CN101128580B - For the enzyme of starch processing - Google Patents

For the enzyme of starch processing Download PDF

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Publication number
CN101128580B
CN101128580B CN200580048598.0A CN200580048598A CN101128580B CN 101128580 B CN101128580 B CN 101128580B CN 200580048598 A CN200580048598 A CN 200580048598A CN 101128580 B CN101128580 B CN 101128580B
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ser
gly
ala
asp
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CN101128580A (en
Inventor
福山志朗
松井知子
宋子良
埃里克·阿兰
安德斯·维克索-尼尔森
宇田川裕晃
刘晔
段俊欣
吴文平
利尼·N·安德森
萨拉·兰德维克
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Novo Nordisk AS
Novozymes North America Inc
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Novo Nordisk AS
Novozymes North America Inc
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Priority to CN201610591291.5A priority Critical patent/CN106397601A/en
Priority claimed from PCT/US2005/046725 external-priority patent/WO2006069290A2/en
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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
    • C12N9/2411—Amylases
    • C12N9/2414—Alpha-amylase (3.2.1.1.)
    • C12N9/2417—Alpha-amylase (3.2.1.1.) from microbiological source
    • C12N9/242—Fungal source
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
    • C12N9/2411—Amylases
    • C12N9/2428—Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01001—Alpha-amylase (3.2.1.1)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01003—Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide

Abstract

The present invention relates to the polypeptide that comprises carbohydrate binding modules amino acid sequence and alpha amylase amino acid sequence, and the application of these polypeptide.

Description

For the enzyme of starch processing
Cross reference with sequence table and conserving microorganism
The information that the application comprises sequence table form, it is additional to the application, follows the application also to submit its number to simultaneouslyThe body of refusing to take a passenger. In addition, the application relates to the microorganism of preservation. Herein the microorganism of the content of data medium and preservation is added completelyAs a reference.
Field that the present invention belongs to
The present invention relates to the polypeptide that comprises carbohydrate binding modules (" CBM ") and AMS catalyst structure domain. Separately, the present invention relates to include the AMS catalyst structure domain of use and/or the wild type AMS polypeptide of CBM outward, also relate toCatalyst structure domain sequence and/or CBM sequence. The invention still further relates to these polypeptide by starch degradation be less oligosaccharides and/orPurposes in the starch liquefacation process of polysaccharide fragment.
Background of invention
Describe many starch is converted into starch hydrolysate, as the enzyme of maltose, glucose or extraordinary syrupAnd method, described starch hydrolysate or as sweetener or as the precursor of for example fructose of other carbohydrate. Also can be byGlucose fermentation is ethanol or other tunning, as citric acid, monosodium glutamate, gluconic acid, gluconic acid sodium salt, calcium gluconate,Potassium gluconate, gluconic acid Δ lactone (gluconodelta lactone) or sodium isoascorbate, itaconic acid, lactic acid, glucoseAcid; Ketone; Amino acid, glutamic acid (monosodium glutamate (sodium monoglutaminate)), penicillin, tetracycline; Enzyme; Support one's familyElement, as riboflavin, B12, beta carotene or hormone.
The HMW polymer that starch is made up of the chain of glucose unit. Its conventionally by approximately 80% amylopectin and20% amylose forms. Amylopectin is side chain polysaccharide, and wherein the linear chain of α-Isosorbide-5-Nitrae D-Glucose residue is by α-1,6 sugarGlycosidic bond is connected.
Amylose is linear polysaccharide, by the D-glucopyranose unit group linking together by α-Isosorbide-5-Nitrae glycosidic bondBecome. In the situation that starch is converted into soluble starch hydrolysate, described starch is depolymerizated. Conventional depolymerization method is by gelatinizationStep and two continuous treatment steps, i.e. liquefaction is processed and composition is processed in saccharification.
Pearl starch is made up of trickle particle, and it is at room temperature water insoluble. In the time of heating water-based starch slurry, described inParticle expands and finally breaks, and starch molecule is distributed in solution. In this " gelatinization " process, viscosity sharply increases. Due toIn typical industry method, solid level is 30-40%, thus must dilute or " liquefaction " starch processed to enable. Existing, this viscosity reduce mostly obtain by enzymatic degradation. During liquefaction step, long-chain starch is degraded to by AMSLittle branch and linear unit (maltodextrin). Typically, liquefaction process is implemented approximately 5 to 10 minutes at about 105-110 DEG C, itAfter approximately 95 DEG C implement about 1-2 hour. Then temperature is reduced to 60 DEG C, adds glucoamylase (also referred to as GA or AMG)Or beta amylase and optional debranching enzyme, as isoamylase or amylopectase, and carry out saccharifying approximately 24 to 72 hours.
Can obviously find out that by above-mentioned discussion traditional starch conversion process consumes energy very much because during different stepThere is different demands temperature aspect. Therefore wish to select and/or to be designed for the enzyme of described process, to can implement wholeIndividual process and without by starch gelatinization. United States Patent (USP) 4,591,560,4,727,026 and 4,009,074, EP patent 0171218And Danish Patent Application PA200300949 has such " raw starch " processing procedure. The present invention discloses be in particular suchThe polypeptide of Process Design, the amino acid sequence that it comprises CBM and the amino acid sequence of starch degrading enzyme. Heterozyme isThe theme of WO9814601, WO0077165 and PCT/US2004/020499.
Summary of the invention
Inventor has surprisingly been found that by adding carbohydrate binding modules (CBM) energy to specific AMSEnough change activity and specificity, thereby strengthen effect of different starch degradation processes, for example, comprise rawly, for example non-gelatinization is formed sedimentThe degraded of powder and/or gelatinized starch. Also can change activity and specificity by substituting a kind of CBM with another kind of CBM.
These are by having alpha-amylase activity and mainly having the carbohydrate binding modules for the affinity of starchThe more existing AMS of heterozygote of polypeptide composition have superiority, this has catalyst structure domain of desirable characteristics by selectionsRealize, desirable characteristics is pH spectrum, TEMPERATURE SPECTROSCOPY, non-oxidizability, calcium stability, substrate affinity or production spectra for example, this catalytic structureTerritory can be combined with carbohydrate binding modules, and described carbohydrate binding modules has more by force or weak binding affinity morePower, described affinity for example for the specificity affinity of amylose, for specificity affinity or the pin of amylopectinTo the affinity of the ad hoc structure in carbohydrate. Therefore the present invention relates to respect to the AMS and/or the phase that do not contain CBMThere is for the amylase of prior art the heterozygote of characteristic of change, as at low pH, for example, at the pH lower than 4, as at 3.5 o'clockThere is stability and/or the activity of enhancing, even lacking glucoamylase in the situation that or at low glucose starch at low pHWhen enzyme level, have for enhanced activity and/or the pearl starch degraded of pearl starch and strengthen, and/or there is the product of changeThing spectrum.
Due to the superior hydrolysing activity of these polypeptide, whole starch conversion processing can be carried out without gelatinized starch,It is the shallow lake of the pearl starch during the raw starch of described polypeptide hydrolysis is processed and the gelatinization wholly or in part in the processing of traditional starchPowder.
Therefore first aspect the invention provides and comprises first amino acid sequence that contains catalytic module and contain carbon waterThe polypeptide of second amino acid sequence of compound binding modules, described catalytic module has alpha-amylase activity, wherein saidSecond amino acid sequence has at least 60% homology with the arbitrary amino acid sequence that is selected from lower group: 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 IDNO：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, SEQID NO:141 and SEQ ID NO:143.
Second aspect the invention provides the polypeptide with alpha-amylase activity, and it is selected from lower group: (a) have and be selected from downThe amino acid of the mature polypeptide of group has the polypeptide of the amino acid sequence of at least 75% homology: the amino acid in SEQ ID NO:14In amino acid/11-471 in 1-441, SEQ ID NO:18, amino acid/11-450 in SEQ IDNO:20, SEQ ID NO:22Amino acid/11 8-513, SEQ ID in amino acid/11-498, SEQ ID NO:28 in amino acid/11-445, SEQ ID NO:26Amino acid/11-481 in amino acid/11-507, SEQ ID NO:32 in NO:30, amino acid/11-495 in SEQ ID NO:34,Amino acid/11-449 in amino acid/11-477, SEQ ID NO:42 in SEQ ID NO:38, the amino in SEQ ID NO:115Amino acid/11-441, amino acid/11-477 in SEQID NO:125, SEQ ID NO in acid 1-442, SEQ ID NO:117:Amino acid 22-in amino acid 41-481, SEQ ID NO:159 in amino acid/11-446, SEQ IDNO:157 in 131626, in amino acid 27-602, the SEQ IDNO:165 in the amino acid 24-630 in SEQ IDNO:161, SEQ ID NO:163Amino acid 21-643, SEQ ID NO:167 in amino acid 29-566, amino acid 22-613, the SEQ in SEQ IDNO:169Amino in amino acid 21-587, SEQ ID NO:175 in amino acid 21-463, SEQ IDNO:173 in ID NO:171Amino acid 22-586, the amino acid 20-582 in SEQ ID NO:179 in acid 30-773, SEQ IDNO:177, (b) by nucleosidesThe polypeptide of acid sequence coding, described nucleotide sequence (i) under at least low stringent condition with SEQ IDNO:13 in nucleotides 1-1326, in nucleotides 1-1350, the SEQ ID NO:21 in nucleotides 1-1413, the SEQ IDNO:19 in SEQ ID NO:17Nucleotides 1-1338, SEQ IDNO:25 in nucleotides 1-1494, nucleotides 52-1539, the SEQ in SEQ ID NO:27Nucleotides 1-1443, the nucleotides 1-in SEQ IDNO:33 in nucleotides 1-1521, SEQ ID NO:31 in IDNO:291485, in nucleotides 1-1347, the SEQ ID NO:114 in nucleotides 1-1431, the SEQ IDNO:41 in SEQ ID NO:37Nucleotides 1-1326, SEQ IDNO:116 in nucleotides 1-1323, nucleotides 1-1431, the SEQ in SEQ ID NO:124Nucleotides 121-1443 in nucleotides 1-1338, SEQ ID NO:156 in IDNO:130, the nucleosides in SEQ IDNO:158Nucleotides 70-1890, nucleotides 79-1806, the SEQ ID in SEQ IDNO:162 in acid 64-1878, SEQ ID NO:160Nucleotides in nucleotides 85-1701, SEQ ID NO:168 in nucleotides 61-1929, SEQ IDNO:166 in NO:164Nucleotides 61-1764, SEQ in nucleotides 61-1389, SEQ ID NO:172 in 64-1842, SEQ IDNO:170Nucleotides 64-1761 in nucleotides 61-2322, SEQ ID NO:176 in IDNO:174, the nucleosides in SEQ IDNO:178Acid 58-1749 hybridization, or (ii) nucleotides 1-1326, SEQ under at least medium stringent condition and in SEQID NO:13Nucleotides 1-1338 in nucleotides 1-1350, SEQ ID NO:21 in nucleotides 1-1413, SEQ ID NO:19 in ID NO:17,Nucleotides 1-in nucleotides 52-1539, SEQ ID NO:29 in nucleotides 1-1494, SEQ ID NO:27 in SEQ ID NO:251521, nucleosides in nucleotides 1-1485, SEQ IDNO:37 in nucleotides 1-1443, SEQ ID NO:33 in SEQ ID NO:31Nucleotides 1-1326, SEQ ID NO:116 in nucleotides 1-1347, SEQ ID NO:114 in acid 1-1431, SEQ ID NO:41Nucleotides 1-1338, SEQ ID in nucleotides 1-1431, SEQ ID NO:130 in middle nucleotides 1-1323, SEQ ID NO:124Nucleotides 70-in nucleotides 64-1878, SEQ ID NO:160 in nucleotides 121-1443, SEQ ID NO:158 in NO:1561890, nucleotides 61-1929, SEQ ID NO:166 in nucleotides 79-1806, SEQ ID NO:164 in SEQ ID NO:162Nucleotides 61-1389, SEQ in nucleotides 64-1842, SEQ ID NO:170 in middle nucleotides 85-1701, SEQ ID NO:168Nucleotides in nucleotides 61-2322, SEQ ID NO:176 in nucleotides 61-1764, SEQ ID NO:174 in ID NO:172The cDNA sequence hybridization comprising in polynucleotides shown in nucleotides 58-1749 in 64-1761, SEQ ID NO:178, or(iii), complementary strand (i) or (ii); (c) in the amino acid sequence that is selected from lower group, comprise one or more amino acid whose guarantorsThe variant that keeping property is replaced, lacked and/or insert: the ammonia in amino acid/11-441, SEQ ID NO:18 in SEQ ID NO:14Amino acid/11-450, amino acid/11-445 in SEQ ID NO:22, SEQ ID NO in base acid 1-471, SEQ ID NO:20:Amino acid/11 8-513 in amino acid/11-498, SEQ ID NO:28 in 26, amino acid/11-507 in SEQ ID NO:30,Amino acid/11-495 in amino acid/11-481, SEQ ID NO:34 in SEQ ID NO:32, the amino in SEQ ID NO:38Amino acid/11-449, amino acid/11-442 in SEQ IDNO:115, SEQ ID NO:117 in acid 1-477, SEQ ID NO:42In amino acid/11-441, amino acid/11-446, the SEQ in amino acid/11-477, SEQ ID NO:131 in SEQ IDNO:125Amino acid 22-626 in amino acid 41-481, SEQ ID NO:159 in ID NO:157, the amino in SEQ ID NO:161Amino acid 27-602, amino acid 21-643, the SEQ ID in SEQ ID NO:165 in acid 24-630, SEQ ID NO:163Amino acid 22-613 in amino acid 29-566, SEQ ID NO:169 in NO:167, the amino acid in SEQ ID NO:171Amino acid 30-773, SEQ ID NO in amino acid 21-587, SEQ ID NO:175 in 21-463, SEQ ID NO:173:Amino acid 20-582 in amino acid 22-586 in 177 and SEQ ID NO:179.
