185 190

Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr Val Lys His Val

195 200 205

Gln Lys Ser Phe Trp Pro Gly Tyr Asn Ser Ala Ala Gly Val Tyr Cys

210 215 220

Val Gly Glu Val Phe Asp Gly Asp Pro Ala Tyr Thr Cys Pro Tyr Gln

225 230 235 240

Ser Tyr Leu Asp Gly Val Leu Asn Tyr Pro Ile Tyr Tyr Gln Leu Leu

245 250 255

Tyr Ala Phe Glu Ser Thr Ser Gly Ser Ile Ser Gly Leu Tyr Asn Met

260 265 270

Ile Asn Ser Val Ala Ser Asp Cys Ser Asp Pro Thr Leu Leu Gly Asn

275 280 285

Phe Ile Glu Asn His Asp Asn Pro Arg Phe Ala Ser Tyr Thr Ser Asp

290 295 300

Tyr Ser Gln Ala Lys Asn Val Ile Ser Phe Ile Phe Phe Ser Asp Gly

305 310 315 320

Ile Pro Ile Val Tyr Ala Gly Gln Glu Gln His Tyr Ser Gly Gly Ser

325 330 335

Asp Pro Ala Asn Arg Glu Ala Thr Trp Leu Ser Gly Tyr Asp Lys Thr

340 345 350

Ala Gln Leu Tyr Thr Tyr Ile Thr Thr Thr Asn Lys Ile Arg Ala Leu

355 360 365

Ala Ile Ser Lys Asp Ser Ala Tyr Ile Ser Ser Lys Asn Asn Ala Phe

370 375 380

Tyr Thr Asp Ser Asn Thr Ile Ala Met Lys Lys Gly Ser Ser Gly Ser

385 390 395 400

Gln Val Ile Thr Val Leu Ser Asn Arg Gly Ser Ser Gly Ser Ser Tyr

405 410 415

Thr Leu Thr Leu Ser Gly Ser Gly Tyr Ser Ser Gly Thr Lys Leu Met

420 425 430

Glu Met Tyr Thr Cys Thr Ala Val Thr Val Asp Ser Ser Gly Asn Ile

435 440 445

Ala Val Pro Met Ala Ser Gly Leu Pro Arg Val Tyr Met Leu Ala Ser

450 455 460

Ser Ala Cys Ser Ile Cys Ser Ser Ala Cys Ser Ala

465 470 475

<210>122

<211>1353

<212>DNA

<213>Valsaria spartii

<220>

<221> CDS

<222>(1)..(1353)

<400>122

gcc agc aac gcg gat tgg aaa tcg cgc aac atc tac ttt gcc ttg acg 48

Ala Ser Asn Ala Asp Trp Lys Ser Arg Asn Ile Tyr Phe Ala Leu Thr

1 5 10 15

gac cgc gtc gct ggt cct acc ggg gga tca tgc ggc aac ctg gga aac 96

Asp Arg Val Ala Gly Pro Thr Gly Gly Ser Cys Gly Asn Leu Gly Asn

20 25 30

tac tgc ggc ggt acc tgg aac gga ttg acg gat aag ttg gac tac atc 144

Tyr Cys Gly Gly Thr Trp Asn Gly Leu Thr Asp Lys Leu Asp Tyr Ile

35 40 45

cag ggc atg gga ttc gat gcc atc tgg atc acc ccg gtc atc aag aac 192

Gln Gly Met Gly Phe Asp Ala Ile Trp Ile Thr Pro Val Ile Lys Asn

50 55 60

agc ccc ggc ggt tat cac gga tat tgg gct caa gat ctc tac agc gtg 240

Ser Pro Gly Gly Tyr His Gly Tyr Trp Ala Gln Asp Leu Tyr Ser Val

65 70 75 80

aac gag aac tat ggc act gcg caa gat ctg aag gat ttc gta aat gcg 288

Asn Glu Asn Tyr Gly Thr Ala Gln Asp Leu Lys Asp Phe Val Asn Ala

85 90 95

gcg cac gca aag ggg atc tac gtc atg gtc gac gtg gtc gca aac cac 336

Ala His Ala Lys Gly Ile Tyr Val Met Val Asp Val Val Ala Asn His

100 105 110

atg ggc aac ggt gga atc tca act ctc tcc cca cct ccc ttg aac cag 384

Met Gly Asn Gly Gly Ile Ser Thr Leu Ser Pro Pro Pro Leu Asn Gln

115 120 125

gag agt tcc tat cac tcc aaa tgc aac atc gac tac agc agc caa aac 432

Glu Ser Ser Tyr His Ser Lys Cys Asn Ile Asp Tyr Ser Ser Gln Asn

130 135 140

agc atc gag aat tgc tgg atc gct gac ctg ccc gac ctc gtc acc acc 480

Ser Ile Glu Asn Cys Trp Ile Ala Asp Leu Pro Asp Leu Val Thr Thr

145 150 155 160

gac aac acc atc cgc gat gtc ttc aag gac tgg atc gcc aac ctc acc 528

Asp Asn Thr Ile Arg Asp Val Phe Lys Asp Trp Ile Ala Asn Leu Thr

165 170 175

acc acc tac tcc ttc gac ggc ctc cgc gtc gac acc gtc aag cat gta 576

Thr Thr Tyr Ser Phe Asp Gly Leu Arg Val Asp Thr Val Lys His Val

180 185 190

gag aag gac ttt tgg ccg ggc ttc gtc gag gct gcc ggc atg tat gcc 624

Glu Lys Asp Phe Trp Pro Gly Phe Val Glu Ala Ala Gly Met Tyr Ala

195 200 205

atc ggc gag gtt ctc gat ggc ggc acc tcc tac gtt gcc ggc tac cag 672

Ile Gly Glu Val Leu Asp Gly Gly Thr Ser Tyr Val Ala Gly Tyr Gln

210 215 220

agc gtg atg cca ggc ctt ctc aac tat ccc atg tac tat cct ctc atc 720

Ser Val Met Pro Gly Leu Leu Asn Tyr Pro Met Tyr Tyr Pro Leu Ile

225 230 235 240

cgc acc ttt acc cag ggc gcc tcc ttc aac gac ttc gtc aac agt cac 768

Arg Thr Phe Thr Gln Gly Ala Ser Phe Asn Asp Phe Val Asn Ser His

245 250 255

aac gag gtt ggt tcc gga ttc tcc gat ccc acc ctc ctc ggc acc ttc 816

Asn Glu Val Gly Ser Gly Phe Ser Asp Pro Thr Leu Leu Gly Thr Phe

260 265 270

atc gac aac cac gac cag cag cgc ttc ctc tac aag aac agc gac cac 864

Ile Asp Asn His Asp Gln Gln Arg Phe Leu Tyr Lys Asn Ser Asp His

275 280 285

gcc ctc ttg aag aac gct ctg gcc tac gtg atc ctt ggc cga ggt atc 912

Ala Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile Leu Gly Arg Gly Ile

290 295 300

cca atc gtg tac tac ggc acc gag caa gcc tac ggc ggt ggt gac gac 960

Pro Ile Val Tyr Tyr Gly Thr Glu Gln Ala Tyr Gly Gly Gly Asp Asp

305 310 315 320

ccg gcg aac cgc gag gac ctc tgg cga agc ggc tac tcc acc acc tcc 1008

Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Gly Tyr Ser Thr Thr Ser

325 330 335

gag ata tac acc acc atc tcg ggc cta tcc tcc gct cgc aaa tcc gcc 1056

Glu Ile Tyr Thr Thr Ile Ser Gly Leu Ser Ser Ala Arg Lys Ser Ala

340 345 350

ggc ggc ctc cca ggc aac gac cac tcc cac ctc tac acc acc aac aac 1104

Gly Gly Leu Pro Gly Asn Asp His Ser His Leu Tyr Thr Thr Asn Asn

355 360 365

gcg tac gcc tgg tcc cgc gcg gac ggg aag gtg atc gcg ttg gtg acc 1152

Ala Tyr Ala Trp Ser Arg Ala Asp Gly Lys Val Ile Ala Leu Val Thr

370 375 380

aac gcc ggc ggc tcc gac acc agc acc cac tgc ttc aac acc aag aaa 1200

Asn Ala Gly Gly Ser Asp Thr Ser Thr His Cys Phe Asn Thr Lys Lys

385 390 395 400

ccg agc ggc acg cgc tgg acc agc gtc ctc cgc agc ggc gga acc agc 1248

Pro Ser Gly Thr Arg Trp Thr Ser Val Leu Arg Ser Gly Gly Thr Ser

405 410 415

tac acc gcc gac ggc aac ggc caa atc tgc atc cag atc caa aac ggc 1296

Tyr Thr Ala Asp Gly Asn Gly Gln Ile Cys Ile Gln Ile Gln Asn Gly

420 425 430

ggg ccc gag gca atc gtc ctc tcc acc ggc acc ggc acc gaa acc aca 1344

Gly Pro Glu Ala Ile Val Leu Ser Thr Gly Thr Gly Thr Glu Thr Thr

435 440 445

tcc agc gcc 1353

Ser Ser Ala

450

<210>123

<211>451

<212>PRT

<213>Valsaria spartii

<400>123

Ala Ser Asn Ala Asp Trp Lys Ser Arg Asn Ile Tyr Phe Ala Leu Thr

1 5 10 15

Asp Arg Val Ala Gly Pro Thr Gly Gly Ser Cys Gly Asn Leu Gly Asn

20 25 30

Tyr Cys Gly Gly Thr Trp Asn Gly Leu Thr Asp Lys Leu Asp Tyr Ile

35 40 45

Gln Gly Met Gly Phe Asp Ala Ile Trp Ile Thr Pro Val Ile Lys Asn

50 55 60

Ser Pro Gly Gly Tyr His Gly Tyr Trp Ala Gln Asp Leu Tyr Ser Val

65 70 75 80

Asn Glu Asn Tyr Gly Thr Ala Gln Asp Leu Lys Asp Phe Val Asn Ala

85 90 95

Ala His Ala Lys Gly Ile Tyr Val Met Val Asp Val Val Ala Asn His

100 105 110

Met Gly Asn Gly Gly Ile Ser Thr Leu Ser Pro Pro Pro Leu Asn Gln

115 120 125

Glu Ser Ser Tyr His Ser Lys Cys Asn Ile Asp Tyr Ser Ser Gln Asn

130 135 140

Ser Ile Glu Asn Cys Trp Ile Ala Asp Leu Pro Asp Leu Val Thr Thr

145 150 155 160

Asp Asn Thr Ile Arg Asp Val Phe Lys Asp Trp Ile Ala Asn Leu Thr

165 170 175

Thr Thr Tyr Ser Phe Asp Gly Leu Arg Val Asp Thr Val Lys His Val

180 185 190

Glu Lys Asp Phe Trp Pro Gly Phe Val Glu Ala Ala Gly Met Tyr Ala

195 200 205

Ile Gly Glu Val Leu Asp Gly Gly Thr Ser Tyr Val Ala Gly Tyr Gln

210 215 220

Ser Val Met Pro Gly Leu Leu Asn Tyr Pro Met Tyr Tyr Pro Leu Ile

225 230 235 240

Arg Thr Phe Thr Gln Gly Ala Ser Phe Asn Asp Phe Val Asn Ser His

245 250 255

Asn Glu Val Gly Ser Gly Phe Ser Asp Pro Thr Leu Leu Gly Thr Phe

260 265 270

Ile Asp Asn His Asp Gln Gln Arg Phe Leu Tyr Lys Asn Ser Asp His

275 280 285

Ala Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile Leu Gly Arg Gly Ile

290 295 300

Pro Ile Val Tyr Tyr Gly Thr Glu Gln Ala Tyr Gly Gly Gly Asp Asp

305 310 315 320

Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Gly Tyr Ser Thr Thr Ser

325 330 335

Glu Ile Tyr Thr Thr Ile Ser Gly Leu Ser Ser Ala Arg Lys Ser Ala

340 345 350

Gly Gly Leu Pro Gly Asn Asp His Ser His Leu Tyr Thr Thr Asn Asn

355 360 365

Ala Tyr Ala Trp Ser Arg Ala Asp Gly Lys Val Ile Ala Leu Val Thr

370 375 380

Asn Ala Gly Gly Ser Asp Thr Ser Thr His Cys Phe Asn Thr Lys Lys

385 390 395 400

Pro Ser Gly Thr Arg Trp Thr Ser Val Leu Arg Ser Gly Gly Thr Ser

405 410 415

Tyr Thr Ala Asp Gly Asn Gly Gln Ile Cys Il e Gln Ile Gln Asn Gly

420 425 430

Gly Pro Glu Ala Ile Val Leu Ser Thr Gly Thr Gly Thr Glu Thr Thr

435 440 445

Ser Ser Ala

450

<210>124

<211>1431

<212>DNA

<213> Thermoascus auranticus

<220>

<221> CDS

<222>(1)..(1431)

<400>124

gcc acg cca gcc caa tgg cgc tct cga tca gta tac ttc ctt ctg acg 48

Ala Thr Pro Ala Gln Trp Arg Ser Arg Ser Val Tyr Phe Leu Leu Thr

1 5 10 15

gac agg ttt gca agg agt gat ggg tca acc acc gct gcc tgt gac acc 96

Asp Arg Phe Ala Arg Ser Asp Gly Ser Thr Thr Ala Ala Cys Asp Thr

20 25 30

agt gca agg caa tac tgc ggc gga act tgg cag ggg ata atc gac cat 144

Ser Ala Arg Gln Tyr Cys Gly Gly Thr Trp Gln Gly Ile Ile Asp His

35 40 45

ctc gac tat atc caa gga atg gga ttc act gct att tgg att tcc ccc 192

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Ser Pro

50 55 60

gtc acc gaa cag ctg cct cag gat acg gga gat ggg aca gcg tat cat 240

Val Thr Glu Gln Leu Pro Gln Asp Thr Gly Asp Gly Thr Ala Tyr His

65 70 75 80

ggc tac tgg cag caa gat att tac tcc ctg aat ccc aac ttt ggc aca 288

Gly Tyr Trp Gln Gln Asp Ile Tyr Ser Leu Asn Pro Asn Phe Gly Thr

85 90 95

gcc gac gac ctc cgc gcg ctc gca gac gct ctc cat gca cgc gga atg 336

Ala Asp Asp Leu Arg Ala Leu Ala Asp Ala Leu His Ala Arg Gly Met

100 105 110

tac ctc atg gtc gac gtc gta gcc aac cat atg gga tac gcc ggc ccg 384

Tyr Leu Met Val Asp Val Val Ala Asn His Met Gly Tyr Ala Gly Pro

115 120 125

ggg aac tct gtc gac tac agc gtc ttc aac ccc ttc aac aaa cag gaa 432

Gly Asn Ser Val Asp Tyr Ser Val Phe Asn Pro Phe Asn Lys Gln Glu

130 135 140

tac ttc cac ccc tac tgc gag ata acc aac tac gac gac caa tcc aac 480

Tyr Phe His Pro Tyr Cys Glu Ile Thr Asn Tyr Asp Asp Gln Ser Asn

145 150 155 160

gtc gag aat tgc tgg ctc gga gac aca ata gtc tca ctg ccc gat ctg 528

Val Glu Asn Cys Trp Leu Gly Asp Thr Ile Val Ser Leu Pro Asp Leu

165 170 175

aat acg gcc agg tcg gat gta gag gat ata tgg tac agt tgg gtg agg 576

Asn Thr Ala Arg Ser Asp Val Glu Asp Ile Trp Tyr Ser Trp Val Arg

180 185 190

gct ctg gtg tcg aac tac tcg gtc gac ggc ctc cgc atc gac acc gtc 624

Ala Leu Val Ser Asn Tyr Ser Val Asp Gly Leu Arg Ile Asp Thr Val

195 200 205

aaa cac gtc cag aag gac ttc tgg ccc ggc tac aac gac gcc gcg ggc 672

Lys His Val Gln Lys Asp Phe Trp Pro Gly Tyr Asn Asp Ala Ala Gly

210 215 220

gtc tac tgc gtg ggc gag gtg ttc gac ggt gac ccc agc tac acc tgc 720

Val Tyr Cys Val Gly Glu Val Phe Asp Gly Asp Pro Ser Tyr Thr Cys

225 230 235 240

gac tac cag aac tat ctg gat ggg gtg ctg aac tat ccg atg tac tac 768

Asp Tyr Gln Asn Tyr Leu Asp Gly Val Leu Asn Tyr Pro Met Tyr Tyr

245 250 255

ccc ctc ctc aga gcg ttc tcc tcc acg agc ggc agc atc agc gac ctg 816

Pro Leu Leu Arg Ala Phe Ser Ser Thr Ser Gly Ser Ile Ser Asp Leu

260 265 270

tac aac atg atc aac acg gtg aaa tcg cag tgc gcg gat tcg acc ctc 864

Tyr Asn Met Ile Asn Thr Val Lys Ser Gln Cys Ala Asp Ser Thr Leu

275 280 285

ctg ggt acc ttt gtc gag aac cat gac gtg ccg agg ttt gct tca tac 912

Leu Gly Thr Phe Val Glu Asn His Asp Val Pro Arg Phe Ala Ser Tyr

290 295 300

acg agc gac atc gcc ctc gcc aag aac gcg atc gcg ttc acc atc ctc 960

Thr Ser Asp Ile Ala Leu Ala Lys Asn Ala Ile Ala Phe Thr Ile Leu

305 310 315 320

tcg gac ggc atc cct att atc tat gcc ggc cag gag cag cac tac agc 1008

Ser Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ser

325 330 335

ggc ggc aac gac ccc gcg aac cgc gag gcg gtc tgg ctg tcc ggc tac 1056

Gly Gly Asn Asp Pro Ala Asn Arg Glu Ala Val Trp Leu Ser Gly Tyr

340 345 350

tcg acg acc agc gag ctc tac cag ttc atc gcg gtc tcg aac cag atc 1104

Ser Thr Thr Ser Glu Leu Tyr Gln Phe Ile Ala Val Ser Asn Gln Ile

355 360 365

cgc aat tac gcc atc tat gtg gac gag ggg tat ttg acg tac aag gcc 1152

Arg Asn Tyr Ala Ile Tyr Val Asp Glu Gly Tyr Leu Thr Tyr Lys Ala

370 375 380

tgg ccc atc tat caa gac agc cac acg ctc gca atc cgc aaa gga ttc 1200

Trp Pro Ile Tyr Gln Asp Ser His Thr Leu Ala Ile Arg Lys Gly Phe

385 390 395 400

gac ggc aat cag gtc atc acc gtg ctc tcg aac ctg ggt tcc tcc ggc 1248

Asp Gly Asn Gln Val Ile Thr Val Leu Ser Asn Leu Gly Ser Ser Gly

405 410 415

agc tcg tac acg ctc tcg ctg agc ggg acg ggc tat gct gcc ggc cag 1296

Ser Ser Tyr Thr Leu Ser Leu Ser Gly Thr Gly Tyr Ala Ala Gly Gln

420 425 430

cag gtg acc gag atc tac tcc tgc acg gat gtc acg gcc gac tcg aac 1344

Gln Val Thr Glu Ile Tyr Ser Cys Thr Asp Val Thr Ala Asp Ser Asn

435 440 445

ggg aat atc gcg gtc tcc atg ggt ggt ggg ctt ccg aag gcg ttt ttc 1392

Gly Asn Ile Ala Val Ser Met Gly Gly Gly Leu Pro Lys Ala Phe Phe

450 455 460

ccg aca gca aag ctg gct ggg agt gga atc tgt tgg aaa 1431

Pro Thr Ala Lys Leu Ala Gly Ser Gly Ile Cys Trp Lys

465 470 475

<210>125

<211>477

<212>PRT

<213> Thermoascus auranticus

<400>125

Ala Thr Pro Ala Gln Trp Arg Ser Arg Ser Val Tyr Phe Leu Leu Thr

1 5 10 15

Asp Arg Phe Ala Arg Ser Asp Gly Ser Thr Thr Ala Ala Cys Asp Thr

20 25 30

Ser Ala Arg Gln Tyr Cys Gly Gly Thr Trp Gln Gly Ile Ile Asp His

35 40 45

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Ser Pro

50 55 60

Val Thr Glu Gln Leu Pro Gln Asp Thr Gly Asp Gly Thr Ala Tyr His

65 70 75 80

Gly Tyr Trp Gln Gln Asp Ile Tyr Ser Leu Asn Pro Asn Phe Gly Thr

85 90 95

Ala Asp Asp Leu Arg Ala Leu Ala Asp Ala Leu His Ala Arg Gly Met

100 105 110

Tyr Leu Met Val Asp Val Val Ala Asn His Met Gly Tyr Ala Gly Pro

115 120 125

Gly Asn Ser Val Asp Tyr Ser Val Phe Asn Pro Phe Asn Lys Gln Glu

130 135 140

Tyr Phe His Pro Tyr Cys Glu Ile Thr Asn Tyr Asp Asp Gln Ser Asn

145 150 155 160

Val Glu Asn Cys Trp Leu Gly Asp Thr Ile Val Ser Leu Pro Asp Leu

165 170 175

Asn Thr Ala Arg Ser Asp Val Glu Asp Ile Trp Tyr Ser Trp Val Arg

180 185 190

Ala Leu Val Ser Asn Tyr Ser Val Asp Gly Leu Arg Ile Asp Thr Val

195 200 205

Lys His Val Gln Lys Asp Phe Trp Pro Gly Tyr Asn Asp Ala Ala Gly

210 215 220

Val Tyr Cys Val Gly Glu Val Phe Asp Gly Asp Pro Ser Tyr Thr Cys

225 230 235 240

Asp Tyr Gln Asn Tyr Leu Asp Gly Val Leu Asn Tyr Pro Met Tyr Tyr

245 250 255

Pro Leu Leu Arg Ala Phe Ser Ser Thr Ser Gly Ser Ile Ser Asp Leu

260 265 270

Tyr Asn Met Ile Asn Thr Val Lys Ser Gln Cys Ala Asp Ser Thr Leu

275 280 285

Leu Gly Thr Phe Val Glu Asn His Asp Val Pro Arg Phe Ala Ser Tyr

290 295 300

Thr Ser Asp Ile Ala Leu Ala Lys Asn Ala Ile Ala Phe Thr Ile Leu

305 310 315 320

Ser Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ser

325 330 335

Gly Gly Asn Asp Pro Ala Asn Arg Glu Ala Val Trp Leu Ser Gly Tyr

340 345 350

Ser Thr Thr Ser Glu Leu Tyr Gln Phe Ile Ala Val Ser Asn Gln Ile

355 360 365

Arg Asn Tyr Ala Ile Tyr Val Asp Glu Gly Tyr Leu Thr Tyr Lys Ala

370 375 380

Trp Pro Ile Tyr Gln Asp Ser His Thr Leu Ala Ile Arg Lys Gly Phe

385 390 395 400

Asp Gly Asn Gln Val Ile Thr Val Leu Ser Asn Leu Gly Ser Ser Gly

405 410 415

Ser Ser Tyr Thr Leu Ser Leu Ser Gly Thr Gly Tyr Ala Ala Gly Gln

420 425 430

Gln Val Thr Glu Ile Tyr Ser Cys Thr Asp Val Thr Ala Asp Ser Asn

435 440 445

Gly Asn Ile Ala Val Ser Met Gly Gly Gly Leu Pro Lys Ala Phe Phe

450 455 460

Pro Thr Ala Lys Leu Ala Gly Ser Gly Ile Cys Trp Lys

465 470 475

<210>126

<211>1347

<212>DNA

<213> Phanerochaete chryosporium

<220>

<221> CDS

<222>(1)..(1347)

<400>126

gcg ccc gcg cac cat gcc gtg cgc gcg ccc tcg cag gcc aag acc gtc 48

Ala Pro Ala His His Ala Val Arg Ala Pro Ser Gln Ala Lys Thr Val

1 5 10 15

atc gcg cag atg ttc gag tgg acg tgg gac agc gtc gcc gcc gag tgc 96

Ile Ala Gln Met Phe Glu Trp Thr Trp Asp Ser Val Ala Ala Glu Cys

20 25 30

acc gcg ttc ctc ggc ccc gcc ggc tac ggc ttc gtg cag gtc agc ccc 144

Thr Ala Phe Leu Gly Pro Ala Gly Tyr Gly Phe Val Gln Val Ser Pro

35 40 45

gcg cag gag cac gtc cag ggc ccg cag tgg tgg acg gac tac cag ccc 192

Ala Gln Glu His Val Gln Gly Pro Gln Trp Trp Thr Asp Tyr Gln Pro

50 55 60

gtg tcg tac acc ctc acc tcc aag cgc ggc acg cgc gcg cag cac cag 240

Val Ser Tyr Thr Leu Thr Ser Lys Arg Gly Thr Arg Ala Gln His Gln

65 70 75 80

aac atg gtc aat acg tgc caa gcc gcc ggc gtg gga gtc att gcg gac 288

Asn Met Val Asn Thr Cys Gln Ala Ala Gly Val Gly Val Ile Ala Asp

85 90 95

acg atc ttc aat cac atg agc ggc cag gac aat ggc ggc gtc ggc gtc 336

Thr Ile Phe Asn His Met Ser Gly Gln Asp Asn Gly Gly Val Gly Val

100 105 110

gcg ggg tcg tcc ttc cag cac tat gta tac ccc ggc atc tac cag aac 384

Ala Gly Ser Ser Phe Gln His Tyr Val Tyr Pro Gly Ile Tyr Gln Asn

115 120 125

cag gac ttc cac cac tgc ggc ctc gag ccc ggc gac gac atc gtg aac 432

Gln Asp Phe His His Cys Gly Leu Glu Pro Gly Asp Asp Ile Val Asn

130 135 140

tac gac aat gcc gtc gag gtg cag acc tgc gag ctc gtg aac ctc gcc 480

Tyr Asp Asn Ala Val Glu Val Gln Thr Cys Glu Leu Val Asn Leu Ala

145 150 155 160

gac ctt gct aca gag acc gag tat gtt cgc agc cgg ctc gca gag tac 528

Asp Leu Ala Thr Glu Thr Glu Tyr Val Arg Ser Arg Leu Ala Glu Tyr

165 170 175

gcc aac gat ttg ctg tcg ttg ggc gtc gac ggg ctg cgg ctc gac gca 576

Ala Asn Asp Leu Lcu Ser Leu Gly Val Asp Gly Leu Arg Leu Asp Ala

180 185 190

gcg aag cac atc aat gcg aat gac att gcc aac atc acg tct cgc ttc 624

Ala Lys His Ile Asn Ala Asn Asp Ile Ala Asn Ile Thr Ser Arg Phe

195 200 205

acg cgg aag ccc tac cta aca cag gag gtc atc tae ggg gcc ggg gag 672

Thr Arg Lys Pro Tyr Leu Thr Gln Glu Val Ile Tyr Gly Ala Gly Glu

210 215 220

ccc atc acg ccc aat caa tac gtc ttc att ggt gat gtg caa gac gcc 720

Pro Ile Thr Pro Asn Gln Tyr Val Phe Ile Gly Asp Val Gln Asp Ala

225 230 235 240

ttc tct ggc ggc ggg atc tcg agc ctg cag aac ctc gac aac caa ggc 768

Phe Ser Gly Gly Gly Ile Ser Ser Leu Gln Asn Leu Asp Asn Gln Gly

245 250 255

tgg gtc ccg ggc acc tct gcg aac gte ttc gtc acg atc cac gac acg 816

Trp Val Pro Gly Thr Ser Ala Asn Val Phe Val Thr I1e His Asp Thr

260 265 270

gag agg aac gga gcc tcg ctg aac gca aac tcg cca tcg aac aca tac 864

Glu Arg Asn Gly Ala Ser Leu Asn Ala Asn Ser Pro Ser Asn Thr Tyr

275 280 285

acg ctc gcg atg gtc ttc tcg ctc gca cac ccg tac ggc acg ccg acg 912

Thr Leu Ala Met Val Phe Ser Leu Ala His Pro Tyr Gly Thr Pro Thr

290 295 300

atc ctc tcg agc tac agc ggc ttc acg gac acg gac gcc ggt gca ccc 960

Ile Leu Ser Ser Tyr Ser Gly Phe Thr Asp Thr Asp Ala Gly Ala Pro

305 310 315 320

aac ggc ggc aca ggc acc tgc acg gcc ggc ggc ggc gcg gac ggc tgg 1008

Asn Gly Gly Thr Gly Thr Cys Thr Ala Gly Gly Gly Ala Asp Gly Trp

325 330 335

ctg tgc cag cac cgc tgg acg gcc gtc gcg ggc atg gtc ggc ttc cgg 1056

Leu Cys Gln His Arg Trp Thr Ala Val Ala Gly Met Val Gly Phe Arg

340 345 350

aac acc gtc ggc ggc gcg ccg ctc acg aac tgg gcc gcg ccg agc gct 1104

Asn Thr Val Gly Gly Ala Pro Leu Thr Asn Trp Ala Ala Pro Ser Ala

355 360 365

gag caa att gcg ttc ggg cgc ggc gcg ctc ggg ttc gtc gcg ctc aac 1152

Glu Gln Ile Ala Phe Gly Arg Gly Ala Leu Gly Phe Val Ala Leu Asn

370 375 380

aac gcg gac gcg gtg tgg agc gcg gcg ttc agc acg gcg ctc ccc gac 1200

Asn Ala Asp Ala Val Trp Ser Ala Ala Phe Ser Thr Ala Leu Pro Asp

385 390 395 400

ggc acg tac tgc gat gtc gtc ggc ggc gcg agc cag ggt ggg aag tgc 1248

Gly Thr Tyr Cys Asp Val Val Gly Gly Ala Ser Gln Gly Gly Lys Cys

405 410 415

acg ggc agc gcg ttt acg gtc aag ggc ggg gcg ttc acc gcg aac gta 1296

Thr Gly Ser Ala Phe Thr Val Lys Gly Gly Ala Phe Thr Ala Asn Val

420 425 430

cag gcg cgc aac gcg att gcg ata cac gtc ggc gcg aag ggc acc gcg 1344

Gln Ala Arg Asn Ala Ile Ala Ile His yal Gly Ala Lys Gly Thr Ala

435 440 445

ggc 1347

Gly

<210>127

<211>449

<212>PRT

<213> Phanerochaete chryosporium

<400>127

Ala Pro Ala His His Ala Val Arg Ala Pro Ser Gln Ala Lys Thr Val

1 5 10 15

Ile Ala Gln Met Phe Glu Trp Thr Trp Asp Ser Val Ala Ala Glu Cys

20 25 30

Thr Ala Phe Leu Gly Pro Ala Gly Tyr Gly Phe Val Gln Val Ser Pro

35 40 45

Ala Gln Glu His Val Gln Gly Pro Gln Trp Trp Thr Asp Tyr Gln Pro

50 55 60

Val Ser Tyr Thr Leu Thr Ser Lys Arg Gly Thr Arg Ala Gln His Gln

65 70 75 80

Asn Met Val Asn Thr Cys Gln Ala Ala Gly Val Gly Val Ile Ala Asp

85 90 95

Thr Ile Phe Asn His Met Ser Gly Gln Asp Asn Gly Gly Val Gly Val

100 105 110

Ala Gly Ser Ser Phe Gln His Tyr Val Tyr Pro Gly Ile Tyr Gln Asn

115 120 125

Gln Asp Phe His His Cys Gly Leu Glu Pro Gly Asp Asp Ile Val Asn

130 135 140

Tyr Asp Asn Ala Val Glu Val Gln Thr Cys Glu Leu Val Asn Leu Ala

145 150 155 160

Asp Leu Ala Thr Glu Thr Glu Tyr Val Arg Ser Arg Leu Ala Glu Tyr

165 170 175

Ala Asn Asp Leu Leu Ser Leu Gly Val Asp Gly Leu Arg Leu Asp Ala

180 185 190

Ala Lys His Ile Asn Ala Asn Asp Ile Ala Asn Ile Thr Ser Arg Phe

195 200 205

Thr Arg Lys Pro Tyr Leu Thr Gln Glu Val Ile Tyr Gly Ala Gly Glu

210 215 220

Pro Ile Thr Pro Asn Gln Tyr Val Phe Ile Gly Asp Val Gln Asp Ala

225 230 235 240

Phe Ser Gly Gly Gly Ile Ser Ser Leu Gln Asn Leu Asp Asn Gln Gly

245 250 255

Trp Val Pro Gly Thr Ser Ala Asn Val Phe Val Thr Ile His Asp Thr

260 265 270

Glu Arg Asn Gly Ala Ser Leu Asn Ala Asn Ser Pro Ser Asn Thr Tyr

275 280 285

Thr Leu Ala Met Val Phe Ser Leu Ala His Pro Tyr Gly Thr Pro Thr

290 295 300

Ile Leu Ser Ser Tyr Ser Gly Phe Thr Asp Thr Asp Ala Gly Ala Pro

305 310 315 320

Asn Gly Gly Thr Gly Thr Cys Thr Ala Gly Gly Gly Ala Asp Gly Trp

325 330 335

Leu Cys Gln His Arg Trp Thr Ala Val Ala Gly Met Val Gly Phe Arg

340 345 350

Asn Thr Val Gly Gly Ala Pro Leu Thr Asn Trp Ala Ala Pro Ser Ala

355 360 365

Glu Gln Ile Ala Phe Gly Arg Gly Ala Leu Gly Phe Val Ala Leu Asn

370 375 380

Asn Ala Asp Ala Val Trp Ser Ala Ala Phe Ser Thr Ala Leu Pro Asp

385 390 395 400

Gly Thr Tyr Cys Asp Val Val Gly Gly Ala Ser Gln Gly Gly Lys Cys

405 410 415

Thr Gly Ser Ala Phe Thr Val Lys Gly Gly Ala Phe Thr Ala Asn Val

420 425 430

Gln Ala Arg Asn Ala Ile Ala Ile His Val Gly Ala Lys Gly Thr Ala

435 440 445

Gly

<210>128

<211>1308

<212>DNA

<213>Rhizopus oryzae

<220>

<221> CDS

<222>(1)..(1308)