Second aspect the invention provides the polypeptide with carbohydrate binding affinity, is selected from lower group: (a) i) compriseThere is the polypeptide of the amino acid sequence of at least 60% homology with the sequence that is selected from lower group: the amino acid of SEQ ID NO:159The amino acid 533-630 of 529-626, SEQ ID NO:161, the amino acid 508-602 of SEQ ID NO:163, SEQ ID NO:The amino acid 513-613 of 165 amino acid 540-643, the amino acid 502-566 of SEQID NO:167, SEQ ID NO:169,The amino acid 487-of the 492-587 of SEQ IDNO:173, the amino acid 30-287 of SEQ ID NO:175, SEQ ID NO:177586 and the amino acid 482-582 of SEQ ID NO:179; (b) by the core of hybridizing with polynucleotide probes under low stringent conditionThe polypeptide that nucleotide sequence is coded, described polynucleotide probes is selected from lower group: the complementary strand that (i) is selected from the sequence of lower group: SEQIn nucleotides 1597-1890, SEQ ID NO:162 in nucleotides 1585-1878, SEQ ID NO:160 in ID NO:158Nucleotides 1522-1806, SEQ ID NO:164 in nucleotides 1618-1929, the nucleotides in SEQ ID NO:166Nucleotides 1474-1764 in nucleotides 1537-1842, SEQ ID NO:172 in 1504-1701, SEQ ID NO:168,Nucleotides 1459-1761 and SEQ ID NO in nucleotides 61-861, SEQ ID NO:176 in SEQ ID NO:174:Nucleotides 1444-1749 in 178, (c) (a) or the fragment with carbohydrate binding affinity (b).
The invention provides first in other side, polypeptide aspect second and/or the 3rd is for saccharification, for bagDraw together in the process of fermentation, for starch conversion process, for example produce maltodextrin or grape for the production of the process of oligosaccharidesIn the process of sugar and/or fructose syrup, for the production of fuel or drinking alcohol, for the production of beverage and/or for the production of organicCompound is as the purposes in the fermentation process of citric acid, ascorbic acid, lysine, glutamic acid.
Another aspect the invention provides comprise first, the composition of the polypeptide of second and/or the 3rd aspect.
The invention provides on the other hand the method for starch saccharification, wherein use first, second and/or the 3rd aspectPolypeptide is processed starch.
Another aspect the invention provides a kind of method, comprising: a) by starch with comprise the catalysis with alpha-amylase activityModule contacts with the polypeptide of carbohydrate binding modules, described polypeptide for example, first, second and/or the 3rd aspectPolypeptide; B) described starch is incubated together with described polypeptide; C) fermenting and producing tunning, d) optionally reclaims tunning,Wherein there is enzyme or the disappearance of glucoamylase activity, or exist with the amount that is less than 0.5AGU/g DS starch substrates, andWherein step a, b, c and/or d can separate or carry out simultaneously.
The invention provides on the other hand a kind of method, comprising: a) by starch substrates and the yeast with expression polypeptide through conversionCells contacting, described polypeptide comprises catalytic module and the carbohydrate binding modules with alpha-amylase activity, for example, firstThe polypeptide of individual and/or second aspect; B) described starch substrates is preserved together with described yeast; C) fermentative production of ethanol; D)The optional ethanol that reclaims, wherein step a), b) and c) is separated or is carried out simultaneously. Be included at least 90% in preferred embodimentsThe described starch substrates of w/w is enough to be converted into the time of fermentable sugars and at temperature, preserves described substrate together with described yeast.
Another aspect the invention provides the method by starch-containing manufacture of materials ethanol by fermentation, and described method comprises: (i)There is the catalytic module of alpha-amylase activity and the described starch-containing material of the polypeptide of carbohydrate binding modules liquefaction with comprising,For example, the polypeptide of first and/or second aspect; (ii) liquefied fermented glutinous rice (mash) that saccharification obtains; (iii) at fermenting organismThere is the material obtaining in bottom fermentation step (ii) and optionally comprise recovery ethanol.
Many-sided the invention provides coding according to first, the DNA order of polypeptide aspect second and/or the 3rdRow, the DNA construct that comprises described DNA sequence dna, carries the recombinant expression carrier of described DNA construct, uses described DNA constructOr the host cell that transforms of described carrier, described host cell, its be microorganism, particularly bacterium or fungal cell, yeast orPlant cell.
Detailed Description Of The Invention
The starch that (raw) that make a living do not boil understood in term " pearl starch ",, not yet carries out the starch of gelatinization that is. Form sedimentPowder forms in plant with small water-fast particle. These particles are kept at shallow lake with the temperature lower than initial gelatinization pointIn powder. In the time putting in cold water, particle can absorb a small amount of liquid. Swelling in the time of 50 DEG C to 70 DEG C is all reversible, canContrary property degree depends on specific starch. When temperature is higher, the irreversible swelling that is called gelatinization starts.
Term " initial gelatinization point " is interpreted as that starch starts the minimum temperature of gelatinization. The starch heating in water is at 50 DEG CAnd between 75 DEG C, start gelatinization, the accurate temperature of gelatinization depends on specific starch, and those of skill in the art can survey easilyFixed. Therefore, initial gelatinization point can be different according to the certain species of plant species, plant species and growth conditions.In the context of the present invention, the initial gelatinization point of given starch refers to the Lii.C. with Gorinstein S.and,, when the described method of Vol.44 (12) pp.461-466 (1992) is measured, birefringence in 5% starch granulesTemperature when forfeiture.
Term " soluble starch hydrolysate " is interpreted as the soluble product of the inventive method, can comprise monose, twoSugar and oligosaccharides, as glucose, maltose, maltodextrin, cyclodextrin and these any mixture. Preferably, graininess is formed sedimentThe drying solid of powder 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% is converted into soluble starch hydrolysate.
Term polypeptide " homology " is interpreted as two homogeneity degree between sequence, and it shows that first sequence is by secondIndividual sequence is derivative. Can be by the mode of computer program known in the art as the GAP (Wei Sikang providing in GCG program packageThe procedure manual of star (Wisconsin) program package, the 8th edition, in August, 1994, Genetics Computer Group, 575Science Drive, Madison, Wisconsin, USA 53711) suitably measure homology (Needleman, S.B.andWunsch, C.D., (1970), Journal of Molecular Biology, 48,443-453). Amino acid sequence is relatively adoptedSetting with following: breach builds point penalty 3.0, breach extends point penalty 0.1. The relevant amino acid sequence portion measuring for homologyDividing is mature polypeptide, containing signal peptide. Be used for measuring nucleotide probe and homologous dna or RNA sequence at low, or Gao YanThe suitable experiment condition of hybridizing under sigma compactness comprises treats that by comprising the filter of hybrid dna fragment or RNA is immersed in 5x SSC (chlorination in advanceSodium/natrium citricum, Sambrook et al.1989) middle 10min, filter is at 5x SSC, 5x Denhardt ' s solutionUltrasonic processing salmon sperm DNA (the Sambrook et of (Sambrook et al.1989), 0.5%SDS and 100 micrograms/ml sex changeAl.1989) prehybridization in solution, is comprising (Feinberg, the A.P.and that concentration is the random primer of 10ng/ml afterwards Vogelstein，B.(1983)Anal.Biochem.132:6-13)、32P-dCTP mark (specific activity > 1x109Cpm/ microgram) visitIn the same solution of pin, hybridize 12 hours in approximately 45 DEG C. Then described filter is (low tight in approximately 55 DEG C in 2x SSC, 0.5%SDSSigma compactness), more preferably in approximately 60 DEG C (medium stringencies), then be preferable over approximately 65 DEG C (medium/high stringencies), be more preferable over approximately 70DEG C (high stringency) even more preferably washed twice under approximately 75 DEG C (high stringencies).
Detect under these conditions and the molecule of described oligonucleotide probe hybridization with x-radiographic film.
Polypeptide
Polypeptide of the present invention can be heterozyme, or described polypeptide can be to have comprised to have alpha-amylase activityThe wild-type enzyme of catalytic module and carbohydrate binding modules. Polypeptide of the present invention can be also the change of this wild-type enzymeBody. Heterozygote can pass through first DNA sequence dna of first amino acid sequence of coding and second amino acid sequence of encodingThe fusion of second DNA sequence dna is produced, or CBM, joint and catalyst structure domain that heterozygote can be based on about suitableThe knowledge of amino acid sequence is produced as completely synthetic gene.
Herein term " heterozyme " or " hybrid polypeptide " comprises and contains at least one catalytic module for characterizing the present inventionFirst amino acid sequence and contain those of second amino acid sequence comprising at least one carbohydrate binding modulesPolypeptide, described catalytic module has alpha-amylase activity, and wherein first and second amino acid sequence are from different sources.Term " source " is interpreted as such as, but not limited to parent enzyme, for example amylase or glucoamylase, or comprise suitable catalysis mouldOther catalytic activity of piece and/or suitable CBM and/or suitable joint.
Enzyme classification numbering (EC numbering) according toThe recommendation of international bio chemistry and NK of molecular biology federation (Recommendations(1992)of the Nomenclature Committee of theInternational Union of Biochemistry and Molecular Biology，Academic Press Inc，1992)。
Polypeptide mentioned in this article comprises the polypeptide kind of the amino acid sequence that comprises AMS (EC3.2.1.1), described inThe amino acid sequence of AMS connects (, covalent bond) in the amino acid order that comprises carbohydrate binding modules (CBM)Row.
Containing the heterozyme of CBM, with and the detailed description of preparation and purifying be known in the art [referring to, for example, WO90/00609, WO 94/24158 and WO 95/16782, and Greenwood et al.Biotechnology and Bioengineering 44(1994) pp.1295-1305]. For example can be by DNA construct is transformed in host cell,And cultivate the host cell that transforms and prepare them to express fusion, described DNA construct be at least included in have orThere is no to be connected in joint situation the DNA sheet of the encoding carbohydrate binding modules of the DNA sequence dna of the interested polypeptide of codingSection. CBM in polypeptide of the present invention can be positioned at peptide C-end, N-end or inside. Described in an embodiment, polypeptide canTo comprise the CBM that exceedes, for example, two CBM; One is positioned at C-end, and another is positioned at N-end, or two CBMsOne in front and one in back be positioned at C-end, N-end or inside. But same consideration has the polypeptide that exceedes two CBM.
AMS of the present invention
The AMS of donor (parent's amylase) that the present invention relates to can be used as CBM, joint and/or catalytic module is manyPeptide. Polypeptide of the present invention can be that wild type AMS (EC3.2.1.1) or described polypeptide can be also this wild typesThe variant of enzyme. Polypeptide of the present invention can be the fragment of this kind of enzyme in addition, and for example, catalyst structure domain, has AMS and liveSeparated fragment when property but CBM are present in wild-type enzyme, or for example CBM, have carbohydrate binding modulesFragment. It can be also the heterozyme of the fragment that comprises this AMS, for example, comprise and come from AMS of the present inventionCatalyst structure domain, joint and/or CBM.
In addition, polypeptide of the present invention can be the fragment of this kind of enzyme, for example, still comprise functional catalyst structure domain andIf be present in the fragment of the CBM in described wild-type enzyme, or, for example, the fragment of wild-type enzyme, this wild-type enzyme does not compriseCBM, and wherein said fragment comprises functional catalyst structure domain.
AMS:The present invention relates to comprise carbohydrate binding modules (" CBM ") and there is alpha-amylase activityNew polypeptide. These polypeptide can come from any biology, those of preferred fungi or bacterium origin.
AMS of the present invention comprises the AMS that can be obtained by the species that are selected from lower dependent of dead military hero: Absidia(Absidia), the branch mould genus of top spore (Acremonium), cone Chaetomium (Coniochaeta), Coriolus Qu61 (Coriolus),Cryptosporiopsis, Dichotomocladium, thorn shell bistrichiasis Pseudomonas (Dinemasporium), look two spore Pseudomonas(Diplodia), Fusarium (Fusarium), Gliocladium (Gliocladium), Malbranchea, sub-grifola frondosus Pseudomonas(Meripilus), the red shell bacterium of clump (Necteria), Penicillium (Penicillium), Rhizomucor (Rhizomucor), tough leatherPseudomonas (Stereum), streptomyces (Streptomyces), Subulispora, Syncephalastrum (Syncephalastrum),Thamindium, Thermoascus, thermophilic trichosporon spp (Thermomyces), Trametes (Trametes), TrichophaeaAnd Valsaria. AMS can come from table 1 listed any genus and species or sequence.
Preferred described AMS comes from any species that are selected from lower group: Thermomyces lanuginosus (ThermomycesLanuginosus), particularly there is the polypeptide of amino acid/11-441 in SEQ ID NO:14; The bacterial classification that Malbranchea belongs to(Malbranchea sp.), particularly has the polypeptide of amino acid/11-471 in SEQ ID NO:18; Rhizomucor pusillus(Rhizomucor pusillus), particularly has the polypeptide of amino acid/11-450 in SEQ ID NO:20;Dichotomocladium hesseltinei, particularly has the polypeptide of amino acid/11-445 in SEQ ID NO:22; Tough leatherThe bacterial classification (Stereumsp.) of bacterium, particularly has the polypeptide of amino acid/11-498 in SEQ ID NO:26; The bacterial classification of Trametes(Trametes sp.), particularly has the polypeptide of the amino acid/11 8-513 in SEQ ID NO:28; Salmon shellfish leather covers bacterium(Coriolus consors), particularly has the polypeptide of amino acid/11-507 in SEQ ID NO:30; Thorn shell bistrichiasis PseudomonasBacterial classification (Dinemasporium sp.), particularly has the polypeptide of amino acid/11-481 in SEQ ID NO:32;The bacterial classification of Cryptosporiopsis, particularly has the polypeptide of amino acid/11-495 in SEQ IDNO:34; Look two spore PseudomonasBacterial classification (Diplidia sp.), particularly there is the polypeptide of amino acid/11-477 in SEQ ID NO:38; The bacterium of GliocladiumPlant (Gliocladium sp.), particularly there is the polypeptide of amino acid/11-449 in SEQ ID NO:42; The red shell Pseudomonas of clumpBacterial classification (Nectria sp.), particularly has the polypeptide of amino acid/11-442 in SEQ ID NO:115; The bacterial classification of Fusarium(Fusarium sp.), particularly has the polypeptide of amino acid/11-441 in SEQ ID NO:117; Thermophilic ascomycete(Thermoascus auranticus), particularly has the polypeptide of amino acid/11-477 in SEQ ID NO:125;Thamindium elegans, particularly has the polypeptide of amino acid/11-446 in SEQ ID NO:131; Pappus colter is mould(Absidiacristata), particularly there is the polypeptide of the amino acid 41-481 in SEQ ID NO:157; The mould genus of branch top sporeBacterial classification (Acremonium sp.), particularly has the polypeptide of the amino acid 22-626 in SEQ ID NO:159; Cone ChaetomiumBacterial classification (Coniochaeta sp.), particularly there is the polypeptide of the amino acid 24-630 in SEQ IDNO:161; Huge bracket fungus(Meripilus giganteus), particularly has the polypeptide of the amino acid 27-602 in SEQ ID NO:163; PenicilliumBacterial classification (Penicilliumsp.), particularly has the polypeptide of the amino acid 21-643 in SEQ ID NO:165; Mud streptomycete(Streptomyces limosus), particularly has the polypeptide of the amino acid 29-566 in SEQ ID NO:167;Subulispora procurvata, particularly has the polypeptide of the amino acid 22-613 in SEQ ID NO:169; Total shape head altogetherMould (Syncephalastrum racemosum), particularly has the polypeptide of the amino acid 21-463 in SEQ IDNO:171; WrinklePleat bolt bacterium (Trametes currugata), particularly has the polypeptide of the amino acid 21-587 in SEQ ID NO:173;Trichophaea saccata, particularly has the polypeptide of the amino acid 30-773 in SEQ ID NO:175; ValsariaRubricosa, particularly has polypeptide and the Valsaria spartii of the amino acid 22-586 in SEQ ID NO:177,Particularly there is the polypeptide of the amino acid 20-582 in SEQ ID NO:179.
Also preferably with aforementioned polypeptide in any mature peptide have at least 60%, at least 65%, at least 70%, at least75%, the AMS amino of at least 80%, at least 85%, at least 90%, at least 95% or even at least 98% homologyAcid sequence. In another preferred embodiment, described AMS amino acid sequence has and is being no more than 10 sites, is being no more than9 sites, be no more than 8 sites, be no more than 7 sites, be no more than 6 sites, be no more than 5 sites, be no more than 4 positionsPoint, be no more than 3 sites, be no more than 2 sites or even do not exceed 1 site and be different from aforementioned amino acid sequenceThe amino acid sequence of any.
Also preferably by the AMS amino acid sequence of DNA sequence encoding, described DNA sequence dna be selected from the multinuclear glycosides of lower groupArbitrary sequence of acid has at least 50%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least85%, at least 90%, at least 95% or even at least 98% homology, described polynucleotide sequence is expressed 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 IDNO： 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 IDNO：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、 SEQID NO：114、SEQ ID NO：116、SEQ ID NO：118、SEQ ID NO：120、SEQ IDNO：122、SEQ ID NO：124、SEQ ID NO：126、SEQ ID NO：128、SEQ IDNO：130、SEQ ID NO：132、SEQ ID NO：134、SEQ ID NO:154 and SEQ IDNO: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、SEQID NO：116、SEQ ID NO：124、SEQ ID NO：130、SEQ ID NO：156、SEQ IDNO：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 andSEQ ID NO:178. More preferably by under low, medium, medium/high, high and/or high stringency with aforementioned AMSThe coded any AMS amino acid sequence of DNA sequence dna of any hybridization in DNA sequence dna. Also optimized encoding alphalise starchEnzyme amino acid sequence and with aforementioned AMS DNA sequence dna in any 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%, at least 99% or even 100%The DNA sequence dna of homology.
AMS catalyst structure domain:In an embodiment, the present invention relates to come from and comprise carbohydrate binding modules(" CBM ") and have the catalyst structure domain of the polypeptide of alpha-amylase activity, is selected from SEQ ID NO:14, SEQ ID NO as come from: 18、SEQ ID NO：20、SEQ ID NO：22、SEQID NO：26、SEQ ID NO：28、SEQ ID NO：30、SEQ ID NO： 32、SEQ IDNO：34、SEQ ID NO：38、SEQ ID NO：42、SEQ ID NO：115、SEQ IDNO：117、SEQ ID NO：125、SEQ ID NO：131、SEQ ID NO：157、SEQID NO：159、SEQ ID NO：161、SEQ ID NO：163、 SEQ ID NO：165、SEQID NO：167、SEQ ID NO：169、SEQ ID NO：171、SEQ ID NO：173、SEQIDThe catalyst structure domain of the polypeptide of the AMS shown in NO:175, SEQ ID NO:177 and SEQ ID NO:179. SEQ IDAmino acid/11-471 in amino acid/11-441, SEQ ID NO:18 in NO:14, amino acid/11-450 in SEQ ID NO:20,Amino acid/11-498 in amino acid/11-445, SEQ ID NO:26 in SEQ ID NO:22, the amino in SEQ ID NO:28Amino acid/11-507 in acid 18-513, SEQ ID NO:30, amino acid/11-481, the SEQ IDNO:34 in SEQ ID NO:32In amino acid/11-495, amino acid/11-449, the SEQ in amino acid/11-477, SEQ ID NO:42 in SEQ ID NO:38Amino acid/11-441 in amino acid/11-442, SEQ ID NO:117 in ID NO:115, the amino acid in SEQ ID NO:125Amino acid 41-481, SEQ ID NO in amino acid/11-446, SEQ ID NO:157 in 1-477, SEQ ID NO:131:Amino acid 24-499 in amino acid 22-502, SEQ ID NO:161 in 159, the amino acid 27-in SEQ ID NO:163492, amino acid 29-501, the SEQ ID NO:169 in the amino acid 21-496 in SEQ ID NO:165, SEQ ID NO:167In amino acid 22-487, amino acid 21-477 in amino acid 21-463, SEQ ID NO:173 in SEQ ID NO:171,In amino acid 22-471 and SEQ ID NO:179 in amino acid 288-773, SEQ ID NO:177 in SEQ ID NO:175Amino acid 20-470 shown in catalyst structure domain be preferred. Have at least with any in aforementioned catalyst structure domain sequence60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% is sameThe catalyst structure domain sequence of source property is also preferred. In another preferred embodiment, described catalyst structure domain sequence hasBe no more than 10 sites, be no more than 9 sites, be no more than 8 sites, be no more than 7 sites, be no more than 6 sites, be no more than5 sites, be no more than 4 sites, be no more than 3 sites, be no more than 2 sites or even do not exceed 1 site and aforementionedAny different amino acid sequence in catalyst structure domain sequence.