<400>128

gcc tca gcc agc gac tgg gag aac cga gtc atc tac caa ttg tta act 48

Ala Ser Ala Ser Asp Trp Glu Asn Arg Val Ile Tyr Gln Leu Leu Thr

1 5 10 15

gat cga ttt gca aaa tcg acc gat gat acc aat ggc tgc aat aac ctg 96

Asp Arg Phe Ala Lys Ser Thr Asp Asp Thr Asn Gly Cys Asn Asn Leu

20 25 30

agt gac tac tgt ggc gga aca ttt caa gga atc att aat cac ttg gat 144

Ser Asp Tyr Cys Gly Gly Thr Phe Gln Gly Ile Ile Asn His Leu Asp

35 40 45

tac att gcc gga atg gga ttt gat gct atc tgg ata tca cct atc ccc 192

Tyr Ile Ala Gly Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro

50 55 60

aaa aat gcg aat gga ggt tac cat ggc tat tgg gct act gac ttt tct 240

Lys Asn Ala Asn Gly Gly Tyr His Gly Tyr Trp Ala Thr Asp Phe Ser

65 70 75 80

caa ata aat gag cat ttt gga act gct gat gac ttg aaa aag ttg gtt 288

Gln Ile Asn Glu His Phe Gly Thr Ala Asp Asp Leu Lys Lys Leu Val

85 90 95

gca gct gct cat gca aag aac atg tac gtt atg ctg gac gtt gtt gcc 336

Ala Ala Ala His Ala Lys Asn Met Tyr Val Met Leu Asp Val Val Ala

100 105 110

aat cat gct ggc att cct tca tca ggt ggc gac tac tct ggc tac acg 384

Asn His Ala Gly Ile Pro Ser Ser Gly Gly Asp Tyr Ser Gly Tyr Thr

115 120 125

ttc ggt caa agc tct gaa tac cac aca gcc tgt gat atc aat tac aac 432

Phe Gly Gln Ser Ser Glu Tyr His Thr Ala Cys Asp Ile Asn Tyr Asn

130 135 140

agc cag acc tct att gag cag tgc tgg att tct ggt ttg cct gat atc 480

Ser Gln Thr Ser Ile Glu Gln Cys Trp Ile Ser Gly Leu Pro Asp Ile

145 150 155 160

aac act gaa gac tcg gcc att gtt agc aaa ttg aat tcg att gtt tct 528

Asn Thr Glu Asp Ser Ala Ile Val Ser Lys Leu Asn Ser Ile Val Ser

165 170 175

ggt tgg gta tct gat tat ggc ttt gac ggt ctt cga atc gac act gtg 576

Gly Trp Val Ser Asp Tyr Gly Phe Asp Gly Leu Arg Ile Asp Thr Val

180 185 190

aag cac att cgt aaa gat ttc tgg gac ggc tat gtc tct gct gct ggt 624

Lys His Ile Arg Lys Asp Phe Trp Asp Gly Tyr Val Ser Ala Ala Gly

195 200 205

gta ttt gct acc gga gaa gtg ctt agc ggc gat gtt tct tat gtc tca 672

Val Phe Ala Thr Gly Glu Val Leu Ser Gly Asp Val Ser Tyr Val Ser

210 215 220

ccc tat cag cag cat gtt cct tct tta ctc aac tac cca ttg tat tat 720

Pro Tyr Gln Gln His Val Pro Ser Leu Leu Asn Tyr Pro Leu Tyr Tyr

225 230 235 240

cca gtc tat gat gta ttc acc aaa tcc cgt acc atg agc cgt tta agc 768

Pro Val Tyr Asp Val Phe Thr Lys Ser Arg Thr Met Ser Arg Leu Scr

245 250 255

tct ggc ttt tct gat att aaa aat gga aac ttt aaa gac att gat gtc 816

Ser Gly Phe Ser Asp Ile Lys Asn Gly Asn Phe Lys Asp Ile Asp Val

260 265 270

ttg gtc aac ttt att gac aat cac gat cag cct cgt ttg tta tcc aaa 864

Leu Val Asn Phe Ile Asp Asn His Asp Gln Pro Arg Leu Leu Ser Lys

275 280 285

gct gat caa agt ctc gtc aag aat gct ctt gct tat tct ttc atg gtc 912

Ala Asp Gln Ser Leu Val Lys Asn Ala Leu Ala Tyr Ser Phe Met Val

290 295 300

caa ggt atc cct gtc ttg tac tat ggt aca gaa caa tcc ttc aag ggt 960

Gln Gly Ile Pro Val Leu Tyr Tyr Gly Thr Glu Gln Ser Phe Lys Gly

305 310 315 320

ggt aac gat cct aac aac aga gag gtc tta tgg acc act ggt tac tcg 1008

Gly Asn Asp Pro Asn Asn Arg Glu Val Leu Trp Thr Thr Gly Tyr Ser

325 330 335

acc aca tct gat atg tac aag ttt gtc act act ctt gtc aag gca cgc 1056

Thr Thr Ser Asp Met Tyr Lys Phe Val Thr Thr Leu Val Lys Ala Arg

340 345 350

aag ggc tca aac tcc aca gta aat atg gga att gct caa acc gat aac 1104

Lys Gly Ser Asn Ser Thr Val Asn Met Gly Ile Ala Gln Thr Asp Asn

355 360 365

gtc tat gtg ttc caa aga ggt ggc tct ctg gtt gtt gtc aat aac tat 1152

Val Tyr Val Phe Gln Arg Gly Gly Ser Leu Val Val Val Asn Asn Tyr

370 375 380

ggt caa gga tca aca aac aca att act gta aag gct ggc tcg ttc tct 1200

Gly Gln Gly Ser Thr Asn Thr Ile Thr Val Lys Ala Gly Ser Phe Ser

385 390 395 400

aat gga gat act ttg act gat gtg ttc tcc aac aaa tct gtt act gtt 1248

Asn Gly Asp Thr Leu Thr Asp Val Phe Ser Asn Lys Ser Val Thr Val

405 410 415

caa aat aac cag atc aca ttc caa ttg cag aat gga aac cct gcc ata 1296

Gln Asn Asn Gln Ile Thr Phe Gln Leu Gln Asn Asn Gly Asn Pro Ala Ile

420 425 430

ttc caa aag aaa 1308

Phe Gln Lys Lys

435

<210>129

<211>436

<212>PRT

<213>Rhizopus oryzae

<400>129

Ala Ser Ala Ser Asp Trp Glu Asn Arg Val Ile Tyr Gln Leu Leu Thr

1 5 10 15

Asp Arg Phe Ala Lys Ser Thr Asp Asp Thr Asn Gly Cys Asn Asn Leu

20 25 30

Ser Asp Tyr Cys Gly Gly Thr Phe Gln Gly Ile Ile Asn His Leu Asp

35 40 45

Tyr Ile Ala Gly Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro

50 55 60

Lys Asn Ala Asn Gly Gly Tyr His Gly Tyr Trp Ala Thr Asp Phe Ser

65 70 75 80

Gln Ile Asn Glu His Phe Gly Thr Ala Asp Asp Leu Lys Lys Leu Val

85 90 95

Ala Ala Ala His Ala Lys Asn Met Tyr Val Met Leu Asp Val Val Ala

100 105 110

Asn His Ala Gly Ile Pro Ser Ser Gly Gly Asp Tyr Ser Gly Tyr Thr

115 120 125

Phe Gly Gln Ser Ser Glu Tyr His Thr Ala Cys Asp Ile Asn Tyr Asn

130 135 140

Ser Gln Thr Ser Ile Glu Gln Cys Trp Ile Ser Gly Leu Pro Asp Ile

145 150 155 160

Asn Thr Glu Asp Ser Ala Ile Val Ser Lys Leu Asn Ser Ile Val Ser

165 170 175

Gly Trp Val Ser Asp Tyr Gly Phe Asp Gly Leu Arg Ile Asp Thr Val

180 185 190

Lys His Ile Arg Lys Asp Phe Trp Asp Gly Tyr Val Ser Ala Ala Gly

195 200 205

Val Phe Ala Thr Gly Glu Val Leu Ser Gly Asp Val Ser Tyr Val Ser

210 215 220

Pro Tyr Gln Gln His Val Pro Ser Leu Leu Asn Tyr Pro Leu Tyr Tyr

225 230 235 240

Pro Val Tyr Asp Val Phe Thr Lys Ser Arg Thr Met Ser Arg Leu Ser

245 250 255

Ser Gly Phe Ser Asp Ile Lys Asn Gly Asn Phe Lys Asp Ile Asp Val

260 265 270

Leu Val Asn Phe Ile Asp Asn His Asp Gln Pro Arg Leu Leu Ser Lys

275 280 285

Ala Asp Gln Ser Leu Val Lys Asn Ala Leu Ala Tyr Ser Phe Met Val

290 295 300

Gln Gly Ile Pro Val Leu Tyr Tyr Gly Thr Glu Gln Ser Phe Lys Gly

305 310 315 320

Gly Asn Asp Pro Asn Asn Arg Glu Val Leu Trp Thr Thr Gly Tyr Ser

325 330 335

Thr Thr Ser Asp Met Tyr Lys Phe Val Thr Thr Leu Val Lys Ala Arg

340 345 350

Lys Gly Ser Asn Ser Thr Val Asn Met Gly Ile Ala Gln Thr Asp Asn

355 360 365

Val Tyr Val Phe Gln Arg Gly Gly Ser Leu Val Val Val Asn Asn Tyr

370 375 380

Gly Gln Gly Ser Thr Asn Thr Ile Thr Val Lys Ala Gly Ser Phe Ser

385 390 395 400

Asn Gly Asp Thr Leu Thr Asp Val Phe Ser Asn Lys Ser Val Thr Val

405 410 415

Gln Asn Asn Gln Ile Thr Phe Gln Leu Gln Asn Asn Gly Asn Pro Ala Ile

420 425 430

Phe Gln Lys Lys

435

<210>130

<211>1338

<212>DNA

<213>Thaminidium elegans

<220>

<221> CDS

<222>(1)..(1338)

<400>130

aac ggt gtc acg act ttg agc aag cgt gca gct gct gat gac tgg aaa 48

Asn Gly Val Thr Thr Leu Ser Lys Arg Ala Ala Ala Asp Asp Trp Lys

1 5 10 15

tcc cgg tcc att tac caa gtt gtg acg gat cgt ttc ggt cgc tcg gat 96

Ser Arg Ser Ile Tyr Gln Val Val Thr Asp Arg Phe Gly Arg Ser Asp

20 25 30

ggc tcg acc tct gct tgc ggt gac ctg tcc aac tac tgc ggc ggt gac 144

Gly Ser Thr Ser Ala Cys Gly Asp Leu Ser Asn Tyr Cys Gly Gly Asp

35 40 45

tac aag ggc att cag aat cag ctc gac tac att gct ggc atg ggc ttc 192

Tyr Lys Gly Ile Gln Asn Gln Leu Asp Tyr Ile Ala Gly Met Gly Phe

50 55 60

gac gcc att tgg atc tcg cct att cct gag aac aca gac ggc ggc tac 240

Asp Ala Ile Trp Ile Ser Pro Ile Pro Glu Asn Thr Asp Gly Gly Tyr

65 70 75 80

cat ggt tac tgg gca aag gac ttt gaa aag ctc aac acc aat ttt ggc 288

His Gly Tyr Trp Ala Lys Asp Phe Glu Lys Leu Asn Thr Asn Phe Gly

85 90 95

agt gcg gat gat ctc aag gct ctc gtg aca gct gcg cac ggc aag ggc 336

Ser Ala Asp Asp Leu Lys Ala Leu Val Thr Ala Ala His Gly Lys Gly

100 105 110

atg tat gtc atg ctg gat gtc gtc aca aac cac gca ggt ccc gcc agc 384

Met Tyr Val Met Leu Asp Val Val Thr Asn His Ala Gly Pro Ala Ser

115 120 125

ggc gac tac agc ggc ttc acc ttc agc tcc gcc agt aat tat cat ccg 432

Gly Asp Tyr Ser Gly Phe Thr Phe Ser Ser Ala Ser Asn Tyr His Pro

130 135 140

cag tgc acg atc gac tgc gac aac cag act tcc gtc gag cag tgc tgg 480

Gln Cys Thr Ile Asp Cys Asp Asn Gln Thr Ser Val Glu Gln Cys Trp

145 150 155 160

gtg gcg gac aac ctg ccc gac att aac acc gag gat gat acc att gtt 528

Val Ala Asp Asn Leu Pro Asp Ile Asn Thr Glu Asp Asp Thr Ile Val

165 170 175

tcc aag ctg cac agc att gtc tct gat tgg gtc acc acc tac gat ttt 576

Ser Lys Leu His Ser Ile Val Ser Asp Trp Val Thr Thr Tyr Asp Phe

180 185 190

gat ggc att cgt atc gat act gtc aag cat atc cgt aaa gac ttc tgg 624

Asp Gly Ile Arg Ile Asp Thr Val Lys His Ile Arg Lys Asp Phe Trp

195 200 205

tct ggc tac gaa gag gct gct gga gtc ttt gct act ggc gaa gtc ttt 672

Ser Gly Tyr Glu Glu Ala Ala Gly Val Phe Ala Thr Gly Glu Val Phe

210 215 220

gac ggc gac gcg gct tat gtc ggt cct tac cag gac cag ttg agc tcg 720

Asp Gly Asp Ala Ala Tyr Val Gly Pro Tyr Gln Asp Gln Leu Ser Ser

225 230 235 240

ctc atc aac tac cca ctt tac tat gct atc cgc gat gtc ttc acc gcc 768

Leu Ile Asn Tyr Pro Leu Tyr Tyr Ala Ile Arg Asp Val Phe Thr Ala

245 250 255

ggc tcg ggc ttt agc cgc atc agc gac atg ctt tcc agc atc aac tcg 816

Gly Ser Gly Phe Ser Arg Ile Ser Asp Met Leu Ser Ser Ile Asn Ser

260 265 270

aac ttc aag gac ccc tcc gcg ctc acg acc ttt gtg gat aac caa gac 864

Asn Phe Lys Asp Pro Ser Ala Leu Thr Thr Phe Val Asp Asn Gln Asp

275 280 285

aac gcc cgc ttc ctc agt gtg aag agt gac atg tct ctg tac aag aat 912

Asn Ala Arg Phe Leu Ser Val Lys Ser Asp Met Ser Leu Tyr Lys Asn

290 295 300

gct ctt gcg ttc acg att ctg acc gag ggt atc cct gtt gtg tac tac 960

Ala Leu Ala Phe Thr Ile Leu Thr Glu Gly Ile Pro Val Val Tyr Tyr

305 310 315 320

ggc acc gag caa ggc ttc aaa ggt ggt gat gac ccc aag aac cgt gag 1008

Gly Thr Glu Gln Gly Phe Lys Gly Gly Asp Asp Pro Lys Asn Arg Glu

325 330 335

gtc ctc tgg acc tcc aac tat gat acc tcc tcg gat ctc tac aag ttt 1056

Val Leu Trp Thr Ser Asn Tyr Asp Thr Ser Ser Asp Leu Tyr Lys Phe

340 345 350

atc aag att gtg aac aat gat gtt cgc cag aaa tca aac aag tct gtg 1104

Ile Lys Ile Val Asn Asn Asp Val Arg Gln Lys Ser Asn Lys Ser Val

355 360 365

act ctg aac gta gac gtg gga acc aac acc tac gcg ttc aca cac ggc 1152

Thr Leu Asn Val Asp Val Gly Thr Asn Thr Tyr Ala Phe Thr His Gly

370 375 380

aag aat ctc atc gtt gtc aac aac tat ggc agt ggt tcc act gcg tct 1200

Lys Asn Leu Ile Val Val Asn Asn Tyr Gly Ser Gly Ser Thr Ala Ser

385 390 395 400

gtc act gtc aag gct ggt gac att gca gac ggc aca aaa ctg gtg gat 1248

Val Thr Val Lys Ala Gly Asp Ile Ala Asp Gly Thr Lys Leu Val Asp

405 410 415

gct gtc agt aac att acg gct acc gtc tcg gga ggc agc atc aca ttc 1296

Ala Val Ser Asn Ile Thr Ala Thr Val Ser Gly Gly Ser Ile Thr Phe

420 425 430

tcc ttg aag gac ggt ctt ccg gct ctt ttc gtg ccc agc tcg 1338

Ser Leu Lys Asp Gly Leu Pro Ala Leu Phe Val Pro Ser Ser

435 440 445

<210>131

<211>446

<212>PRT

<213>Thaminidium elegans

<400>131

Asn Gly Val Thr Thr Leu Ser Lys Arg Ala Ala Ala Asp Asp Trp Lys

1 5 10 15

Ser Arg Ser Ile Tyr Gln Val Val Thr Asp Arg Phe Gly Arg Ser Asp

20 25 30

Gly Ser Thr Ser Ala Cys Gly Asp Leu Ser Asn Tyr Cys Gly Gly Asp

35 40 45

Tyr Lys Gly Ile Gln Asn Gln Leu Asp Tyr Ile Ala Gly Met Gly Phe

50 55 60

Asp Ala Ile Trp Ile Ser Pro Ile Pro Glu Asn Thr Asp Gly Gly Tyr

65 70 75 80

His Gly Tyr Trp Ala Lys Asp Phe Glu Lys Leu Asn Thr Asn Phe Gly

85 90 95

Ser Ala Asp Asp Leu Lys Ala Leu Val Thr Ala Ala His Gly Lys Gly

100 105 110

Met Tyr Val Met Leu Asp Val Val Thr Asn His Ala Gly Pro Ala Ser

115 120 125

Gly Asp Tyr Ser Gly Phe Thr Phe Ser Ser Ala Ser Asn Tyr His Pro

130 135 140

Gln Cys Thr Ile Asp Cys Asp Asn Gln Thr Ser Val Glu Gln Cys Trp

145 150 155 165

Val Ala Asp Asn Leu Pro Asp Ile Asn Thr Glu Asp Asp Thr Ile Val

165 170 175

Ser Lys Leu His Ser Ile Val Ser Asp Trp Val Thr Thr Tyr Asp Phe

180 185 190

Asp Gly Ile Arg Ile Asp Thr Val Lys His Ile Arg Lys Asp Phe Trp

195 200 205

Ser Gly Tyr Glu Glu Ala Ala Gly Val Phe Ala Thr Gly Glu Val Phe

210 215 220

Asp Gly Asp Ala Ala Tyr Val Gly Pro Tyr Gln Asp Gln Leu Ser Ser

225 230 235 240

Leu Ile Asn Tyr Pro Leu Tyr Tyr Ala Ile Arg Asp Val Phe Thr Ala

245 250 255

Gly Ser Gly Phe Ser Arg Ile Ser Asp Met Leu Ser Ser Ile Asn Ser

260 265 270

Asn Phe Lys Asp Pro Ser Ala Leu Thr Thr Phe Val Asp Asn Gln Asp

275 280 285

Asn Ala Arg Phe Leu Ser Val Lys Ser Asp Met Ser Leu Tyr Lys Asn

290 295 300

Ala Leu Ala Phe Thr Ile Leu Thr Glu Gly Ile Pro Val Val Tyr Tyr

305 310 315 320

Gly Thr Glu Gln Gly Phe Lys Gly Gly Asp Asp Pro Lys Asn Arg Glu

325 330 335

Val Leu Trp Thr Ser Asn Tyr Asp Thr Ser Ser Asp Leu Tyr Lys Phe

340 345 350

Ile Lys Ile Val Asn Asn Asp Val Arg Gln Lys Ser Asn Lys Ser Val

355 360 365

Thr Leu Asn Val Asp Val Gly Thr Asn Thr Tyr Ala Phe Thr His Gly

370 375 380

Lys Asn Leu Ile Val Val Asn Asn Tyr Gly Ser Gly Ser Thr Ala Ser

385 390 395 400

Val Thr Val Lys Ala Gly Asp Ile Ala Asp Gly Thr Lys Leu Val Asp

405 410 415

Ala Val Ser Asn Ile Thr Ala Thr Val Ser Gly Gly Ser Ile Thr Phe

420 425 430

Ser Leu Lys Asp Gly Leu Pro Ala Leu Phe Val Pro Ser Ser

435 440 445

<210>132

<211>1305

<212>DNA

<213>Absidia crista

<220>

<221> CDS

<222>(1)..(1305)

<400>132

gca ggc gcc gat gat tgg aga tca cgt tcc atc tat caa tta ttg act 48

Ala Gly Ala Asp Asp Trp Arg Ser Arg Ser Ile Tyr Gln Leu Leu Thr

1 5 10 15

gat cgc ttt gct ggt ggc ggt gat tgt tct gat tta tcc gat tat tgt 96

Asp Arg Phe Ala Gly Gly Gly Asp Cys Ser Asp Leu Ser Asp Tyr Cys

20 25 30

ggt ggt aat tat aaa ggc atg att gaa cac ctg gat tat atc caa gga 144

Gly Gly Asn Tyr Lys Gly Met Ile Glu His Leu Asp Tyr Ile Gln Gly

35 40 45

atg gga ttc gat gcc atc tgg att tcc ccc atc cct acc aac tca ccc 192

Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro Thr Asn Ser Pro

50 55 60

ggc ggt tac cat ggc tac tgg gca act gac ttc aat ggt tta aat gaa 240

Gly Gly Tyr His Gly Tyr Trp Ala Thr Asp Phe Asn Gly Leu Asn Glu

65 70 75 80

aac ttt gga acc aag gac gat ctc aag gct ttg gtg gat gca gca cat 288

Asn Phe Gly Thr Lys Asp Asp Leu Lys Ala Leu Val Asp Ala Ala His

85 90 95

aag ctc gac atg tat gtc atg ttg gat gtc gtt gcc aat cat gct gga 336

Lys Leu Asp Met Tyr Val Met Leu Asp Val Val Ala Asn His Ala Gly

100 105 110

caa ccc agt acg gca ggt gac tat tct ggc tac aca ttc gat tct aaa 384

Gln Pro Ser Thr Ala Gly Asp Tyr Ser Gly Tyr Thr Phe Asp Ser Lys

115 120 125

gac caa tac cat tcc caa tgc aaa atc gat tat gat gat caa aac tct 432

Asp Gln Tyr His Ser Gln Cys Lys Ile Asp Tyr Asp Asp Gln Asn Ser

130 135 140

att gag cag tgt tgg gtg gct gat gtg ttg cct gac atc aac act gag 480

Ile Glu Gln Cys Trp Val Ala Asp Val Leu Pro Asp Ile Asn Thr Glu

145 150 155 160

gat gat aac gtg gtc aag acg ctc aat gat att gtc agc aac tgg gta 528

Asp Asp Asn Val Val Lys Thr Leu Asn Asp Ile Val Ser Asn Trp Val

165 170 175

act aca tat ggc ttt gat ggt att cgc att gac act gtc aag cat gta 576

Thr Thr Tyr Gly Phe Asp Gly Ile Arg Ile Asp Thr Val Lys His Val

180 185 190

cgt caa gac ttt tgg gat gga tac aat gaa gca gct ggt gta ttt gct 624

Arg Gln Asp Phe Trp Asp Gly Tyr Asn Glu Ala Ala Gly Val Phe Ala

195 200 205

aca gga gaa gtc ttt gat ggt gat tca tcc tat gtt ggt gga tat caa 672

Thr Gly Glu Val Phe Asp Gly Asp Ser Ser Tyr Val Gly Gly Tyr Gln

210 215 220

aag cat ttg gac tcg ctt ctc aat tac cca atg tat tac gca ctc aat 720

Lys His Leu Asp Ser Leu Leu Asn Tyr Pro Met Tyr Tyr Ala Leu Asn

225 230 235 240

gat gta ttt ggt tct gga aag ggt ttt agt cgt atc agc gag atg att 768

Asp Val Phe Gly Ser Gly Lys Gly Phe Ser Arg Ile Ser Glu Met Ile

245 250 255

gca acc aat gca gat gca ttt gct gat acc agt gtt ctg acc aac ttt 816

Ala Thr Asn Ala Asp Ala Phe Ala Asp Thr Ser Val Leu Thr Asn Phe

260 265 270

att gac aac cat gat aac cca cgt ttc ctt aat acc aac aag gat act 864

Ile Asp Asn His Asp Asn Pro Arg Phe Leu Asn Thr Asn Lys Asp Thr

275 280 285

act ctc ttc aag aac gct ttg acc tac gtg ttg ctc gct gat ggt att 912

Thr Leu Phe Lys Asn Ala Leu Thr Tyr Val Leu Leu Ala Asp Gly Ile

290 295 300

cca gtg gtg tat tat gga tca gaa caa ggc ttt tca ggt ggt gct gat 960

Pro Val Val Tyr Tyr Gly Ser Glu Gln Gly Phe Ser Gly Gly Ala Asp

305 310 315 320

cct gcc aat cgt gaa gca tta tgg tca act gac ttt gac acc tcg tcc 1008

Pro Ala Asn Arg Glu Ala Leu Trp Ser Thr Asp Phe Asp Thr Ser Ser

325 330 335

gat ttg tac aag ttt atg gct act gtc aac aag gat gtt cgt caa aag 1056

Asp Leu Tyr Lys Phe Met Ala Thr Val Asn Lys Asp Val Arg Gln Lys

340 345 350

gaa aac aaa aag gtg gtg atg gat gtt gat gtg caa gac aac gtg tat 1104

Glu Asn Lys Lys Val Val Met Asp Val Asp Val Gln Asp Asn Val Tyr

355 360 365

gca ttc atg cac ggc gat gct ctt gtg gta ttg aac aac tac ggc agt 1152

Ala Phe Met His Gly Asp Ala Leu Val Val Leu Asn Asn Tyr Gly Ser

370 375 380

gga gcc agc aac gag gtt act gtc aag gtc gga tca cat gtt gat gat 1200

Gly Ala Ser Asn Glu Val Thr Val Lys Val Gly Ser His Val Asp Asp

385 390 395 400

gga gcc aag atg aac gac gtc ttt acc aat agc aca gtc tcg gta tct 1248

Gly Ala Lys Met Asn Asp Val Phe Thr Asn Ser Thr Val Ser Val Ser

405 410 415

ggt ggt tca ttc act ttc aaa ctt gac aat gga aat cct gcc atc ttt 1296

Gly Gly Ser Phe Thr Phe Lys Leu Asp Asn Gly Asn Pro Ala Ile Phe

420 425 430

acc act gct 1305

Thr Thr Ala

435

<210>133

<211>435

<212>PRT

<213>Absidia crista

<400>133

Ala Gly Ala Asp Asp Trp Arg Ser Arg Ser Ile Tyr Gln Leu Leu Thr

1 5 10 15

Asp Arg Phe Ala Gly Gly Gly Asp Cys Ser Asp Leu Ser Asp Tyr Cys

20 25 30

Gly Gly Asn Tyr Lys Gly Met Ile Glu His Leu Asp Tyr Ile Gln Gly

35 40 45

Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro Thr Asn Ser Pro

50 55 60

Gly Gly Tyr His Gly Tyr Trp Ala Thr Asp Phe Asn Gly Leu Asn Glu

65 70 75 80

Asn Phe Gly Thr Lys Asp Asp Leu Lys Ala Leu Val Asp Ala Ala His

85 90 95

Lys Leu Asp Met Tyr Val Met Leu Asp Val Val Ala Asn His Ala Gly

100 105 110

Gln Pro Ser Thr Ala Gly Asp Tyr Ser Gly Tyr Thr Phe Asp Ser Lys

115 120 125

Asp Gln Tyr His Ser Gln Cys Lys Ile Asp Tyr Asp Asp Gln Asn Ser

130 135 140

Ile Glu Gln Cys Trp Val Ala Asp Val Leu Pro Asp Ile Asn Thr Glu

145 150 155 160

Asp Asp Asn Val Val Lys Thr Leu Asn Asp Ile Val Ser Asn Trp Val

165 170 175

Thr Thr Tyr Gly Phe Asp Gly Ile Arg Ile Asp Thr Val Lys His Val

180 185 190

Arg Gln Asp Phe Trp Asp Gly Tyr Asn Glu Ala Ala Gly Val Phe Ala

195 200 205

Thr Gly Glu Val Phe Asp Gly Asp Ser Ser Tyr Val Gly Gly Tyr Gln

210 215 220

Lys His Leu Asp Ser Leu Leu Asn Tyr Pro Met Tyr Tyr Ala Leu Asn

225 230 235 240

Asp Val Phe Gly Ser Gly Lys Gly Phe Ser Arg Ile Ser Glu Met Ile

245 250 255

Ala Thr Asn Ala Asp Ala Phe Ala Asp Thr Ser Val Leu Thr Asn Phe

260 265 270

Ile Asp Asn His Asp Asn Pro Arg Phe Leu Asn Thr Asn Lys Asp Thr

275 280 285

Thr Leu Phe Lys Asn Ala Leu Thr Tyr Val Leu Leu Ala Asp Gly Ile

290 295 300

Pro Val Val Tyr Tyr Gly Ser Glu Gln Gly Phe Ser Gly Gly Ala Asp

305 310 315 320

Pro Ala Asn Arg Glu Ala Leu Trp Ser Thr Asp Phe Asp Thr Ser Ser

325 330 335

Asp Leu Tyr Lys Phe Met Ala Thr Val Asn Lys Asp Val Arg Gln Lys

340 345 350

Glu Asn Lys Lys Val Val Met Asp Val Asp Val Gln Asp Asn Val Tyr

355 360 365

Ala Phe Met His Gly Asp Ala Leu Val Val Leu Asn Asn Tyr Gly Ser

370 375 380

Gly Ala Ser Asn Glu Val Thr Val Lys Val Gly Ser His Val Asp Asp

385 390 395 400

Gly Ala Lys Met Asn Asp Val Phe Thr Asn Ser Thr Val Ser Val Ser

405 410 415

Gly Gly Ser Phe Thr Phe Lys Leu Asp Asn Gly Asn Pro Ala Ile Phe

420 425 430

Thr Thr Ala

435

<210>134

<211>1308

<212>DNA

<213> Syncephalastrum racemosum

<220>

<221> CDS

<222>(1)..(1308)

<400>134

gcg act gct agt gac tgg gaa aat cga gtt atc tac caa ttg ttg aca 48

Ala Thr Ala Ser Asp Trp Glu Asn Arg Val Ile Tyr Gln Leu Leu Thr

1 5 10 15

gat cga ttt gct aaa agc tct gac gac aca aac ggt tgc tcc aac cta 96

Asp Arg Phe Ala Lys Ser Ser Asp Asp Thr Asn Gly Cys Ser Asn Leu

20 25 30

ggc aat tat tgt ggc ggg acg ttt caa ggg att atc aat cat cta gac 144

Gly Asn Tyr Cys Gly Gly Thr Phe Gln Gly Ile Ile Asn His Leu Asp

35 40 45

tat att gcc ggt atg gga ttc gat gcg atc tgg ata tcg cca att cct 192

Tyr Ile Ala Gly Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro

50 55 60

gaa aac tcg gat ggg ggg tat cac ggt tac tgg gct acc aac ttt tct 240

Glu Asn Ser Asp Gly Gly Tyr His Gly Tyr Trp Ala Thr Asn Phe Ser

65 70 75 80

gcc atc aac tca cat ttt ggg tcg tct aat gat ttg aag aaa ttg gtg 288

Ala Ile Asn Ser His Phe Gly Ser Ser Asn Asp Leu Lys Lys Leu Val

85 90 95

tca gca gct cat gac aag ggc atg tat gtt atg ctt gac gtg gtt gct 336

Ser Ala Ala His Asp Lys Gly Met Tyr Val Met Leu Asp Val Val Ala

100 105 110

aac cac gtt ggc ata cct tcc tcc agt ggc caa tac tcg gga tac acg 384

Asn His Val Gly Ile Pro Ser Ser Ser Gly Gln Tyr Ser Gly Tyr Thr

115 120 125

ttt gat caa agc tct cag tat cat agt tct tgt gat att aac tat gac 432

Phe Asp Gln Ser Ser Gln Tyr His Ser Ser Cys Asp Ile Asn Tyr Asp

130 135 140

aac caa aac tct att gaa caa tgc tgg atc tct ggc tta cct gat ctt 480

Asn Gln Asn Ser Ile Glu Gln Cys Trp Ile Ser Gly Leu Pro Asp Leu

145 150 155 160

aac acc gaa gat tca gcg gta gtc agc aag cta aac tcg att gtg tca 528

Asn Thr Glu Asp Ser Ala Val Val Ser Lys Leu Asn Ser Ile Val Ser

165 170 175

aac tgg gta tcc gaa tat gac ttt gat ggg ctt cgt att gat act gtc 576

Asn Trp Val Ser Glu Tyr Asp Phe Asp Gly Leu Arg Ile Asp Thr Val

180 185 190

aag cac att cgc aag gat ttt tgg gat ggc tat gta tct gct gca ggt 624

Lys His Ile Arg Lys Asp Phe Trp Asp Gly Tyr Val Ser Ala Ala Gly

195 200 205

gta ttt gcc act ggg gaa gtc ttg aac ggt gct gtt tct tat gtt gct 672

Val Phe Ala Thr Gly Glu Val Leu Asn Gly Ala Val Ser Tyr Val Ala

210 215 220

cca tac caa caa cat gtt ccc tct tta ctc aac tac cca ctg tat ttc 720

Pro Tyr Gln Gln His Val Pro Ser Leu Leu Asn Tyr Pro Leu Tyr Phe

225 230 235 240

ccc gtc aat gat gtg ttc acg aag gct tct acc atg agt cgt ttg gga 768

Pro Val Asn Asp Val Phe Thr Lys Ala Ser Thr Met Ser Arg Leu Gly

245 250 255

tca ggc tat gct gat atc cag tct ggc agc ttt aca aac aga aac cat 816

Ser Gly Tyr Ala Asp Ile Gln Ser Gly Ser Phe Thr Asn Arg Asn His

260 265 270

ctg gtt aac ttt atc gac aac cat gac aat cct cgt ttg tta tcc aag 864

Lcu Val Asn Phe Ile Asp Asn His Asp Asn Pro Arg Leu Leu Ser Lys

275 280 285

tct gat cag gtc ttg gtg aag aat gct ctt aca tac acc atg atg att 912

Ser Asp Gln Val Leu Val Lys Asn Ala Leu Thr Tyr Thr Met Met Ile

290 295 300

gaa gga atc cca gcc atg tac tat ggt acc gag caa tca ttc aat gga 960

Glu Gly Ile Pro Ala Met Tyr Tyr Gly Thr Glu Gln Ser Phe Asn Gly

305 310 315 320

ggc tct gac cct gcc aac aga gag gtc tta tgg acc acg aat tat tcg 1008

Gly Ser Asp Pro Ala Asn Arg Glu Val Leu Trp Thr Thr Asn Tyr Ser

325 330 335

acc aca tcc gac atg tac aag ttt gtc act tta ctc gtc aaa aca cgc 1056

Thr Thr Ser Asp Met Tyr Lys Phe Val Thr Leu Leu Val Lys Thr Arg

340 345 350

aag agc tcg gga aac acg gtt act aca ggc att gac cag acc aac aat 1104

Lys Ser Ser Gly Asn Thr Val Thr Thr Gly Ile Asp Gln Thr Asn Asn

355 360 365

gtt tat gtg ttt caa aga gac aag tat ctg gtt gtt gtg aac aat tac 1152

Val Tyr Val Phe Gln Arg Asp Lys Tyr Leu Val Val Val Asn Asn Tyr

370 375 380

ggc tca gga tcc acc aat tcg atc act gta aag gct ggt tca ttc tcc 1200

Gly Ser Gly Ser Thr Asn Ser Ile Thr Val Lys Ala Gly Ser Phe Ser

385 390 395 400

aat ggt gtt acc ctt gtg gat ata ttc tcg aat aaa aca gtg act gtg 1248

Asn Gly Val Thr Leu Val Asp Ile Phe Ser Asn Lys Thr Val Thr Val

405 410 415

tca aac gga tcg atc acc ttc cag ctt caa aat ggt aat cct gct gta 1296

Ser Asn Gly Ser Ile Thr Phe Gln Leu Gln Asn Gly Asn Pro Ala Val

420 425 430

ttc caa agc aaa 1308

Phe Gln Ser Lys

435

<210>135

<211>436

<212>PRT

<213> Syncephalastrum racemosum

<400>135

Ala Thr Ala Ser Asp Trp Glu Asn Arg Val Ile Tyr Gln Leu Leu Thr

1 5 10 15

Asp Arg Phe Ala Lys Ser Ser Asp Asp Thr Asn Gly Cys Ser Asn Leu

20 25 30

Gly Asn Tyr Cys Gly Gly Thr Phe Gln Gly lle Ile Asn His Leu Asp

35 40 45

Tyr Ile Ala Gly Met Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro

50 55 60

Glu Asn Ser Asp Gly Gly Tyr His Gly Tyr Trp Ala Thr Asn Phe Ser

65 70 75 80

Ala Ile Asn Ser His Phe Gly Ser Ser Asn Asp Leu Lys Lys Leu Val

85 90 95

Ser Ala Ala His Asp Lys Gly Met Tyr Val Met Leu Asp Val Val Ala

100 105 110

Asn His Val Gly Ile Pro Ser Ser Ser Gly Gln Tyr Ser Gly Tyr Thr

115 120 125

Phe Asp Gln Ser Ser Gln Tyr His Ser Ser Cys Asp Ile Asn Tyr Asp

130 135 140

Asn Gln Asn Ser Ile Glu Gln Cys Trp Ile Ser Gly Leu Pro Asp Leu

145 150 155 160

Asn Thr Glu Asp Ser Ala Val Val Ser Lys Leu Asn Ser Ile Val Ser

165 170 175

Asn Trp Val Ser Glu Tyr Asp Phe Asp Gly Leu Arg Ile Asp Thr Val

180 185 190

Lys His Ile Arg Lys Asp Phe Trp Asp Gly Tyr Val Ser Ala Ala Gly

195 200 205

Val Phe Ala Thr Gly Glu Val Leu Asn Gly Ala Val Ser Tyr Val Ala

210 215 220

Pro Tyr Gln Gln His Val Pro Ser Leu Leu Asn Tyr Pro Leu Tyr Phe

225 230 235 240

Pro Val Asn Asp Val Phe Thr Lys Ala Ser Thr Met Ser Arg Leu Gly

245 250 255

Ser Gly Tyr Ala Asp Ile Gln Ser Gly Ser Phe Thr Asn Arg Asn His

260 265 270

Leu Val Asn Phe Ile Asp Asn His Asp Asn Pro Arg Leu Leu Ser Lys

275 280 285

Ser Asp Gln Val Leu Val Lys Asn Ala Leu Thr Tyr Thr Met Met Ile

290 295 300

Glu Gly Ile Pro Ala Met Tyr Tyr Gly Thr Glu Gln Ser Phe Asn Gly

305 310 315 320

Gly Ser Asp Pro Ala Asn Arg Glu Val Leu Trp Thr Thr Asn Tyr Ser

325 330 335

Thr Thr Ser Asp Met Tyr Lys Phe Val Thr Leu Leu Val Lys Thr Arg

340 345 350

Lys Ser Ser Gly Asn Thr Val Thr Thr Gly Ile Asp Gln Thr Asn Asn

355 360 365

Val Tyr Val Phe Gln Arg Asp Lys Tyr Leu Val Val Val Asn Asn Tyr

370 375 380

Gly Ser Gly Ser Thr Asn Ser Ile Thr Val Lys Ala Gly Ser Phe Ser

385 390 395 400

Asn Gly Val Thr Leu Val Asp Ile Phe Ser Asn Lys Thr Val Thr Val

405 410 415

Ser Asn Gly Ser Ile Thr Phe Gln Leu Gln Asn Gly Asn Pro Ala Val

420 425 430

Phe Gln Ser Lys

435

<210>136

<211>297

<212>DNA

<213> Coniochaeta sp.