Also preferably by having at least 50%, at least 60%, at least 65% with any sequence of polynucleotides that is selected from lower group,The DNA sequence dna institute of at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% homologyThe catalytic structure domain amino acid sequence of coding, described polynucleotides are as the nucleotides 1-1326 in SEQ ID NO:13, SEQ IDNucleotides 1-1350 in nucleotides 1-1413, SEQ ID NO:19 in NO:17, the nucleotides 1-in SEQ ID NO:211338, nucleotides 52-1539, the SEQ ID NO:29 in the nucleotides 1-1494 in SEQ ID NO:25, SEQ ID NO:27In nucleotides 1-1521, nucleotides 1-1485 in nucleotides 1-1443, SEQ ID NO:33 in SEQ ID NO:31,Nucleotides 1-1347 in nucleotides 1-1431, SEQ ID NO:41 in SEQ ID NO:37, the core in SEQ ID NO:114Nucleotides 1-1431, SEQ ID in nucleotides 1-1323, SEQ ID NO:124 in thuja acid 1-1326, SEQ ID NO:116Nucleotides 121-1443 in nucleotides 1-1338, SEQ ID NO:156 in NO:130, the nucleosides in SEQ ID NO:158Nucleotides 70-1497, nucleotides 79-1476, the SEQ in SEQ ID NO:162 in acid 64-1506, SEQ ID NO:160Nucleotides 85-1503 in nucleotides 61-1488, SEQ ID NO:166 in ID NO:164, the core in SEQ ID NO:168Nucleotides 61-1431, SEQ in nucleotides 61-1389, SEQ ID NO:172 in thuja acid 64-1461, SEQ ID NO:170In nucleotides 64-1413 in nucleotides 862-2322, SEQ ID NO:176 in ID NO:174 and SEQ ID NO:178Shown in nucleotides 58-1410. More preferably by under low, medium, medium/high, high and/or high stringency with aforementioned DNAThe coded any catalytic structure domain amino acid sequence of DNA sequence dna of any hybridization in sequence. Also optimized encoding catalysis knotStructure domain amino acid sequence and with aforementioned catalyst structure domain DNA sequence dna in any have at least 50%, at least 60%, at least65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 99% or evenThe DNA sequence dna of 100% homology.
Joint sequence:The present invention relates in one embodiment come from and comprise carbohydrate binding modules (" CBM ")And there is the joint sequence of the polypeptide of alpha-amylase activity. Be preferably selected from the joint amino acid sequence of lower group: as SEQ ID NO:Amino acid 500-532 in amino acid 503-528, SEQ ID NO:161 in 159, the amino acid in SEQ ID NO:163Amino acid 488-512, SEQ ID in amino acid 497-539, SEQ ID NO:169 in 493-507, SEQ ID NO:165Amino acid 472-486 in amino acid 478-491, SEQ ID NO:177 in NO:173 and the amino in SEQ ID NO:179Joint amino acid sequence shown in acid 471-481. Also preferably with aforementioned joint sequence in any have at least 60%, at least65%, the joint of at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% homologyAmino acid sequence. In another preferred embodiment, described joint sequence has and is being no more than 10 sites, is being no more than 9 positionsPoint, be no more than 8 sites, be no more than 7 sites, be no more than 6 sites, be no more than 5 sites, be no more than 4 sites, superCross 3 sites, be no more than 2 sites or even do not exceed in 1 site and aforementioned joint sequence that any is differentAmino acid sequence.
Carbohydrate binding modules: the present invention relates in one embodiment come from and comprise carbohydrate in conjunction with mouldPiece (" CBM ") and there is the CBM of the polypeptide of alpha-amylase activity, described CBM comes from and is 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 IDNO：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、SEQID NO：161、SEQ ID NO： 163、SEQ ID NO：165、SEQ ID NO：167、SEQ IDNO：169、SEQ ID NO：171、SEQ ID NO：173、SEQThe polypeptide of the AMS shown in ID NO:175, SEQ IDNO:177 and SEQ ID NO:179. Be preferably selected from lower group of sequenceCBM amino acid sequence: there is the amino acid 533-in amino acid 529-626, the SEQ ID NO:161 in SEQ ID NO:159630, amino acid 540-643, the SEQ ID NO in the amino acid 508-602 in SEQ ID NO:163, SEQ ID NO:165:Amino acid 513-613 in amino acid 502-566, SEQ ID NO:169 in 167, the amino acid in SEQ ID NO:173Amino acid 487-586 and SEQ ID in amino acid 30-287, SEQ ID NO:177 in 492-587, SEQ ID NO:175The sequence of amino acid 482-582 in NO:179. Also any preferably and in aforementioned CBM amino acid sequence has at least60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% is sameThe CBM amino acid sequence of source property. In another preferred embodiment, described CBM sequence has and is being no more than 10 sites, superCross 9 sites, be no more than 8 sites, be no more than 7 sites, be no more than 6 sites, be no more than 5 sites, be no more than 4 positionsPoint, be no more than 3 sites, be no more than 2 sites or even do not exceed 1 site and be different from arbitrary in aforementioned CBM sequenceIndividual amino acid sequence.
Also preferably by having at least 50%, at least 60%, at least 65% with any sequence of polynucleotides that is selected from lower group,The DNA sequence dna institute of at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% homologyThe CBM amino acid sequence of coding, described polynucleotides are as the nucleotides 1585-1878 in SEQ ID NO:158, SEQ ID NO:Nucleotides 1522-1806 in nucleotides 1597-1890, SEQ ID NO:162 in 160, the nucleosides in SEQ ID NO:164Nucleotides 1504-1701, the nucleotides 1537-in SEQ ID NO:168 in acid 1618-1929, SEQ ID NO:1661842, nucleotides 61-861, the SEQ ID in the nucleotides 1474-1764 in SEQ ID NO:172, SEQ ID NO:174Nucleotides 1444-1749 in nucleotides 1459-1761 in NO:176 and SEQ ID NO:178, SEQ ID NO:1, SEQ ID NO：3、SEQ ID NO：5、SEQ IDNO：7、SEQ ID NO：9、SEQ ID NO：11、SEQ ID NO：13、SEQ ID NO：15、SEQID 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、SEQID 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, SEQID NO:154 and SEQShown in ID NO:156. More preferably by under low, medium, medium/high, high and/or high stringency with aforementioned CBM DNAThe coded any CBM amino acid sequence of DNA sequence dna of the complementary dna sequence hybridization of any in sequence. Also optimized encodingCBM amino acid sequence and with aforementioned CBM DNA sequence dna in any has at least 50%, at least 60%, at least 65%, at least70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 99% or even 100% homologyThe DNA sequence dna of property.
Shown in nucleotides 61-861 in nucleotides 1504-1701 in SEQ ID NO:166 and SEQ ID NO:174DNA sequence dna and coded amino acid sequence also comprise joint sequence except CBM.
Table 1
AMS polypeptide can be applied in starch degradation process and/or as the catalyst structure domain of hybrid polypeptide and/Or the donor of CBM. The preferred polypeptide of the present invention, for example, hybrid polypeptide, comprises first amino acid sequence that contains catalytic moduleWith second amino acid sequence that contains carbohydrate binding modules, described catalytic module has alpha-amylase activity, whereinDescribed second amino acid sequence and any amino acid sequence that is selected from lower group have at least 60%, at least 70%, at least 80%,At least 85%, at least 90%, as at least 95% homology: amino acid 529-626, SEQ IDNO in SEQ ID NO:159:Amino acid 508-602 in amino acid 533-630, SEQ ID NO:163 in 161, the amino acid in SEQ IDNO:165Amino acid 502-566 in 540-643, SEQ ID NO:167, amino acid 513-613, the SEQ ID in SEQ IDNO:169Amino acid in amino acid 30-287, SEQ ID NO:177 in amino acid 492-587, SEQ IDNO:175 in NO:173Amino acid 482-582 in 487-586 and SEQ IDNO:179. More preferably polypeptide, for example, hybrid polypeptide, wherein said firstIndividual amino acid sequence and any amino acid sequence that is selected from lower group have at least 60%, at least 70%, at least 80%, at least85%, at least 90%, as at least 95% homology: the ammonia in amino acid/11-441, SEQ ID NO:18 in SEQ ID NO:14Amino acid/11-450, amino acid/11-445 in SEQ ID NO:22, SEQ ID NO in base acid 1-471, SEQ ID NO:20:Amino acid/11-507, SEQ in amino acid/11 8-513, SEQ ID NO:30 in amino acid/11-498, SEQ IDNO:28 in 26Amino acid/11-495 in amino acid/11-481, SEQ ID NO:34 in ID NO:32, the amino acid/11 in SEQ ID NO:38-477, in amino acid/11-442 in amino acid/11-449 in SEQ ID NO:42, SEQ ID NO:115, SEQ ID NO:117Amino acid/11-441, SEQ ID NO:125 in amino acid/11-477, amino acid/11-446, the SEQ in SEQ ID NO:131Amino acid 22-502 in amino acid 41-481, SEQ ID NO:159 in ID NO:157, the amino in SEQ ID NO:161Amino acid 27-492, amino acid 21-496, the SEQ ID in SEQ ID NO:165 in acid 24-499, SEQ ID NO:163Amino acid 22-487 in amino acid 29-501, SEQ ID NO:169 in NO:167, the amino acid in SEQ ID NO:17121-463, SEQ ID NO; Amino acid 288-773, SEQ ID in amino acid 21-477, SEQ ID NO:175 in 173Amino acid 20-470 in amino acid 22-471 in NO:177 and SEQ ID NO:179. Also preferred polypeptide, for example, heterozygosis is manyPeptide, wherein joint sequence is present in the position between described first and described second amino acid sequence, described joint sequenceHave at least 60%, at least 70%, at least 80%, at least 85%, at least 90% with any amino acid sequence that is selected from lower group, asAt least 95% homology: amino acid 500-532 in amino acid 503-528, SEQ ID NO:161 in SEQ ID NO:159,In amino acid 497-539, SEQ ID NO:169 in amino acid 493-507, SEQ ID NO:165 in SEQ ID NO:163Amino acid 488-512, SEQ ID NO:173 in amino acid 478-491, the amino acid 472-486 in SEQ ID NO:177With the amino acid 471-481 in SEQ ID NO:179.
AMS sequence
Be suitable for the catalyst structure domain of the polypeptide that builds type of the present invention, that is, and (the particularly acid of AMS catalyst structure domainStable AMS) can come from any biology, those of preferred fungi or bacterium origin.
Preferred described AMS is wild-type enzyme. More preferably described AMS be comprise amino acid modified variant α-Amylase, described amino acid modified cause strengthen activity, low pH and/or high pH under strengthen protein stability, for calciumThe stability strengthening when the stability of the enhancing of loss and/or temperature increase.