<220>

<221> CDS

<222>(1)..(297)

<400>136

gta gcc atc acg ttc aac gag ctc gtg tcc aca gcc tac ggc gat acg 48

Val Ala Ile Thr Phe Asn Glu Leu Val Ser Thr Ala Tyr Gly Asp Thr

1 5 10 15

atc aag ctc tcc ggc aac ata acc gcc cta ggc agc tgg aac gcg gcc 96

Ile Lys Leu Ser Gly Asn Ile Thr Ala Leu Gly Ser Trp Asn Ala Ala

20 25 30

aac gcc gtc agc ctg agc gcg tcg ggg tac acg gcc gcc aac ccg ctg 144

Asn Ala Val Ser Leu Ser Ala Ser Gly Tyr Thr Ala Ala Asn Pro Leu

35 40 45

tgg tcg ggc acg gtg aac ctc gcg ccg ggg acc ggg gtg cag tac aag 192

Trp Ser Gly Thr Val Asn Leu Ala Pro Gly Thr Gly Val Gln Tyr Lys

50 55 60

ttc gtg aag gtc ggc agc tcg gga agc gtc acc tgg gag gcg gac ccg 240

Phe Val Lys Val Gly Ser Ser Ser Gly Ser Val Thr Trp Glu Ala Asp Pro

65 70 75 80

aat cac acg tac gcc gtg ccg tgc gcg ggg gct act gtt agt ggg agc 288

Asn His Thr Tyr Ala Val Pro Cys Ala Gly Ala Thr Val Ser Gly Ser

85 90 95

tgg cag agc 297

Trp Gln Ser

<210>137

<211>99

<212>PRT

<213> Coniochaeta sp.

<400>137

Val Ala Ile Thr Phe Asn Glu Leu Val Ser Thr Ala Tyr Gly Asp Thr

1 5 10 15

Ile Lys Leu Ser Gly Asn Ile Thr Ala Leu Gly Ser Trp Asn Ala Ala

20 25 30

Asn Ala Val Ser Leu Ser Ala Ser Gly Tyr Thr Ala Ala Asn Pro Leu

35 40 45

Trp Ser Gly Thr Val Asn Leu Ala Pro Gly Thr Gly Val Gln Tyr Lys

50 55 60

Phe Val Lys Val Gly Ser Ser Ser Gly Ser Val Thr Trp Glu Ala Asp Pro

65 70 75 80

Asn His Thr Tyr Ala Val Pro Cys Ala Gly Ala Thr Val Ser Gly Ser

85 90 95

Trp Gln Ser

<210>138

<211>300

<212>DNA

<213> Trametes corrugata

<220>

<221> CDS

<222>(1)..(300)

<400>138

gtt gca gta tcg ttc acg cac agc atc acc act gtg ccc ggc gac act 48

Val Ala Val Ser Phe Thr His Ser Ile Thr Thr Val Pro Gly Asp Thr

1 5 10 15

atc aag atc gcg ggt aac acg acg caa ctc ggt agc tgg act gta gct 96

Ile Lys Ile Ala Gly Asn Thr Thr Gln Leu Gly Ser Trp Thr Val Ala

20 25 30

tcc gca ccc gcg ctc tca gcg tca tcg tac acg tcg agt aac cct gta 144

Ser Ala Pro Ala Leu Ser Ala Ser Ser Ser Tyr Thr Ser Ser Asn Pro Val

35 40 45

tgg acg att acg ctg agc atg ccg gcg aag cag gcg gtg cag tat aag 192

Trp Thr Ile Thr Leu Ser Met Pro Ala Lys Gln Ala Val Gln Tyr Lys

50 55 60

Ltt gtt aag gtg gcg agt ggg ggc gcg gtg acg tgg gag agc gat ccg 240

Phe Val Lys Val Ala Ser Gly Gly Ala Val Thr Trp Glu Ser Asp Pro

65 70 75 80

aat cgt agt tat agc gtc ccg gcg tgt cag gcg agt gcg gcg gtg agt 288

Asn Arg Ser Tyr Ser Val Pro Ala Cys Gln Ala Ser Ala Ala Val Ser

85 90 95

agt agt tgg cag 300

Ser Ser Trp Gln

100

<210>139

<211>100

<212>PRT

<213> Trametes corrugata

<400>139

Val Ala Val Ser Phe Thr His Ser Ile Thr Thr Val Pro Gly Asp Thr

1 5 10 15

Ile Lys Ile Ala Gly Asn Thr Thr Gln Leu Gly Ser Trp Thr Val Ala

20 25 30

Ser Ala Pro Ala Leu Ser Ala Ser Ser Ser Tyr Thr Ser Ser Asn Pro Val

35 40 45

Trp Thr Ile Thr Leu Ser Met Pro Ala Lys Gln Ala Val Gln Tyr Lys

50 55 60

Phe Val Lys Val Ala Ser Gly Gly Ala Val Thr Trp Glu Ser Asp Pro

65 70 75 80

Asn Arg Ser Tyr Ser Val Pro Ala Cys Gln Ala Ser Ala Ala Val Ser

85 90 95

Ser Ser Trp Gln

100

<210>140

<211>306

<212>DNA

<213>Valsario spartii

<220>

<221> CDS

<222>(1)..(306)

<400>140

gtc tcc gtc aca ttc acc aac ctc gtc aca acc cag gtc ggc gac acc 48

Val Ser Val Thr Phe Thr Asn Leu Val Thr Thr Gln Val Gly Asp Thr

1 5 10 15

atc aaa gtc acc ggc aac gtc tcg cag ctg ggc aac tgg aac cct tcc 96

Ile Lys Val Thr Gly Asn Val Ser Gln Leu Gly Asn Trp Asn Pro Ser

20 25 30

tcc gcc ccc gcc tta tcc gca acc gga tac acg gcc agc aac ccc aaa 144

Ser Ala Pro Ala Leu Ser Ala Thr Gly Tyr Thr Ala Ser Asn Pro Lys

35 40 45

tgg agc gga acc gtc aag ttg ccc gcc ggc tcg acg gtg cag tat aag 192

Trp Ser Gly Thr Val Lys Leu Pro Ala Gly Ser Thr Val Gln Tyr Lys

50 55 60

ttt gtg aag gtc gct agc ggg ggt ggc gcc gtg act tgg gag agc gat 240

Phe Val Lys Val Ala Ser Gly Gly Gly Ala Val Thr Trp Glu Ser Asp

65 70 75 80

ccc aac agg agt tat agc gtt cct agt tgt cag gct agc gcg act gtt 288

Pro Asn Arg Ser Tyr Ser Val Pro Ser Cys Gln Ala Ser Ala Thr Val

85 90 95

gat tcg agc tgg aag taa 306

Asp Ser Ser Trp Lys

100

<210>141

<211>101

<212>PRT

<213>Valsario spartii

<400>141

Val Ser Val Thr Phe Thr Asn Leu Val Thr Thr Gln Val Gly Asp Thr

1c 5 10 15

Ile Lys Val Thr Gly Asn Val Ser Gln Leu Gly Asn Trp Asn Pro Ser

20 25 30

Ser Ala Pro Ala Leu Ser Ala Thr Gly Tyr Thr Ala Ser Asn Pro Lys

35 40 45

Trp Ser Gly Thr Val Lys Leu Pro Ala Gly Ser Thr Val Gln Tyr Lys

50 55 60

Phe Val Lys Val Ala Ser Gly Gly Gly Ala Val Thr Trp Glu Ser Asp

65 70 75 80

Pro Asn Arg Ser Tyr Ser Val Pro Ser Cys Gln Ala Ser Ala Thr Val

85 90 95

Asp Ser Ser Trp Lys

100

<210>142

<211>312

<212>DNA

<213> Penicillium sp.

<220>

<221> CDS

<222>(1)..(312)

<400>142

ttg cca gtt ttg ttc aaa gag att gtc acc act tca tac ggg cag agt 48

Leu Pro Val Leu Phe Lys Glu Ile Val Thr Thr Ser Tyr Gly Gln Ser

1 5 10 15

atc tat atc tca ggc tct ata agt caa ctc gga agc tgg gac acg tct 96

Ile Tyr Ile Ser Gly Ser Ile Ser Gln Leu Gly Ser Trp Asp Thr Ser

20 25 30

agc gcc gtt gcc ctc tct gct gat cag tac aca tca tcc agc cat ctg 144

Ser Ala Val Ala Leu Ser Ala Asp Gln Tyr Thr Ser Ser Ser His Leu

35 40 45

tgg tat gtt gtc gtg aca att cca gtg ggc acc tcg ttc cag tac aag 192

Trp Tyr Val Val Val Thr Ile Pro Val Gly Thr Ser Phe Gln Tyr Lys

50 55 60

ttc atc gag gag acg agc ggg tct agt act att act tgg gag agt gat 240

Phe Ile Glu Glu Thr Ser Gly Ser Ser Thr Ile Thr Trp Glu Ser Asp

65 70 75 80

ccg aac cgc tct tat acg gtg cca acg ggc tgt gca ggc tca acg gct 288

Pro Asn Arg Ser Tyr Thr Val Pro Thr Gly Cys Ala Gly Ser Thr Ala

85 90 95

acc gtc aca gcg acc tgg aga tag 312

Thr Val Thr Ala Thr Trp Arg

100

<210>143

<211>103

<212>PRT

<213> Penicillium sp.

<400>143

Leu Pro Val Leu Phe Lys Glu Ile Val Thr Thr Ser Tyr Gly Gln Ser

1 5 10 15

Ile Tyr Ile Ser Gly Ser Ile Ser Gln Leu Gly Ser Trp Asp Thr Ser

20 25 30

Ser Ala Val Ala Leu Ser Ala Asp Gln Tyr Thr Ser Ser Ser His Leu

35 40 45

Trp Tyr Val Val Val Thr Ile Pro Val Gly Thr Ser Phe Gln Tyr Lys

50 55 60

Phe Ile Glu Glu Thr Ser Gly Ser Ser Thr Ile Thr Trp Glu Ser Asp

65 70 75 80

Pro Asn Arg Ser Tyr Thr Val Pro Thr Gly Cys Ala Gly Ser Thr Ala

85 90 95

Thr Val Thr Ala Thr Trp Arg

100

<210>144

<211>123

<212>DNA

<213> Coniochaeta sp.

<220>

<221> CDS

<222>(1)..(123)

<400>144

acg acg tcg acg agt acg ggg acg agc tcg acc acg agg agg acg ggg acg 48

Thr Thr Ser Thr Ser Thr Gly Thr Ser Ser Thr Thr Arg Thr Gly Thr

1 5 10 15

acg ctg acg ag tcc acg aag act acg gcg tcg acg acg acg aag aag 96

Thr Leu Thr Thr Ser Thr Lys Thr Thr Ala Ser Thr Thr Thr Thr Lys

20 25 30

agc agc agt Lcc tgc acc gcc aca gca 123

Ser Ser Ser Ser Ser Cys Thr Ala Thr Ala

35 40

<210>145

<211>41

<212>PRT

<213> Coniochaeta sp.

<400>145

Thr Thr Ser Thr Ser Thr Gly Thr Ser Ser Thr Thr Arg Thr Gly Thr

1 5 10 15

Thr Leu Thr Thr Ser Thr Lys Thr Thr Ala Ser Thr Thr Thr Thr Lys

20 25 30

Ser Ser Ser Ser Ser Cys Thr Ala Thr Ala

35 40

<210>146

<211>30

<212>DNA

<213> Trametes corrugata

<220>

<221> CDS

<222>(1)..(30)

<400>146

act acc aca gcc tcc gcg tgt ccg act tcc 30

Thr Thr Thr Ala Ser Ala Cys Pro Thr Ser

1 5 10

<210>147

<211>10

<212>PRT

<213> Trametes corrugata

<400>147

Thr Thr Thr Ala Ser Ala Cys Pro Thr Ser

1 5 10

<210>148

<211>33

<212>DNA

<213>Valsario spartii

<220>

<221> CDS

<222>(1)..(33)

<400>148

acc acc tcc cca acc gcc ggc tgc ccc tcc acc 33

Thr Thr Ser Pro Thr Ala Gly Cys Pro Ser Thr

1 5 10

<210>149

<211>11

<212>PRT

<213>Valsario spartii

<400>149

Thr Thr Ser Pro Thr Ala Gly Cys Pro Ser Thr

1 5 10

<210>150

<211>132

<212>DNA

<213> Penicillium sp.

<220>

<221> CDS

<222>(1)..(132)

<400>150

act acc aca acc tcg tcg acg gct tct act tca acg aca acg tca acc 48

Thr Thr Thr Thr Ser Ser Thr Ala Ser Thr Ser Thr Thr Thr Ser Thr

1 5 10 15

aca ctg aag act acc acg aca acg tca act act tcg aaa act act acg 96

Thr Leu Lys Thr Thr Thr Thr Thr Thr Ser Thr Thr Ser Lys Thr Thr Thr Thr

20 25 30

tcc act aca tcc acg agc tgc aca cag gct act gca 132

Set Thr Thr Ser Thr Ser Cys Thr Gln Ala Thr Ala

35 40

<210>151

<211>44

<212>PRT

<213> Penicillium sp.

<400>151

Thr Thr Thr Thr Ser Ser Thr Ala Ser Thr Ser Thr Thr Thr Ser Thr

1 5 10 15

Thr Leu Lys Thr Thr Thr Thr Thr Thr Ser Thr Thr Ser Lys Thr Thr Thr Thr

20 25 30

Ser Thr Thr Ser Ser Thr Ser Cys Thr Gln Ala Thr Ala

35 40

<210>152

<400>152

000

<210>153

<400>153

000

<210>154

<211>1221

<212>DNA

<213> Streptomyces limosus

<220>

<221> CDS

<222>(1)..(1221)

<400>154

gcc ccg ccc ggg gcg aag gac gtc acc gcc gtc ctc ttc gag tgg aag 48

Ala Pro Pro Gly Ala Lys Asp Val Thr Ala Val Leu Phe Glu Trp Lys

1 5 10 15

ttc gcc tcc gta gcc cgc gcc tgc acc gac agc ctc ggc ccg gcc ggc 96

Phe Ala Ser Val Ala Arg Ala Cys Thr Asp Ser Leu Gly Pro Ala Gly

20 25 30

tac gga tac gtc cag gtc tcg ccg ccc cag gag cac atc cag ggc agc 144

Tyr Gly Tyr Val Gln Val Ser Pro Pro Gln Glu His Ile Gln Gly Ser

35 40 45

cag tgg tgg acc tcc tac cag ccc gtc agc tac aag atc gcc gga cgg 192

Gln Trp Trp Thr Ser Tyr Gln Pro Val Ser Tyr Lys Ile Ala Gly Arg

50 55 60

ctc ggc gac cgc gcc gcc ttc aag tcc atg gtc gac acc tgc cac gcg 240

Leu Gly Asp Arg Ala Ala Phe Lys Ser Met Val Asp Thr Cys His Ala

65 70 75 80

gcc ggc gtc aag gtc gtc gcc gac tcg gtc atc aac cac atg gcc gcg 288

Ala Gly Val Lys Val Val Ala Asp Ser Val Ile Asn His Met Ala Ala

85 90 95

ggt tcc ggc acc ggc acc ggc ggc agc gcg tac cag aag tac gac tac 336

Gly Ser Gly Thr Gly Thr Gly Gly Ser Ala Tyr Gln Lys Tyr Asp Tyr

100 105 110

ccg ggc atc tgg tcc ggc gcc gac atg gac gac tgc cgc agc gag atc 384

Pro Gly Ile Trp Ser Gly Ala Asp Met Asp Asp Cys Arg Ser Glu Ile

115 120 125

aac gac tac ggc aac cgc gcc aac gtc cag aac tgc gaa ctg gtc ggc 432

Asn Asp Tyr Gly Asn Arg Ala Asn Val Gln Asn Cys Glu Leu Val Gly

130 135 140

ctc gcc gac ctc gac acc ggt gag tcg tac gtc cgc gac cgc atc gcc 480

Leu Ala Asp Leu Asp Thr Gly Glu Ser Tyr Val Arg Asp Arg Ile Ala

145 150 155 160

gcc tac ctc aac gac ctg ctc tcg ctc ggt gtg gac ggc ttc cgc atc 528

Ala Tyr Leu Asn Asp Leu Leu Ser Leu Gly Val Asp Gly Phe Arg Ile

165 170 175

gac gcc gcc aag cac atg ccc gcc gcc gac ctc acc gcc atc aag gcc 576

Asp Ala Ala Lys His Met Pro Ala Ala Asp Leu Thr Ala Ile Lys Ala

180 185 190

aag gtc ggc aac ggg agc acg tac tgg aag cag gag gcc atc cac ggc 624

Lys Val Gly Asn Gly Ser Thr Tyr Trp Lys Gln Glu Ala Ile His Gly

195 200 205

gcg ggc gag gcc gtc cag ccc agc gag tac ctc ggc acc ggc gac gtc 672

Ala Gly Glu Ala Val Gln Pro Ser Glu Tyr Leu Gly Thr Gly Asp Val

210 215 220

cag gag ttc cgc tac gcc cgc gac ctc aag cgg gtc ttc cag aac gag 720

Gln Glu Phe Arg Tyr Ala Arg Asp Leu Lys Arg Val Phe Gln Asn Glu

225 230 235 240

aac ctc gcc cac ctg aag aac ttc ggc gag gac tgg ggc tac atg gcg 768

Asn Leu Ala His Leu Lys Asn Phe Gly Glu Asp Trp Gly Tyr Met Ala

245 250 255

agc ggc aag tcc gcc gtc ttc gtc gac aac cac gac acc gag cgg ggc 816

Ser Gly Lys Ser Ala Val Phe Val Asp Asn His Asp Thr Glu Arg Gly

260 265 270

ggc gac acc ctc aac tac aag aac ggc tcc gcc tac acc ctc gcc ggc 864

Gly Asp Thr Leu Asn Tyr Lys Asn Gly Ser Ala Tyr Thr Leu Ala Gly

275 280 285

gtc ttc atg ctg gcc tgg ccc tac ggc tcc ccg gac gtc cac tcc ggc 912

Val Phe Met Leu Ala Trp Pro Tyr Gly Ser Pro Asp Val His Ser Gly

290 295 300

tac gag ttc acc gac cac gac gcc ggc ccg ccc aac ggc ggc acc gtc 960

Tyr Glu Phe Thr Asp His Asp Ala Gly Pro Pro Asn Gly Gly Thr Val

305 310 315 320

aac gcc tgc tac agc gac ggc tgg aag tgc cag cac gcc tgg ccc gag 1008

Asn Ala Cys Tyr Ser Asp Gly Trp Lys Cys Gln His Ala Trp Pro Glu

325 330 335

ctc tcc tcc atg gtc ggc ctg cgc aac acc gcc tcc ggg cag ccc gtc 1056

Leu Ser Ser Met Val Gly Leu Arg Asn Thr Ala Ser Gly Gln Pro Val

340 345 350

acc aac tgg tgg gac aac ggc ggc gac cag atc gcc ttc ggc cgc ggc 1104

Thr Asn Trp Trp Asp Asn Gly Gly Asp Gln Ile Ala Phe Gly Arg Gly

355 360 365

gac aag gcg tac gtc gcc atc aac cac gag ggc tcc gcg ctg aac cgc 1152

Asp Lys Ala Tyr Val Ala Ile Asn His Glu Gly Ser Ala Leu Asn Arg

370 375 380

acc ttc cag agc ggc ctg ccc ggc ggc gcc tac tgc gac gtc cag agc 1200

Thr Phe Gln Ser Gly Leu Pro Gly Gly Ala Tyr Cys Asp Val Gln Ser

385 390 395 400

ggc agg tcc gtc acg gtc ggc 1221

Gly Arg Ser Val Thr Val Gly

405

<210>155

<211>407

<212>PRT

<213> Streptomyces limosus

<400>155

Ala Pro Pro Gly Ala Lys Asp Val Thr Ala Val Leu Phe Glu Trp Lys

1 5 10 15

Phe Ala Ser Val Ala Arg Ala Cys Thr Asp Ser Leu Gly Pro Ala Gly

20 25 30

Tyr Gly Tyr Val Gln Val Ser Pro Pro Gln Glu His Ile Gln Gly Ser

35 40 45

Gln Trp Trp Thr Ser Tyr Gln Pro Val Ser Tyr Lys Ile Ala Gly Arg

50 55 60

Leu Gly Asp Arg Ala Ala Phe Lys Ser Met Val Asp Thr Cys His Ala

65 70 75 80

Ala Gly Val Lys Val Val Ala Asp Ser Val Ile Asn His Met Ala Ala

85 90 95

Gly Ser Gly Thr Gly Thr Gly Gly Ser Ala Tyr Gln Lys Tyr Asp Tyr

100 105 110

Pro Gly Ile Trp Ser Gly Ala Asp Met Asp Asp Cys Arg Ser Glu Ile

115 120 125

Asn Asp Tyr Gly Asn Arg Ala Asn Val Gln Asn Cys Glu Leu Val Gly

130 135 140

Leu Ala Asp Leu Asp Thr Gly Glu Ser Tyr Val Arg Asp Arg Ile Ala

145 150 155 160

Ala Tyr Leu Asn Asp Leu Leu Ser Leu Gly Val Asp Gly Phe Arg Ile

165 170 175

Asp Ala Ala Lys His Met Pro Ala Ala Asp Leu Thr Ala Ile Lys Ala

                                                                                   

Lys Val Gly Asn Gly Ser Thr Tyr Trp Lys Gln Glu Ala Ile His Gly

195 200 205

Ala Gly Glu Ala Val Gln Pro Ser Glu Tyr Leu Gly Thr Gly Asp Val

210 215 220

Gln Glu Phe Arg Tyr Ala Arg Asp Leu Lys Arg Val Phe Gln Asn Glu

225 230 235 240

Asn Leu Ala His Leu Lys Asn Phe Gly Glu Asp Trp Gly Tyr Met Ala

245 250 255

Ser Gly Lys Ser Ala Val Phe Val Asp Asn His Asp Thr Glu Arg Gly

260 265 270

Gly Asp Thr Leu Asn Tyr Lys Asn Gly Ser Ala Tyr Thr Leu Ala Gly

275 280 285

Val Phe Met Leu Ala Trp Pro Tyr Gly Ser Pro Asp Val His Ser Gly

290 295 300

Tyr Glu Phe Thr Asp His Asp Ala Gly Pro Pro Asn Gly Gly Thr Val

305 310 315 320

Asn Ala Cys Tyr Ser Asp Gly Trp Lys Cys Gln His Ala Trp Pro Glu

325 330 335

Leu Ser Ser Met Val Gly Leu Arg Asn Thr Ala Ser Gly Gln Pro Val

340 345 350

Thr Asn Trp Trp Asp Asn Gly Gly Asp Gln Ile Ala Phe Gly Arg Gly

355 360 365

Asp Lys Ala Tyr Val Ala Ile Asn His Glu Gly Ser Ala Leu Asn Arg

370 375 380

Thr Phe Gln Ser Gly Leu Pro Gly Gly Ala Tyr Cys Asp Val Gln Ser

385 390 395 400

Gly Arg Ser Val Thr Val Gly

405

<210>156

<211>1443

<212>DNA

<213>Absidia cristata

<220>

<221> CDS

<222>(1)..(1443)

<220>

<221>sig_peptide

<222>(1)..(120)

<220>

<221>misc_feature

<222>(121)..(1443)

<223> catalytic domain

<400>156

atg cat cca acg cgt tgg gag ctc tcc cat atg gtc gac ctg cag gcg 48

Met His Pro Thr Arg Trp Glu Leu Ser His Met Val Asp Leu Gln Ala

1 5 10 15

gcc gca cta gtg att atg aag ctt tcc att ctt aca tta tcc aca ctc 96

Ala Ala Leu Val Ile Met Lys Leu Ser Ile Leu Thr Leu Ser Thr Leu

20 25 30

ctt tgt gct act gct gtt ctt ggt cgt ccc att gtg aag cgt gca ggc 144

Leu Cys Ala Thr Ala Val Leu Gly Arg Pro Ile Val Lys Arg Ala Gly

35 40 45

gcc gat gat tgg aga tca cgt tcc atc tat caa tta ttg act gat cgc 192

Ala Asp Asp Trp Arg Ser Arg Ser Ile Tyr Gln Leu Leu Thr Asp Arg

50 55 60

ttt gct ggt ggc ggt gat tgt tct gat tta tcc gat tat tgt ggt ggt 240

Phc Ala Gly Gly Gly Asp Cys Ser Asp Leu Ser Asp Tyr Cys Gly Gly

65 70 75 80

aat tat aaa ggc atg att gaa cac ctg gat tat atc caa gga atg gga 288

Asn Tyr Lys Gly Met Ile Glu His Leu Asp Tyr Ile Gln Gly Met Gly

85 90 95

ttc gat gcc atc tgg att tcc ccc atc cct acc aac tca ccc ggc ggt 336

Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro Thr Asn Ser Pro Gly Gly

100 105 110

tac cat ggc tac tgg gca act gac ttc aat ggt tta aat gaa aac ttt 384

Tyr His Gly Tyr Trp Ala Thr Asp Phe Asn Gly Leu Asn Glu Asn Phe

115 120 125

gga acc aag gac gat ctc aag gct ttg gtg gat gca gca cat aag ctc 432

Gly Thr Lys Asp Asp Leu Lys Ala Leu Val Asp Ala Ala His Lys Leu

130 135 140

gac atg tat gtc atg ttg gat gtc gtt gcc aat cat gct gga caa ccc 480

Asp Met Tyr Val Met Leu Asp Val Val Ala Asn His Ala Gly Gln Pro

145 150 155 160

agt acg gca ggt gac tat tct ggc tac aca ttc gat tct aaa gac caa 528

Ser Thr Ala Gly Asp Tyr Ser Gly Tyr Thr Phe Asp Ser Lys Asp Gln

165 170 175

tac cat tcc caa tgc aaa atc gat tat gat gat caa aac tct att gag 576

Tyr His Ser Gln Cys Lys Ile Asp Tyr Asp Asp Gln Asn Ser Ile Glu

180 185 190

cag tgt tgg gtg gct gat gtg ttg cct gac atc aac act gag gat gat 624

Gln Cys Trp Val Ala Asp Val Leu Pro Asp Ile Asn Thr Glu Asp Asp

195 200 205

aac gtg gtc aag acg ctc aat gat att gtc agc aac tgg gta act aca 672

Asn Val Val Lys Thr Leu Asn Asp Ile Val Ser Asn Trp Val Thr Thr

210 215 220

tat ggc ttt gat ggt att cgc att gac act gtc aag cat gta cgt caa 720

Tyr Gly Phe Asp Gly Ile Arg Ile Asp Thr Val Lys His Val Arg Gln

225 230 235 240

gac ttt tgg gat gga tac aat gaa gca gct ggt gta ttt gct aca gga 768

Asp Phe Trp Asp Gly Tyr Asn Glu Ala Ala Gly Val Phe Ala Thr Gly

245 250 255

gaa gtc ttt gat ggt gat tca tcc tat gtt ggt gga tat caa aag cat 816

Glu Val Phe Asp Gly Asp Ser Ser Tyr Val Gly Gly Tyr Gln Lys His

260 265 270

ttg gac tcg ctt ctc aat tac cca atg tat tac gca ctc aat gat gta 864

Leu Asp Ser Leu Leu Asn Tyr Pro Met Tyr Tyr Ala Leu Asn Asp Val

275 280 285

ttt ggt tct gga aag ggt ttt agt cgt atc agc gag atg att gca acc 912

Phe Gly Ser Gly Lys Gly Phe Ser Arg Ile Ser Glu Met Ile Ala Thr

290 295 300

aat gca gat gca ttt gct gat acc agt gtt ctg acc aac ttt att gac 960

Asn Ala Asp Ala Phe Ala Asp Thr Ser Val Leu Thr Asn Phe Ile Asp

305 310 315 320

aac cat gat aac cca cgt ttc ctt aat acc aac aag gat act act ctc 1008

Asn His Asp Asn Pro Arg Phe Leu Asn Thr Asn Lys Asp Thr Thr Leu

325 330 335

ttc aag aac gct ttg acc tac gtg ttg ctc gct gat ggt att cca gtg 1056

Phe Lys Asn Ala Leu Thr Tyr Val Leu Leu Ala Asp Gly Ile Pro Val

340 345 350

gtg tat tat gga tca gaa caa ggc ttt tca ggt ggt gct gat cct gcc 1104

Val Tyr Tyr Gly Ser Glu Gln Gly Phe Ser Gly Gly Ala Asp Pro Ala

355 360 365

aat cgt gaa gca tta tgg tca act gac ttt gac acc tcg tcc gat ttg 1152

Asn Arg Glu Ala Leu Trp Ser Thr Asp Phe Asp Thr Ser Ser Asp Leu

370 375 380

tac aag ttt atg gct act gtc aac aag gat gtt cgt caa aag gaa aac 1200

Tyr Lys Phe Met Ala Thr Val Asn Lys Asp Val Arg Gln Lys Glu Asn

385 390 395 400

aaa aag gtg gtg atg gat gtt gat gtg caa gac aac gtg tat gca ttc 1248

Lys Lys Val Val Met Asp Val Asp Val Gln Asp Asn Val Tyr Ala Phe

405 410 415

atg cac ggc gat gct ctt gtg gta ttg aac aac tac ggc agt gga gcc 1296

Met His Gly Asp Ala Leu Val Val Leu Asn Asn Tyr Gly Ser Gly Ala

420 425 430

agc aac gag gtt act gtc aag gtc gga tca cat gtt gat gat gga gcc 1344

Ser Asn Glu Val Thr Val Lys Val Gly Ser His Val Asp Asp Gly Ala

435 440 445

aag atg aac gac gtc ttt acc aat agc aca gtc tcg gta tct ggt ggt 1392

Lys Met Asn Asp Val Phe Thr Asn Ser Thr Val Ser Val Ser Gly Gly

450 455 460

tca ttc act ttc aaa ctt gac aat gga aat cct gcc atc ttt acc act 1440

Ser Phe Thr Phe Lys Leu Asp Asn Gly Asn Pro Ala Ile Phe Thr Thr

465 470 475 480

gct 1443

Ala

<210>157

<211>481

<212>PRT

<213>Absidia cristata

<400>157

Met His Pro Thr Arg Trp Glu Leu Ser His Met Val Asp Leu Gln Ala

1 5 10 15

Ala Ala Leu Val Ile Met Lys Leu Ser Ile Leu Thr Leu Ser Thr Leu

20 25 30

Leu Cys Ala Thr Ala Val Leu Gly Arg Pro Ile Val Lys Arg Ala Gly

35 40 45

Ala Asp Asp Trp Arg Ser Arg Ser Ile Tyr Gln Leu Leu Thr Asp Arg

50 55 60

Phe Ala Gly Gly Gly Asp Cys Ser Asp Leu Ser Asp Tyr Cys Gly Gly

65 70 75 80

Asn Tyr Lys Gly Met Ile Glu His Leu Asp Tyr Ile Gln Gly Met Gly

85 90 95

Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro Thr Asn Ser Pro Gly Gly

100 105 110

Tyr His Gly Tyr Trp Ala Thr Asp Phe Asn Gly Leu Asn Glu Asn Phe

115 120 125

Gly Thr Lys Asp Asp Leu Lys Ala Leu Val Asp Ala Ala His Lys Leu

130 135 140

Asp Met Tyr Val Met Leu Asp Val Val Ala Asn His Ala Gly Gln Pro

145 150 155 160

Ser Thr Ala Gly Asp Tyr Ser Gly Tyr Thr Phe Asp Ser Lys Asp Gln

                                                                                       

Tyr His Ser Gln Cys Lys Ile Asp Tyr Asp Asp Gln Asn Ser Ile Glu

180 185 190

Gln Cys Trp Val Ala Asp Val Leu Pro Asp Ile Asn Thr Glu Asp Asp

195 200 205

Asn Val Val Lys Thr Leu Asn Asp Ile Val Ser Asn Trp Val Thr Thr

210 215 220

Tyr Gly Phe Asp Gly Ile Arg Ile Asp Thr Val Lys His Val Arg Gln

225 230 235 240

Asp Phe Trp Asp Gly Tyr Asn Glu Ala Ala Gly Val Phe Ala Thr Gly

245 250 255

Glu Val Phe Asp Gly Asp Ser Ser Tyr Val Gly Gly Tyr Gln Lys His

260 265 270

Leu Asp Ser Leu Leu Asn Tyr Pro Met Tyr Tyr Ala Leu Asn Asp Val

275 280 285

Phe Gly Ser Gly Lys Gly Phe Ser Arg Ile Ser Glu Met Ile Ala Thr

290 295 300

Asn Ala Asp Ala Phe Ala Asp Thr Ser Val Leu Thr Asn Phe Ile Asp

305 310 315 320

Asn His Asp Asn Pro Arg Phe Leu Asn Thr Asn Lys Asp Thr Thr Leu

325 330 335

Phe Lys Asn Ala Leu Thr Tyr Val Leu Leu Ala Asp Gly Ile Pro Val

340 345 350

Val Tyr Tyr Gly Ser Glu Gln Gly Phe Ser Gly Gly Ala Asp Pro Ala

355 360 365

Asn Arg Glu Ala Leu Trp Ser Thr Asp Phe Asp Thr Ser Ser Asp Leu

370 375 380

Tyr Lys Phe Met Ala Thr Val Asn Lys Asp Val Arg Gln Lys Glu Asn

385 390 395 400

Lys Lys Val Val Met Asp Val Asp Val Gln Asp Asn Val Tyr Ala Phe

405 410 415

Met His Gly Asp Ala Leu Val Val Leu Asn Asn Tyr Gly Ser Gly Ala

420 425 430

Ser Asn Glu Val Thr Val Lys Val Gly Ser His Val Asp Asp Gly Ala

435 440 445

Lys Met Asn Asp Val Phe Thr Asn Ser Thr Val Ser Val Ser Gly Gly

450 455 460

Ser Phe Thr Phe Lys Leu Asp Asn Gly Asn Pro Ala Ile Phe Thr Thr

465 470 475 480

Ala

<210>158

<211>1878

<212>DNA

<213>Acremonium sp.