Comprise the α-shallow lake that can obtain from being selected from the following species of listing for the relevant AMS of heterozygote of the present inventionPowder enzyme: colter is mould, branch top spore is mould, aspergillus (Aspergillus), cone cupreum, cone cupreum, Cryptosporiopsis,The bacterial classification of Dichotomocladium, thorn shell bistrichiasis Pseudomonas, look two spore bacterium, sickle-like bacteria, sticky broom are mould, Malbranchea, sub-ash treeFlower bacterium (Meripilus), bolt bacterium, the red shell bacterium of clump, the red shell bacterium of clump, Penicillium notatum, Phanerochaete, root Mucor, head mold(Rhizopus), streptomycete, Subulispora, altogether mould, Thaminidium, Thermoascus, thermophilic hyphomycete, bolt bacterium,Trichophaea and Valsaria. AMS catalyst structure domain also can derive from bacterium, for example, and bacillus (Bacillus)。
Preferred selected AMS amino acid sequence derives from any species that are selected from lower group: pappus colter is mould, branchThe bacterial classification of the mould genus of top spore, aspergillus niger (Aspergillus niger), aspergillus albicans (Aspergilluskawachii), aspergillus oryzaeThe bacterium of the bacterial classification of (Aspergillus oryzae), cone Chaetomium, the bacterial classification of cone Chaetomium, Cryptosporiopsis genusKind, Dichotomocladium hesseltinei, the bacterial classification of thorn shell bistrichiasis Pseudomonas, bacterial classification, the Fusarium of look two spore PseudomonasThe bacterial classification, the bacterial classification that Malbranchea belongs to, huge bracket fungus, the bacterial classification of the red shell Pseudomonas of clump, the red shell bacterium of clump of bacterial classification, GliocladiumThe bacterial classification of bacterial classification, the Penicillium belonging to, Phanerochaete chrysosporium (Phanerochaete chrysosporium), Rhizomucor pusillus,Rhizopus oryzae (Rhizopus oryzae), the bacterial classification of Stereum, Streptomycesthermocyaneoviolaceus, mudStreptomycete, Subulispora procurvata, Syncephalastrum racemosum, Thaminidium elegans, thermophilic ascomycete,Bacterial classification, Thermomyces lanuginosus, gauffer bolt bacterium, the bacterial classification of Trametes, Trichophaea that Thermoascus belongs toSaccata, Valsaria rubricosa, Valsaria spartii and Bacillus flavothermus (synonym: Anoxybacillus contaminans)。
Preferred described heterozygote comprises the AMS amino acid sequence that is selected from table 1 or 2 listed AMS catalytic module.
Most preferably described heterozygote comprises AMS amino acid sequence, described AMS amino acid sequence be selected from fromAspergillus 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), bacterial classification (SEQ ID NO:16), the Malbranchea of Thermomyces lanuginosus (SEQ ID NO:14), the mould genus of branch top sporeThe bacterial classification (SEQ IDNO:18), Rhizomucor pusillus (SEQ ID NO:20), the Dichotomocladium hesseltinei that belong to(SEQ IDNO:22), huge bracket fungus (SEQ ID NO:24), the bacterial classification AMY1179 (SEQ IDNO:26) of Stereum, bolt bacteriumBacterial classification (SEQ ID NO:28), the salmon shellfish leather belonging to covers bacterium (Coriolus censors) (SEQID NO:30), thorn shell bistrichiasis PseudomonasThe bacterial classification (SEQ ID NO:34) that belongs to of bacterial classification (SEQ ID NO:32), Cryptosporiopsis, the bacterial classification of cone ChaetomiumThe bacterial classification (SEQ ID NO:40) of the bacterial classifications (SEQ ID NO:38) of (SEQ ID NO:36), look two spore Pseudomonas, the red shell Pseudomonas of clump,The bacterial classification (SEQ ID NO:42) of Gliocladium, Streptomyces thermocyaneoviolaceus (SEQ ID NO:44) the bacterial classification II (SEQ ID NO:111) that, Thermoascus belongs to, bacterial classification (SEQ ID NO:113), the Cong Chi of cone ChaetomiumThe bacterial classification (SEQ ID NO:115) of shell Pseudomonas, the bacterial classification (SEQ ID NO:117) of Fusarium, gauffer bolt bacterium (SEQ ID NO:119), the bacterial classification of Penicillium (SEQ ID NO:121), Valsariaspartii (SEQ ID NO:123), ThermoascusAurantiacus (SEQ ID NO:125), Phanerochaete chrysosporium (SEQ ID NO:127), Rhizopus oryzae (SEQ ID NO:129), Thaminidiumelegans (SEQ ID NO:131), pappus colter mould (SEQ ID NO:133), Syncephalastrum racemosumThe AMS of (SEQID NO:135) and mud streptomycete (SEQ ID NO:155).
The present invention also preferably comprises the heterozygote of AMS amino acid sequence, described AMS amino acid sequence and choosingHave at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, extremely from any sequence of lower groupFew 90% or even at least 95% homology: SEQ IDNO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO: 8、SEQ ID NO：10、SEQID 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 IDNO：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 IDNO：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 IDNO:131, SEQ ID NO:133, SEQ ID NO:135 and SEQ ID NO:155.
Have and be no more than 10 sites, be no more than 9 sites, do not surpassing at heterozyme described in another preferred embodimentCross 8 sites, be no more than 7 sites, be no more than 6 sites, be no more than 5 sites, be no more than 4 sites, be no more than 3 positionsPoint, be no more than 2 sites, be no more than the AMS sequence that 1 site is different from the amino acid sequence that is selected from lower group: 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 IDNO： 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、SEQID 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, SEQID NO:133, SEQ ID NO:135 and SEQ ID NO：155。
Also preferably comprise the heterozygote of AMS amino acid sequence, described AMS amino acid sequence by be selected from downAny sequence of group has at least 50%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least85%, at least 90% or even at least 95% homology: 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、SEQID 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 IDNO：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、 SEQID NO：120、SEQ ID NO：122、SEQ ID NO：124、SEQ ID NO：126、SEQ ID NO：128、SEQ IDNO:130, SEQ ID NO:132, SEQ ID NO:134 and SEQ ID NO:154.
More preferably comprise the heterozygote of AMS, described AMS is by low, medium, medium/high, height and/or the utmost pointThe DNA sequence dna of hybridizing with any DNA sequence dna that is selected from lower group under high stringency is coded: SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO：5、SEQ ID NO：7、SEQ IDNO：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 IDNO：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 IDNO：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 IDNO:128, SEQ ID NO:130, SEQ ID NO:132, SEQ ID NO:134 and SEQID NO:154.
Joint sequence
Joint sequence can be any suitable joint sequence, for example, derives from connecing of AMS or glucoamylaseHeader sequence. Described joint can be key, or comprises approximately 2 to approximately 100 carbon atoms, and particularly 2 to 40 carbon atoms is shortLinking group. But described joint is preferably the sequence of approximately 2 to approximately 100 amino acid residues, more preferably 4 to 40 aminoAcid residue, for example 6 to 15 amino acid residues.
Preferred described heterozygote comprises the joint sequence that derives from any species that are selected from lower group: branch top spore is mould, cone hair shellBacterium, cone cupreum, sub-Grifolas frondosa germ (Meripilus), thick spore pore fungi (Pachykytospora), Penicillium notatum, Sublispora,Bolt bacterium, Trichophaea, Valsaria, Ah too bacterium (Athelia), Aspergillus, bolt bacterium and stake mushroom (Leucopaxillus). InstituteState joint and also can derive from bacterium, for example, from the bacterial strain of bacillus bacterial classification. More preferably described joint derives from and is selected from downThe species of group: the bacterial classification of branch top spore mould genus, the bacterial classification of cone Chaetomium, the bacterial classification of cone Chaetomium, huge bracket fungus, PenicilliumBacterial classification, Sublispora provurvata, gauffer bolt bacterium, Trichophaea saccata, Valsariarubricosa,Valsario spartii, aspergillus albicans, aspergillus niger, Luo Eratai bacterium (Athelia rolfsii), leucopaxillus giganteus(Leucopaxillus gigantus), the large decorative pattern spore of papery (Pachykytospora papayracea), lobe ring bolt bacterium(Trametes cingulata) and Bacillus flavothermus.
Preferred described heterozygote comprises the joint amino acid sequence that is selected from listed joint in table 1 or 2.
More preferably described joint is from the joint of glucoamylase that is selected from lower group: large decorative pattern spore (the SEQ ID of paperyNO:46), lobe ring bolt bacterium (SEQ ID NO:48), leucopaxillus giganteus (SEQ ID NO:50), Luo Eratai bacterium (SEQ ID NO:68), aspergillus albicans (SEQ ID NO:70), aspergillus niger (SEQ ID NO:72), or from the AMS that is selected from lower groupJoint: Sublispora provurvata (SEQ IDNO:54), Valsaria rubricosa (SEQ ID NO:56), branch topThe bacterial classification (SEQ IDNO:58) of the mould genus of spore, huge bracket fungus (SEQ ID NO:60), Bacillus flavothermus (SEQ IDNO:62, SEQ ID NO:64 or SEQ ID NO:66), cone Chaetomium bacterial classification AM603 (SEQ IDNO:74), cone cupreumThe bacterial classification (SEQ ID NO:145), gauffer bolt bacterium (SEQ ID NO:147), Valsario spartii that belong to (SEQ ID NO:149), the bacterial classification of Penicillium (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% with the arbitrary sequence that is selected from lower group, at least75%, any joint amino acid sequence of at least 80%, at least 85%, at least 90% or even at least 95% homology: 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、SEQID 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：149With SEQ ID NO:151.
Have and be no more than 10 sites, be no more than 9 sites, do not surpassing at heterozyme described in another preferred embodimentCross 8 sites, be no more than 7 sites, be no more than 6 sites, be no more than 5 sites, be no more than 4 sites, be no more than 3 positionsPoint, be no more than 2 sites, be no more than the joint sequence that 1 site is different from the amino acid sequence that is selected from lower 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、SEQID NO： 58、SEQ ID NO：60、SEQ ID NO：62、SEQ ID NO：64、SEQ ID NO：66、SEQ ID NO：68、SEQ IDNO: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 preferably comprise the heterozygote of joint sequence, described joint sequence is by having at least with the arbitrary sequence that is selected from lower group60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% is sameThe DNA sequence dna of source property is coded: SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO：53、SEQ IDNO：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 IDNO：73、SEQ ID NO：144、SEQID NO:146, SEQ ID NO:148 and SEQ ID NO:150.
More preferably comprise the heterozygote of joint sequence, described joint sequence by under high, medium or low stringency be selected fromThe DNA sequence dna of the arbitrary DNA sequence dna hybridization of lower group is coded: SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO：51、SEQ ID NO：53、SEQ IDNO：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 IDNO：73、SEQ ID NO:144, SEQ ID NO:146, SEQ ID NO:148 and SEQ ID NO:150.
Use in preferred embodiments the joint that originates from CBM source, for example, when using from Luo Eratai bacterium glucoseWhen diastatic CBM, equally the joint sequence from Luo Eratai bacterium glucoamylase is used for to described heterozygote.
Carbohydrate binding modules
Carbohydrate binding modules (CBM), or so-called carbohydrate binding structural domain (CBM), refer to preferentialIn conjunction with polysaccharide or oligosaccharides (carbohydrate), often---but inevitable exclusively---(comprise crystalline substance in conjunction with its water-insolubleBody) polypeptid acid sequence of form.
The CBM that comes from starch degrading enzyme is commonly referred to starch binding modules (starch-bindingmodule) or SBM(may reside in specific diastatic enzyme, in specific glucoamylase (GA), or be present in enzyme as cyclodextrinIn glycosyl transferase, or be present in the CBM in AMS). Equally, other subclass of CBM will comprise, for example, and fiberElement binding modules (from the CBM of cellulolytic enzyme), chitin binding modules (are typically present in chitinaseCBM), xylan binding modules (being typically present in the CBM in zytase), mannosan binding modules (typically existCBM in mannase). SBM is commonly referred to SBD (StarchBinding Domain) (starch binding structural domain).