<220>

<221> CDS

<222>(1)..(1878)

<220>

<221>sig_peptide

<222>(1)..(63)

<220>

<221>misc_feature

<222>(64)..(1506)

<223> catalytic domain

<220>

<221>misc_feature

<222>(1507)..(1584)

<223> connector

<220>

<221>misc_feature

<222>(1585)..(1878)

<223>CBM

<400>158

atg cgc act ctc cac caa gcc ctt ctt gtc ctg gcc gga gca gtc ctg 48

Met Arg Thr Leu His Gln Ala Leu Leu Val Leu Ala Gly Ala Val Leu

1 5 10 15

gaa gct tcg caa ggt gct gcc ggg ctc tcg gct gcc gag tgg cgg agc 96

Glu Ala Ser Gln Gly Ala Ala Gly Leu Ser Ala Ala Glu Trp Arg Ser

20 25 30

cag tcc atc tac cag gtt gtc acc gac agg ttc gcc cgg acc gac ctg 144

Gln Ser Ile Tyr Gln Val Val Thr Asp Arg Phe Ala Arg Thr Asp Leu

35 40 45

tcg acc acg gcg tcg tgc aac acg gca gac caa gtc tac tgc gga ggg 192

Ser Thr Thr Ala Ser Cys Asn Thr Ala Asp Gln Val Tyr Cys Gly Gly

50 55 60

aca tgg cag ggg ctc atc tcc aag ctg gac tac atc cag ggc atg ggt 240

Thr Trp Gln Gly Leu Ile Ser Lys Leu Asp Tyr Ile Gln Gly Met Gly

65 70 75 80

ttc acc gcc gta tgg atc tca cea gtg gtc aag cag gtg gaa ggc aat 288

Phe Thr Ala Val Trp Ile Ser Pro Val Val Lys Gln Val Glu Gly Asn

85 90 95

tcc cag gac ggg tcg gcc tat cac gga tac tgg gcg cag gat atc tgg 336

Ser Gln Asp Gly Ser Ala Tyr His Gly Tyr Trp Ala Gln Asp Ile Trp

100 105 110

gcc ttg aat ccg gct ttt ggg acc gag gag gat ctc gct gcg ctt gcc 384

Ala Leu Asn Pro Ala Phe Gly Thr Glu Glu Asp Leu Ala Ala Leu Ala

115 120 125

gcg gcg ctg cat gcc cga ggc atg tac ctc atg gtt gac att gtc acc 432

Ala Ala Leu His Ala Arg Gly Met Tyr Leu Met Val Asp Ile Val Thr

130 135 140

aac cac atg gca tac atg ggc tgc ggc acc tgt gta gac tac agc ctg 480

Asn His Met Ala Tyr Met Gly Cys Gly Thr Cys Val Asp Tyr Ser Leu

145 150 155 160

ttc aac ccc ttc tca tcg tca tcg tac ttc cac cca tat tgc gcc atc 528

Phe Asn Pro Phe Ser Ser Ser Ser Ser Tyr Phe His Pro Tyr Cys Ala Ile

165 170 175

gac tac agc aac cag acg tcg gtc gag gtt tgc tgg caa ggg gat aac 576

Asp Tyr Ser Asn Gln Thr Ser Val Glu Val Cys Trp Gln Gly Asp Asn

180 185 190

att gtc agt ctg cct gac ctg cgc acc gag gat gac acg gtg cgc agc 624

Ile Val Ser Leu Pro Asp Leu Arg Thr Glu Asp Asp Thr Val Arg Ser

195 200 205

atc tgg aac cgc tgg gtt agc cag ctc gtg tcc aac tac tcc atc gac 672

Ile Trp Asn Arg Trp Val Ser Gln Leu Val Ser Asn Tyr Ser Ile Asp

210 215 220

ggc ttc cga gtc gac agc gca aaa cac gtc gag acg tcc ttt tgg caa 720

Gly Phe Arg Val Asp Ser Ala Lys His Val Glu Thr Ser Phe Trp Gln

225 230 235 240

gac ttc tcg aca gcg gcg ggc gtg tac ctg ctg ggc gag gtc ttt gac 768

Asp Phe Ser Thr Ala Ala Gly Val Tyr Leu Leu Gly Glu Val Phe Asp

245 250 255

ggg gac ccg tcg tac gtg gcg cct tac cag aac tac ctc aac ggg gtt 816

Gly Asp Pro Ser Tyr Val Ala Pro Tyr Gln Asn Tyr Leu Asn Gly Val

260 265 270

ctg gat tat ccc agc tac tac tgg atc ctc cgg gct ttc cag tca tcc 864

Leu Asp Tyr Pro Ser Tyr Tyr Trp Ile Leu Arg Ala Phe Gln Ser Ser

275 280 285

agc ggc agc atc agc gac ctc gtc tcc ggg ctc aac acg ctc cat ggc 912

Ser Gly Ser Ile Ser Asp Leu Val Ser Gly Leu Asn Thr Leu His Gly

290 295 300

gtt gct ctg gac ctg agt cta tat ggg tcc ttc ctc gag aac cac gat 960

Val Ala Leu Asp Leu Ser Leu Tyr Gly Ser Phe Leu Glu Asn His Asp

305 310 315 320

gtg gcg cgg ttt gcg tcc ttc acg cag gac atg tcc cta gcg aag aat 1008

Val Ala Arg Phe Ala Ser Phe Thr Gln Asp Met Ser Leu Ala Lys Asn

325 330 335

gcc atc gca ttc aca atg ctg aaa gac ggc atc ccc atc ata tac cag 1056

Ala Ile Ala Phe Thr Met Leu Lys Asp Gly Ile Pro Ile Ile Tyr Gln

340 345 350

gga caa gag caa cat tac gct ggc gga acg acg ccc aac aac cgc gag 1104

Gly Gln Glu Gln His Tyr Ala Gly Gly Thr Thr Pro Asn Asn Arg Glu

355 360 365

gcg ctc tgg ctc tcg ggc tac tcg act agc tcc gag ctc tac aag tgg 1152

Ala Leu Trp Leu Ser Gly Tyr Ser Thr Ser Ser Glu Leu Tyr Lys Trp

370 375 380

att gcc gcc ttg aac cag atc cgg gcc cga gct att gct caa gat agc 1200

Ile Ala Ala Leu Asn Gln Ile Arg Ala Arg Ala Ile Ala Gln Asp Ser

385 390 395 400

ggc tac ctc tcc tac agc agc caa gcc atc tac tcg gac agc cat acc 1248

Gly Tyr Leu Ser Tyr Ser Ser Ser Gln Ala Ile Tyr Ser Asp Ser His Thr

405 410 415

att gcc atg cgc aaa ggt acc tcg gga tac cag atc gtg ggc gtg ttc 1296

Ile Ala Met Arg Lys Gly Thr Ser Gly Tyr Gln Ile Val Gly Val Phe

420 425 430

acc aat gtc ggg gcc tcg tcg tcg gct acg gtc acc cta acc tct tcc 1344

Thr Asn Val Gly Ala Ser Ser Ser Ala Thr Val Thr Leu Thr Ser Ser

435 440 445

gca acg ggc ttc ggg gcg aac caa gca ctc gtc gac gtg atg agc tgc 1392

Ala Thr Gly Phe Gly Ala Asn Gln Ala Leu Val Asp Val Met Ser Cys

450 455 460

acc gct tac acc aca gat tcg acg gga gcc ctc acg gta acc ctg aac 1440

Thr Ala Tyr Thr Thr Asp Ser Thr Gly Ala Leu Thr Val Thr Leu Asn

465 470 475 480

gac ggc ctg ccc aag gtg ctt tat ccg att gcg cgg ctc tcg ggc agc 1488

Asp Gly Leu Pro Lys Val Leu Tyr Pro Ile Ala Arg Leu Ser Gly Ser

485 490 495

ggt atc tgc cca ggg cag acc agc aca gcg ctg ccg acg tca agc ttg 1536

Gly Ile Cys Pro Gly Gln Thr Ser Thr Ala Leu Pro Thr Ser Ser Leu

500 505 510

act gca gca tca gcc acg acg act gcc tca gcc tgc tcc ttg tcg gcg 1584

Thr Ala Ala Ser Ala Thr Thr Thr Ala Ser Ala Cys Ser Leu Ser Ala

515 520 525

gtg aac atc acc ttc aac gag ctc gtc acc acg gtg tgg ggg gac acg 1632

Val Asn Ile Thr Phe Asn Glu Leu Val Thr Thr Val Trp Gly Asp Thr

530 535 540

atc aag ctg gcc ggc aac ata tcc gct ctc ggc agc tgg agc cca agc 1680

Ile Lys Leu Ala Gly Asn Ile Ser Ala Leu Gly Ser Trp Ser Pro Ser

545 550 555 560

agc gcc ttg aca ctg agc gca tcg cag tat tca caa agc aat ccg ctc 1728

Ser Ala Leu Thr Leu Ser Ala Ser Gln Tyr Ser Gln Ser Asn Pro Leu

565 570 575

tgg tcg gtc tca acc ctg ctc ggt cca gga acg gtg atc gag tac aag 1776

Trp Ser Val Ser Thr Leu Leu Gly Pro Gly Thr Val Ile Glu Tyr Lys

580 585 590

ttt atc aag gtc agc gcc tcc ggg act gta acg tgg gag tca gac ccg 1824

Phe Ile Lys Val Ser Ala Ser Gly Thr Val Thr Trp Glu Ser Asp Pro

595 600 605

aac cgc gtc tac act gtg ccc tgc gca act gcg acg gtc agt agc act 1872

Asn Arg Val Tyr Thr Val Pro Cys Ala Thr Ala Thr Val Ser Ser Thr

610 615 620

tgg cga 1878

Trp Arg

625

<210>159

<211>626

<212>PRT

<213>Acremonium sp.

<400>159

Met Arg Thr Leu His Gln Ala Leu Leu Val Leu Ala Gly Ala Val Leu

1 5 10 15

Glu Ala Ser Gln Gly Ala Ala Gly Leu Ser Ala Ala Glu Trp Arg Ser

20 25 30

Gln Ser Ile Tyr Gln Val Val Thr Asp Arg Phe Ala Arg Thr Asp Leu

35 40 45

Ser Thr Thr Ala Ser Cys Asn Thr Ala Asp Gln Val Tyr Cys Gly Gly

50 55 60

Thr Trp Gln Gly Leu Ile Ser Lys Leu Asp Tyr Ile Gln Gly Met Gly

65 70 75 80

Phe Thr Ala Val Trp Ile Ser Pro Val Val Lys Gln Val Glu Gly Asn

85 90 95

Ser Gln Asp Gly Ser Ala Tyr His Gly Tyr Trp Ala Gln Asp Ile Trp

100 105 110

Ala Leu Asn Pro Ala Phe Gly Thr Glu Glu Asp Leu Ala Ala Leu Ala

115 120 125

Ala Ala Leu His Ala Arg Gly Met Tyr Leu Met Val Asp Ile Val Thr

130 135 140

Asn His Met Ala Tyr Met Gly Cys Gly Thr Cys Val Asp Tyr Ser Leu

145 150 155 160

Phe Asn Pro Phe Ser Ser Ser Ser Ser Tyr Phe His Pro Tyr Cys Ala Ile

165 170 175

Asp Tyr Ser Asn Gln Thr Ser Val Glu Val Cys Trp Gln Gly Asp Asn

180 185 190

Ile Val Ser Leu Pro Asp Leu Arg Thr Glu Asp Asp Thr Val Arg Ser

195 200 205

Ile Trp Asn Arg Trp Val Ser Gln Leu Val Ser Asn Tyr Ser Ile Asp

210 215 220

Gly Phe Arg Val Asp Ser Ala Lys His Val Glu Thr Ser Phe Trp Gln

225 230 235 240

Asp Phe Ser Thr Ala Ala Gly Val Tyr Leu Leu Gly Glu Val Phe Asp

245 250 255

Gly Asp Pro Ser Tyr Val Ala Pro Tyr Gln Asn Tyr Leu Asn Gly Val

260 265 270

Leu Asp Tyr Pro Ser Tyr Tyr Trp Ile Leu Arg Ala Phe Gln Ser Ser

275 280 285

Ser Gly Ser Ile Ser Asp Leu Val Ser Gly Leu Asn Thr Leu His Gly

290 295 300

Val Ala Leu Asp Leu Ser Leu Tyr Gly Ser Phe Leu Glu Asn His Asp

305 310 315 320

Val Ala Arg Phe Ala Ser Phe Thr Gln Asp Met Ser Leu Ala Lys Asn

325 330 335

Ala Ile Ala Phe Thr Met Leu Lys Asp Gly Ile Pro Ile Ile Tyr Gln

340 345 350

Gly Gln Glu Gln His Tyr Ala Gly Gly Thr Thr Pro Asn Asn Arg Glu

355 360 365

Ala Leu Trp Leu Ser Gly Tyr Ser Thr Ser Ser Glu Leu Tyr Lys Trp

370 375 380

Ile Ala Ala Leu Asn Gln Ile Arg Ala Arg Ala Ile Ala Gln Asp Ser

385 390 395 400

Gly Tyr Leu Ser Tyr Ser Ser Ser Gln Ala Ile Tyr Ser Asp Ser His Thr

405 410 415

Ile Ala Met Arg Lys Gly Thr Ser Gly Tyr Gln Ile Val Gly Val Phe

420 425 430

Thr Asn Val Gly Ala Ser Ser Ser Ala Thr Val Thr Leu Thr Ser Ser

435 440 445

Ala Thr Gly Phe Gly Ala Asn Gln Ala Leu Val Asp Val Met Ser Cys

450 455 460

Thr Ala Tyr Thr Thr Asp Ser Thr Gly Ala Leu Thr Val Thr Leu Asn

465 470 475 480

Asp Gly Leu Pro Lys Val Leu Tyr Pro Ile Ala Arg Leu Ser Gly Ser

485 490 495

Gly Ile Cys Pro Gly Gln Thr Ser Thr Ala Leu Pro Thr Ser Ser Leu

500 505 510

Thr Ala Ala Ser Ala Thr Thr Thr Ala Ser Ala Cys Ser Leu Ser Ala

515 520 525

Val Asn Ile Thr Phe Asn Glu Leu Val Thr Thr Val Trp Gly Asp Thr

530 535 540

Ile Lys Leu Ala Gly Asn Ile Ser Ala Leu Gly Ser Trp Ser Pro Ser

545 550 555 560

Ser Ala Leu Thr Leu Ser Ala Ser Gln Tyr Ser Gln Ser Asn Pro Leu

565 570 575

Trp Ser Val Ser Thr Leu Leu Gly Pro Gly Thr Val Ile Glu Tyr Lys

580 585 590

Phe Ile Lys Val Ser Ala Ser Gly Thr Val Thr Trp Glu Ser Asp Pro

595 600 605

Asn Arg Val Tyr Thr Val Pro Cys Ala Thr Ala Thr Val Ser Ser Thr

610 615 620

Trp Arg

625

<210>160

<211>1890

<212>DNA

<213> Coniochaeta sp.

<220>

<221> CDS

<222>(1)..(1890)

<220>

<221>sig_peptide

<222>(1)..(69)

<220>

<221>misc_feature

<222>(70)..(1497)

<223> catalytic domain

<220>

<221>misc_feature

<222>(1498)..(1596)

<223> connector

<220>

<221>misc_feature

<222>(1597)..(1890)

<223>CBM

<400>160

atg cgg cct atc cta agc tgc ctc ttt ctc gcg tcc gtc gtg gcc cag 48

Met Arg Pro Ile Leu Ser Cys Leu Phe Leu Ala Ser Val Val Ala Gln

1 5 10 15

gtg gcg tgg ggc ctc agc gca gca gac tgg cgt gag cag tcc atc tac 96

Val Ala Trp Gly Leu Ser Ala Ala Asp Trp Arg Glu Gln Ser Ile Tyr

20 25 30

cag gtc gtg acg gac cgc ttc gcg cgg acg gac ctg tcc acc acg gcc 144

Gln Val Val Thr Asp Arg Phe Ala Arg Thr Asp Leu Ser Thr Thr Ala

35 40 45

acg tgc gac acc tcg gcg cag gtg tat tgc ggc ggc acg tac aag ggt 192

Thr Cys Asp Thr Ser Ala Gln Val Tyr Cys Gly Gly Thr Tyr Lys Gly

50 55 60

ctg atc tcc aag ctg gat tac att cag ggc atg ggc ttc act gcc atc 240

Leu Ile Ser Lys Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile

65 70 75 80

tgg ata tcg ccc atc gtc gag cag atg gac ggt aat act gcc gac ggc 288

Trp Ile Ser Pro Ile Val Glu Gln Met Asp Gly Asn Thr Ala Asp Gly

85 90 95

tcc tcg tat cac ggt tac tgg gcg cag gat att tgg agt ctg aac ccg 336

Ser Ser Tyr His Gly Tyr Trp Ala Gln Asp Ile Trp Ser Leu Asn Pro

100 105 110

tcg ttc gga tcg gct ggc gac ctg atc gcg ctc tcc aac gcg ctg cac 384

Ser Phe Gly Ser Ala Gly Asp Leu Ile Ala Leu Ser Asn Ala Leu His

115 120 125

gcc cgg ggc atg tac ctc atg ctg gac gtg gtg acc aac cac ttt gct 432

Ala Arg Gly Met Tyr Leu Met Leu Asp Val Val Thr Asn His Phe Ala

130 135 140

tac aac ggc tgc ggc aac tgc gtc gac tac agc atc ttc acc ccg ttc 480

Tyr Asn Gly Cys Gly Asn Cys Val Asp Tyr Ser Ile Phe Thr Pro Phe

145 150 155 160

aac tcg tcg tcg tac ttc cac ccc ttc tgc ttg atc gac tac aac aac 528

Asn Ser Ser Ser Tyr Phe His Pro Phe Cys Leu Ile Asp Tyr Asn Asn

165 170 175

cag acg tcg atc gag cag tgc tgg gag gga gac aac acc gtc agc ctg 576

Gln Thr Ser Ile Glu Gln Cys Trp Glu Gly Asp Asn Thr Val Ser Leu

180 185 190

ccg gac ctg cgg acg gag aac tcc aac gta cgc gcg ata tgg aac gac 624

Pro Asp Leu Arg Thr Glu Asn Ser Asn Val Arg Ala Ile Trp Asn Asp

195 200 205

tgg atc acg cag att gtg gcg gcg tac ggc atc gac ggt ctg cgc atc 672

Trp Ile Thr Gln Ile Val Ala Ala Tyr Gly Ile Asp Gly Leu Arg Ile

210 215 220

gac agc gtc aag cac cag gag acg tcg ttc tgg tcc ggt ttc ggg tcg 720

Asp Ser Val Lys His Gln Glu Thr Ser Phe Trp Ser Gly Phe Gly Ser

225 230 235 240

gcc gcc ggc gtg ttc atg ctg ggc gag gtg tac aac ggc gat ccg acg 768

Ala Ala Gly Val Phe Met Leu Gly Glu Val Tyr Asn Gly Asp Pro Thr

245 250 255

cag ctg gcg ccg tac cag gat tac atg ccc gga ctg ctg gac tac gcg 816

Gln Leu Ala Pro Tyr Gln Asp Tyr Met Pro Gly Leu Leu Asp Tyr Ala

260 265 270

agc tac tac tgg atc acg agg gcg ttc cag tcg agc agc ggg agt atg 864

Ser Tyr Tyr Trp Ile Thr Arg Ala Phe Gln Ser Ser Ser Gly Ser Met

275 280 285

agc gat ctg gcg tct ggt gtc aac aca ctc aag agc att gcc agg aac 912

Ser Asp Leu Ala Ser Gly Val Asn Thr Leu Lys Ser Ile Ala Arg Asn

290 295 300

aca agc ctg tac gga tct ttc ctg gag aac cac gac cag ccg cgg ttc 960

Thr Ser Leu Tyr Gly Ser Phe Leu Glu Asn His Asp Gln Pro Arg Phe

305 310 315 320

gcg tcg ctt acc tcg gac gtc gcc ttg gcg aag aat gcg ata gcg ttt 1008

Ala Ser Leu Thr Ser Asp Val Ala Leu Ala Lys Asn Ala Ile Ala Phe

325 330 335

act atg ctg aag gac ggt atc ccg gtc gtt tac cag ggc caa gag cag 1056

Thr Met Leu Lys Asp Gly Ile Pro Val Val Tyr Gln Gly Gln Glu Gln

340 345 350

cac tat gcg ggc gga aat gtc cca gct gac cgc gaa gcg atc tgg ttg 1104

His Tyr Ala Gly Gly Asn Val Pro Ala Asp Arg Glu Ala Ile Trp Leu

355 360 365

tcg ggg tac tcc acg tct gcg acg ctg tac acc tgg atc gcc gcg ctg 1152

Ser Gly Tyr Ser Thr Ser Ala Thr Leu Tyr Thr Trp Ile Ala Ala Leu

370 375 380

aac aag gtc cgt tcg agg gct atc gcg caa gac agc agc tac ctg agc 1200

Asn Lys Val Arg Ser Arg Ala Ile Ala Gln Asp Ser Ser Tyr Leu Ser

385 390 395 400

tat cag gcg tat cct gtc tat acg gac agc aac acc att gcc atg cgc 1248

Tyr Gln Ala Tyr Pro Val Tyr Thr Asp Ser Asn Thr Ile Ala Met Arg

405 410 415

aag gga cgg gac gga tac cag gtc atc ggg gtg ttc acc aac aag gga 1296

Lys Gly Arg Asp Gly Tyr Gln Val Ile Gly Val Phe Thr Asn Lys Gly

420 425 430

tcg agc ggg ttg tcc agt ctc acc ctc acg acg tcg atg acc gga ttc 1344

Ser Ser Gly Leu Ser Ser Leu Thr Leu Thr Thr Ser Met Thr Gly Phe

435 440 445

acg gcg ggc cag gcg gtc gtg gat gtc atg agc tgc acc act ttc acg 1392

Thr Ala Gly Gln Ala Val Val Asp Val Met Ser Cys Thr Thr Phe Thr

450 455 460

acg gac tac agc ggt agc ctc gct gtc acc ctt tcg gga ggc att ccg 1440

Thr Asp Tyr Ser Gly Ser Leu Ala Val Thr Leu Ser Gly Gly Ile Pro

465 470 475 480

cgg gtg ttc tat cca agc gcg agg ttg agt ggc tca gga ata tgt ggc 1488

Arg Val Phe Tyr Pro Ser Ala Arg Leu Ser Gly Ser Gly Ile Cys Gly

485 490 495

tcc aat ggg acc acg aca aca gct acg acg aag acg agc acg acg ctg 1536

Ser Asn Gly Thr Thr Thr Thr Ala Thr Thr Lys Thr Ser Thr Thr Leu

500 505 510

acc acg tcg acg aca aca acc tcc aca aag aca agt agt agt tct tgc acc 1584

Thr Thr Ser Thr Thr Thr Thr Thr Ser Thr Lys Thr Ser Ser Ser Cys Thr

515 520 525

gcc acc gcg gta gca atc ac cttc aac gag ctc gtg tcg acc tcc tac 1632

Ala Thr Ala Val Ala Ile Thr Phe Asn Glu Leu Val Ser Thr Ser Tyr

530 535 540

ggc gac aca gtc aag ctc acg ggc aac ata aca gcc ctg ggc agc tgg 1680

Gly Asp Thr Val Lys Leu Thr Gly Asn Ile Thr Ala Leu Gly Ser Trp

545 550 555 560

aac acg gcc aac gcc gtc agc ctc agc gca tcg cag tac aca tct ggt 1728

Asn Thr Ala Asn Ala Val Ser Leu Ser Ala Ser Gln Tyr Thr Ser Gly

565 570 575

agc ccg ctc tgg tcg ggc acc gtg tct ctg cct ccg ggc gtc ggg gta 1776

Ser Pro Leu Trp Ser Gly Thr Val Ser Leu Pro Pro Gly Val Gly Val

580 585 590

cag tac aag ttc gtc agg gtc ggc agc tcg ggg agc gtg acg tgg gag 1824

Gln Tyr Lys Phe Val Arg Val Gly Ser Ser Gly Ser Val Thr Trp Glu

595 600 605

gcg gac ccg aac cac act tat tct gtg ccg tgc gcg gct gct act gtc 1872

Ala Asp Pro Asn His Thr Tyr Ser Val Pro Cys Ala Ala Ala Thr Val

610 615 620

ggt ggg agt tgg cag agc 1890

Gly Gly Ser Trp Gln Ser

625 630

<210>161

<211>630

<212>PRT

<213> Coniochacta sp.

<400>161

Met Arg Pro Ile Leu Ser Cys Leu Phe Leu Ala Ser Val Val Ala Gln

1 5 10 15

Val Ala Trp Gly Leu Ser Ala Ala Asp Trp Arg Glu Gln Ser Ile Tyr

20 25 30

Gln Val Val Thr Asp Arg Phe Ala Arg Thr Asp Leu Ser Thr Thr Ala

35 40 45

Thr Cys Asp Thr Ser Ala Gln Val Tyr Cys Gly Gly Thr Tyr Lys Gly

50 55 60

Leu Ile Ser Lys Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile

65 70 75 80

Trp Ile Ser Pro Ile Val Glu Gln Met Asp Gly Asn Thr Ala Asp Gly

85 90 95

Ser Ser Tyr His Gly Tyr Trp Ala Gln Asp Ile Trp Ser Leu Asn Pro

100 105 110

Ser Phe Gly Ser Ala Gly Asp Leu Ile Ala Leu Ser Asn Ala Leu His

115 120 125

Ala Arg Gly Met Tyr Leu Met Leu Asp Val Val Thr Asn His Phe Ala

130 135 140

Tyr Asn Gly Cys Gly Asn Cys Val Asp Tyr Ser Ile Phe Thr Pro Phe

145 150 155 160

Asn Ser Ser Ser Tyr Phe His Pro Phe Cys Leu Ile Asp Tyr Asn Asn

165 170 175

Gln Thr Ser Ile Glu Gln Cys Trp Glu Gly Asp Asn Thr Val Ser Leu

180 185 190

Pro Asp Leu Arg Thr Glu Asn Ser Asn Val Arg Ala Ile Trp Asn Asp

195 200 205

Trp Ile Thr Gln Ile Val Ala Ala Tyr Gly Ile Asp Gly Leu Arg Ile

210 215 220

Asp Ser Val Lys His Gln Glu Thr Ser Phe Trp Ser Gly Phe Gly Ser

225 230 235 240

Ala Ala Gly Val Phe Met Leu Gly Glu Val Tyr Asn Gly Asp Pro Thr

245 250 255

Gln Leu Ala Pro Tyr Gln Asp Tyr Met Pro Gly Leu Leu Asp Tyr Ala

260 265 270

Ser Tyr Tyr Trp Ile Thr Arg Ala Phe Gln Ser Ser Ser Gly Ser Met

275 280 285

Ser Asp Leu Ala Ser Gly Val Asn Thr Leu Lys Ser Ile Ala Arg Asn

290 295 300

Thr Ser Leu Tyr Gly Ser Phe Leu Glu Asn His Asp Gln Pro Arg Phe

305 310 315 320

Ala Ser Leu Thr Ser Asp Val Ala Leu Ala Lys Asn Ala Ile Ala Phe

325 330 335

Thr Met Leu Lys Asp Gly Ile Pro Val Val Tyr Gln Gly Gln Glu Gln

340 345 350

His Tyr Ala Gly Gly Asn Val Pro Ala Asp Arg Glu Ala Ile Trp Leu

355 360 365

Ser Gly Tyr Ser Thr Ser Ala Thr Leu Tyr Thr Trp Ile Ala Ala Leu

370 375 380

Asn Lys Val Arg Ser Arg Ala Ile Ala Gln Asp Ser Ser Tyr Leu Ser

385 390 395 400

Tyr Gln Ala Tyr Pro Val Tyr Thr Asp Ser Asn Thr Ile Ala Met Arg

405 410 415

Lys Gly Arg Asp Gly Tyr Gln Val Ile Gly Val Phe Thr Asn Lys Gly

420 425 430

Ser Ser Gly Leu Ser Ser Leu Thr Leu Thr Thr Ser Met Thr Gly Phe

435 440 445

Thr Ala Gly Gln Ala Val Val Asp Val Met Ser Cys Thr Thr Phe Thr

450 455 460

Thr Asp Tyr Ser Gly Ser Leu Ala Val Thr Leu Ser Gly Gly Ile Pro

465 470 475 480

Arg Val Phe Tyr Pro Ser Ala Arg Leu Ser Gly Ser Gly Ile Cys Gly

485 490 495

Ser Asn Gly Thr Thr Thr Thr Ala Thr Thr Lys Thr Ser Thr Thr Leu

500 505 510

Thr Thr Ser Thr Thr Thr Thr Thr Ser Thr Lys Thr Ser Ser Ser Cys Thr

515 520 525

Ala Thr Ala Val Ala Ile Thr Phe Asn Glu Leu Val Ser Thr Ser Tyr

530 535 540

Gly Asp Thr Val Lys Leu Thr Gly Asn Ile Thr Ala Leu Gly Ser Trp

545 550 555 560

Asn Thr Ala Asn Ala Val Ser Leu Ser Ala Ser Gln Tyr Thr Ser Gly

565 570 575

Ser Pro Leu Trp Ser Gly Thr Val Ser Leu Pro Pro Gly Val Gly Val

580 585 590

Gln Tyr Lys Phe Val Arg Val Gly Ser Ser Gly Ser Val Thr Trp Glu

595 600 605

Ala Asp Pro Asn His Thr Tyr Ser Val Pro Cys Ala Ala Ala Thr Val

610 615 620

Gly Gly Ser Trp Gln Ser

625 630

<210>162

<211>1806

<212>DNA

<213>Meripilus giganteus

<220>

<221> CDS

<222>(1)..(1806)

<220>

<221>sig_peptide

<222>(1)..(78)

<220>

<221>misc_feature

<222>(79)..(1476)

<223> catalytic domain

<220>

<221>misc_feature

<222>(1477)..(1521)

<223> connector

<220>

<221>misc_feature

<222>(1522)..(1806)