The large-scale polypeptide that discovery CBM is made up of two or more polypeptid acid sequence regions or the main portion of proteinPoint, especially typically comprising in the water-disintegrable enzyme (hydrolase) of catalytic module and carbohydrate binding modules (CBM), itsDescribed in the catalytic module avtive spot that contains substrate hydrolysis, carbohydrate binding modules (CBM) is in conjunction with discussingCarbohydrate substrate. These enzymes may comprise and exceed a catalytic module and one, two or three CBM and optionally enter oneStep comprises one or more polypeptide amino acid orders that one or more CBM and one or more catalytic module are linked togetherRow, the region of a rear type is commonly called " joint ". The example of the water-disintegrable enzyme that comprises CBM---some of them aboveMention---be cellulase, zytase, mannonase arabinofuranosidase, acetylesterase and chitinase. AlsoIn algae, for example, in red algae Porphyrapurpurea, find the CBM of non-water-disintegrable many carbohydrate-binding proteins form.
For example exist therein, in the protein/polypeptide (, enzyme, typically water-disintegrable enzyme) of CBM, CBM can be positioned at N or CEnd or be positioned at interior location.
Form the polypeptide of CBM itself or the part of protein (for example, water-disintegrable enzyme) by exceeding approximately 30 and be less than approximately 250Individual amino acid residue composition.
In the context of the invention, " carbohydrate binding modules family 20 " or CBM-20 module definition are about 100 ammoniaThe sequence of base acid, in itself and Fig. 1 by Joergensen et al. (1997) in Biotechnol.Lett.19:1027-1031The carbohydrate binding modules (CBM) of the polypeptide disclosing has at least 45% homology. Described CBM comprises the last of polypeptide102 amino acid, the i.e. subsequence to amino acid 683 from amino acid 582. Be applied to the glycoside hydrolysis enzyme family in this descriptionNumbering follow at URL:http://afmb.cnrs-mrs.fr/～cazy/CAZY/index.htmlOn Coutinho,P.M.&Henrissat, B. (1999) CAZy-Carbohydrate-Active Enzymes server, or alternatively follow Coutinho，P.M.&Henrissat，B.1999；The modular structure of cellulasesand otherCarbohydrate-active enzymes:an integrated database approach. exists " Genetics, Biochemistry and Ecology of Cellulose Degradation″，K.Ohmiya，K.Hayashi， K.Sakka，Y.Kobayashi，S.Karita and T.Kimura eds.，Uni PublishersCo.，Tokyo，pp.15-In 23, and Bourne, Y.& Henrissat, B.2001; Glycosidehydrolases and glycosyltransferases：families and functional modules，CurrentOpinion inThe thought of Structural Biology 11:593-600.
The example of the enzyme that comprises the CBM that is suitable for the context of the invention is AMS, product maltogenic alpha-amylase enzyme, fibreTie up plain enzyme, zytase, mannonase arabinofuranosidase, acetylesterase and chitinase. Relevant with the present inventionInterested more CBM comprise derived from glucoamylase (EC3.2.1.3) or cyclodextrin glycosyl transferases (CGTase) (EC2.4.1.19) CBM.
CBM derived from fungi, bacterium or plant origin will be suitable in heterozygote of the present invention conventionally. Preferred fungiThe CBM of origin. In this connection, the technology that is suitable for separating related gene is well known in the art.
Preferably comprise the heterozygote of the CBM of carbohydrate binding modules family 20,21 or 25. Be suitable for carbon of the present inventionThe CBM of hydrate binding modules family 20 can come from aspergillus awamori (Aspergillus awamori) (SWISSPROTQ12537), aspergillus albicans (SWISSPROT P23176), aspergillus niger (SWISSPROT P04064), aspergillus oryzae (SWISSPROTP36914) glucoamylase, comes from aspergillus albicans (EMBL:#_AB008370), aspergillus nidulans (AspergillusNidulans) AMS (NCBIAAF17100.1), comes from Bacillus cercus (Bacillus cereus)(SWISSPROTP36924) beta amylase, or come from Bacillus circulans (Bacillus circulans)(SWISSPROTP43379) CGTases. Preferably from the CBM of aspergillus albicans (EMBL:#_AB008370) AMS and withThe CBM of aspergillus albicans (EMBL:#_AB008370) AMS has at least 60%, at least 65%, at least 70%, at least 75%, extremelyThe CBM of few 80%, at least 85%, at least 90% or even at least 95% homology. Preferred CBM comprises glucoamylaseCBM, the bacterial classification belonging to from Hormoconis, as from Hormoconis resinae, (synonym is creasote (Creosote)Fungi, or Amorphotheca resinae), asSWISSPROT：Q03045CBM, from Lentinus (Lentinula)Bacterial classification, as from mushroom (Lentinula edodes) (mushroom (shiitakemushroom)), asSPTREMBL：Q9P4C5'sCBM, from the bacterial classification of Neurospora, as from Neurospora crassa (Neurospora crassa), asSWISSPROT：P14804CBM, from the bacterial classification (Talaromyces sp.) of Talaromyces, as from T. byssochlamydioides(Talaromycesbyssochlamydioides), from belong to bacterial classification (Geosmithia sp.), as fromGeosmithiacylindrospora, from belong to bacterial classification (Scorias sp.), as from Scorias spongiosa, comeFrom the bacterial classification (Eupenicillium sp.) of Eupenicillium sp, as from Eupenicillium ludwigii, from aspergillusBacterial classification, as from aspergillus japonicus (Aspergillus japonicus), from the bacterial classification of Penicillium, as from PenicilliumCf.miczynskii, from the bacterial classification (Thysanophora sp.) belonging to, and from the bacterial classification (Humicola of humic PseudomonasSp.), as from the mutation of grey humicola lanuginosa high temperature (Humicolagrisea var.Thermoidea), as SPTREMBL:Q12623CBM.
Preferred described heterozygote comprises to come from and is selected from arbitrary section of lower group or the CBM of species: the mould genus of branch top spore, aspergillus,Ah too bacterium, cone Chaetomium, Cryptosporiopsis, Dichotomocladium, thorn shell bistrichiasis Pseudomonas, look two spore Pseudomonas,Gliocladium, stake mushroom, Malbranchea, sub-Grifolas frondosa germ, the red shell Pseudomonas of clump, thick spore pore fungi, Penicillium notatum, Rhizomucor, smallRoot Mucor, streptomycete, Subulispora, thermophilic hyphomycete, Trametes, Trichophaea saccata and Valsaria.CBM also can derive from for example corn of plant (for example, Zea mays) or derive from such as bacillus of bacterium. More preferably instituteState heterozygote and comprise the CBM that derives from any species that are selected from lower group: bacterial classification, aspergillus albicans, aspergillus niger, the meter Qu of the mould genus of branch top sporeThe bacterial classification of mould, Luo Eratai bacterium, Bacillus flavothermus, cone Chaetomium, the bacterial classification that Cryptosporiopsis belongs toBacterial classification, look two spores of (Cryptosporiopsis sp.), Dichotomocladium hesseltinei, thorn shell bistrichiasis PseudomonasBacterial classification (Malbranchea sp.) that the bacterial classification of Pseudomonas, the bacterial classification of Gliocladium, leucopaxillus giganteus, Malbranchea belong to, huge manyThe large decorative pattern spore of bacterial classification, papery, the bacterial classification of Penicillium, Rhizomucor pusillus, the Streptomyces of pore fungi, the red shell Pseudomonas of clumpThermocyaneoviolaceus, mud streptomycete, Subulisporaprovurvata, Thermomyces lanuginosus, lobe ringBolt bacterium, gauffer bolt bacterium, Trichophaeasaccata, Valsariarubricosa, Valsariospartii and corn.
Preferred described heterozygote comprises the CBM amino acid sequence that is selected from listed CBM in table 1 or 2.
Most preferably described heterozygote comprises from the CBM of glucoamylase that is selected from lower group: large decorative pattern spore (the SEQ ID of paperyNO:76), lobe ring bolt bacterium (SEQ ID NO:78), leucopaxillus giganteus (SEQ ID NO:80), Luo Eratai bacterium (SEQ ID NO:92), aspergillus albicans (SEQ ID NO:94), aspergillus niger (SEQ IDNO:96), or from the CBM of AMS that is selected from lower group: Trichopheraea saccata(SEQID NO：52)、Subulispora provurvata(SEQ ID NO：82)、Bacterial classification (SEQ ID NO:86), huge bracket fungus (the SEQ ID of Valsariarubricosa (SEQID NO:84), the mould genus of branch top sporeNO:88), bacterial classification (SEQ ID NO:98), the jade of Bacillus flavothermus (SEQ ID NO:90), cone ChaetomiumThe bacterial classification (SEQ ID NO:137), gauffer bolt bacterium (SEQID NO:139) of rice (SEQ ID NO:109), cone Chaetomium,The bacterial classification (SEQ IDNO:143) of Valsario spartii (SEQ ID NO:141) and Penicillium.
Have and be no more than 10 sites, be no more than 9 sites, do not surpassing at heterozyme described in another preferred embodimentCross 8 sites, be no more than 7 sites, be no more than 6 sites, be no more than 5 sites, be no more than 4 sites, be no more than 3 positionsPoint, be no more than 2 sites or even do not exceed the CBM sequence that is different from the amino acid sequence that is selected from lower group on 1 site: 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、SEQID 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。
Also preferably by having at least 60%, at least 65%, at least 70%, at least 75% with any sequence that is selected from lower group,Any CBM:SEQ ID of the DNA sequence encoding of at least 80%, at least 85%, at least 90% or even at least 95% homology 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 IDNO：89、SEQ ID NO：91、SEQ ID NO：93、SEQ ID NO：95、SEQ ID NO97、SEQ IDNO:108, SEQ ID NO:136, SEQ ID NO:140, SEQ ID NO:142. More preferably by with any DNA that is selected from lower groupCoded any CBM:SEQ ID NO:75, the SEQ ID NO of DNA sequence dna that sequence is hybridized under high, medium or low stringency: 77、SEQ ID NO：79、SEQ ID NO：81、SEQ ID NO：83、SEQ ID NO：85、SEQ ID NO：87、SEQ IDNO： 89、SEQ ID NO：91、SEQ ID NO：93、SEQ ID NO：95、SEQ ID NO：97、SEQ ID NO：108、SEQ IDNO:136, SEQ ID NO:138, SEQ ID NO:140 and SEQID NO:142.
The how applicable CBM of carbohydrate binding modules family 20,21 or 25 can be at URL:http:// afmb.cnrs-mrs.fr/～cazy/CAZY/index.html)Find.
Once identify as cDNA or as the coding Binding Capacity of chromosomal DNA (carbohydrate in conjunction with) regionNucleotide sequence, can be by the DNA sequence dna that operate in every way after it to be fused to the interested polypeptide of coding.Then with or connect the DNA fragmentation of encoding carbohydrate binding amino acid sequence and coding polypeptide of interest without jointDNA. The DNA that then can operate in every way obtained connection expresses to realize.
Particular
In preferred embodiments, described polypeptide comprises and derives from Luo Eratai bacterium, the large decorative pattern spore of papery, ValsariaThe CBM of rubricosa or huge bracket fungus. Preferably comprise any polypeptide of the CBM amino acid sequence that is selected from lower group: Luo Eratai bacteriumGlucoamylase (SEQ ID NO:92), the large decorative pattern spore of papery glucoamylase (SEQ ID NO:76), ValsariaRubricosa AMS (SEQ ID NO:84) and huge bracket fungus AMS (SEQ ID NO:88).