<223>CBM

<400>162

atg tca aac tgg gtc aag ctc gcc gca ctc gcc gca ctc gcc gcc ctc 48

Met Ser Asn Trp Val Lys Leu Ala Ala Leu Ala Ala Leu Ala Ala Leu

1 5 10 15

gga gtg ttc tgc acc gcc gcc gtc gac gcc cgc cct act gtc ttt gac 96

Gly Val Phe Cys Thr Ala Ala Val Asp Ala Arg Pro Thr Val Phe Asp

20 25 30

gcc ggc gcg gac gca cac tcg ctg cat gcc cgg gcc ccc tcc ggc agc 144

Ala Gly Ala Asp Ala His Ser Leu His Ala Arg Ala Pro Ser Gly Ser

35 40 45

aag gat gtc atc atc cag atg ttt gag tgg aac tgg gac agc gtc gct 192

Lys Asp Val Ile Ile Gln Met Phe Glu Trp Asn Trp Asp Ser Val Ala

50 55 60

gcc gag tgc act aac ttc atc ggc ccc gcc ggg tac ggc ttc gtg caa 240

Ala Glu Cys Thr Asn Phe Ilc Gly Pro Ala Gly Tyr Gly Phe Val Gln

65 70 75 80

gtg agc ccg ccc cag gag acc atc cag ggc gcg cag tgg tgg acc gac 288

Val Ser Pro Pro Gln Glu Thr Ile Gln Gly Ala Gln Trp Trp Thr Asp

85 90 95

tac cag ccg gtg tcg tac acg ctc act ggg aag cgg ggc gac cgc tcc 336

Tyr Gln Pro Val Ser Tyr Thr Leu Thr Gly Lys Arg Gly Asp Arg Ser

100 105 110

cag ttt gcg aac atg atg att act acg tgc cac gcc gcg ggc gtc ggc gtg 384

Gln Phe Ala Asn Met Ile Thr Thr Cys His Ala Ala Gly Val Gly Val

115 120 125

atc gtt gac acc atc tgg aac cac atg gcg ggc gtc gac tcc ggc acg 432

Ile Val Asp Thr Ile Trp Asn His Met Ala Gly Val Asp Ser Gly Thr

130 135 140

ggt acc gcc ggc tcg tcc ttc acg cac tac aac tac ccc ggc atc tac 480

Gly Thr Ala Gly Ser Ser Phe Thr His Tyr Asn Tyr Pro Gly Ile Tyr

145 150 155 160

caa aac cag gac ttt cac cac tgc ggc ctc gag ccg ggc gat gac atc 528

Gln Asn Gln Asp Phe His His Cys Gly Leu Glu Pro Gly Asp Asp Ile

165 170 175

gtc aac tac gac aac gcg gtt gag gtc cag acc tgc gag ctt gtc aac 576

Val Asn Tyr Asp Asn Ala Val Glu Val Gln Thr Cys Glu Leu Val Asn

180 185 190

ctc gct gac ctc gcc acc gac acg gag tat gtg cgc ggt cgc ctt gcc 624

Leu Ala Asp Leu Ala Thr Asp Thr Glu Tyr Val Arg Gly Arg Leu Ala

195 200 205

cag tac gga aac gac ctg ctc tcg ctc ggt gcc gat ggc ctg cgt ctt 672

Gln Tyr Gly Asn Asp Leu Leu Ser Leu Gly Ala Asp Gly Leu Arg Leu

210 215 220

gac gct tcc aaa cac att cct gtg ggc gac atc gcg aac atc ctg tct 720

Asp Ala Ser Lys His Ile Pro Val Gly Asp Ile Ala Asn Ile Leu Ser

225 230 235 240

cgc ctc agt cgc tct gtc tac atc acc cag gaa gtc atc ttt ggg gcc 768

Arg Leu Ser Arg Ser Val Tyr Ile Thr Gln Glu Val Ile Phe Gly Ala

245 250 255

ggc gag ccc atc acg ccg aac cag tac acc acc ggg aac ggc gac gtt cag 816

Gly Glu Pro Ile Thr Pro Asn Gln Tyr Thr Gly Asn Gly Asp Val Gln

260 265 270

gag ttc cgc tac acc tct gcg cta aag gac gcc ttc ttg agc tcg ggc 864

Glu Phe Arg Tyr Thr Ser Ala Leu Lys Asp Ala Phe Leu Ser Ser Ser Gly

275 280 285

ata tcc aac ctg cag gac ttc gaa aac cgt gga tgg gta cct ggc tcg 912

Ile Ser Asn Leu Gln Asp Phe Glu Asn Arg Gly Trp Val Pro Gly Ser

290 295 300

ggc gcc aac gtg ttc gtc gtc aac cat gac acc gag cgg aac ggc gcg 960

Gly Ala Asn Val Phe Val Val Asn His Asp Thr Glu Arg Asn Gly Ala

305 310 315 320

tcg ctg aac aac aac tcg cct tcg aac acc tac gtc acc gcg acg atc 1008

Ser Leu Asn Asn Asn Ser Pro Ser Asn Thr Tyr Val Thr Ala Thr Ile

325 330 335

ttc tcg ctc gca cac ccg tac ggc acg ccc acg atc ctc tcc tcg tat 1056

Phe Ser Leu Ala His Pro Tyr Gly Thr Pro Thr Ile Leu Ser Ser Tyr

340 345 350

gat ggc ttc acg aac acc gac gcc ggt gcg ccg aac aac aac gtc ggc 1104

Asp Gly Phe Thr Asn Thr Asp Ala Gly Ala Pro Asn Asn Asn Val Gly

355 360 365

aca tgc tcg acc agc ggt ggt gcg aac ggg tgg ctc tgc cag cac cgc 1152

Thr Cys Ser Thr Ser Gly Gly Ala Asn Gly Trp Leu Cys Gln His Arg

370 375 380

tgg acc gcg atc gcc ggc atg gtc ggc ttc cgc aac aac gtc ggc agc 1200

Trp Thr Ala Ile Ala Gly Met Val Gly Phe Arg Asn Asn Val Gly Ser

385 390 395 400

gct gca ctc aac aac tgg cag gcc ccg cag tcg cag cag att gcg ttc 1248

Ala Ala Leu Asn Asn Trp Gln Ala Pro Gln Ser Gln Gln Ile Ala Phe

405 410 415

ggt cgc ggc gca ctt ggc ttc gtc gcg atc aac aac gcc gac tcg gcc 1296

Gly Arg Gly Ala Leu Gly Phe Val Ala Ile Asn Asn Ala Asp Ser Ala

420 425 430

tgg tct acg acg ttc acc act tcc ctc ccc gat ggt tcc tac tgc gat 1344

Trp Ser Thr Thr Phe Thr Thr Ser Leu Pro Asp Gly Ser Tyr Cys Asp

435 440 445

gtc atc agc ggc aag gcc tcc ggc agt agc tgc acc ggt tct tcg ttc 1392

Val Ile Ser Gly Lys Ala Ser Gly Ser Ser Cys Thr Gly Ser Ser Phe

450 455 460

acc gtc tcc ggc ggg aag ctg acc gcc acg gtg ccg gcg cgt agc gcc 1440

Thr Val Ser Gly Gly Gly Lys Leu Thr Ala Thr Val Pro Ala Arg Ser Ala

465 470 475 480

atc gcc gtg cac acc ggt cag aaa ggt tct ggt ggt gcc acg ccc acc 1488

Ile Ala Val His Thr Gly Gln Lys Gly Ser Gly Gly Ala Thr Pro Thr

485 490 495

tcc gcc cct agt act aca cca acc agc ggc act gtc agc atg acc ttc 1536

Ser Ala Pro Ser Thr Thr Pro Thr Ser Gly Thr Val Ser Met Thr Phe

500 505 510

gct gag cag gcg acg acc acc ttc ggc gag aac atc ttc ctc gtc ggc 1584

Ala Glu Gln Ala Thr Thr Thr Phe Gly Glu Asn Ile Phe Leu Val Gly

515 520 525

agt att tcg cag ctc ggg aac tgg aac cca gcc agc gcg atc gcc ctg 1632

Ser Ile Ser Gln Leu Gly Asn Trp Asn Pro Ala Ser Ala Ile Ala Leu

530 535 540

tcc tct gcg gcg tac cct acg tgg tct gtg tct gtg aac att ccc gct 1680

Ser Ser Ala Ala Tyr Pro Thr Trp Ser Val Ser Val Asn Ile Pro Ala

545 550 555 560

gga acg acc ttc cag tac aag ttc atc cgc aag gag acg gac ggt agc 1728

Gly Thr Thr Phe Gln Tyr Lys Phe Ile Arg Lys Glu Thr Asp Gly Ser

565 570 575

gtc gtc tgg gag tcg gac ccc aac cgc cag gct acc gcg ccc gcg tcc 1776

Val Val Trp Glu Ser Asp Pro Asn Arg Gln Ala Thr Ala Pro Ala Ser

580 585 590

ggt acc acc acg ctc acg tcc agc tgg cgg 1806

Gly Thr Thr Thr Leu Thr Ser Ser Trp Arg

595 600

<210>163

<211>602

<212>PRT

<213>Meripilus giganteus

<400>163

Met Ser Asn Trp Val Lys Leu Ala Ala Leu Ala Ala Leu Ala Ala Leu

1 5 10 15

Gly Val Phe Cys Thr Ala Ala Val Asp Ala Arg Pro Thr Val Phe Asp

20 25 30

Ala Gly Ala Asp Ala His Ser Leu His Ala Arg Ala Pro Ser Gly Ser

35 40 45

Lys Asp Val Ile Ile Gln Met Phe Glu Trp Asn Trp Asp Ser Val Ala

50 55 60

Ala Glu Cys Thr Asn Phe Ile Gly Pro Ala Gly Tyr Gly Phe Val Gln

65 70 75 80

Val Ser Pro Pro Gln Glu Thr Ile Gln Gly Ala Gln Trp Trp Thr Asp

85 90 95

Tyr Gln Pro Val Ser Tyr Thr Leu Thr Gly Lys Arg Gly Asp Arg Ser

100 105 110

Gln Phe Ala Asn Met Ile Thr Thr Cys His Ala Ala Gly Val Gly Val

115 120 125

Ile Val Asp Thr Ile Trp Asn His Met Ala Gly Val Asp Ser Gly Thr

130 135 140

Gly Thr Ala Gly Ser Ser Phe Thr His Tyr Asn Tyr Pro Gly Ile Tyr

145 150 155 160

Gln Asn Gln Asp Phe His His Cys Gly Leu Glu Pro Gly Asp Asp Ile

165 170 175

Val Asn Tyr Asp Asn Ala Val Glu Val Gln Thr Cys Glu Leu Val Asn

180 185 190

Leu Ala Asp Leu Ala Thr Asp Thr Glu Tyr Val Arg Gly Arg Leu Ala

195 200 205

Gln Tyr Gly Asn Asp Leu Leu Ser Leu Gly Ala Asp Gly Leu Arg Leu

210 215 220

Asp Ala Ser Lys His Ile Pro Val Gly Asp Ile Ala Asn Ile Leu Ser

225 230 235 240

Arg Leu Ser Arg Ser Val Tyr Ile Thr Gln Glu Val Ile Phe Gly Ala

245 250 255

Gly Glu Pro Ile Thr Pro Asn Gln Tyr Thr Gly Asn Gly Asp Val Gln

260 265 270

Glu Phe Arg Tyr Thr Ser Ala Leu Lys Asp Ala Phe Leu Ser Ser Ser Gly

275 280 285

Ile Ser Asn Leu Gln Asp Phe Glu Asn Arg Gly Trp Val Pro Gly Ser

290 295 300

Gly Ala Asn Val Phe Val Val Asn His Asp Thr Glu Arg Asn Gly Ala

305 310 315 320

Ser Leu Asn Asn Asn Ser Pro Ser Asn Thr Tyr Val Thr Ala Thr Ile

325 330 335

Phe Ser Leu Ala His Pro Tyr Gly Thr Pro Thr Ile Leu Ser Ser Tyr

340 345 350

Asp Gly Phe Thr Asn Thr Asp Ala Gly Ala Pro Asn Asn Asn Val Gly

355 360 365

Thr Cys Ser Thr Ser Gly Gly Ala Asn Gly Trp Leu Cys Gln His Arg

370 375 380

Trp Thr Ala Ile Ala Gly Met Val Gly Phe Arg Asn Asn Val Gly Ser

385 390 395 400

Ala Ala Leu Asn Asn Trp Gln Ala Pro Gln Ser Gln Gln Ile Ala Phe

405 410 415

Gly Arg Gly Ala Leu Gly Phe Val Ala Ile Asn Asn Ala Asp Ser Ala

420 425 430

Trp Ser Thr Thr Phe Thr Thr Ser Leu Pro Asp Gly Ser Tyr Cys Asp

435 440 445

Val Ile Ser Gly Lys Ala Ser Gly Ser Ser Cys Thr Gly Ser Ser Phe

450 455 460

Thr Val Ser Gly Gly Gly Lys Leu Thr Ala Thr Val Pro Ala Arg Ser Ala

465 470 475 480

Ile Ala Val His Thr Gly Gln Lys Gly Ser Gly Gly Ala Thr Pro Thr

485 490 495

Ser Ala Pro Ser Thr Thr Pro Thr Ser Gly Thr Val Ser Met Thr Phe

500 505 510

Ala Glu Gln Ala Thr Thr Thr Phe Gly Glu Asn Ile Phe Leu Val Gly

515 520 525

Ser Ile Ser Gln Leu Gly Asn Trp Asn Pro Ala Ser Ala Ile Ala Leu

530 535 540

Ser Ser Ala Ala Tyr Pro Thr Trp Ser Val Ser Val Asn Ile Pro Ala

545 550 555 560

Gly Thr Thr Phe Gln Tyr Lys Phe Ile Arg Lys Glu Thr Asp Gly Ser

565 570 575

Val Val Trp Glu Ser Asp Pro Asn Arg Gln Ala Thr Ala Pro Ala Ser

580 585 590

Gly Thr Thr Thr Leu Thr Ser Ser Trp Arg

595 600

<210>164

<211>1929

<212>DNA

<213> Penicillium sp.

<220>

<221> CDS

<222>(1)..(1929)

<220>

<221>sig_peptide

<222>(1)..(60)

<220>

<221>misc_feature

<222>(61)..(1488)

<223> catalytic domain

<220>

<221>misc_feature

<222>(1489)..(1617)

<223> connector

<220>

<221>misc_feature

<222>(1618)..(1929)

<223>CBM

<400>164

atg aag gca ctt gcg ttg gcc gca cta tgc ctc gcg aag gct gtt gcc 48

Met Lys Ala Leu Ala Leu Ala Ala Leu Cys Leu Ala Lys Ala Val Ala

1 5 10 15

ggt ctg acg gct gca gaa tgg cgc agt cag tcg atc tac ttt ctt cta 96

Gly Leu Thr Ala Ala Glu Trp Arg Ser Gln Ser Ile Tyr Phe Leu Leu

20 25 30

act gat cgc ttt ggc cga acg gac aat tcc acc acg gca gca tgc aat 144

Thr Asp Arg Phe Gly Arg Thr Asp Asn Ser Thr Thr Ala Ala Cys Asn

35 40 45

gtc agc gat cgg gtc tac tgt ggt ggc agc tgg caa gga atc atc aat 192

Val Ser Asp Arg Val Tyr Cys Gly Gly Ser Trp Gln Gly Ile Ile Asn

50 55 60

cac ttg gat tac att cag ggc atg gga ttc acc gcg att tgg att acc 240

His Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Thr

65 70 75 80

cct gtc aca gaa cag ctc tct caa gac act gga gat ggc gag gca tac 288

Pro Val Thr Glu Gln Leu Ser Gln Asp Thr Gly Asp Gly Glu Ala Tyr

85 90 95

cac gga tac tgg caa caa gag ata tac aac gtc aac aca aac tat ggc 336

His Gly Tyr Trp Gln Gln Glu Ile Tyr Asn Val Asn Thr Asn Tyr Gly

100 105 110

act gct gct gac ctt ttg gca ctt tct aaa gcc ctg cac agt cgt ggc 384

Thr Ala Ala Asp Leu Leu Ala Leu Ser Lys Ala Leu His Ser Arg Gly

115 120 125

atg tac ctc atg gta gac gtg gtt gca aac cac atg ggc tat gat gga 432

Met Tyr Leu Met Val Asp Val Val Ala Asn His Met Gly Tyr Asp Gly

130 135 140

gct gga aat act gtt gac tac agt gtc ttt aat cca ttc gac tct tcg 480

Ala Gly Asn Thr Val Asp Tyr Ser Val Phe Asn Pro Phe Asp Ser Ser

145 150 155 160

tct tac ttc cac tcg tat tgt gag atc agc gat tac tct gat cag aca 528

Ser Tyr Phe His Ser Tyr Cys Glu Ile Ser Asp Tyr Ser Asp Gln Thr

165 170 175

aac gtg gag gac tgt tgg ctt gga gac act aca gtt tct ctt cca gat 576

Asn Val Glu Asp Cys Trp Leu Gly Asp Thr Thr Val Ser Leu Pro Asp

180 185 190

ctc gac acg acc ctt act tct gtt cag acg atc tgg tat aac tgg gtc 624

Leu Asp Thr Thr Leu Thr Ser Val Gln Thr Ile Trp Tyr Asn Trp Val

195 200 205

act gaa ttg gtg tcc aac tac tcc att gat ggt ttg cga att gat aca 672

Thr Glu Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr

210 215 220

gtc aaa cac gtg cag aag tcg ttc tgg ccg ggc tac aac agt gct gca 720

Val Lys His Val Gln Lys Ser Phe Trp Pro Gly Tyr Asn Ser Ala Ala

225 230 235 240

ggt gtc tac tgt gtg gga gag gtg ttt gat ggg gac cca gca tac act 768

Gly Val Tyr Cys Val Gly Glu Val Phe Asp Gly Asp Pro Ala Tyr Thr

245 250 255

tgc ccc tac cag agc tac ctc gat ggt gtt ctg aac tat ccg att tat 816

Cys Pro Tyr Gln Ser Tyr Leu Asp Gly Val Leu Asn Tyr Pro Ile Tyr

260 265 270

tac caa ctg ctg tac gca ttc gag tcg aca agt ggc agt atc agc ggt 864

Tyr Gln Leu Leu Tyr Ala Phe Glu Ser Thr Ser Gly Ser Ile Ser Gly

275 280 285

cta tat aat atg atc aac tcc gtt gca tct gac tgt tcc gat cca acc 912

Leu Tyr Asn Met Ile Asn Ser Val Ala Ser Asp Cys Ser Asp Pro Thr

290 295 300

ttg ctc gga aac ttc atc gag aat cat gac aac cca cgc ttt gct tcc 960

Leu Leu Gly Asn Phe Ile Glu Asn His Asp Asn Pro Arg Phe Ala Ser

305 310 315 320

tac acg agc gat tat tct caa gcg aag aat gtg att tct ttc atc ttc 1008

Tyr Thr Ser Asp Tyr Ser Gln Ala Lys Asn Val Ile Ser Phe Ile Phe

325 330 335

ttc tcg gat ggt att cca atc gtc tat gct ggc cag gaa caa cac tat 1056

Phe Ser Asp Gly Ile Pro Ile Val Tyr Ala Gly Gln Glu Gln His Tyr

340 345 350

agc ggt ggc agt gac cct gcc aat cgt gaa gca act tgg cta tcc gga 1104

Ser Gly Gly Ser Asp Pro Ala Asn Arg Glu Ala Thr Trp Leu Ser Gly

355 360 365

tac gac aag aca gct cag ctt tac acc tac atc acc acc aca aac aag 1152

Tyr Asp Lys Thr Ala Gln Leu Tyr Thr Tyr Ile Thr Thr Thr Asn Lys

370 375 380

atc cgt gcc cta gcc att tca aag gac agc gcc tac ata agt tcc aag 1200

Ile Arg Ala Leu Ala Ile Ser Lys Asp Ser Ala Tyr Ile Ser Ser Lys

385 390 395 400

aat aat gct ttc tac act gat agc aat act att gcc atg aag aaa gga 1248

Asn Asn Ala Phe Tyr Thr Asp Ser Asn Thr Ile Ala Met Lys Lys Gly

405 410 415

tct agc ggc tcg caa gtt ata act gtt ctt tca aac cgt ggc tca tcg 1296

Ser Ser Gly Ser Gln Val Ile Thr Val Leu Ser Asn Arg Gly Ser Ser

420 425 430

ggt agc tcg tat acc ttg act ctt agc gga agc ggt tac tcg tct ggc 1344

Gly Ser Ser Tyr Thr Leu Thr Leu Ser Gly Ser Gly Tyr Ser Ser Gly

435 440 445

acg aag ctc atg gag atg tac acc tgc aca gcc gtg act gtg gac tct 1392

Thr Lys Leu Met Glu Met Tyr Thr Cys Thr Ala Val Thr Val Asp Ser

450 455 460

agt ggc aac atc gcc gtg ccg atg gct tcc gga ctc cct cga gtc tac 1440

Ser Gly Asn Ile Ala Val Pro Met Ala Ser Gly Leu Pro Arg Val Tyr

465 470 475 480

atg ctt gct tcc tcg gct tgc tct att tgc agt tct gcc tgt tca gca 1488

Met Leu Ala Ser Ser Ala Cys Ser Ile Cys Ser Ser Ala Cys Ser Ala

485 490 495

act acc aca acc tcg tcg acg gct tct act tca acg aca acg tca acc 1536

Thr Thr Thr Thr Ser Ser Thr Ala Ser Thr Ser Thr Thr Thr Ser Thr

500 505 510

aca ctg aag act acc acg aca acg tca act act tcg aaa act act acg 1584

Thr Leu Lys Thr Thr Thr Thr Thr Thr Ser Thr Thr Ser Lys Thr Thr Thr Thr

515 520 525

tcc act aca tcc acg agc tgc aca cag gct act gca ttg cca gtt ttg 1632

Ser Thr Thr Ser Ser Thr Ser Cys Thr Gln Ala Thr Ala Leu Pro Val Leu

530 535 540

ttc aaa gag att gtc acc act tca tac ggg cag agt atc tat atc tca 1680

Phe Lys Glu Ile Val Thr Thr Ser Tyr Gly Gln Ser Ile Tyr Ile Ser

545 550 555 560

ggc tct ata agt caa ctc gga agc tgg gac acg tct agc gcc gtt gcc 1728

Gly Ser Ile Ser Gln Leu Gly Ser Trp Asp Thr Ser Ser Ala Val Ala

565 570 575

ctc tct gct gat cag tac aca tca tcc agc cat ctg tgg tat gtt gtc 1776

Leu Ser Ala Asp Gln Tyr Thr Ser Ser Ser His Leu Trp Tyr Val Val

580 585 590

gtg aca att cca gtg ggc acc tcg ttc cag tac aag ttc atc gag gag 1824

Val Thr Ile Pro Val Gly Thr Ser Phe Gln Tyr Lys Phe Ile Glu Glu

595 600 605

acg agc ggg tct agt act att act tgg gag agt gat ccg aac cgc tct 1872

Thr Ser Gly Ser Ser Thr Ile Thr Trp Glu Ser Asp Pro Asn Arg Ser

610 615 620

tat acg gtg cca acg ggc tgt gca ggc tca acg gct acc gtc aca gcg 1920

Tyr Thr Val Pro Thr Gly Cys Ala Gly Ser Thr Ala Thr Val Thr Ala

625 630 635 640

acc tgg aga 1929

Thr Trp Arg

<210>165

<211>643

<212>PRT

<213> Penicillium sp.

<400>165

Met Lys Ala Leu Ala Leu Ala Ala Leu Cys Leu Ala Lys Ala Val Ala

1 5 10 15

Gly Leu Thr Ala Ala Glu Trp Arg Ser Gln Ser Ile Tyr Phe Leu Leu

20 25 30

Thr Asp Arg Phe Gly Arg Thr Asp Asn Ser Thr Thr Ala Ala Cys Asn

35 40 45

Val Ser Asp Arg Val Tyr Cys Gly Gly Ser Trp Gln Gly Ile Ile Asn

50 55 60

His Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Thr

65 70 75 80

Pro Val Thr Glu Gln Leu Ser Gln Asp Thr Gly Asp Gly Glu Ala Tyr

85 90 95

His Gly Tyr Trp Gln Gln Glu Ile Tyr Asn Val Asn Thr Asn Tyr Gly

100 105 110

Thr Ala Ala Asp Leu Leu Ala Leu Ser Lys Ala Leu His Ser Arg Gly

115 120 125

Met Tyr Leu Met Val Asp Val Val Ala Asn His Met Gly Tyr Asp Gly

130 135 140

Ala Gly Asn Thr Val Asp Tyr Ser Val Phe Asn Pro Phe Asp Ser Ser

145 150 155 160

Ser Tyr Phe His Ser Tyr Cys Glu Ile Ser Asp Tyr Ser Asp Gln Thr

165 170 175

Asn Val Glu Asp Cys Trp Leu Gly Asp Thr Thr Val Ser Leu Pro Asp

180 185 190

Leu Asp Thr Thr Leu Thr Ser Val Gln Thr Ile Trp Tyr Asn Trp Val

195 200 205

Thr Glu Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile Asp Thr

210 215 220

Val Lys His Val Gln Lys Ser Phe Trp Pro Gly Tyr Asn Ser Ala Ala

225 230 235 240

Gly Val Tyr Cys Val Gly Glu Val Phe Asp Gly Asp Pro Ala Tyr Thr

245 250 255

Cys Pro Tyr Gln Ser Tyr Leu Asp Gly Val Leu Asn Tyr Pro Ile Tyr

260 265 270

Tyr Gln Leu Leu Tyr Ala Phe Glu Ser Thr Ser Gly Ser Ile Ser Gly

275 280 285

Leu Tyr Asn MetIle A sn Ser Val Ala Ser Asp Cys Ser Asp Pro Thr

290 295 300

Leu Leu Gly Asn Phe Ile Glu Asn His Asp Asn Pro Arg Phe Ala Ser

305 310 315 320

Tyr Thr Ser Asp Tyr Ser Gln Ala Lys Asn Val Ile Ser Phe Ile Phe

325 330 335

Phe Ser Asp Gly Ile Pro Ile Val Tyr Ala Gly Gln Glu Gln His Tyr

340 345 350

Ser Gly Gly Ser Asp Pro Ala Asn Arg Glu Ala Thr Trp Leu Ser Gly

355 360 365

Tyr Asp Lys Thr Ala Gln Leu Tyr Thr Tyr Ile Thr Thr Thr Asn Lys

370 375 380

Ile Arg Ala Leu Ala Ile Ser Lys Asp Ser Ala Tyr Ile Ser Ser Lys

385 390 395 400

Asn Asn Ala Phe Tyr Thr Asp Ser Asn Thr Ile Ala Met Lys Lys Gly

405 410 415

Ser Ser Gly Ser Gln Val Ile Thr Val Leu Ser Asn Arg Gly Ser Ser

420 425 430

Gly Ser Ser Tyr Thr Leu Thr Leu Ser Gly Ser Gly Tyr Ser Ser Gly

435 440 445

Thr Lys Leu Met Glu Met Tyr Thr Cys Thr Ala Val Thr Val Asp Ser

450 455 460

Ser Gly Asn Ile Ala Val Pro Met Ala Ser Gly Leu Pro Arg Val Tyr

465 470 475 480

Met Leu Ala Ser Ser Ala Cys Ser Ile Cys Ser Ser Ala Cys Ser Ala

485 490 495

Thr Thr Thr Thr Ser Ser Thr Ala Ser Thr Ser Thr Thr Thr Ser Thr

500 505 510

Thr Leu Lys Thr Thr Thr Thr Thr Thr Ser Thr Thr Ser Lys Thr Thr Thr Thr

515 520 525

Ser Thr Thr Ser Ser Thr Ser Cys Thr Gln Ala Thr Ala Leu Pro Val Leu

530 535 540

Phe Lys Glu Ile Val Thr Thr Ser Tyr Gly Gln Ser Ile Tyr Ile Ser

545 550 555 560

Gly Ser Ile Ser Gln Leu Gly Ser Trp Asp Thr Ser Ser Ala Val Ala

565 570 575

Leu Ser Ala Asp Gln Tyr Thr Ser Ser Ser His Leu Trp Tyr Val Val

580 585 590

Val Thr Ile Pro Val Gly Thr Ser Phe Gln Tyr Lys Phe Ile Glu Glu

595 600 605

Thr Ser Gly Ser Ser Thr Ile Thr Trp Glu Ser Asp Pro Ash Arg Ser

610 615 620

Tyr Thr Val Pro Thr Gly Cys Ala Gly Ser Thr Ala Thr Val Thr Ala

625 630 635 640

Thr Trp Arg

<210>166

<211>1698

<212>DNA

<213> Streptomyces limosus

<220>

<221> CDS

<222>(1)..(1698)

<220>

<221>sig_peptide

<222>(1)..(84)

<220>

<221>misc_feature

<222>(85)..(1503)

<223> catalytic domain

<220>

<221>misc_feature

<222>(1504)..(1701)

<223> Connector + CBM

<400>166

atg gcc cgc aga ctc gcc acc gcg tcc cta gcc gtg ctg gcg gcg gcc 48

Met Ala Arg Arg Leu Ala Thr Ala Ser Leu Ala Val Leu Ala Ala Ala

1 5 10 15

gcc acc gcc ctc acc gcg ccc aca ccc gcc gct gcc gcc ccg ccc ggg 96

Ala Thr Ala Leu Thr Ala Pro Thr Pro Ala Ala Ala Ala Pro Pro Gly

20 25 30

gcg aag gac gtc acc gcc gtc ctc ttc gag tgg aag ttc gcc tcc gta 144

Ala Lys Asp Val Thr Ala Val Leu Phe Glu Trp Lys Phe Ala Ser Val

35 40 45

gcc cgc gcc tgc acc gac agc ctc ggc ccg gcc ggc tac gga tac gtc 192

Ala Arg Ala Cys Thr Asp Ser Leu Gly Pro Ala Gly Tyr Gly Tyr Val

50 55 60

cag gtc tcg ccg ccc cag gag cac atc cag ggc agc cag tgg tgg acc 240

Gln Val Ser Pro Pro Gln Glu His Ile Gln Gly Ser Gln Trp Trp Thr

65 70 75 80

tcc tac cag ccc gtc agc tac aag atc gcc gga cgg ctc ggc gac cgc 288

Ser Tyr Gln Pro Val Ser Tyr Lys Ile Ala Gly Arg Leu Gly Asp Arg

85 90 95

gcc gcc ttc aag tcc atg gtc gac acc tgc cac gcg gcc ggc gtc aag 336

Ala Ala Phe Lys Ser Met Val Asp Thr Cys His Ala Ala Gly Val Lys

100 105 110

gtc gtc gcc gac tcg gtc atc aac cac atg gcc gcg ggt tcc ggc acc 384

Val Val Ala Asp Ser Val Ile Asn His Met Ala Ala Gly Ser Gly Thr

115 120 125

ggc acc ggc ggc agc gcg tac cag aag tac gac tac ccg ggc atc tgg 432

Gly Thr Gly Gly Ser Ala Tyr Gln Lys TyrA sp Tyr Pro Gly Ile Trp

130 135 140

tcc ggc gcc gac atg gac gac tgc cgc agc gag atc aac gac tac ggc 480

Ser Gly Ala Asp Met Asp Asp Cys Arg Ser Glu Ile Asn Asp Tyr Gly

145 150 155 160

aac cgc gcc aac gtc cag aac tgc gaa ctg gtc ggc ctc gcc gac ctc 528

Asn Arg Ala Asn Val Gln Asn Cys Glu Leu Val Gly Leu Ala Asp Leu

165 170 175

gac acc ggt gag tcg tac gtc cgc gac cgc atc gcc gcc tac ctc aac 576

Asp Thr Gly Glu Ser Tyr Val Arg Asp Arg Ile Ala Ala Tyr Leu Asn

180 185 190

gac ctg ctc tcg ctc ggt gtg gac ggc ttc cgc atc gac gcc gcc aag 624

Asp Leu Leu Ser Leu Gly Val Asp Gly Phe Arg Ile Asp Ala Ala Lys

195 200 205

cac atg ccc gcc gcc gac ctc acc gcc atc aag gcc aag gtc ggc aac 672

His Met Pro Ala Ala Asp Leu Thr Ala Ile Lys Ala Lys Val Gly Asn

210 215 220

ggg agc acg tac tgg aag cag gag gcc atc cac ggc gcg ggc gag gcc 720

Gly Ser Thr Tyr Trp Lys Gln Glu Ala Ile His Gly Ala Gly Glu Ala

225 230 235 240

gtc cag ccc agc gag tac ctc ggc acc ggc gac gtc cag gag ttc cgc 768

Val Gln Pro Ser Glu Tyr Leu Gly Thr Gly Asp Val Gln Glu Phe Arg

245 250 255

tac gcc cgc gac ctc aag cgg gtc ttc cag aac gag aac ctc gcc cac 816

Tyr Ala Arg Asp Leu Lys Arg Val Phe Gln Asn Glu Asn Leu Ala His

260 265 270

ctg aag aac ttc ggc gag gac tgg ggc tac atg gcg agc ggc aag tcc 864

Leu Lys Asn Phe Gly Glu Asp Trp Gly Tyr Met Ala Ser Gly Lys Ser

275 280 285

gcc gtc ttc gtc gac aac cac gac acc gag cgg ggc ggc gac acc ctc 912

Ala Val Phe Val Asp Asn His Asp Thr Glu Arg Gly Gly Asp Thr Leu

290 295 300

aac tac aag aac ggc tcc gcc tac acc ctc gcc ggc gtc ttc atg ctg 960

Asn Tyr Lys Asn Gly Ser Ala Tyr Thr Leu Ala Gly Val Phe Met Leu

305 310 315 320

gcc tgg ccc tac ggc tcc ccg gac gtc cac tcc ggc tac gag ttc acc 1008

Ala Trp Pro Tyr Gly Ser Pro Asp Val His Ser Gly Tyr Glu Phe Thr

325 330 335

gac cac gac gcc ggc ccg ccc aac ggc ggc acc gtc aac gcc tgc tac 1056

Asp His Asp Ala Gly Pro Pro Asn Gly Gly Thr Val Asn Ala Cys Tyr

340 345 350

agc gac ggc tgg aag tgc cag cac gcc tgg ccc gag ctc tcc tcc atg 1104

Ser Asp Gly Trp Lys Cys Gln His Ala Trp Pro Glu Leu Ser Ser Ser Met

355 360 365

gtc ggc ctg cgc aac acc gcc tcc ggg cag ccc gtc acc aac tgg tgg 1152

Val Gly Leu Arg Asn Thr Ala Ser Gly Gln Pro Val Thr Asn Trp Trp

370 375 380

gac aac ggc ggc gac cag atc gcc ttc ggc cgc ggc gac aag gcg tac 1200

Asp Asn Gly Gly Asp Gln Ile Ala Phe Gly Arg Gly Asp Lys Ala Tyr

385 390 395 400

gtc gcc atc aac cac gag ggc tcc gcg ctg aac cgc acc ttc cag agc 1248

Val Ala Ile Asn His Glu Gly Ser Ala Leu Asn Arg Thr Phe Gln Ser

405 410 415

ggc ctg ccc ggc ggc gcc tac tgc gac gtc cag agc ggc agg tcc gtc 1296

Gly Leu Pro Gly Gly Ala Tyr Cys Asp Val Gln Ser Gly Arg Ser Val

420 425 430

acg gtc ggc tcc gac ggc acc ttc acc gcc acc gtc gcc gcc ggc acc 1344

Thr Val Gly Ser Asp Gly Thr Phe Thr Ala Thr Val Ala Ala Gly Thr

435 440 445

gcc ctg gcc ctg cac acc ggg gcc cgt acc tgc tcc ggc ggc gga acc 1392

Ala Leu Ala Leu His Thr Gly Ala Arg Thr Cys Ser Gly Gly Gly Thr

450 455 460

ggc ccc ggc acc ggg cag acc tcc gcc tcc ttc cac gtc aac gcc acc 1440

Gly Pro Gly Thr Gly Gln Thr Ser Ala Ser Phe His Val Asn Ala Thr

465 470 475 480

acc gcc tgg ggc gag aac atc tac gtc acc ggt gac cag gcc gcc ctc 1488

Thr Ala Trp Gly Glu Asn Ile Tyr Val Thr Gly Asp Gln Ala Ala Leu

485 490 495

ggc aac tgg gac ccg gcc cgc gcc ctc aag ctc gac ccg gcc gcc tac 1536

Gly Asn Trp Asp Pro Ala Arg Ala Leu Lys Leu Asp Pro Ala Ala Tyr

500 505 510

ccg gtg tgg aag ctc gac gtg ccg ctg gcc gcc gga acc ccc ttc cag 1584

Pro Val Trp Lys Leu Asp Val Pro Leu Ala Ala Gly Thr Pro Phe Gln

515 520 525

tac aag tac ctg cgc aag gac gcc gcg ggg aag gcc gtc tgg gag tcc 1632

Tyr Lys Tyr Leu Arg Lys Asp Ala Ala Gly Lys Ala Val Trp Glu Ser

530 535 540

ggc gcc aac cgc acg gcg acc gtc ggc acc acc ggc gcc ctc acc ctc 1680

Gly Ala Asn Arg Thr Ala Thr Val Gly Thr Thr Gly Ala Leu Thr Leu

545 550 555 560

aac gac acc tgg cgc ggc 1698

Asn Asp Thr Trp Arg Gly

565

<210>167

<211>566

<212>PRT

<213> Streptomyces limosus

<400>167

Met Ala Arg Arg Leu Ala Thr Ala Ser Leu Ala Val Leu Ala Ala Ala

1 5 10 15

Ala Thr Ala Leu Thr Ala Pro Thr Pro Ala Ala Ala Ala Pro Pro Gly

20 25 30

Ala Lys Asp Val Thr Ala Val Leu Phe Glu Trp Lys Phe Ala Ser Val

35 40 45

Ala Arg Ala Cys Thr Asp Ser Leu Gly Pro Ala Gly Tyr Gly Tyr Val

50 55 60

Gln Val Ser Pro Pro Gln Glu His Ile Gln Gly Ser Gln Trp Trp Thr

65 70 75 80

Ser Tyr Gln Pro Val Ser Tyr Lys Ile Ala Gly Arg Leu Gly Asp Arg

85 90 95

Ala Ala Phe Lys Ser Met Val Asp Thr Cys His Ala Ala Gly Val Lys

100 105 110

Val Val Ala Asp Ser Val Ile Asn His Met Ala Ala Gly Ser Gly Thr

115 120 125

Gly Thr Gly Gly Ser Ala Tyr Gln Lys Tyr Asp Tyr Pro Gly Ile Trp

130 135 140

Ser Gly Ala Asp Met Asp Asp Cys Arg Ser Glu Ile Asn Asp Tyr Gly

145 150 155 160

Asn Arg Ala Asn Val Gln Asn Cys Glu Leu Val Gly Leu Ala Asp Leu

165 170 175

Asp Thr Gly Glu Ser Tyr Val Arg Asp Arg Ile Ala Ala Tyr Leu Asn

180 185 190

Asp Leu Leu Ser Leu Gly Val Asp Gly Phe Arg Ile Asp Ala Ala Lys

195 200 205

His Met Pro Ala Ala Asp Leu Thr Ala Ile Lys Ala Lys Val Gly Asn

210 215 220

Gly Ser Thr Tyr Trp Lys Gln Glu Ala Ile His Gly Ala Gly Glu Ala

225 230 235 240

Val Gln Pro Ser Glu Tyr Leu Gly Thr Gly Asp Val Gln Glu Phe Arg

245 250 255

Tyr Ala Arg Asp Leu Lys Arg Val Phe Gln Asn Glu Asn Leu Ala His

260 265 270

Leu Lys Asn Phe Gly Glu Asp Trp Gly Tyr Met Ala Ser Gly Lys Ser

275 280 285

Ala Val Phe Val Asp Asn His Asp Thr Glu Arg Gly Gly Asp Thr Leu

290 295 300

Asn Tyr Lys Asn Gly Ser Ala Tyr Thr Leu Ala Gly Val Phe Met Leu

305 310 315 320

Ala Trp Pro Tyr Gly Ser Pro Asp Val His Ser Gly Tyr Glu Phe Thr

325 330 335

Asp His Asp Ala Gly Pro Pro Asn Gly Gly Thr Val Asn Ala Cys Tyr

340 345 350

Ser Asp Gly Trp Lys Cys Gln His Ala Trp Pro Glu Leu Ser Ser Ser Met

355 360 365

Val Gly Leu Arg Asn Thr Ala Ser Gly Gln Pro Val Thr Asn Trp Trp

370 375 380

Asp Asn Gly Gly Asp Gln Ile Ala Phe Gly Arg Gly Asp Lys Ala Tyr

385 390 395 400

Val Ala Ile Asn His Glu Gly Ser Ala Leu Asn Arg Thr Phe Gln Ser

405 410 415

Gly Leu Pro Gly Gly Ala Tyr Cys Asp Val Gln Ser Gly Arg Ser Val

420 425 430

Thr Val Gly Ser Asp Gly Thr Phe Thr Ala Thr Val Ala Ala Gly Thr

435 440 445

Ala Leu Ala Leu His Thr Gly Ala Arg Thr Cys Ser Gly Gly Gly Thr

450 455 460

Gly Pro Gly Thr Gly Gln Thr Ser Ala Ser Phe His Val Asn Ala Thr

465 470 475 480

Thr Ala Trp Gly Glu Asn Ile Tyr Val Thr Gly Asp Gln Ala Ala Leu

485 490 495

Gly Asn Trp Asp Pro Ala Arg Ala Leu Lys Leu Asp Pro Ala Ala Tyr

500 505 510

Pro Val Trp Lys Leu Asp Val Pro Leu Ala Ala Gly Thr Pro Phe Gln

515 520 525

Tyr Lys Tyr Leu Arg Lys Asp Ala Ala Gly Lys Ala Val Trp Glu Ser

530 535 540

Gly Ala Asn Arg Thr Ala Thr Val Gly Thr Thr Gly Ala Leu Thr Leu

545 550 555 560

Asn Asp Thr Trp Arg Gly

565

<210>168

<211>1842

<212>DNA

<213> Subulispora provurta

<220>

<221> CDS

<222>(1)..(1842)