In another preferred embodiment, described polypeptide comprises the AMS order that derives from aspergillus oryzae acid alpha-amylaseRow (SEQ ID NO:4), preferred wherein said aspergillus oryzae amino acid sequence comprises and is selected from one or more amino acid of lower group and getsGeneration: A128P, K138V, S141N, Q143A, D144S, Y155W, E156D, D157N, N244E, M246L, G446D, D448S andN450D. Most preferably described polypeptide comprises the catalyst structure domain with amino acid sequence shown in SEQ ID NO:6. In preferred enforcementIn scheme, described polypeptide further comprises the CBM that derives from Luo Eratai bacterium, and preferred described polypeptide further comprises and has SEQThe CBM of amino acid sequence shown in ID NO:92. Most preferably described polypeptide has amino acid sequence shown in SEQ ID NO:100, orDescribed in person, polypeptide has with aforementioned amino acid sequence and has at least 60%, at least 65%, at least 70%, at least 75%, at least80%, the amino acid sequence of at least 85%, at least 90% or even at least 95% homology.
Also preferably by having at least 60%, at least 65%, at least 70% with DNA sequence dna shown in SEQ ID NO:99, at least75%, coded any many of the DNA sequence dna of at least 80%, at least 85%, at least 90% or even at least 95% homologyPeptide.
In another preferred embodiment, described polypeptide comprises the catalytic module that derives from Rhizomucor pusillus AMSAnd/or derive from the CBM of Luo Eratai bacterium. In particularly preferred embodiments, described polypeptide has SEQ ID NO:101 instituteThe amino acid sequence showing or described polypeptide have with aforementioned any amino acid sequence and have at least 60%, at least 65%, extremelyThe amino acid sequence of few 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% homology.
In another preferred embodiment, described polypeptide comprise derive from huge bracket fungus AMS catalytic module and/Or derive from the CBM of Luo Eratai bacterium. In particularly preferred embodiments, described polypeptide has shown in SEQ ID NO:102Amino acid sequence or described polypeptide have with aforementioned amino acid sequence and have at least 60%, at least 65%, at least 70%, extremelyThe amino acid sequence of few 75%, at least 80%, at least 85%, at least 90% or even at least 95% homology.
In another preferred embodiment, described polypeptide has being no more than 10 sites, is no more than 9 sites, superCross 8 sites, be no more than 7 sites, be no more than 6 sites, be no more than 5 sites, be no more than 4 sites, be no more than 3 positionsPoint, be no more than 2 sites or even do not exceed 1 site and be different from SEQ ID NO:100, SEQ ID NO:101 and SEQThe amino acid sequence of any amino acid sequence shown in ID NO:102.
Also preferred any polypeptide by DNA sequence encoding, described DNA sequence dna and coding SEQ IDNO:100, SEQ IDAny DNA sequence dna of any amino acid sequence shown in NO:101 and SEQ ID NO:102 has at least 60%, at least 65%, extremelyFew 70%, at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% homology.
More preferably by under high, medium or low stringency with coding SEQ ID NO:100, SEQ ID NO:101 and SEQThe coded any CBM of DNA sequence dna of any DNA sequence dna hybridization of arbitrary amino acid sequence shown in ID NO:102.
Other preferred embodiment of polypeptide of the present invention is as shown in embodiment part table 3,4,5 and 6. Also preferably and table 1 to 7Shown in any amino acid sequence of polypeptide there is at least 70%, more preferably at least 80% and even more preferably at least 90% homologyAny polypeptide of property. More preferably by under low, medium or high stringency with any amino acid order of polypeptide shown in coding schedule 1 to 7The coded any polypeptide of DNA sequence dna of the DNA sequence dna hybridization of row.
In preferred embodiments, described polypeptide comprises with aspergillus oryzae catalyst structure domain (SEQ ID NO:6) and has at leastThe catalyst structure domain of 75% homology and with the CBM that is selected from lower group have 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, SEQID NO:92, SEQ ID NO:52 and SEQ ID NO:90. In a more preferred embodiment,Described polypeptide comprises aspergillus oryzae catalyst structure domain (SEQ ID NO:6) and is selected from CBM:SEQID NO:82, the SEQ ID of lower group NO：84、SEQ ID NO：86、SEQ ID NO：76、SEQ ID NO：78、SEQ ID NO：80、SEQ ID NO：88、SEQ IDNO:52, SEQ ID NO:92, SEQ IDNO:52 and SEQ ID NO:90.
In preferred embodiments, described polypeptide comprises the tool with Luo Eratai bacterium glucoamylase CBM (SEQIDNO:92)There is the CBM of at least 75% homology and there is the catalyst structure domain of at least 75% homology with the catalyst structure domain that is selected from lower group: 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、SEQID 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、SEQID 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, SEQID NO:131, SEQ ID NO:133 and SEQ ID NO:135. In a more preferred embodiment, described polypeptide bagContain Luo Eratai bacterium glucoamylase CBM (SEQ ID NO:92) and be selected from the catalyst structure domain of lower group: 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、SEQID 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、SEQID 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、SEQID NO:133 and SEQ ID NO:135.
In preferred embodiments, described polypeptide comprise with SEQ ID NO:145 in the large decorative pattern spore of papery glucose starchEnzyme CBM has the CBM of at least 75% homology and has the catalyst structure domain of at least 75% homology with the CBM that is selected from lower group:Rhizomucor pusillus α-shallow lake in AMS CBM, the SEQ ID NO:20 of the bacterial classification of the mould genus of branch top spore in SEQ ID NO:16Huge bracket fungus AMS CBM in powder enzyme CBM and SEQ IDNO:24. In a more preferred embodiment, described polypeptide comprisesThe large decorative pattern spore of papery glucoamylase CBM in SEQ ID NO:145 and be selected from the branch in the CBM:SEQ ID NO:16 of lower groupRhizomucor pusillus AMS CBM in AMS CBM, the SEQ IDNO:20 of the bacterial classification of the mould genus of top spore and SEQ ID NO:Huge bracket fungus AMS CBM in 24.
In preferred embodiments, described polypeptide comprises and Rhizomucor pusillus AMS catalyst structure domain (SEQ IDNO:20) there is the catalyst structure domain of at least 75% homology and there is the CBM of at least 75% homology with the CBM that is selected from lower group:Aspergillus niger glucoamylase CBM in aspergillus albicans glucoamylase CBM in SEQ ID NO:94 and SEQ ID NO:96. MoreIn preferred embodiment, described polypeptide comprises Rhizomucor pusillus AMS catalyst structure domain (SEQ ID NO:20) and is selected fromAspergillus niger glucose starch in aspergillus albicans glucoamylase CBM and SEQ ID NO:96 in the CBM:SEQ ID NO:94 of lower groupEnzyme CBM.
In preferred embodiments, described polypeptide comprise with huge bracket fungus AMS catalyst structure domain (SEQ ID NO:24) there is the catalyst structure domain of at least 75% homology and there is the CBM:SEQ of at least 75% homology with the CBM that is selected from lower groupValsariarub ricosa α-shallow lake in the large decorative pattern spore of papery glucoamylase CBM, SEQ ID NO:84 in ID NO:145Corn C BM in powder enzyme CBM and SEQ ID NO:109. In a more preferred embodiment, described polypeptide comprise huge bracket fungus α-Catalyzed by amylase domain (SEQ ID NO:24) and be selected from the large decorative pattern spore of the papery Portugal in the CBM:SEQ ID NO:145 of lower groupCorn in Valsaria rubricosa AMS CBM and SEQ ID NO:109 in saccharogenic amylase, SEQ ID NO:84 CBM。
In preferred embodiments, described polypeptide comprises and Rhizomucor pusillus AMS catalyst structure domain (SEQ IDNO:20) there is the catalyst structure domain of at least 75% homology and there is the CBM of at least 75% homology with the CBM that is selected from lower group:Corn C BM, SEQ ID NO in Luo Eratai bacterium glucoamylase CBM and SEQ ID NO:109 in SEQ ID NO:92:Gauffer bolt bacterium AMS CBM, SEQ in AMS CBM, the SEQ ID NO:119 of the bacterial classification of the cone Chaetomium in 113α-the shallow lake of the bacterial classification of the Penicillium in Valsaria spartii AMS CBM, SEQ ID NO:121 in ID NO:123Huge bracket fungus AMS CBM in powder enzyme CBM and SEQ ID NO:88. In a more preferred embodiment, described polypeptide bagContaining Rhizomucor pusillus AMS catalyst structure domain (SEQ ID NO:20) be selected from the CBM:SEQ ID NO:92 of lower groupCone Chaetomium in corn C BM, SEQ ID NO:113 in Luo Eratai bacterium glucoamylase CBM and SEQ ID NO:109AMS CBM, the SEQ ID NO:119 of bacterial classification in gauffer bolt bacterium AMS CBM, SEQ ID NO:123 inAMS CBM and the SEQ ID of the bacterial classification of the Penicillium in Valsaria spartii AMS CBM, SEQID NO:121Huge bracket fungus AMS CBM in NO:88.
Described polypeptide is selected from lower group in particularly preferred embodiments: 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 invention still further relates to recombinant expression carrier, it can comprise DNA sequence dna, promoter, the signal peptide order of coded polypeptideBe listed as and transcribe and translate stop signal. Above-mentioned various DNA and control sequence can be linked together to prepare recombinant expressed yearBody, it can comprise that one or more restriction sites are easily to allow the DNA sequence dna of coding said polypeptide in these sitesInsertion or replacement. Or, can be by the DNA sequence dna that comprises described sequence or DNA construct be inserted into suitable carrierIn for express. In construction of expression vector process, described coded sequence is arranged in carrier, to described coded sequence can be graspedMake ground and link together with suitable control sequence, for expressing and possible secretion.
Described recombinant expression carrier can be any carrier (for example, plasmid or virus), can use it for easily heavilyGroup DNA process also can cause the expression of described DNA sequence dna. The selection of carrier typically depends on described carrier and this carrier instituteThe compatibility of the host cell importing. Described carrier can be plasmid linear or closed ring. Described carrier canTo be autonomously replicationg vector, that is, the carrier existing as the outer entity of chromosome, it copies and is independent of chromosome replication, for example, matterGrain, the outer assembly of chromosome, minichromosome, clay (cosmid) or artificial chromosome. Described carrier can comprise for guaranteeingAny mode of self-replacation. Or described carrier can be in the time importing in host cell, be incorporated in genome and withThe carrier that its one or more chromosomes that are integrated into copy together. Described carrier system can be to comprise to import to placeThe single carrier of all DNA in the genome of chief cell or plasmid or two or more carrier or plasmid, or transposons.
Mark
Carrier of the present invention preferably comprises one or more can selected marker, and it allows easily to select the cell transforming.Selectable mark is gene, and its product provides antiseptic or virus resistance, heavy metal resistance, prototrophy to auxotroph,Etc..
For filamentous fungal host cell can selected marker example can be selected from and include but not limited to: amdS (acetylAmine enzyme), (hygromycin phosphoric acid shifts for argB (ornithine transcarbamylase), bar (careless ammonium phosphinothricin acetyl based transferase), hygBEnzyme), niaD (nitrate reductase), pyrG (orotidine-5 '-phosphate decarboxylase), sC (sulfate adenylyl transferase (sulfateAdenyltransferase)), trpC (o-amino benzoyl acid synthase) and careless fourth phosphine resistance marker and from other speciesThe group of equivalent. What be preferred for aspergillus cell is amdS and pyrG mark and the water suction strepto-of aspergillus nidulans or aspergillus oryzaeThe bar mark of bacterium (Streptomyceshygroscopicus). In addition, can complete selection by cotransformation, for example WO91/Described in 17243, wherein said selection to be marked at independently on carrier.
Carrier of the present invention preferably comprise allow described carrier stable integration in host cell gene group or allow instituteState carrier and in cell, be independent of cellular genome and one or more elements of self-replicating.