<220>

<221>sig_peptide

<222>(1)..(63)

<220>

<221>misc_feature

<222>(64)..(1461)

<223> catalytic domain

<220>

<221>misc_feature

<222>(1462)..(1536)

<223> connector

<220>

<221>misc_feature

<222>(1537)..(1842)

<223>CBM

<400>168

atg aag acg aac gcg ctg ttg ctg ccc ggc ctc tgg gct gcc act gcc 48

Met Lys Thr Asn Ala Leu Leu Leu Pro Gly Leu Trp Ala Ala Thr Ala

1 5 10 15

caa gcc ttg tct gcc acc gaa tgg ggg agt cag tcc atc tac cag gta 96

Gln Ala Leu Ser Ala Thr Glu Trp Gly Ser Gln Ser Ile Tyr Gln Val

20 25 30

ttg acg gat cgc ttt gcc cgc act gat ggg tct act acc gcc tcc tgt 144

Leu Thr Asp Arg Phe Ala Arg Thr Asp Gly Ser Thr Thr Ala Ser Cys

35 40 45

gat gtg aac aag tac tgc ggc ggc acc tgg cag ggc ata atc gac aag 192

Asp Val Asn Lys Tyr Cys Gly Gly Thr Trp Gln Gly Ile Ile Asp Lys

50 55 60

ctg gac tac atc cag ggc atg ggt ttc act gcg atc tgg att tcg cct 240

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Ser Pro

65 70 75 80

atc gtc gac aac atc gac gcc gat act gtt gat ggc acc tct tat cac 288

Ile Val Asp Asn Ile Asp Ala Asp Thr Val Asp Gly Thr Ser Tyr His

85 90 95

ggt tac tgg gcc cag gac atc acc tca gtg aac tcg gcg ttc ggc acg 336

Gly Tyr Trp Ala Gln Asp Ile Thr Ser Val Asn Ser Ala Phe Gly Thr

100 105 110

gag cag gac ctc atc aac ctc tca gca gct ctg cac gac agg ggc atg 384

Glu Gln Asp Leu Ile Asn Leu Ser Ala Ala Leu His Asp Arg Gly Met

115 120 125

tat ctg atg gta gac gtg gta aac aac cac atg gga tac aac ggc tgc 432

Tyr Leu Met Val Asp Val Val Asn Asn His Met Gly Tyr Asn Gly Cys

130 135 140

ggc gat tgt gtt gac tac agc ata tac acg cca ttc aac cag cag tcc 480

Gly Asp Cys Val Asp Tyr Ser Ile Tyr Thr Pro Phe Asn Gln Gln Ser

145 150 155 160

tac tac cac ccg tac tgc gcc act gat tac agc aac ctg acc tcc atc 528

Tyr Tyr His Pro Tyr Cys Ala Thr Asp Tyr Ser Asn Leu Thr Ser Ile

165 170 175

cag gtg tgc tgg gag ggt gac aac att gtc agt ctc ccc gac ctg agg 576

Gln Val Cys Trp Glu Gly Asp Asn Ile Val Ser Leu Pro Asp Leu Arg

180 185 190

aca gag gat gac gat gtc cgc acc atg tgg tac gac tgg atc acg ccg 624

Thr Glu Asp Asp Asp Val Arg Thr Met Trp Tyr Asp Trp Ile Thr Pro

195 200 205

ttg gta acc aag tac tcg atc gat gga ctg cgc atg gac agc gcc gag 672

Leu Val Thr Lys Tyr Ser Ile Asp Gly Leu Arg Met Asp Ser Ala Glu

210 215 220

cat gtc gag aag ag agc ttc tgg cct ggt tgg gta tcc gcc tcg gga gta 720

His Val Glu Lys Ser Phe Trp Pro Gly Trp Val Ser Ala Ser Gly Val

225 230 235 240

tac aac ata gga gag gtt gat gag ggc gac ccc acc atc ttc cca gac 768

Tyr Asn Ile Gly Glu Val Asp Glu Gly Asp Pro Thr Ile Phe Pro Asp

245 250 255

tgg ctg aac tac atc gac gga acc ttg aac tat cca gct tac tac tgg 816

Trp Leu Asn Tyr Ile Asp Gly Thr Leu Asn Tyr Pro Ala Tyr Tyr Trp

260 265 270

atc act caa gct ttc cag tca act tct ggt tct atc agc aac ctg gtt 864

Ile Thr Gln Ala Phe Gln Ser Thr Ser Gly Ser Ile Ser Asn Leu Val

275 280 285

aat gga atc aac caa atg aag ggc tca atg aaa acc agc acc ctc ggg 912

Asn Gly Ile Asn Gln Met Lys Gly Ser Met Lys Thr Ser Thr Leu Gly

290 295 300

tcg ttc ctt gag aat cac gac cag cca cga ttc cct tct ctg act agt 960

Ser Phe Leu Glu Asn His Asp Gln Pro Arg Phe Pro Ser Leu Thr Ser

305 310 315 320

gat gcg gat ttg gcg aag aac gct atc gct ttt gct atg ctt gct gat 1008

Asp Ala Asp Leu Ala Lys Asn Ala Ile Ala Phe Ala Met Leu Ala Asp

325 330 335

ggc gtc cca atc gtc tac tat ggt caa gag cag gcc tac tcg ggt ggt 1056

Gly Val Pro Ile Val Tyr Tyr Gly Gln Glu Gln Ala Tyr Ser Gly Gly

340 345 350

ggc gtg cct aat gac cgt gag cca ctg tgg aca tcg gga tac agc acc 1104

Gly Val Pro Asn Asp Arg Glu Pro Leu Trp Thr Ser Gly Tyr Ser Thr

355 360 365

aca tcg gca ggt tac acg ttc atc acg acc atc aac aaa atc cgc cgc 1152

Thr Ser Ala Gly Tyr Thr Phe Ile Thr Thr Ile Asn Lys Ile Arg Arg

370 375 380

ctg gct ctc acc cag gac agt gcc tac gta gca tac cag acc tac ccg 1200

Leu Ala Leu Thr Gln Asp Ser Ala Tyr Val Ala Tyr Gln Thr Tyr Pro

385 390 395 400

atc tat tcg gat tct cac gtc atc gcc atg aag aag agc agc gtc gtc 1248

Ile Tyr Ser Asp Ser His Val Ile Ala Met Lys Lys Ser Ser Val Val

405 410 415

tcc gtc tat agc aac att ggc tcc agc ggc agc acc tat tcg atc acc 1296

Ser Val Tyr Ser Asn Ile Gly Ser Ser Gly Ser Thr Tyr Ser Ile Thr

420 425 430

cta cct gcc ggc aca ttc act ggg agt gta gcg ctc aca gac gtg gtg 1344

Leu Pro Ala Gly Thr Phe Thr Gly Ser Val Ala Leu Thr Asp Val Val

435 440 445

agc tgc cag acg tac acg gcg agc tct act ggc agc ctc acc ttc acc 1392

Ser Cys Gln Thr Tyr Thr Ala Ser Ser Thr Gly Ser Leu Thr Phe Thr

450 455 460

ttc gga caa gtt ccc tcc gtc ttc tac ccg acg gca agc ctg tcc ggc 1440

Phe Gly Gln Val Pro Ser Val Phe Tyr Pro Thr Ala Ser Leu Ser Gly

465 470 475 480

agc ggg ctc tgc tct agc tcc gga ggc agc ggt acc act acc acg acc 1488

Ser Gly Leu Cys Ser Ser Ser Ser Gly Gly Ser Gly Thr Thr Thr Thr Thr Thr

485 490 495

act acc agc act gca ggc aca tcg cca act tcg aca gcg tgc tcc tcg 1536

Thr Thr Ser Thr Ala Gly Thr Ser Pro Thr Ser Thr Ala Cys Ser Ser

500 505 510

gtc ccc gta acg ttc cgc gaa acg gtc aca act acg gta gga cag aca 1584

Val Pro Val Thr Phe Arg Glu Thr Val Thr Thr Thr Val Gly Gln Thr

515 520 525

atc aag ata tct ggc gac gtc tcc gcc ctt gga aac tgg gat acg gac 1632

Ile Lys Ile Ser Gly Asp Val Ser Ala Leu Gly Asn Trp Asp Thr Asp

530 535 540

gac gcg gtg gcc ctg agc gcc gcg agc tac acg tcc agc aac ccc gtg 1680

Asp Ala Val Ala Leu Ser Ala Ala Ser Tyr Thr Ser Ser Asn Pro Val

545 550 555 560

tgg gac gtg acc gtc agc ttc gcc ccc ggc acc gtc atc gag tac aag 1728

Trp Asp Val Thr Val Ser Phe Ala Pro Gly Thr Val Ile Glu Tyr Lys

565 570 575

tac atc aac gtg gcg agc ggc ggc gcc gtg acc tgg gag gcc gac ccg 1776

Tyr Ile Asn Val Ala Ser Gly Gly Ala Val Thr Trp Glu Ala Asp Pro

580 585 590

aac cac acc tac acg gtg cct tcg tcc tgc gcc acc gcc gtg gtc tcc 1824

Asn His Thr Tyr Thr Val Pro Ser Ser Cys Ala Thr Ala Val Val Ser

595 600 605

aac acc tgg cag acg tga 1842

Asn Thr Trp Gln Thr

610

<210>169

<211>613

<212>PRT

<213> Subulispora provurta

<400>169

Met Lys Thr Asn Ala Leu Leu Leu Pro Gly Leu Trp Ala Ala Thr Ala

1 5 10 15

Gln Ala Leu Ser Ala Thr Glu Trp Gly Ser Gln Ser Ile Tyr Gln Val

20 25 30

Leu Thr Asp Arg Phe Ala Arg Thr Asp Gly Ser Thr Thr Ala Ser Cys

35 40 45

Asp Val Asn Lys Tyr Cys Gly Gly Thr Trp Gln Gly Ile Ile Asp Lys

50 55 60

Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp Ile Ser Pro

65 70 75 80

Ile Val Asp Asn Ile Asp Ala Asp Thr Val Asp Gly Thr Ser Tyr His

85 90 95

Gly Tyr Trp Ala Gln Asp Ile Thr Ser Val Asn Ser Ala Phe Gly Thr

100 105 110

Glu Gln Asp Leu Ile Asn Leu Ser Ala Ala Leu His Asp Arg Gly Met

115 120 125

Tyr Leu Met Val Asp Val Val Asn Asn His Met Gly Tyr Asn Gly Cys

130 135 140

Gly Asp Cys Val Asp Tyr Ser Ile Tyr Thr Pro Phe Asn Gln Gln Ser

145 150 155 160

Tyr Tyr His Pro Tyr Cys Ala Thr Asp Tyr Ser Asn Leu Thr Ser Ile

165 170 175

Gln Val Cys Trp Glu Gly Asp Asn Ile Val Ser Leu Pro Asp Leu Arg

180 185 190

Thr Glu Asp Asp Asp Val Arg Thr Met Trp Tyr Asp Trp Ile Thr Pro

195 200 205

Leu Val Thr Lys Tyr Ser Ile Asp Gly Leu Arg Met Asp Ser Ala Glu

210 215 220

His Val Glu Lys Ser Phe Trp Pro Gly Trp Val Ser Ala Ser Gly Val

225 230 235 240

Tyr Asn Ile Gly Glu Val Asp Glu Gly Asp Pro Thr Ile Phe Pro Asp

245 250 255

Trp Leu Asn Tyr Ile Asp Gly Thr Leu Asn Tyr Pro Ala Tyr Tyr Trp

260 265 270

Ile Thr Gln Ala Phe Gln Ser Thr Ser Gly Ser Ile Ser Asn Leu Val

275 280 285

Asn Gly Ile Asn Gln Met Lys Gly Ser Met Lys Thr Ser Thr Leu Gly

290 295 300

Ser Phe Leu Glu Asn His Asp Gln Pro Arg Phe Pro Ser Leu Thr Ser

305 310 315 320

Asp Ala Asp Leu Ala Lys Asn Ala Ile Ala Phe Ala Met Leu Ala Asp

325 330 335

Gly Val Pro Ile Val Tyr Tyr Gly Gln Glu Gln Ala Tyr Ser Gly Gly

340 345 350

Gly Val Pro Asn Asp Arg Glu Pro Leu Trp Thr Ser Gly Tyr Ser Thr

355 360 365

Thr Ser Ala Gly Tyr Thr Phe Ile Thr Thr Ile Asn Lys Ile Arg Arg

370 375 380

Leu Ala Leu Thr Gln Asp Ser Ala Tyr Val Ala Tyr Gln Thr Tyr Pro

385 390 395 400

Ile Tyr Ser Asp Ser His Val Ile Ala Met Lys Lys Ser Ser Val Val

405 410 415

Ser Val Tyr Ser Asn Ile Gly Ser Ser Gly Ser Thr Tyr Ser Ile Thr

420 425 430

Leu Pro Ala Gly Thr Phe Thr Gly Ser Val Ala Leu Thr Asp Val Val

435 440 445

Ser Cys Gln Thr Tyr Thr Ala Ser Ser Thr Gly Ser Leu Thr Phe Thr

450 455 460

Phe Gly Gln Val Pro Ser Val Phe Tyr Pro Thr Ala Ser Leu Ser Gly

465 470 475 480

Ser Gly Leu Cys Ser Ser Ser Ser Gly Gly Ser Gly Thr Thr Thr Thr Thr Thr

485 490 495

Thr Thr Ser Thr Ala Gly Thr Ser Pro Thr Ser Thr Ala Cys Ser Ser

500 505 510

Val Pro Val Thr Phe Arg Glu Thr Val Thr Thr Thr Val Gly Gln Thr

515 520 525

Ile Lys Ile Ser Gly Asp Val Ser Ala Leu Gly Asn Trp Asp Thr Asp

530 535 540

Asp Ala Val Ala Leu Ser Ala Ala Ser Tyr Thr Ser Ser Asn Pro Val

545 550 555 560

Trp Asp Val Thr Val Ser Phe Ala Pro Gly Thr Val Ile Glu Tyr Lys

565 570 575

Tyr Ile Asn Val Ala Ser Gly Gly Ala Val Thr Trp Glu Ala Asp Pro

580 585 590

Asn His Thr Tyr Thr Val Pro Ser Ser Cys Ala Thr Ala Val Val Ser

595 600 605

Asn Thr Trp Gln Thr

610

<210>170

<211>1389

<212>DNA

<213> Syncephalastrum racemosum

<220>

<221> CDS

<222>(1)..(1389)

<220>

<221>sig_peptide

<222>(1)..(60)

<220>

<221>misc_feature

<222>(61)..(1389)

<223> catalytic domain

<400>170

atg aag gtc ttt atg aac gtt ctc tgt ggg gtc ctt ttc ctg tct ctt 48

Met Lys Val Phe Met Asn Val Leu Cys Gly Val Leu Phe Leu Ser Leu

1 5 10 15

ttg act gaa tcc aaa cct att gtg aaa aaa cgt gcg act gct agt gac 96

Leu Thr Glu Ser Lys Pro Ile Val Lys Lys Arg Ala Thr Ala Ser Asp

20 25 30

tgg gaa aat cga gtt atc tac caa ttg ttg aca gat cga ttt gct aaa 144

Trp Glu Asn Arg Val Ile Tyr Gln Leu Leu Thr Asp Arg Phe Ala Lys

35 40 45

agc tct gac gac aca aac ggt tgc tcc aac cta ggc aat tat tgt ggc 192

Ser Ser Asp Asp Thr Asn Gly Cys Ser Asn Leu Gly Asn Tyr Cys Gly

50 55 60

ggg acg ttt caa ggg att atc aat cat cta gac tat att gcc ggt atg 240

Gly Thr Phe Gln Gly Ile Ile Asn His Leu Asp Tyr Ile Ala Gly Met

65 70 75 80

gga ttc gat gcg atc tgg ata tcg cca att cct gaa aac tcg gat ggg 288

Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro Glu Asn Ser Asp Gly

85 90 95

ggg tat cac ggt tac tgg gct acc aac ttt tct gcc atc aac tca cat 336

Gly Tyr His Gly Tyr Trp Ala Thr Asn Phe Ser Ala Ile Asn Ser His

100 105 110

ttt ggg tcg tct aat gat ttg aag aaa ttg gtg tca gca gct cat gac 384

Phe Gly Ser Ser Asn Asp Leu Lys Lys Leu Val Ser Ala Ala His Asp

115 120 125

aag ggc atg tat gtt atg ctt gac gtg gtt gct aac cac gtt ggc ata 432

Lys Gly Met Tyr Val Met Leu Asp Val Val Ala Asn His Val Gly Ile

130 135 140

cct tcc tcc agt ggc caa tac tcg gga tac acg ttt gat caa agc tct 480

Pro Ser Ser Ser Gly Gln Tyr Ser Gly Tyr Thr Phe Asp Gln Ser Ser

145 150 155 160

cag tat cat agt tct tgt gat att aac tat gac aac caa aac tct att 528

Gln Tyr His Ser Ser Cys Asp Ile Asn Tyr Asp Asn Gln Asn Ser Ile

165 170 175

gaa caa tgc tgg atc tct ggc tta cct gat ctt aac acc gaa gat tca 576

Glu Gln Cys Trp Ile Ser Gly Leu Pro Asp Leu Asn Thr Glu Asp Ser

180 185 190

gcg gta gtc agc aag cta aac tcg att gtg tca aac tgg gta tcc gaa 624

Ala Val Val Ser Lys Leu Asn Ser Ile Val Ser Asn Trp Val Ser Glu

195 200 205

tat gac ttt gat ggg ctt cgt att gat act gtc aag cac att cgc aag 672

Tyr Asp Phe Asp Gly Leu Arg Ile Asp Thr Val Lys His Ile Arg Lys

210 215 220

gat ttt tgg gat ggc tat gta tct gct gca ggt gta ttt gcc act ggg 720

Asp Phe Trp Asp Gly Tyr Val Ser Ala Ala Gly Val Phe Ala Thr Gly

225 230 235 240

gaa gtc ttg aac ggt gct gtt tct tat gtt gct cca tac caa caa cat 768

Glu Val Leu Asn Gly Ala Val Ser Tyr Val Ala Pro Tyr Gln Gln His

245 250 255

gtt ccc tct tta ctc aac tac cca ctg tat ttc ccc gtc aat gat gtg 816

Val Pro Ser Leu Leu Asn Tyr Pro Leu Tyr Phe Pro Val Asn Asp Val

260 265 270

ttc acg aag gct tct acc atg agt cgt ttg gga tca ggc tat gct gat 864

Phe Thr Lys Ala Ser Thr Met Ser Arg Leu Gly Ser Gly Tyr Ala Asp

275 280 285

atc cag tct ggc agc ttt aca aac aga aac cat ctg gtt aac ttt atc 912

Ile Gln Ser Gly Ser Phe Thr Asn Arg Asn His Leu Val Asn Phe Ile

290 295 300

gac aac cat gac aat cct cgt ttg tta tcc aag tct gat cag gtc ttg 960

Asp Asn His Asp Asn Pro Arg Leu Leu Ser Lys Ser Asp Gln Val Leu

305 310 315 320

gtg aag aat gct ctt aca tac acc atg atg att gaa gga atc cca gcc 1008

Val Lys Asn Ala Leu Thr Tyr Thr Met Met Ile Glu Gly Ile Pro Ala

325 330 335

atg tac tat ggt acc gag caa tca ttc aat gga ggc tct gac cct gcc 1056

Met Tyr Tyr Gly Thr Glu Gln Ser Phe Asn Gly Gly Ser Asp Pro Ala

340 345 350

aac aga gag gtc tta tgg acc acg aat tat tcg acc aca tcc gac atg 1104

Asn Arg Glu Val Leu Trp Thr Thr Asn Tyr Ser Thr Thr Ser Asp Met

355 360 365

tac aag ttt gtc act tta ctc gtc aaa aca cgc aag agc tcg gga aac 1152

Tyr Lys Phe Val Thr Leu Leu Val Lys Thr Arg Lys Ser Ser Gly Asn

370 375 380

acg gtt act aca ggc att gac cag acc aac aat gtt tat gtg ttt caa 1200

Thr Val Thr Thr Gly Ile Asp Gln Thr Asn Asn Val Tyr Val Phe Gln

385 390 395 400

aga gac aag tat ctg gtt gtt gtg aac aat tac ggc tca gga tcc acc 1248

Arg Asp Lys Tyr Leu Val Val Val Asn Asn Tyr Gly Ser Gly Ser Thr

405 410 415

aat tcg atc act gta aag gct ggt tca ttc tcc aat ggt gtt acc ctt 1296

Asn Ser Ile Thr Val Lys Ala Gly Ser Phe Ser Asn Gly Val Thr Leu

420 425 430

gtg gat ata ttc tcg aat aaa aca gtg act gtg tca aac gga tcg atc 1344

Val Asp Ile Phe Ser Asn Lys Thr Val Thr Val Ser Asn Gly Ser Ile

435 440 445

acc ttc cag ctt caa aat ggt aat cct gct gta ttc caa agc aaa 1389

Thr Phe Gln Leu Gln Asn Gly Asn Pro Ala Val Phe Gln Ser Lys

450 455 460

<210>171

<211>463

<212>PRT

<213> Syncephalastrum racemosum

<400>171

Met Lys Val Phe Met Asn Val Leu Cys Gly Val Leu Phe Leu Ser Leu

1 5 10 15

Leu Thr Glu Ser Lys Pro Ile Val Lys Lys Arg Ala Thr Ala Ser Asp

20 25 30

Trp Glu Asn Arg Val Ile Tyr Gln Leu Leu Thr Asp Arg Phe Ala Lys

35 40 45

Ser Ser Asp Asp Thr Asn Gly Cys Ser Asn Leu Gly Asn Tyr Cys Gly

50 55 60

Gly Thr Phe Gln Gly Ile Ile Asn His Leu Asp Tyr Ile Ala Gly Met

65 70 75 80

Gly Phe Asp Ala Ile Trp Ile Ser Pro Ile Pro Glu Asn Ser Asp Gly

85 90 95

Gly Tyr His Gly Tyr Trp Ala Thr Asn Phe Ser Ala Ile Asn Ser His

100 105 110

Phe Gly Ser Ser Asn Asp Leu Lys Lys Leu Val Ser Ala Ala His Asp

115 120 125

Lys Gly Met Tyr Val Met Leu Asp Val Val Ala Asn His Val Gly Ile

130 135 140

Pro Ser Ser Ser Gly Gln Tyr Ser Gly Tyr Thr Phe Asp Gln Ser Ser

145 150 155 160

Gln Tyr His Ser Ser Cys Asp Ile Asn Tyr Asp Asn Gln Asn Ser Ile

165 170 175

Glu Gln Cys Trp Ile Ser Gly Leu Pro Asp Leu Asn Thr Glu Asp Ser

180 185 190

Ala Val Val Ser Lys Leu Asn Ser Ile Val Ser Asn Trp Val Ser Glu

195 200 205

Tyr Asp Phe Asp Gly Leu Arg Ile Asp Thr Val Lys His Ile Arg Lys

210 215 220

Asp Phe Trp Asp Gly Tyr Val Ser Ala Ala Gly Val Phe Ala Thr Gly

225 230 235 240

Glu Val Leu Asn Gly Ala Val Ser Tyr Val Ala Pro Tyr Gln Gln His

245 250 255

Val Pro Ser Leu Leu Asn Tyr Pro Leu Tyr Phe Pro Val Asn Asp Val

260 265 270

Phe Thr Lys Ala Ser Thr Met Ser Arg Leu Gly Ser Gly Tyr Ala Asp

275 280 285

Ile Gln Ser Gly Ser Phe Thr Asn Arg Asn His Leu Val Asn Phe Ile

290 295 300

Asp Asn His Asp Asn Pro Arg Leu Leu Ser Lys Ser Asp Gln Val Leu

305 310 315 320

Val Lys Asn Ala Leu Thr Tyr Thr Met Met Ile Glu Gly Ile Pro Ala

325 330 335

Met Tyr Tyr Gly Thr Glu Gln Ser Phe Asn Gly Gly Ser Asp Pro Ala

340 345 350

Asn Arg Glu Val Leu Trp Thr Thr Asn Tyr Ser Thr Thr Ser Asp Met

355 360 365

Tyr Lys Phe Val Thr Leu Leu Val Lys Thr Arg Lys Ser Ser Gly Asn

370 375 380

Thr Val Thr Thr Gly Ile Asp Gln Thr Asn Asn Val Tyr Val Phe Gln

385 390 395 400

Arg Asp Lys Tyr Leu Val Val Val Asn Asn Tyr Gly Ser Gly Ser Thr

405 410 415

Asn Ser Ile Thr Val Lys Ala Gly Ser Phe Ser Asn Gly Val Thr Leu

420 425 430

Val Asp Ile Phe Ser Asn Lys Thr Val Thr Val Ser Asn Gly Ser Ile

435 440 445

Thr Phe Gln Leu Gln Asn Gly Asn Pro Ala Val Phe Gln Ser Lys

450 455 460

<210>172

<211>1764

<212>DNA

<213> Trametes corrugata

<220>

<221> CDS

<222>(1)..(1764)

<220>

<221>sig_peptide

<222>(1)..(60)

<220>

<221>misc_feature

<222>(61)..(1431)

<223> catalytic domain

<220>

<221>misc_feature

<222>(1432)..(1473)

<223> connector

<220>

<221>misc_feature

<222>(1474)..(1764)

<223>CBM

<400>172

atg ttg ttc ctt tct acg ctc ctc tcg ttc ttc ttt tac ttc agc tcc 48

Met Leu Phe Leu Ser Thr Leu Leu Ser Phe Phe Phe Tyr Phe Ser Ser

1 5 10 15

att gtg aca gcg gcg gat acg agt gca tgg aag tcc cgc agc atc tac 96

Ile Val Thr Ala Ala Asp Thr Ser Ala Trp Lys Ser Arg Ser Ile Tyr

20 25 30

ttc gtt ctg acc gat cgt gtt gct cga agc agc agc gac acc ggc ggt 144

Phe Val Leu Thr Asp Arg Val Ala Arg Ser Ser Ser Asp Thr Gly Gly

35 40 45

tcc tct tgc agc aac ctg ggc aat tac tgt gga gga act ttc aaa ggt 192

Ser Ser Cys Ser Asn Leu Gly Asn Tyr Cys Gly Gly Thr Phe Lys Gly

50 55 60

ctc gaa tct aag ctg gat tac atc caa ggc ttg ggc ttt gac gct atc 240

Leu Glu Ser Lys Leu Asp Tyr Ile Gln Gly Leu Gly Phe Asp Ala Ile

65 70 75 80

tgg atc acg cct gtc gtt gct aac agt gct ggt ggc tac cat ggc tat 288

Trp Ile Thr Pro Val Val Ala Asn Ser Ala Gly Gly Tyr His Gly Tyr

85 90 95

tgg gca caa gac ttg tat tct gtc aac tcg aat tat ggt act gca gac 336

Trp Ala Gln Asp Leu Tyr Ser Val Asn Ser Asn Tyr Gly Thr Ala Asp

100 105 110

gac cta aag ag agc ctg gtc agc tct gct cat gcg aag ggc ata tat gtg 384

Asp Leu Lys Ser Leu Val Ser Ser Ser Ala His Ala Lys Gly Ile Tyr Val

115 120 125

atg gtc gat gtc gta gcc aat cat atg ggt aac ggt gca att gcc gat 432

Met Val Asp Val Val Ala Asn His Met Gly Asn Gly Ala Ile Ala Asp

130 135 140

aac cgc cct gag cct ttg aac cag gct tca tcc tac cac cca gcc tgc 480

Asn Arg Pro Glu Pro Leu Asn Gln Ala Ser Ser Tyr His Pro Ala Cys

145 150 155 160

gac atc aac tac gat aac cag acc agc atc gag cag tgc agc atc ggc 528

Asp Ile Asn Tyr Asp Asn Gln Thr Ser Ile Glu Gln Cys Ser Ile Gly

165 170 175

ggt ctt gct gat ctt aac act gag agt acc gag gtt cgc act gtt ctc 576

Gly Leu Ala Asp Leu Asn Thr Glu Ser Thr Glu Val Arg Thr Val Leu

180 185 190

aac acc tgg gtt tca tgg ctc gtc gac gag tac agc ttc gac gga gta 624

Asn Thr Trp Val Ser Trp Leu Val Asp Glu Tyr Ser Phe Asp Gly Val

195 200 205

cgt atc gac aca gtc aag cac gtt caa aag gac ttc tgg cca gac ttc 672

Arg Ile Asp Thr Val Lys His Val Gln Lys Asp Phe Trp Pro Asp Phe

210 215 220

gtg tct tcc ata ggc gaa tac agc atc ggt gag gtg ttt gac ggc aac 720

Val Ser Ser Ile Gly Glu Tyr Ser Ile Gly Glu Val Phe Asp Gly Asn

225 230 235 240

cct cca tac ctc gct gag tat gcc aag ctc atg cct ggg gtt cta aac 768

Pro Pro Tyr Leu Ala Glu Tyr Ala Lys Leu Met Pro Gly Val Leu Asn

245 250 255

tat gca gtc tac tac ccc atg aat gcc ttc tac cag caa acg ggc tca 816

Tyr Ala Val Tyr Tyr Pro Met Asn Ala Phe Tyr Gln Gln Thr Gly Ser

260 265 270

tct cag gca ctg gtc gac atg atg aac acg att agc agc aca ttc cca 864

Ser Gln Ala Leu Val Asp Met Met Asn Thr Ile Ser Ser Thr Phe Pro

275 280 285

gac ccc tca gca ctc ggc acg ttc ctc gac aac cac gac aac ccg cgc 912

Asp Pro Ser Ala Leu Gly Thr Phe Leu Asp Asn His Asp Asn Pro Arg

290 295 300

tgg cta aac gtg aag aac gac cag aca ctc ctg aag aac gca cta gcc 960

Trp Leu Asn Val Lys Asn Asp Gln Thr Leu Leu Lys Asn Ala Leu Ala

305 310 315 320

tac gtc att cta gcc cga ggc att ccc atc cta tac tac ggc acc gag 1008

Tyr Val Ile Leu Ala Arg Gly Ile Pro Ile Leu Tyr Tyr Gly Thr Glu

325 330 335

caa ggt tac tcc gga ggc gcc gac cca gca aac cgc gaa gat ctt tgg 1056

Gln Gly Tyr Ser Gly Gly Ala Asp Pro Ala Asn Arg Glu Asp Leu Trp

340 345 350

cgc agc agc ttc aat aca aac gcg gac ctc tac caa tcc atc aaa aag 1104

Arg Ser Ser Phe Asn Thr Asn Ala Asp Leu Tyr Gln Ser Ile Lys Lys

355 360 365

ctc acc gca gcc cga aaa gcc gcc ggc ggc ctc gcc ggc aac gac cac 1152

Leu Thr Ala Ala Arg Lys Ala Ala Gly Gly Leu Ala Gly Asn Asp His

370 375 380

acg cat ctc tac gtc gcc gac acg gca tat gcc tgg agc cgg gca aac 1200

Thr His Leu Tyr Val Ala Asp Thr Ala Tyr Ala Trp Ser Arg Ala Asn

385 390 395 400

ggc gcc ctc atc gtg ctc acc acc aac gcc ggc agc agc tcc aac gcg 1248

Gly Ala Leu Ile Val Leu Thr Thr Asn Ala Gly Ser Ser Ser Asn Ala

405 410 415

caa cac tgc ttc aac acg cag atg gca aac ggg aaa tgg acg aac acg 1296

Gln His Cys Phe Asn Thr Gln Met Ala Asn Gly Lys Trp Thr Asn Thr

420 425 430

tat ggt gat ggc gca acg gtg acc gcg gat tcc agc ggt aat atc tgc 1344

Tyr Gly Asp Gly Ala Thr Val Thr Ala Asp Ser Ser Gly Asn Ile Cys

435 440 445

gtc acc gtt agc aac ggc gag cct gtt gtc ctc gtc gcc agc gca tca 1392

Val Thr Val Ser Asn Gly Glu Pro Val Val Leu Val Ala Ser Ala Ser

450 455 460

aca acg ggg gtt acg ccc act aca gct aca acg ctg cgc act acc aca 1440

Thr Thr Gly Val Thr Pro Thr Thr Ala Thr Thr Leu Arg Thr Thr Thr

465 470 475 480

gcc tcc gcg tgt ccg act tcc gtt gca gta tcg ttc acg cac agc atc 1488

Ala Ser Ala Cys Pro Thr Ser Val Ala Val Ser Phe Thr His Ser Ile

485 490 495

acc act gtg ccc ggc gac act atc aag atc gcg ggt aac acg acg caa 1536

Thr Thr Val Pro Gly Asp Thr Ile Lys Ile Ala Gly Asn Thr Thr Gln

500 505 510

ctc ggt agc tgg act gta gct tcc gca ccc gcg ctc tca gcg tca tcg 1584

Leu Gly Ser Trp Thr Val Ala Ser Ala Pro Ala Leu Ser Ala Ser Ser

515 520 525

tac acg tcg agt aac cct gta tgg acg att acg ctg agc atg ccg gcg 1632

Tyr Thr Ser Ser Asn Pro Val Trp Thr Ile Thr Leu Ser Met Pro Ala

530 535 540

aag cag gcg gtg cag tat aag ttt gtt aag gtg gcg agt ggg ggc gcg 1680

Lys Gln Ala Val Gln Tyr Lys Phe Val Lys Val Ala Ser Gly Gly Ala

545 550 555 560

gtg acg tgg gag agc gat ccg aat cgt agt tat agc gtc ccg gcg tgt 1728

Val Thr Trp Glu Ser Asp Pro Asn Arg Ser Tyr Ser Val Pro Ala Cys

565 570 575

cag gcg agt gcg gcg gtg agt agt agt tgg cag tga 1764

Gln Ala Ser Ala Ala Val Ser Ser Ser Trp Gln

580 585

<210>173

<211>587

<212>PRT

<213> Trametes corrugata

<400>173

Met Leu Phe Leu Ser Thr Leu Leu Ser Phe Phe Phe Tyr Phe Ser Ser

1 5 10 15

Ile Val Thr Ala Ala Asp Thr Ser Ala Trp Lys Ser Arg Ser Ile Tyr

20 25 30

Phe Val Leu Thr Asp Arg Val Ala Arg Ser Ser Ser Asp Thr Gly Gly

35 40 45

Ser Ser Cys Ser Asn Leu Gly Asn Tyr Cys Gly Gly Thr Phe Lys Gly

50 55 60

Leu Glu Ser Lys Leu Asp Tyr Ile Gln Gly Leu Gly Phe Asp Ala Ile

65 70 75 80

Trp Ile Thr Pro Val Val Ala Asn Ser Ala Gly Gly Tyr His Gly Tyr

85 90 95

Trp Ala Gln Asp Leu Tyr Ser Val Asn Ser Asn Tyr Gly Thr Ala Asp

100 105 110

Asp Leu Lys Ser Leu Val Ser Ser Ser Ala His Ala Lys Gly Ile Tyr Val

115 120 125

Met Val Asp Val Val Ala Asn His Met Gly Asn Gly Ala Ile Ala Asp

130 135 140

Asn Arg Pro Glu Pro Leu Asn Gln Ala Ser Ser Tyr His Pro Ala Cys

145 150 155 160

Asp Ile Asn Tyr Asp Asn Gln Thr Ser Ile Glu Gln Cys Ser Ile Gly

165 170 175

Gly Leu Ala Asp Leu Asn Thr Glu Ser Thr Glu Val Arg Thr Val Leu

180 185 190

Asn Thr Trp Val Ser Trp Leu Val Asp Glu Tyr Ser Phe Asp Gly Val

195 200 205

Arg Ile Asp Thr Val Lys His Val Gln Lys Asp Phe Trp Pro Asp Phe

210 215 220

Val Ser Ser Ile Gly Glu Tyr Ser Ile Gly Glu Val Phe Asp Gly Asn

225 230 235 240

Pro Pro Tyr Leu Ala Glu Tyr Ala Lys Leu Met Pro Gly Val Leu Asn

245 250 255

Tyr Ala Val Tyr Tyr Pro Met Asn Ala Phe Tyr Gln Gln Thr Gly Ser

260 265 270

Ser Gln Ala Leu Val Asp Met Met Asn Thr Ile Ser Ser Thr Phe Pro

275 280 285

Asp Pro Ser Ala Leu Gly Thr Phe Leu Asp Asn His Asp Asn Pro Arg

290 295 300

Trp Leu Asn Val Lys Asn Asp Gln Thr Leu Leu Lys Asn Ala Leu Ala

305 310 315 320

Tyr Val Ile Leu Ala Arg Gly Ile Pro Ile Leu Tyr Tyr Gly Thr Glu

325 330 335

Gln Gly Tyr Ser Gly Gly Ala Asp Pro Ala Asn Arg Glu Asp Leu Trp

340 345 350

Arg Ser Ser Phe Asn Thr Asn Ala Asp Leu Tyr Gln Ser Ile Lys Lys

355 360 365

Leu Thr Ala Ala Arg Lys Ala Ala Gly Gly Leu Ala Gly Asn Asp His

370 375 380

Thr His Leu Tyr Val Ala Asp Thr Ala Tyr Ala Trp Ser Arg Ala Asn

385 390 395 400

Gly Ala Leu Ile Val Leu Thr Thr Asn Ala Gly Ser Ser Ser Asn Ala

405 410 415

Gln His Cys Phe Asn Thr Gln Met Ala Asn Gly Lys Trp Thr Asn Thr

420 425 430

Tyr Gly Asp Gly Ala Thr Val Thr Ala Asp Ser Ser Gly Asn Ile Cys

435 440 445

Val Thr Val Ser Asn Gly Glu Pro Val Val Leu Val Ala Ser Ala Ser

450 455 460

Thr Thr Gly Val Thr Pro Thr Thr Ala Thr Thr Leu Arg Thr Thr Thr

465 470 475 480

Ala Ser Ala Cys Pro Thr Ser Val Ala Val Ser Phe Thr His Ser Ile

485 490 495

Thr Thr Val Pro Gly Asp Thr Ile Lys Ile Ala Gly Asn Thr Thr Gln

500 505 510

Leu Gly Ser Trp Thr Val Ala Ser Ala Pro Ala Leu Ser Ala Ser Ser

515 520 525

Tyr Thr Ser Ser Asn Pro Val Trp Thr Ile Thr Leu Ser Met Pro Ala

530 535 540

Lys Gln Ala Val Gln Tyr Lys Phe Val Lys Val Ala Ser Gly Gly Ala

545 550 555 560

Val Thr Trp Glu Ser Asp Pro Asn Arg Ser Tyr Ser Val Pro Ala Cys

565 570 575

Gln Ala Ser Ala Ala Val Ser Ser Ser Trp Gln

580 585

<210>174

<211>2322

<212>DNA

<213>Trichopheraea saccata

<220>

<221> CDS

<222>(1)..(2322)

<220>

<221>sig_peptide

<222>(1)..(60)

<220>

<221>misc_feature

<222>(61)..(861)

<223> linker+CBM (N-terminal)

<220>

<221>misc_feature

<222>(862)..(2322)

<223> catalytic domain

<400>174

atg tgt tcg ctg cgt tac ttc gcc ctt ttt ctg ttt cca ttt ctc ctt 48

Met Cys Ser Leu Arg Tyr Phe Ala Leu Phe Leu Phe Pro Phe Leu Leu

1 5 10 15

ttg gtc agt gca tcg cca gtt cat cag aac acc aaa cga tct acc caa 96

Leu Val Ser Ala Ser Pro Val His Gln Asn Thr Lys Arg Ser Thr Gln

20 25 30

gtg tcg ttg atc agc tat acg ttt tct aac aat att ctc tct gga tcc 144

Val Ser Leu Ile Ser Tyr Thr Phe Ser Asn Asn Ile Leu Ser Gly Ser

35 40 45

atc agc att caa aac att gct tac gcc aaa acg gtc agc gtt acc tat 192

Ile Ser Ile Gln Asn Ile Ala Tyr Ala Lys Thr Val Ser Val Thr Tyr

50 55 60

gcc att ggg agc tct tgg agc tcc tct cag gtg ata agc gct gcc tac 240

Ala Ile Gly Ser Ser Trp Ser Ser Ser Gln Val Ile Ser Ala Ala Tyr

65 70 75 80

tcc aca ggt cct gat agc acc ggt tat gaa gtc tgg acg ttt agc ggc 288

Ser Thr Gly Pro Asp Ser Thr Gly Tyr Glu Val Trp Thr Phe Ser Gly

85 90 95

aca gca acg ggg gca act cag ttc tac att gcg tat act gtc tca ggg 336

Thr Ala Thr Gly Ala Thr Gln Phe Tyr Ile Ala Tyr Thr Val Ser Gly

100 105 110

acc acc tac tac gat cct gga aat ggc atc aat tac acg atc ggc acg 384

Thr Thr Tyr Tyr Asp Pro Gly Asn Gly Ile Asn Tyr Thr Ile Gly Thr

115 120 125

ggt tcg tcc act act tcc agc aca tct gcc act tcg aca acc aaa agt 432

Gly Ser Ser Thr Thr Ser Ser Ser Thr Ser Ala Thr Ser Thr Thr Lys Ser

130 135 140

tcc acc act tcc acg agc act gcg act agc aca agc gtg gcg acc agc 480

Ser Thr Thr Ser Ser Thr Ser Thr Ala Thr Ser Ser Thr Ser Val Ala Thr Ser

145 150 155 160

agt ctc cct gct atc att tca tcc agt att cct tct gag gcg gca gcc 528

Ser Leu Pro Ala Ile Ile Ser Ser Ser Ser Ile Pro Ser Glu Ala Ala Ala

165 170 175

acc gcg ctt tct gga tgc aat act tgg gat ggt ttt gac aac tgc caa 576

Thr Ala Leu Ser Gly Cys Asn Thr Trp Asp Gly Phe Asp Asn Cys Gln

180 185 190

act agt ggc gtg tac gac ttt gtg gcc agt gcc gaa aac cgc aga tgg 624

Thr Ser Gly Val Tyr Asp Phe Val Ala Ser Ala Glu Asn Arg Arg Trp

195 200 205

cag acg ccc ccg gac ggc gat cct gcc tat gtc aat acg ttc caa gac 672

Gln Thr Pro Pro Asp Gly Asp Pro Ala Tyr Val Asn Thr Phe Gln Asp

210 215 220

tac cga gat ctc att ggc tac gcc gat atc cag tac agc cct tca cga 720

Tyr Arg Asp Leu Ile Gly Tyr Ala Asp Ile Gln Tyr Ser Pro Ser Arg

225 230 235 240

acc tcc gcc gtt gtg act gtc aat gct gct tcg cgg acc ggc gag act 768

Thr Ser Ala Val Val Thr Val Asn Ala Ala Ser Arg Thr Gly Glu Thr

245 250 255

ttg acc tac aaa ttt ggg gga att act cag acg tct aac gcg tac acc 816

Leu Thr Tyr Lys Phe Gly Gly Ile Thr Gln Thr Ser Asn Ala Tyr Thr

260 265 270

gtg agc agc tcg ttt atc gga acc ctg gca atc aca gtc acc agt tca 864

Val Ser Ser Ser Phe Ile Gly Thr Leu Ala Ile Thr Val Thr Ser Ser

275 280 285

tcc ggc aag aaa tta gag ctg gag gcc ctc aac ttt gtt tgg cag aat 912

Ser Gly Lys Lys Leu Glu Leu Glu Ala Leu Asn Phe Val Trp Gln Asn

290 295 300

gca gtt ctt act ggc gct cag agc act ttc aac aat ggg cag aag ggc 960

Ala Val Leu Thr Gly Ala Gln Ser Thr Phe Asn Asn Gly Gln Lys Gly

305 310 315 320

gct att gtg gag ctt ttt ggg tgg ccg tat gca gat att gca aag gag 1008

Ala Ile Val Glu Leu Phe Gly Trp Pro Tyr Ala Asp Ile Ala Lys Glu

325 330 335

tgc gct ttc ctt gga aaa gcc gga tac atg gga gtc aag gtt tgg cct 1056

Cys Ala Phe Leu Gly Lys Ala Gly Tyr Met Gly Val Lys Val Trp Pro

340 345 350

cca aac gag cac atc tgg gga tcg gac tac tac gaa acc gac aat atg 1104

Pro Asn Glu His Ile Trp Gly Ser Asp Tyr Tyr Glu Thr Asp Asn Met

355 360 365

ttc cgt ccg tgg tat ctg gtg tac cag ccg gtc agt tac aag ctt gtg 1152

Phe Arg Pro Trp Tyr Leu Val Tyr Gln Pro Val Ser Tyr Lys Leu Val

370 375 380

agc cgt caa gga acc cgt gag gag ctt cga gct atg ata act gct tgc 1200

Ser Arg Gln Gly Thr Arg Glu Glu Leu Arg Ala Met Ile Thr Ala Cys

385 390 395 400

cgg agt gct gga gtg cgc gtc tat gcc gac gcc gtc att aat cac atg 1248

Arg Ser Ala Gly Val Arg Val Tyr Ala Asp Ala Val Ile Asn His Met

405 410 415

tct gga aac gga aac gat atc caa aac cat cgt aat acc gcc tgc gcc 1296

Ser Gly Asn Gly Asn Asp Ile Gln Asn His Arg Asn Thr Ala Cys Ala

420 425 430

tac tgg aca ggc cac aac gca acc gcg aat tcg cct tac ttc acc tcc 1344

Tyr Trp Thr Gly His Asn Ala Thr Ala Asn Ser Pro Tyr Phe Thr Ser

435 440 445

ggt tac acc tat ctt att aat ccc ttc acg aac aca cgc ccc acc ttc 1392

Gly Tyr Thr Tyr Leu Ile Asn Pro Phe Thr Asn Thr Arg Pro Thr Phe

450 455 460

gag tac cca gcg gta cca tgg ggc cca act gat ttc cat tgc gtt tcc 1440

Glu Tyr Pro Ala Val Pro Trp Gly Pro Thr Asp Phe His Cys Val Ser

465 470 475 480

tct atc aca gat tgg acc aac ggc caa atc gtc aca aag ggc tat ctc 1488

Ser Ile Thr Asp Trp Thr Asn Gly Gln Ile Val Thr Lys Gly Tyr Leu

485 490 495

gtg gga ctc tcc gat ctc aac aca gag aag gat tac gtc cag gac cgc 1536

Val Gly Leu Ser Asp Leu Asn Thr Glu Lys Asp Tyr Val Gln Asp Arg

500 505 510

atc gcc act tat ctt gtg gat ctc ttg tca atc ggc ttc tcc ggc ttc 1584

Ile Ala Thr Tyr Leu Val Asp Leu Leu Ser Ile Gly Phe Ser Gly Phe

515 520 525

cgt gtt gat gcg gca aaa cat att ggc ccc acc tcc atg gca cag atc 1632

Arg Val Asp Ala Ala Lys His Ile Gly Pro Thr Ser Met Ala Gln Ile

530 535 540

ttc gga agg gtt gca aag aag atg ggc gga agt ctt cca gat gat ttt 1680

Phe Gly Arg Val Ala Lys Lys Met Gly Gly Ser Leu Pro Asp Asp Phe

545 550 555 560

atc act tgg ctt gaa gtg ttg atg ggt ggt gag aag gag cag tat gct 1728

Ile Thr Trp Leu Glu Val Leu Met Gly Gly Glu Lys Glu Gln Tyr Ala

565 570 575

tgc ggc ggc ggt gaa tgg agt tgg tac acc aac ttc aat acc cag ctt 1776

Cys Gly Gly Gly Glu Trp Ser Trp Tyr Thr Asn Phe Asn Thr Gln Leu

580 585 590

tcc aat gcg gga att agt gac act gat atc aat aag atc aag att tgg 1824

Ser Asn Ala Gly Ile Ser Asp Thr Asp Ile Asn Lys Ile Lys Ile Trp

595 600 605

agc tcc gac tat ccc aag gag ttc ccg atc tgc ggt tct tgg atc atc 1872

Ser Ser Asp Tyr Pro Lys Glu Phe Pro Ile Cys Gly Ser Trp Ile Ile

610 615 620

cca tcc act cgc ttt gtc atc caa aat gac gac cat gac cag cag aac 1920

Pro Ser Thr Arg Phe Val Ile Gln Asn Asp Asp His Asp Gln Gln Asn

625 630 635 640

ccg ggc tct tcc tcc aga gat atg ggt gac caa ggc tcc gta ctc atc 1968

Pro Gly Ser Ser Ser Arg Asp Met Gly Asp Gln Gly Ser Val Leu Ile

645 650 655

aaa gat caa gat gta gcc aag cac cgg gca ttt gag gtc aag ctc ttc 2016

Lys Asp Gln Asp Val Ala Lys His Arg Ala Phe Glu Val Lys Leu Phe

660 665 670

acc cgt acc gac ggt gac tgg caa atc agg aat atc ctc tcc tct tat 2064

Thr Arg Thr Asp Gly Asp Trp Gln Ile Arg Asn Ile Leu Ser Ser Tyr

675 680 685

atg ttt gcc tcc aac gga gca aat ggc ttc ccc gat ggt ctt tcg gat 2112

Met Phe Ala Ser Asn Gly Ala Asn Gly Phe Pro Asp Gly Leu Ser Asp

690 695 700

tgt tcc ctt tat act ggc tca cag agt gcg agt ggt tgt ttg ggt atc 2160

Cys Ser Leu Tyr Thr Gly Ser Gln Ser Ala Ser Gly Cys Leu Gly Ile

705 710 715 720

gcg aag gat acc gct tat gta gaa ggt atc tgt ggg tat act atg gtt 2208

Ala Lys Asp Thr Ala Tyr Val Glu Gly Ile Cys Gly Tyr Thr Met Val

725 730 735

gct gga agg tac acc agg ccg cat agg gat ctg agc atc att aat gct 2256

Ala Gly Arg Tyr Thr Arg Pro His Arg Asp Leu Ser Ile Ile Asn Ala

740 745 750

atg agg agt tgg gtc ggg ttg tcg agt acc aca gcg gat gct ctt gga 2304

Met Arg Ser Trp Val Gly Leu Ser Ser Thr Thr Ala Asp Ala Leu Gly

755 760 765

atc ccc ggt tgt agc tga 2322

Ile Pro Gly Cys Ser

770

<210>175

<211>773

<212>PRT

<213>Trichopheraea saccata

<400>175

Met Cys Ser Leu Arg Tyr Phe Ala Leu Phe Leu Phe Pro Phe Leu Leu

1 5 10 15

Leu Val Ser Ala Ser Pro Val His Gln Asn Thr Lys Arg Ser Thr Gln

20 25 30

Val Ser Leu Ile Ser Tyr Thr Phe Ser Asn Asn Ile Leu Ser Gly Ser

35 40 45

Ile Ser Ile Gln Asn Ile Ala Tyr Ala Lys Thr Val Ser Val Thr Tyr

50 55 60

Ala Ile Gly Ser Ser Trp Ser Ser Ser Gln Val Ile Ser Ala Ala Tyr

65 70 75 80

Ser Thr Gly Pro Asp Ser Thr Gly Tyr Glu Val Trp Thr Phe Ser Gly

85 90 95

Thr Ala Thr Gly Ala Thr Gln Phe Tyr Ile Ala Tyr Thr Val Ser Gly

100 105 110

Thr Thr Tyr Tyr Asp Pro Gly Asn Gly Ile Asn Tyr Thr Ile Gly Thr

115 120 125

Gly Ser Ser Thr Thr Ser Ser Ser Thr Ser Ala Thr Ser Thr Thr Lys Ser

130 135 140

Ser Thr Thr Ser Ser Thr Ser Thr Ala Thr Ser Ser Thr Ser Val Ala Thr Ser

145 150 155 160

Ser Leu Pro Ala Ile Ile Ser Ser Ser Ser Ile Pro Ser Glu Ala Ala Ala

165 170 175

Thr Ala Leu Ser Gly Cys Asn Thr Trp Asp Gly Phe Asp Asn Cys Gln

180 185 190

Thr Ser Gly Val Tyr Asp Phe Val Ala Ser Ala Glu Asn Arg Arg Trp

195 200 205

Gln Thr Pro Pro Asp Gly Asp Pro Ala Tyr Val Asn Thr Phe Gln Asp

210 215 220

Tyr Arg Asp Leu Ile Gly Tyr Ala Asp Ile Gln Tyr Ser Pro Ser Arg

225 230 235 240

Thr Ser Ala Val Val Thr Val Asn Ala Ala Ser Arg Thr Gly Glu Thr

245 250 255

Leu Thr Tyr Lys Phe Gly Gly Ile Thr Gln Thr Ser Asn Ala Tyr Thr

260 265 270

Val Ser Ser Ser Phe Ile Gly Thr Leu Ala Ile Thr Val Thr Ser Ser

275 280 285

Ser Gly Lys Lys Leu Glu Leu Glu Ala Leu Asn Phe Val Trp Gln Asn

290 295 300

Ala Val Leu Thr Gly Ala Gln Ser Thr Phe Asn Asn Gly Gln Lys Gly

305 310 315 320

Ala Ile Val Glu Leu Phe Gly Trp Pro Tyr Ala Asp Ile Ala Lys Glu

325 330 335

Cys Ala Phe Leu Gly Lys Ala Gly Tyr Met Gly Val Lys Val Trp Pro

340 345 350

Pro Asn Glu His Ile Trp Gly Ser Asp Tyr Tyr Glu Thr Asp Asn Met

355 360 365

Phe Arg Pro Trp Tyr Leu Val Tyr Gln Pro Val Ser Tyr Lys Leu Val

370 375 380

Ser Arg Gln Gly Thr Arg Glu Glu Leu Arg Ala Met Ile Thr Ala Cys

385 390 395 400

Arg Ser Ala Gly Val Arg Val Tyr Ala Asp Ala Val Ile Asn His Met

405 410 415

Ser Gly Asn Gly Asn Asp Ile Gln Asn His Arg Asn Thr Ala Cys Ala

420 425 430

Tyr Trp Thr Gly His Asn Ala Thr Ala Asn Ser Pro Tyr Phe Thr Ser

435 440 445

Gly Tyr Thr Tyr Leu Ile Asn Pro Phe Thr Asn Thr Arg Pro Thr Phe

450 455 460

Glu Tyr Pro Ala Val Pro Trp Gly Pro Thr Asp Phe His Cys Val Ser

465 470 475 480

Ser Ile Thr Asp Trp Thr Asn Gly Gln Ile Val Thr Lys Gly Tyr Leu

485 490 495

Val Gly Leu Ser Asp Leu Asn Thr Glu Lys Asp Tyr Val Gln Asp Arg

500 505 510

Ile Ala Thr Tyr Leu Val Asp Leu Leu Ser Ile Gly Phe Ser Gly Phe

515 520 525

Arg Val Asp Ala Ala Lys His Ile Gly Pro Thr Ser Met Ala Gln Ile

530 535 540

Phe Gly Arg Val Ala Lys Lys Met Gly Gly Ser Leu Pro Asp Asp Phe

545 550 555 560

Ile Thr Trp Leu Glu Val Leu Met Gly Gly Glu Lys Glu Gln Tyr Ala

565 570 575

Cys Gly Gly Gly Glu Trp Ser Trp Tyr Thr Asn Phe Asn Thr Gln Leu

580 585 590

Ser Asn Ala Gly Ile Ser Asp Thr Asp Ile Asn Lys Ile Lys Ile Trp

595 600 605

Ser Ser Asp Tyr Pro Lys Glu Phe Pro Ile Cys Gly Ser Trp Ile Ile

610 615 620

Pro Ser Thr Arg Phe Val Ile Gln Asn Asp Asp His Asp Gln Gln Asn

625 630 635 640

Pro Gly Ser Ser Ser Arg Asp Met Gly Asp Gln Gly Ser Val Leu Ile

645 650 655

Lys Asp Gln Asp Val Ala Lys His Arg Ala Phe Glu Val Lys Leu Phe

660 665 670

Thr Arg Thr Asp Gly Asp Trp Gln Ile Arg Asn Ile Leu Ser Ser Tyr

675 680 685

Met Phe Ala Ser Asn Gly Ala Asn Gly Phe Pro Asp Gly Leu Ser Asp

690 695 700

Cys Ser Leu Tyr Thr Gly Ser Gln Ser Ala Ser Gly Cys Leu Gly Ile

705 710 715 720

Ala Lys Asp Thr Ala Tyr Val Glu Gly Ile Cys Gly Tyr Thr Met Val

725 730 735

Ala Gly Arg Tyr Thr Arg Pro His Arg Asp Leu Ser Ile Ile Asn Ala

740 745 750

Met Arg Ser Trp Val Gly Leu Ser Ser Thr Thr Ala Asp Ala Leu Gly

755 760 765

Ile Pro Gly Cys Ser

770

<210>176

<211>1761

<212>DNA

<213>Valsaria rubricosa

<220>

<221> CDS

<222>(1)..(1761)

<220>

<221>sig_peptide

<222>(1)..(63)

<220>

<221>misc_feature

<222>(64)..(1413)

<223> catalytic domain

<220>

<221>misc_feature

<222>(1414)..(1458)

<223> connector

<220>

<221>misc_feature

<222>(1459)..(1761)

<223>CBM

<400>176

atg cga tcc ttc ctc gcc ctc tca gcc ttg ctg ctg ctg tac ccg ctg 48

Met Arg Ser Phe Leu Ala Leu Ser Ala Leu Leu Leu Leu Tyr Pro Leu

1 5 10 15

cag ctg ctc gcc gcc agc aac tcc gac tgg agg tcc cgc aat atc tac 96

Gln Leu Leu Ala Ala Ser Asn Ser Asp Trp Arg Ser Arg Asn Ile Tyr

20 25 30

ttt gcc ttg acc gac cgc gtc gcc aat ccg tcc acc acg acc gca tgt 144

Phe Ala Leu Thr Asp Arg Val Ala Asn Pro Ser Thr Thr Thr Ala Cys

35 40 45

agt gac ctg agc aac tac tgc ggc ggc acg tgg agc ggc ctg tcg agc 192

Ser Asp Leu Ser Asn Tyr Cys Gly Gly Thr Trp Ser Gly Leu Ser Ser

50 55 60

aag ctg gac tac atc caa ggg atg ggc ttc gat tcc atc tgg att acc 240

Lys Leu Asp Tyr Ile Gln Gly Met Gly Phe Asp Ser Ile Trp Ile Thr

65 70 75 80

ccc gtg gtc gag aac tgc gac ggt ggc tac cac ggc tac tgg gcc aag 288

Pro Val Val Glu Asn Cys Asp Gly Gly Tyr His Gly Tyr Trp Ala Lys

85 90 95

gcg ctc tac aac gtc aac acg aac tac ggc agt gcg gat gat ctg aag 336

Ala Leu Tyr Asn Val Asn Thr Asn Tyr Gly Ser Ala Asp Asp Leu Lys

100 105 110

aac ttc gtt gcg gcc gcc cat gcg aag ggc atg tac gtg atg gtg gac 384

Asn Phe Val Ala Ala Ala His Ala Lys Gly Met Tyr Val Met Val Asp

115 120 125

gtc gtc gcg aat cac atg ggt tcc tgc ggc atc gcc aac ctc tcc cca 432

Val Val Ala Asn His Met Gly Ser Cys Gly Ile Ala Asn Leu Ser Pro

130 135 140

cct ccc ctg aac gag cag agc tct tat cac acc cag tgc gac att gac 480

Pro Pro Leu Asn Glu Gln Ser Ser Tyr His Thr Gln Cys Asp Ile Asp

145 150 155 160

tac agc agt cag tcc agc att gag acg tgc tgg ata tcc ggc ctc cct 528

Tyr Ser Ser Gln Ser Ser Ile Glu Thr Cys Trp Ile Ser Gly Leu Pro

165 170 175

gac ctg gac acc acc gat agc act atc cga tcc ctc ttc cag acc tgg 576

Asp Leu Asp Thr Thr Asp Ser Thr Ile Arg Ser Leu Phe Gln Thr Trp

180 185 190

gtc cac ggc ctg gtc agc aac tac agc ttc gac ggt ctc cgc gtc gac 624

Val His Gly Leu Val Ser Asn Tyr Ser Phe Asp Gly Leu Arg Val Asp

195 200 205

acc gtc aag cac gtg gag aag gat tac tgg ccc ggc ttc gtg tcg gcg 672

Thr Val Lys His Val Glu Lys Asp Tyr Trp Pro Gly Phe Val Ser Ala

210 215 220

gcg ggc acc tac gcc atc ggc gaa gtc ttc tcc ggc gac acc tcc tac 720

Ala Gly Thr Tyr Ala Ile Gly Glu Val Phe Ser Gly Asp Thr Ser Tyr

225 230 235 240

gtg gcc ggc tat caa tcg gtg atg ccg ggc ttg ctc aac tat ccc atc 768

Val Ala Gly Tyr Gln Ser Val Met Pro Gly Leu Leu Asn Tyr Pro Ile

245 250 255

tac tat ccg ctc atc cgc gtc ttc gcg cag ggt gcg tcc ttc acc gat 816

Tyr Tyr Pro Leu Ile Arg Val Phe Ala Gln Gly Ala Ser Phe Thr Asp

260 265 270

ctc gtc aac aac cac gat acc gtc ggc tcg acc ttc tcc gac ccg acg 864

Leu Val Asn Asn His Asp Thr Val Gly Ser Thr Phe Ser Asp Pro Thr

275 280 285

ctg ctg ggt aac ttt atc gac aac cac gac aac cca cgt ttc ctg agc 912

Leu Leu Gly Asn Phe Ile Asp Asn His Asp Asn Pro Arg Phe Leu Ser

290 295 300

tac acc agc gac cac gcc ctc ctc aag aac gct ctg gcc tac gtc atc 960

Tyr Thr Ser Asp His Ala Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile

305 310 315 320

ctg gcc aga ggc atc ccc atc gtc tac tac ggc acc gag caa ggc tac 1008

Leu Ala Arg Gly Ile Pro Ile Val Tyr Tyr Gly Thr Glu Gln Gly Tyr

325 330 335

tcg ggt tcg tcc gac ccg gcg aac cgc gag gat ctc tgg cgt agc gga 1056

Ser Gly Ser Ser Asp Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Gly

340 345 350

tac agc act acg gga gac atc tac acc acc atc gcc gcg ctc tcc gcc 1104

Tyr Ser Thr Thr Gly Asp Ile Tyr Thr Thr Ile Ala Ala Leu Ser Ala

355 360 365

gcg cgc acc gcg gcc ggt ggc ctc gcc ggt aac gac cac gtc cac ctg 1152

Ala Arg Thr Ala Ala Gly Gly Leu Ala Gly Asn Asp His Val His Leu

370 375 380

tac acg acc gac aac gcg tac gcc tgg tcc cgg gcg agc ggc aag ctc 1200

Tyr Thr Thr Asp Asn Ala Tyr Ala Trp Ser Arg Ala Ser Gly Lys Leu

385 390 395 400

atc gtc gtc acg tcc aac cgc ggc agc tec gac agc agc acc atc tgc 1248

Ile Val Val Thr Ser Asn Arg Gly Ser Ser Asp Ser Ser Thr Ile Cys

405 410 415

ttc agc acc cag cag gcc agc ggc acc acc tgg acc agc acg atc acc 1296

Phe Ser Thr Gln Gln Ala Ser Gly Thr Thr Trp Thr Ser Thr Ile Thr

420 425 430

ggc aac tcg tac acc gcc gac agc aac ggc cag atc tgc gtg cag ctg 1344

Gly Asn Ser Tyr Thr Ala Asp Ser Asn Gly Gln Ile Cys Val Gln Leu

435 440 445

tcc agc ggc gga ccc gag gcg ctc gtc gtc tcc acc gcg acc ggc acc 1392

Ser Ser Gly Gly Pro Glu Ala Leu Val Val Ser Thr Ala Thr Gly Thr

450 455 460

gcc acc gcg acg act ctg tcc acg acc acc aag ag acg tcc acc tcg acc 1440

Ala Thr Ala Thr Thr Leu Ser Thr Thr Thr Lys Thr Ser Thr Ser Thr

465 470 475 480

gcc tcc tgc gcc gcc acc gtc gcc gtc acc ttc aac gag ctc gtc acc 1488

Ala Ser Cys Ala Ala Thr Val Ala Val Thr Phe Asn Glu Leu Val Thr

485 490 495

acg aac tac ggc gac acc atc cgc ctg acg ggc tcc atc tcc cag ctc 1536

Thr Asn Tyr Gly Asp Thr Ile Arg Leu Thr Gly Ser Ile Ser Gln Leu

500 505 510

agc agc tgg agc gca acc tcc ggg ctg gcc ctg agc gcg tcc gcg tac 1584

Ser Ser Trp Ser Ala Thr Ser Gly Leu Ala Leu Ser Ala Ser Ala Tyr

515 520 525

acg tcc agc aac ccg ctc tgg agc gtg acg gtc agc ctg ccg gcc ggc 1632

Thr Ser Ser Asn Pro Leu Trp Ser Val Thr Val Ser Leu Pro Ala Gly

530 535 540

acg tcg ttc gag tac aag ttc gtc cgc atc acg agc gac ggc acc gtg 1680

Thr Ser Phe Glu Tyr Lys Phe Val Arg Ile Thr Ser Asp Gly Thr Val

545 550 555 560

acc tgg gaa tcg gac ccg aac cgc agc tac acc gtc ccg acg tgc gcg 1728

Thr Trp Glu Ser Asp Pro Asn Arg Ser Tyr Thr Val Pro Thr Cys Ala

565 570 575

agc acc gcg acg atc agc aat acc tgg cgg tga 1761

Ser Thr Ala Thr Ile Ser Asn Thr Trp Arg

580 585

<210>177

<211>586

<212>PRT

<213>Valsaria rubricosa

<400>177

Met Arg Ser Phe Leu Ala Leu Ser Ala Leu Leu Leu Leu Tyr Pro Leu

1 5 10 15

Gln Leu Leu Ala Ala Ser Asn Ser Asp Trp Arg Ser Arg Asn Ile Tyr

20 25 30

Phe Ala Leu Thr Asp Arg Val Ala Asn Pro Ser Thr Thr Thr Ala Cys

35 40 45

Ser Asp Leu Ser Asn Tyr Cys Gly Gly Thr Trp Ser Gly Leu Ser Ser

50 55 60

Lys Leu Asp Tyr Ile Gln Gly Met Gly Phe Asp Ser Ile Trp Ile Thr

65 70 75 80

Pro Val Val Glu Asn Cys Asp Gly Gly Tyr His Gly Tyr Trp Ala Lys

85 90 95

Ala Leu Tyr Asn Val Asn Thr Asn Tyr Gly Ser Ala Asp Asp Leu Lys

100 105 110

Asn Phe Val Ala Ala Ala His Ala Lys Gly Met Tyr Val Met Val Asp

115 120 125

Val Val Ala Asn His Met Gly Ser Cys Gly Ile Ala Asn Leu Ser Pro

130 135 140

Pro Pro Leu Asn Glu Gln Ser Ser Tyr His Thr Gln Cys Asp Ile Asp

145 150 155 160

Tyr Ser Ser Gln Ser Ser Ile Glu Thr Cys Trp Ile Ser Gly Leu Pro

165 170 175

Asp Leu Asp Thr Thr Asp Ser Thr Ile Arg Ser Leu Phe Gln Thr Trp

180 185 190

Val His Gly Leu Val Ser Asn Tyr Ser Phe Asp Gly Leu Arg Val Asp

195 200 205

Thr Val Lys His Val Glu Lys Asp Tyr Trp Pro Gly Phe Val Ser Ala

210 215 220

Ala Gly Thr Tyr Ala Ile Gly Glu Val Phe Ser Gly Asp Thr Ser Tyr

225 230 235 240

Val Ala Gly Tyr Gln Ser Val Met Pro Gly Leu Leu Asn Tyr Pro Ile

245 250 255

Tyr Tyr Pro Leu Ile Arg Val Phe Ala Gln Gly Ala Ser Phe Thr Asp

260 265 270

Leu Val Asn Asn His Asp Thr Val Gly Ser Thr Phe Ser Asp Pro Thr

275 280 285

Leu Leu Gly Asn Phe Ile Asp Asn His Asp Asn Pro Arg Phe Leu Ser

290 295 300

Tyr Thr Ser Asp His Ala Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile

305 310 315 320

Leu Ala Arg Gly Ile Pro Ile Val Tyr Tyr Gly Thr Glu Gln Gly Tyr

325 330 335

Ser Gly Ser Ser Asp Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Gly

340 345 350

Tyr Ser Thr Thr Gly Asp Ile Tyr Thr Thr Ile Ala Ala Leu Ser Ala

355 360 365

Ala Arg Thr Ala Ala Gly Gly Leu Ala Gly Asn Asp His Val His Leu

370 375 380

Tyr Thr Thr Asp Asn Ala Tyr Ala Trp Ser Arg Ala Ser Gly Lys Leu

385 390 395 400

Ile Val Val Thr Ser Asn Arg Gly Ser Ser Asp Ser Ser Thr Ile Cys

405 410 415

Phe Ser Thr Gln Gln Ala Ser Gly Thr Thr Trp Thr Ser Thr Ile Thr

420 425 430

Gly Asn Ser Tyr Thr Ala Asp Ser Asn Gly Gln Ile Cys Val Gln Leu

435 440 445

Ser Ser Gly Gly Pro Glu Ala Leu Val Val Ser Thr Ala Thr Gly Thr

450 455 460

Ala Thr Ala Thr Thr Leu Ser Thr Thr Thr Lys Thr Ser Thr Ser Thr

465 470 475 480

Ala Ser Cys Ala Ala Thr Val Ala Val Thr Phe Asn Glu Leu Val Thr

485 490 495

Thr Asn Tyr Gly Asp Thr Ile Arg Leu Thr Gly Ser Ile Ser Gln Leu

500 505 510

Ser Ser Trp Ser Ala Thr Ser Gly Leu Ala Leu Ser Ala Ser Ala Tyr

515 520 525

Thr Ser Ser Asn Pro Leu Trp Ser Val Thr Val Ser Leu Pro Ala Gly

530 535 540

Thr Ser Phe Glu Tyr Lys Phe Val Arg Ile Thr Ser Asp Gly Thr Val

545 550 555 560

Thr Trp Glu Ser Asp Pro Asn Arg Ser Tyr Thr Val Pro Thr Cys Ala

565 570 575

Ser Thr Ala Thr Ile Ser Asn Thr Trp Arg

580 585

<210>178

<211>1749

<212>DNA

<213>Valsaria spartii

<220>

<221> CDS

<222>(1)..(1749)

<220>

<221>sig_peptide

<222>(1)..(57)

<220>

<221>misc_feature

<222>(58)..(1410)

<223> catalytic domain

<220>

<221>misc_feature

<222>(1411)..(1443)

<223> connector

<220>

<221>misc_feature

<222>(1444)..(1749)

<223>CBM

<400>178

atg cag ttc ctt tgc gcc ctt gca gca ctc ctg tgc ttc cca tcg cag 48

Met Gln Phe Leu Cys Ala Leu Ala Ala Leu Leu Cys Phe Pro Ser Gln

1 5 10 15

ctt ctc gcc gcc agc aac gcg gat tgg aaa tcg cgc aac atc tac ttt 96

Leu Leu Ala Ala Ser Asn Ala Asp Trp Lys Ser Arg Asn Ile Tyr Phe

20 25 30

gcc ttg acg gac cgc gtc gct ggt cct acc ggg gga tca tgc ggc aac 144

Ala Leu Thr Asp Arg Val Ala Gly Pro Thr Gly Gly Ser Cys Gly Asn

35 40 45

ctg gga aac tac tgc ggc ggt acc tgg aac gga ttg acg gat aag ttg 192

Leu Gly Asn Tyr Cys Gly Gly Thr Trp Asn Gly Leu Thr Asp Lys Leu

50 55 60

gac tac atc cag ggc atg gga ttc gat gcc atc tgg atc acc ccg gtc 240

Asp Tyr Ile Gln Gly Met Gly Phe Asp Ala Ile Trp Ile Thr Pro Val

65 70 75 80

atc aag aac agc ccc ggc ggt tat cac gga tat tgg gct caa gat ctc 288

Ile Lys Asn Ser Pro Gly Gly Tyr His Gly Tyr Trp Ala Gln Asp Leu

85 90 95

tac agc gtg aac gag aac tat ggc act gcg caa gat ctg aag gat ttc 336

Tyr Ser Val Asn Glu Asn Tyr Gly Thr Ala Gln Asp Leu Lys Asp Phe

100 105 110

gta aat gcg gcg cac gca aag ggg atc tac gtc atg gtc gac gtg gtc 384

Val Asn Ala Ala His Ala Lys Gly Ile Tyr Val Met Val Asp Val Val

115 120 125

gca aac cac atg ggc aac ggt gga atc tca act ctc tcc cca cct ccc 432

Ala Asn His Met Gly Asn Gly Gly Ile Ser Thr Leu Ser Pro Pro Pro

130 135 140

ttg aac cag gag agt tcc tat cac tcc aaa tgc aac atc gac tac agc 480

Leu Asn Gln Glu Ser Ser Tyr His Ser Lys Cys Asn Ile Asp Tyr Ser

145 150 155 160

agc caa aac agc atc gag aat tgc tgg atc gct gac ctg ccc gac ctc 528

Ser Gln Asn Ser Ile Glu Asn Cys Trp Ile Ala Asp Leu Pro Asp Leu

165 170 175

gtc acc acc gac aac acc atc cgc gat gtc ttc aag gac tgg atc gcc 576

Val Thr Thr Asp Asn Thr Ile Arg Asp Val Phe Lys Asp Trp Ile Ala

180 185 190

aac ctc acc acc acc acc tac tcc ttc gac ggc ctc cgc gtc gac acc gtc 624

Asn Leu Thr Thr Thr Tyr Ser Phe Asp Gly Leu Arg Val Asp Thr Val

195 200 205

aag cat gta gag aag gac ttt tgg ccg ggc ttc gtc gag gct gcc ggc 672

Lys His Val Glu Lys Asp Phe Trp Pro Gly Phe Val Glu Ala Ala Gly

210 215 220

atg tat gcc atc ggc gag gtt ctc gat ggc ggc acc tcc tac gtt gcc 720

Met Tyr Ala Ile Gly Glu Val Leu Asp Gly Gly Thr Ser Tyr Val Ala

225 230 235 240

ggc tac cag agc gtg atg cca ggc ctt ctc aac tat ccc atg tac tat 768

Gly Tyr Gln Ser Val Met Pro Gly Leu Leu Asn Tyr Pro Met Tyr Tyr

245 250 255

cct ctc atc cgc acc ttt acc cag ggc gcc tcc ttc aac gac ttc gtc 816

Pro Leu Ile Arg Thr Phe Thr Gln Gly Ala Ser Phe Asn Asp Phe Val

260 265 270

aac agt cac aac gag gtt ggt tcc gga ttc tcc gat ccc acc ctc ctc 864

Asn Ser His Asn Glu Val Gly Ser Gly Phe Ser Asp Pro Thr Leu Leu

275 280 285

ggc acc ttc atc gac aac cac gac cag cag cgc ttc ctc tac aag aac 912

Gly Thr Phe Ile Asp Asn His Asp Gln Gln Arg Phe Leu Tyr Lys Asn

290 295 300

agc gac cac gcc ctc ttg aag aac gct ctg gcc tac gtg atc ctt ggc 960

Ser Asp His Ala Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile Leu Gly

305 310 315 320

cga ggt atc cca atc gtg tac tac ggc acc gag caa gcc tac ggc ggt 1008

Arg Gly Ile Pro Ile Val Tyr Tyr Gly Thr Glu Gln Ala Tyr Gly Gly

325 330 335

ggt gac gac ccg gcg aac cgc gag gac ctc tgg cga agc ggc tac tcc 1056

Gly Asp Asp Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Gly Tyr Ser

340 345 350

acc acc tcc gag ata tac acc acc atc tcg ggc cta tcc tcc gct cgc 1104

Thr Thr Ser Glu Ile Tyr Thr Thr Ile Ser Gly Leu Ser Ser Ala Arg

355 360 365

aaa tcc gcc ggc ggc ctc cca ggc aac gac cac tcc cac ctc tac acc 1152

Lys Ser Ala Gly Gly Leu Pro Gly Asn Asp His Ser His Leu Tyr Thr

370 375 380

acc aac aac gcg tac gcc tgg tcc cgc gcg gac ggg aag gtg atc gcg 1200

Thr Asn Asn Ala Tyr Ala Trp Ser Arg Ala Asp Gly Lys Val Ile Ala

385 390 395 400

ttg gtg acc aac gcc ggc ggc tcc gac acc agc acc cac tgc ttc aac 1248

Leu Val Thr Asn Ala Gly Gly Ser Asp Thr Ser Thr His Cys Phe Asn

405 410 415

acc aag aaa ccg agc ggc acg cgc tgg acc agc gtc ctc cgc agc ggc 1296

Thr Lys Lys Pro Ser Gly Thr Arg Trp Thr Ser Val Leu Arg Ser Gly

420 425 430

gga acc agc tac acc gcc gac ggc aac ggc caa atc tgc atc cag atc 1344

Gly Thr Ser Tyr Thr Ala Asp Gly Asn Gly Gln Ile Cys Ile Gln Ile

435 440 445

caa aac ggc ggg ccc gag gca atc gtc ctc tcc acc ggc acc ggc acc 1392

Gln Asn Gly Gly Pro Glu Ala Ile Val Leu Ser Thr Gly Thr Gly Thr

450 455 460

gaa acc aca tcc agc gcc acc acc tcc cca acc gcc ggc tgc ccc tcc 1440

Glu Thr Thr Ser Ser Ala Thr Thr Ser Pro Thr Ala Gly Cys Pro Ser

465 470 475 480

acc gtc tcc gtc aca ttc acc aac ctc gtc aca acc cag gtc ggc gac 1488

Thr Val Ser Val Thr Phe Thr Asn Leu Val Thr Thr Gln Val Gly Asp

485 490 495

acc atc aaa gtc acc ggc aac gtc tcg cag ctg ggc aac tgg aac cct 1536

Thr Ile Lys Val Thr Gly Asn Val Ser Gln Leu Gly Asn Trp Asn Pro

500 505 510

tcc tcc gcc ccc gcc tta tcc gca acc gga tac acg gcc agc aac ccc 1584

Ser Ser Ala Pro Ala Leu Ser Ala Thr Gly Tyr Thr Ala Ser Asn Pro

515 520 525

aaa tgg agc gga acc gtc aag ttg ccc gcc ggc tcg acg gtg cag tat 1632

Lys Trp Ser Gly Thr Val Lys Leu Pro Ala Gly Ser Thr Val Gln Tyr

530 535 540

aag ttt gtg aag gtc gct agc ggg ggt ggc gcc gtg act tgg gag agc 1680

Lys Phe Val Lys Val Ala Ser Gly Gly Gly Ala Val Thr Trp Glu Ser

545 550 555 560

gat ccc aac agg agt tat agc gtt cct agt tgt cag gct agc gcg act 1728

Asp Pro Asn Arg Ser Tyr Ser Val Pro Ser Cys Gln Ala Ser Ala Thr

565 570 575

gtt gat tcg agc tgg aag taa 1749

Val Asp Ser Ser Trp Lys

580

<210>179

<211>582

<212>PRT

<213>Valsaria spartii

<400>179

Met Gln Phe Leu Cys Ala Leu Ala Ala Leu Leu Cys Phe Pro Ser Gln

1 5 10 15

Leu Leu Ala Ala Ser Asn Ala Asp Trp Lys Ser Arg Asn Ile Tyr Phe

20 25 30

Ala Leu Thr Asp Arg Val Ala Gly Pro Thr Gly Gly Ser Cys Gly Asn

35 40 45

Leu Gly Asn Tyr Cys Gly Gly Thr Trp Asn Gly Leu Thr Asp Lys Leu

50 55 60

Asp Tyr Ile Gln Gly Met Gly Phe Asp Ala Ile Trp Ile Thr Pro Val

65 70 75 80

Ile Lys Asn Ser Pro Gly Gly Tyr His Gly Tyr Trp Ala Gln Asp Leu

85 90 95

Tyr Ser Val Asn Glu Asn Tyr Gly Thr Ala Gln Asp Leu Lys Asp Phe

100 105 110

Val Asn Ala Ala His Ala Lys Gly Ile Tyr Val Met Val Asp Val Val

115 120 125

Ala Asn His Met Gly Asn Gly Gly Ile Ser Thr Leu Ser Pro Pro Pro

130 135 140

Leu Asn Gln Glu Ser Ser Tyr His Ser Lys Cys Asn Ile Asp Tyr Ser

145 150 155 160

Ser Gln Asn Ser Ile Glu Asn Cys Trp Ile Ala Asp Leu Pro Asp Leu

165 170 175

Val Thr Thr Asp Asn Thr Ile Arg Asp Val Phe Lys Asp Trp Ile Ala

180 185 190

Asn Leu Thr Thr Thr Tyr Ser Phe Asp Gly Leu Arg Val Asp Thr Val

195 200 205

Lys His Val Glu Lys Asp Phe Trp Pro Gly Phe Val Glu Ala Ala Gly

210 215 220

Met Tyr Ala Ile Gly Glu Val Leu Asp Gly Gly Thr Ser Tyr Val Ala

225 230 235 240

Gly Tyr Gln Ser Val Met Pro Gly Leu Leu Asn Tyr Pro Met Tyr Tyr

245 250 255

Pro Leu Ile Arg Thr Phe Thr Gln Gly Ala Ser Phe Asn Asp Phe Val

260 265 270

Asn Ser His Asn Glu Val Gly Ser Gly Phe Ser Asp Pro Thr Leu Leu

275 280 285

Gly Thr Phe Ile Asp Asn His Asp Gln Gln Arg Phe Leu Tyr Lys Asn

290 295 300

Ser Asp His Ala Leu Leu Lys Asn Ala Leu Ala Tyr Val Ile Leu Gly

305 310 315 320

Arg Gly Ile Pro Ile Val Tyr Tyr Gly Thr Glu Gln Ala Tyr Gly Gly

325 330 335

Gly Asp Asp Pro Ala Asn Arg Glu Asp Leu Trp Arg Ser Gly Tyr Ser

340 345 350

Thr Thr Ser Glu Ile Tyr Thr Thr Ile Ser Gly Leu Ser Ser Ala Arg

355 360 365

Lys Ser Ala Gly Gly Leu Pro Gly Asn Asp His Ser His Leu Tyr Thr

370 375 380

Thr Asn Asn Ala Tyr Ala Trp Ser Arg Ala Asp Gly Lys Val Ile Ala

385 390 395 400

Leu Val Thr Asn Ala Gly Gly Ser Asp Thr Ser Thr His Cys Phe Asn

405 410 415

Thr Lys Lys Pro Ser Gly Thr Arg Trp Thr Ser Val Leu Arg Ser Gly

420 425 430

Gly Thr Ser Tyr Thr Ala Asp Gly Asn Gly Gln Ile Cys Ile Gln Ile

435 440 445

Gln Asn Gly Gly Pro Glu Ala Ile Val Leu Ser Thr Gly Thr Gly Thr

450 455 460

Glu Thr Thr Ser Ser Ala Thr Thr Ser Pro Thr Ala Gly Cys Pro Ser

465 470 475 480

Thr Val Ser Val Thr Phe Thr Asn Leu Val Thr Thr Gln Val Gly Asp

485 490 495

Thr Ile Lys Val Thr Gly Asn Val Ser Gln Leu Gly Asn Trp Asn Pro

500 505 510

Ser Ser Ala Pro Ala Leu Ser Ala Thr Gly Tyr Thr Ala Ser Asn Pro

515 520 525

Lys Trp Ser Gly Thr Val Lys Leu Pro Ala Gly Ser Thr Val Gln Tyr

530 535 540

Lys Phe Val Lys Val Ala Ser Gly Gly Gly Ala Val Thr Trp Glu Ser

545 550 555 560

Asp Pro Asn Arg Ser Tyr Ser Val Pro Ser Cys Gln Ala Ser Ala Thr

565 570 575

Val Asp Ser Ser Trp Lys

580

Claims (50)

1. A polypeptide comprising a first amino acid sequence comprising a catalytic module and a second amino acid sequence comprising a carbohydrate binding module, wherein the catalytic module has alpha-amylase activity, wherein the second amino acid sequence is selected from Any amino acid sequence of the following group has at least 60% homology: SEQ ID NO: 52, SEQ ID NO: 76, SEQ ID NO: 78, SEQ ID NO: 80, SEQ ID NO: 82, SEQ ID NO: 84 , SEQ ID NO: 86, SEQ ID NO: 88, SEQ ID NO: 90, SEQ ID NO: 92, SEQ ID NO: 94, SEQ ID NO: 96, SEQ ID NO: 98, SEQ ID NO: 109, SEQ ID NO: 137, SEQ ID NO: 139, SEQ ID NO: 141 and SEQ ID NO: 143. 2. The polypeptide of claim 1, wherein said first amino acid sequence has at least 60% homology to any amino acid sequence selected from the group consisting of: SEQ ID NO: 02, SEQ ID NO: 04, SEQ ID NO: 06 , SEQ ID NO: 08, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 20, SEQ ID NO: 22, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO: 36, SEQ ID NO: 38, SEQ ID NO: 40. SEQ ID NO: 42, SEQ ID NO: 44, SEQ ID NO: 111, SEQ ID NO: 113, SEQ ID NO: 115, SEQ ID NO: 117, SEQ ID NO: 119, SEQ ID NO: 121, SEQ ID NO: 123, SEQ ID NO: 125, SEQ ID NO: 127, SEQ ID NO: 129, SEQ ID NO: 131, SEQ ID NO: 133, SEQ ID NO: 135, and SEQ ID NO: 155. 3. The polypeptide of claim 1 or 2, wherein a linker sequence is present at a position between said first and said second amino acid sequence, said linker sequence having at least 60% identity with any amino acid sequence selected from the group consisting of Homology: SEQ ID NO: 46, SEQ ID NO: 48, SEQ ID NO: 50, SEQ ID NO: 54, SEQ ID NO: 56, SEQ ID NO: 58, SEQ ID NO: 60, SEQ ID NO: 62, SEQ ID NO: 64, SEQ ID NO: 66, SEQ ID NO: 68, SEQ ID NO: 70, SEQ ID NO: 72, SEQ ID NO: 74, SEQ ID NO: 145, SEQ ID NO: 147, SEQ ID NO: 149, SEQ ID NO: 151 and SEQ ID NO: 52. 4. The polypeptide according to any one of claims 1-3, wherein said first amino acid sequence has at least 60% homology to the amino acid sequence shown in SEQ ID NO: 4, and wherein said first amino acid sequence comprises an amino acid sequence selected from the group consisting of One or more amino acid substitutions of the group: A128P, K138V, S141N, Q143A, D144S, Y155W, E156D, D157N, N244E, M246L, G446D, D448S and N450D. 5. The polypeptide of claim 4, wherein said polypeptide has the amino acid sequence shown in SEQ ID NO: 100 or an amino acid sequence with at least 60% homology to the amino acid sequence shown in SEQ ID NO: 100. 6. The polypeptide of any one of claims 1-3, wherein said polypeptide has the amino acid sequence shown in SEQ ID NO: 101 or an amino acid sequence with at least 60% homology to the amino acid sequence shown in SEQ ID NO: 101. 7. The polypeptide of any one of claims 1-3, wherein said polypeptide has the amino acid sequence shown in SEQ ID NO: 102 or an amino acid sequence with at least 50% homology to the amino acid sequence shown in SEQ ID NO: 102. 8. The polypeptide of any one of claims 1-7, wherein said polypeptide is a hybrid. 9. A polypeptide having alpha-amylase activity selected from the group consisting of: (a) a polypeptide having an amino acid sequence with at least 75% homology to amino acids of a mature polypeptide selected from the group consisting of amino acids 1-441, SEQ ID NO: 14 Amino acids 1-471 in NO: 18, amino acids 1-450 in SEQ ID NO: 20, amino acids 1-445 in SEQ ID NO: 22, amino acids 1-498 in SEQ ID NO: 26, amino acids 1-498 in SEQ ID NO: 28 Amino acids 18-513 in, amino acids 1-507 in SEQ ID NO:30, amino acids 1-481 in SEQ ID NO:32, amino acids 1-495 in SEQ ID NO:34, amino acids 1-495 in SEQ ID NO:38 Amino acids 1-477, amino acids 1-449 in SEQ ID NO:42, amino acids 1-442 in SEQ ID NO:115, amino acids 1-441 in SEQ ID NO:117, amino acids 1 in SEQ ID NO:125 -477, amino acids 1-446 in SEQ ID NO:131, amino acids 41-481 in SEQ ID NO:157, amino acids 22-626 in SEQ ID NO:159, amino acids 24-630 in SEQ ID NO:161 , amino acids 27-602 in SEQ ID NO: 163, amino acids 21-643 in SEQ ID NO: 165, amino acids 29-566 in SEQ ID NO: 167, amino acids 22-613 in SEQ ID NO: 169, SEQ ID NO: Amino acids 21-463 in 171, amino acids 21-587 in SEQ ID NO: 173, amino acids 30-773 in SEQ ID NO: 175, amino acids 22-586 in SEQ ID NO: 177, amino acids in SEQ ID NO: 179 20-582. (b) a polypeptide encoded by a nucleotide sequence (i) at least under low stringency conditions that is compatible with nucleotides 1-1326 in SEQ ID NO: 13, the nucleus in SEQ ID NO: 17 Nucleotides 1-1413, nucleotides 1-1350 in SEQ ID NO: 19, nucleotides 1-1338 in SEQ ID NO: 21, nucleotides 1-1494 in SEQ ID NO: 25, SEQ ID NO : Nucleotides 52-1539 in 27, Nucleotides 1-1521 in SEQ ID NO: 29, Nucleotides 1-1443 in SEQ ID NO: 31, Nucleotides 1-1 in SEQ ID NO: 33 1485, nucleotides 1-143 of SEQ ID NO: 37 1, nucleotides 1-1347 of SEQ ID NO: 41, nucleotides 1-1326 of SEQ ID NO: 114, SEQ ID NO: 116 Nucleotides 1-1323 in, nucleotides 1-1431 in SEQ ID NO: 124, nucleotides 1-1338 in SEQ ID NO: 130, nucleotides 121-1443 in SEQ ID NO: 156 , nucleotides 64-1878 in SEQ ID NO: 158, nucleotides 70-1890 in SEQ ID NO: 160, nucleotides 79-1806 in SEQ ID NO: 162, nucleotides in SEQ ID NO: 164 Nucleotides 61-1929, nucleotides 85-1701 in SEQ ID NO:166, nucleotides 64-1842 in SEQ ID NO:168, nucleotides 61-1389 in SEQ ID NO:170, SEQ ID NO:170 Nucleotides 61-1764 in ID NO:172, Nucleotides 61-2322 in SEQ ID NO:174, Nucleotides 64-1761 in SEQ ID NO:176, Nucleosides in SEQ ID NO:178 Acid 58-1749, or (ii) at least under moderately stringent conditions with nucleotides 1-1326 contained in SEQ ID NO: 13, nucleotides 1-1413 in SEQ ID NO: 17, nucleotides 1-1413 in SEQ ID NO: 19 1-1350, nucleotides 1-1338 in SEQ ID NO: 21, nucleotides 1-1494 in SEQ ID NO: 25, nucleotides 52-1539 in SEQ ID NO: 27, nucleotides 1-1 in SEQ ID NO: 29 1521, SEQ ID NO: nucleotides 1-1443 in 31, nucleotides 1-1485 in SEQ ID NO: 33, nucleotides 1-1431 in SEQ ID NO: 37, nucleotides 1-1347 in SEQ ID NO: 41, SEQ ID NO: ID NO: nucleotides 1-1326 in 114, SEQ ID NO: nucleotides 1-1323 in 116, nucleotides 1-1431 in SEQ ID NO: 124, nucleotides 1-1338 in SEQ ID NO: 130, SEQ ID NO : Nucleotides 121-1443 in 156, nucleotides 64-1878 in SEQ ID NO: 158, nucleotides 70-1890 in SEQ ID NO: 160, nucleotides 79-1806 in SEQ ID NO: 162, SEQ ID NO: 164 Nucleotides 61-1929, nucleotides 85-1701 in SEQ ID NO: 166, nucleotides 64-1842 in SEQ ID NO: 168, nucleotides 61-1389 in SEQ ID NO: 170, nucleosides in SEQ ID NO: 172 cDNA sequence hybridization in polynucleotides shown in acid 61-1764, nucleotides 61-2322 in SEQ ID NO: 174, nucleotides 64-1761 in SEQ ID NO: 176, nucleotides 58-1749 in SEQ ID NO: 178 , or the complementary strand of (iii), (i) or (ii); and (c) a variant comprising conservative substitutions, deletions, and/or insertions of one or more amino acids in an amino acid sequence selected from the group consisting of: amino acids 1-441, SEQ ID NO in SEQ ID NO: 14 : amino acids 1-471 of 18, amino acids 1-450 of SEQ ID NO:20, amino acids 1-445 of SEQ ID NO:22, amino acids 1-498 of SEQ ID NO:26, SEQ ID NO:28 Amino acids 18-513 in, amino acids 1-507 in SEQ ID NO:30, amino acids 1-481 in SEQ ID NO:32, amino acids 1-495 in SEQ ID NO:34, amino acids 1-495 in SEQ ID NO:38 Amino acids 1-477, amino acids 1-449 in SEQ ID NO:42, amino acids 1-442 in SEQ ID NO:115, amino acids 1-441 in SEQ ID NO:117, amino acids 1-441 in SEQ ID NO:125 477. Amino acids 1-446 of SEQ ID NO:131, Amino acids 41-481 of SEQ ID NO:157, Amino acids 22-626 of SEQ ID NO:159, Amino acids 24-630 of SEQ ID NO:161, SEQ ID NO : amino acids 27-602 in 163, amino acids 21-643 in SEQ ID NO: 165, amino acids 29-566 in SEQ ID NO: 167, amino acids 22-613 in SEQ ID NO: 169, amino acids in SEQ ID NO: 171 Amino acids 21-463, amino acids 21-587 in SEQ ID NO: 173, amino acids 30-773 in SEQ ID NO: 175, amino acids 22-586 in SEQ ID NO: 177, and amino acids 20-582 in SEQ ID NO: 179 . 10. A polypeptide with carbohydrate binding affinity selected from the group consisting of: (a) a polypeptide comprising an amino acid sequence having at least 60% homology to a sequence selected from the group consisting of: amino acids 529-626 of SEQ ID NO: 159, amino acids 533-630 of SEQ ID NO: 161, SEQ ID NO: Amino acids 508-602 of 163, amino acids 540-643 of SEQ ID NO: 165, amino acids 502-566 of SEQ ID NO: 167, amino acids 513-613 of SEQ ID NO: 169, 492-587 of SEQ ID NO: 173, SEQ ID Amino acids 30-287 of NO: 175, amino acids 487-586 of SEQ ID NO: 177, and amino acids 482-582 of SEQ ID NO: 179; (b) a polypeptide encoded by a nucleotide sequence that hybridizes under low stringency conditions to a polynucleotide probe selected from the complementary strand of the following sequence: SEQ ID NO: Nucleotides 1585-1878 in 158, nucleotides 1597-1890 in SEQ ID NO: 160, nucleotides 1522-1806 in SEQ ID NO: 162, nucleotides 1618-1929 in SEQ ID NO: 164 , nucleotides 1504-1701 in SEQ ID NO: 166, nucleotides 1537-1842 in SEQ ID NO: 168, nucleotides 1474-1764 in SEQ ID NO: 172, nucleotides in SEQ ID NO: 174 Nucleotides 61-861, nucleotides 1459-1761 in SEQ ID NO: 176, and nucleotides 1444-1749 in SEQ ID NO: 178; (c) A fragment of (a) or (b) having carbohydrate binding affinity. 11. The polypeptide of claim 10, wherein said carbohydrate binding affinity is starch binding affinity. 12. Use of a polypeptide according to any one of claims 1-11 for liquefaction. 13. Use of a polypeptide according to any one of claims 1-11 for saccharification. 14. Use of a polypeptide according to any one of claims 1-11 in a method comprising fermentation. 15. Use of a polypeptide according to any one of claims 1-11 in a starch conversion process. 16. Use of a polypeptide according to any one of claims 1-11 in a method for the production of oligosaccharides. 17. Use of a polypeptide according to any one of claims 1-11 in a process for the production of maltodextrin or glucose syrup. 18. Use of a polypeptide according to any one of claims 1-11 in a method for producing fuel or drinking ethanol. 19. Use of a polypeptide according to any one of claims 1-11 in a method for producing a beverage. 20. Use of the polypeptide according to any one of claims 1-11 in a fermentation process for the production of organic compounds, such as citric acid, ascorbic acid, lysine, glutamic acid. 21. A composition comprising a polypeptide according to any one of claims 1-11. 22. A method of saccharifying starch, wherein the starch is treated with a polypeptide according to any one of claims 1-11. 23. A method according to claim 22, comprising converting the starch into a syrup containing dextrose and/or maltose. 24. A method according to claim 22 or 23, wherein the starch is gelatinized or granular starch. 25. A method according to any one of claims 22-24, wherein the saccharified starch is contacted with a fermenting organism to produce a fermentation product. 26. The method according to claim 24, wherein the fermenting organism is yeast and the fermentation product is ethanol. 27. A method comprising: (a) contacting starch with a polypeptide comprising a catalytic moiety and a carbohydrate binding moiety, the catalytic moiety having alpha-amylase activity; (b) incubating said starch together with said polypeptide; (c) fermentation to produce a fermentation product, (d) optionally recovering said fermentation product, Wherein the enzyme with glucoamylase activity is either absent, or present in an amount no more than or even less than 0.5 AGU/g DS, more preferably no more than or even less than 0.4 AGU/g DS starch substrate, even more preferably no more than or Even less than 0.3 AGU/g DS starch substrate, and most preferably no more than or even less than 0.1 AGU/g DS starch substrate, such as no more than or even less than 0.05 AGU/gDS starch substrate, and wherein steps a, b, c , and/or d can be performed individually or simultaneously. 28. The method according to claim 27, wherein said polypeptide is a polypeptide according to any one of claims 1 to 11. 29. A method comprising: (a) contacting the starch substrate with a yeast cell transformed to express a polypeptide comprising a catalytic module and a carbohydrate binding module, the catalytic module having alpha-amylase activity; (b) preserving said starch substrate with said yeast; (c) fermentation to produce ethanol; (d) optionally recovering ethanol; Wherein steps a, b, and c are performed separately or simultaneously. 30. The method of claim 29, wherein the yeast cell is the yeast cell of claim 43. 31. A method of producing ethanol from starch-containing material by fermentation, the method comprising: (i) liquefying said starch-containing material with a polypeptide comprising a catalytic moiety and a carbohydrate binding moiety, said catalytic moiety having alpha-amylase activity; (ii) liquefied mash obtained by saccharification; (iii) fermenting the material obtained in step (ii) in the presence of a fermenting organism. 32. The method of claim 31, wherein said polypeptide is a polypeptide according to any one of claims 1-11. 33. The method according to claim 31 or 32, further comprising recovering the ethanol. 34. Process according to any one of claims 31-33, wherein said saccharification and fermentation are carried out in a simultaneous saccharification and fermentation process (SSF process). 35. The method according to any one of claims 31-34, wherein during step iii the ethanol content reaches at least 7%, at least 8%, at least 9%, at least 10%, for example at least 11%, at least 12%, at least 13%, At least 14%, at least 15%, such as at least 16% ethanol. 36. The method according to any one of claims 31-35, wherein the acid alpha-amylase is present at a concentration of 0.01 to 10 AFAU/g DS, preferably 0.1 to 5 AFAU/g DS, especially 0.3 to 2 AFAU/g DS Quantity exists. 37. The method according to any one of claims 31-36, wherein the acid alpha-amylase and glucoamylase are in a ratio of 0.1 to 10 AFAU/AGU, preferably 0.30 to 5 AFAU/AGU, especially 0.5 to 3 AFAU/AGU Add to. 38. A DNA sequence encoding a polypeptide according to any one of claims 1-11. 39. A DNA construct comprising a DNA sequence according to claim 38. 40. A recombinant expression vector carrying a DNA construct according to claim 39. 41. A host cell transformed with a DNA construct according to claim 39 or a vector according to claim 40. 42. The host cell according to claim 41, which is a microorganism, in particular a bacterial or fungal cell. 43. The host cell according to claim 41 or 42, which is yeast. 44. The host cell according to claim 41 or 42, which is a strain from the genus Aspergillus, a strain from the genus Talaromyces, or a strain from the genus Trichoderma, said strain from the genus Aspergillus being in particular Aspergillus niger, said Strains from the genus Talarobacter, in particular T. emersonii. 45. The host cell according to claim 41 which is a plant cell. 46. A composition comprising a polypeptide according to any one of claims 1-11. 47. The composition according to claim 46, further comprising a glucoamylase. 48. The composition according to claim 46 or 47, wherein the glucoamylase is derived from a species of Talaromyces, Aspergillus, Trametes or Pachypora species of strains. 49. The composition according to any one of claims 46-48, wherein the glucoamylase is derived from a species selected from the group consisting of Aspergillus niger, Talaromyces leycettanus, Talaromyces duponti, Talaromyces leycettanus, Talaromyces spp. fungus and papery macrospores. 50. Use of a composition according to any one of claims 46-49 for the liquefaction and/or saccharification of gelatinized, partially gelatinized or granular starch.