In the time being incorporated in host cell, carrier of the present invention can be incorporated in host cell gene group. In order to integrate,Described carrier may rely on coding polypeptide of interest DNA sequence dna or for making carrier stablize whole by homology or non-homogeneous restructuringBe incorporated into any other carrier element in genome. Or described carrier can comprise extra DNA sequence dna, described extraDNA sequence dna is for the genome to host cell by homologous recombination directional integration. Described extra DNA sequence dna makes described carryingBody can be incorporated in host cell gene group the one or more exact positions in one or more chromosome. In order to increaseBe integrated in the possibility of exact position, described integrated assembly should preferably comprise enough several target DNAs, as 100 to 1,500 alkaliBase pair, preferably 400 to 1,500 base-pairs, most preferably 800 to 1,500 base-pairs, it is same with corresponding target sequence heightSource, to increase the probability of homologous recombination. Described integrated element can be the target sequence homology in any and host cell gene groupSequence. In addition, described integrated assembly can be non-coding or DNA sequences encoding. On the other hand, described carrier can be by non-Homologous recombination is incorporated in the genome of host cell. These DNA sequence dnas can be the targets in any and host cell gene groupThe sequence of sequence homology, in addition, these DNA sequence dnas can be non-coding or coded sequence.
For self-replicating, described carrier can further comprise replication origin, and described replication origin makes described carrier energyEnough self-replicatings in discussed host cell.
Can use the episomal replication of disclosed AMA1 plasmid vector in WO00/24883.
The DNA sequence dna of the coding polypeptide of interest that exceedes a copy can be inserted in host cell to increase DNAThe expression of sequence. Can be by using method well known in the art that at least one additional copy of sequence is incorporated into host cellIn genome and select transformant and obtain the stable amplification of DNA sequence dna.
For connect said elements with the method that builds recombinant expression carrier of the present invention to those skilled in the artBe know (referring to, for example, Sambrook et al, 1989, Molecular Cloning, A Laboratory Manual，2ndedition，Cold Spring Harbor，New York)。
Host cell
Host cell of the present invention (the expression that it comprises DNA construct or comprises the DNA sequence dna that contains coding said polypeptideCarrier) for example, in the recombinant production of polypeptide (, the wild-type enzyme of heterozyme, wild-type enzyme or genetic modification), be advantageously used for placeChief cell. Can transform described cell with expression vector. Or, can pass through DNA construct (with one or more easilyCopy) be incorporated in host chromosome, for example, by coding said polypeptide (, the wild type of heterozyme, wild-type enzyme or genetic modificationEnzyme) DNA construct of the present invention transform described cell. DNA construct can be according to tradition to the integration in host chromosomeMethod, for example, is undertaken by homology or heterologous recombination.
Described host cell can be any suitable protokaryon or eukaryotic, and for example, bacterial cell, filamentous fungi are thinBorn of the same parents, yeast, plant cell or mammalian cell.
In preferred embodiments, described host cell is represented by following sac fungus (Ascomycota) class thread trueBacterium, for example comprises, neurospora (Neurospora), penicillium (Eupenicillium) (=mould), naked born of the same parents' shell(Emericella) (=aspergillus), loose capsule bacterium (Eurotium) (=aspergillus).
In a more preferred embodiment, described filamentous fungi comprises Eumycotina (Eumycota) and oomycetes subphylumAll filamentous fungis (Oomycota) (as Hawksworth et al.In, Ainsworth andBisby ' sDictionary of The Fungi，8thEdition, 1995, CAB International, UniversityPress, Cambridge, UK instituteDefinition). Described filamentous fungi is with compound by chitin, cellulose, glucan, chitosan, mannosan and otherThe vegetative mycelium of composition of Salvia polysaccharide is feature. Extending into row by mycelia nourishes and grows and carbon catabolism is strictly aerobic.
In the embodiment being more preferably, described filamentous fungal host cell is to include but not limited to be selected from lower group thinThe cell of born of the same parents' species: aspergillus species, the preferably bacterial strain of aspergillus oryzae, aspergillus niger, aspergillus awamori, aspergillus albicans, or bacillusBelong to bacterial strain or fusarium bacterial strain, as Fusarium oxysporum (Fusarium oxysporium), Fusarium graminearum (FusariumGraminearum) (be more properly expressed as Gibberella zeae (Gribberella zeae), be called Sphaeria beforeZeae, with pink red mould (Gibberella roseum) and pink red mould cereal mutation (Gibberella roseumF.sp.cerealis) synonym) or fusarium sulphureum (Fusarium sulphureum) (be more properly calledGibberellapuricaris, with Fusarium trichothecioides, Fusarium bactridioides,Fusariumsambucium, pink sickle spore (Fusarium roseum) and pink sickle spore cereal mutation (FusariumroseumVar.graminearum) synonym), cereal reaping hook mould (Fusarium cerealis) (with Fusariumcrookwellense withJustice) or the bacterial strain of Fusarium venenatum.
In the most preferred embodiment, described filamentous fungal host cell is aspergillus species, preferably aspergillus oryzae or blackThe cell of the bacterial strain of aspergillus.
Described filamentous fungal host cell can be wild type filamentous fungal host cell or variation, sudden change or heredityThe filamentous fungal host cell of modifying. In a preferred embodiment of the invention described host cell be Deficient In Extracellular Proteases or eggWhite enzyme negativity bacterial strain. Also consider especially aspergillus bacterial strain, as Aspergillus niger strain, its genetically modified destruction or reduced glucose shallow lakePowder enzyme, stable AMS, α-1 of acid, the expression of 6 transglucosidases and proteinase activity.
The conversion of filamentous fungal host cell
Filamentous fungal host cell can by relating to, the protoplast of mode known in the art forms, protoplast turnsThe method of change and cell membrane regeneration transforms. EP238023, EP184438 and Yeltonetal.1984, ProceedingsIn of the NationalAcademy of Sciences USA 81:1470-1474, conversion aspergillus host cell is describedSuitable method. Malardier et al.1989, Gene78:147-156 or U.S. patent 6,060,305 have described conversionThe suitable method of the mould species of reaping hook.
The DNA sequence dna of separation and clones coding parent AMS
For separating of or the technology of the DNA sequence dna of clones coding polypeptide of interest be known in the art, comprise from geneGroup DNA separates, prepares or its combination from cDNA. May be for example from such genomic dna cloning DNA sequence dna of the present invention, profitHave the clone's of common structure feature with detection with the antibody screening of the PCR of knowing (PCR) or expression libraryDNA fragmentation carries out. Referring to, for example, Innis et al., 1990, PCR:A Guide to Methods andApplication, Academic Press, New York. Can use other DNA cloning method as ligase chain reaction(LCR) what, connection activated transcribes (LAT) and the amplification based on DNA sequence dna (NASBA).
Can utilize several different methods well known in the art to separate from any cell or the microorganism that produce described AMSThe DNA sequence dna of coding parent AMS. First, should utilize from the biological dyeing of producing the AMS that will studyBody DNA or mRNA build genomic DNA and/or cDNA library. Then, if the amino acid sequence of described AMS beKnown, oligonucleotide probe that so can complex sign and for from genomic library identification code AMS gramGrand, described genomic library is from discussed biology preparation. Or, adopt the utmost point to be low to moderate hybridization and the detergent bar of high stringencyPart, can be used as probe by the labeled oligonucleotide probe of the sequence that comprises the alpha-amylase gene homology known with another,With the clone of identification code AMS.
The clone's of identification code AMS another kind of method is carried relating to the fragment of genomic DNA to be inserted into expressBody, as in plasmid, with gained genome dna library conversion AMS negative bacteria, is then containing α-shallow lake with the bacterium transformingOn the agar of the substrate (, maltose) of powder enzyme, draw flat board, thereby allow qualification express alpha-diastatic clone.
Or, can be with the standard method of having established by the synthetic DNA sequence dna of preparing coding said polypeptide, for example,S.L.Beaucage and M.H.Caruthers, (1981), Tetrahedron Letters 22, p.1859-1869 describedPhosphoroamidite method, or Matthes et al. (1984), EMBO J.3, p.801-805 describe method. ?In phosphoroamidite method, for example synthetic oligonucleotide in automatic dna synthesizer, purifying, annealing, connects, and cloneEnter suitable carrier.
Finally, described DNA sequence dna can be genome and synthetic mixed source, synthesize and cDNA mixed source or geneGroup and cDNA mixed source, the fragment of synthesizing by connection according to standard technique, genome or cDNA originate (it is suitable,Corresponding to the fragment of the different piece of whole DNA sequence dna) and prepare. Described DNA sequence dna also can be with Auele Specific Primer by poly-Synthase chain reaction (PCR) preparation, for example United States Patent (USP) 4,683,202 or R.K.Saiki et al. (1988),Science239, described in 1988, pp.487-491.
The DNA sequence dna separating
The present invention be more particularly directed to comprise coded polypeptide (for example wild-type enzyme of heterozyme, wild-type enzyme or genetic modification)The DNA sequence dna of the separation of DNA sequence dna, the amino acid sequence that described polypeptide comprises the catalytic module with alpha-amylase activity and carbonThe amino acid sequence of hydrate binding modules, wherein said catalytic module is fungi origin.
Term used herein " DNA sequence dna of separation " relates to the DNA sequence dna that does not basically contain other DNA sequence dna, for example, logicalPure, preferably pure at least about 40%, more preferably pure at least about 60% at least about 20% while crossing agarose electrophoresis mensuration, morePreferably pure at least about 80%, most preferably pure at least about 90%.
For example, the DNA sequence dna of separation can obtain by the standard cloning process for genetic engineering, and described method willDNA sequence dna is reoriented to from its natural place the different loci that it will copy there. Described cloning process may relate to be cutExcept with separate required comprising encode polypeptide of interest DNA sequence dna DNA fragmentation, described fragment is inserted into carrier moleculeIn, by described recombinant vector be incorporated into described DNA sequence dna multicopy or clone by the host cell copying therein. CanOperate the DNA sequence dna separating so that the expression of polypeptide of interest to be provided by several different methods. Depend on described expression vector, insert at itEntering to before in carrier, may be to need or essential to the operation of described DNA sequence dna. Utilize recombinant DNA method modifying DNA orderThe technology of row is well known in the art.
DNA construct
The present invention be more particularly directed to the DNA construct of the DNA sequence dna that comprises coded polypeptide, described polypeptide for for example heterozyme orWild-type enzyme, wherein said heterozyme comprises first amino acid sequence that contains catalytic module and contains carbohydrate combinationSecond amino acid sequence of module, described catalytic module has alpha-amylase activity, or wherein said wild-type enzyme comprisesFirst amino acid sequence that contains catalytic module and second amino acid sequence that contains carbohydrate binding modules, described inCatalytic module has alpha-amylase activity. " DNA construct " is defined as strand or double chain DNA molecule herein, and it is by naturalRaw Gene Isolation, or modified and comprised DNA fragmentation, and described DNA fragmentation combines in the non-existent mode of occurring in natureWith placement arranged side by side. In the time that DNA construct comprises coded sequence of the present invention and expresses required all control sequences, term DNA structureBuild body and term expression cassette is synonym.
Direct mutagenesis
Once separate the DNA sequence dna of coding parent AMS, and determined and can utilize required mutational site and closeThe oligonucleotides becoming is introduced sudden change. These oligonucleotides comprise the nucleotide sequence that is positioned at required mutational site flank. SpecificIn method, in the carrier that carries alpha-amylase gene, build the strand breach as the DNA of AMS coded sequence. ThenThe synthesizing ribonucleotide of required sudden change and the annealing of the homology part of single stranded DNA will be carried. Then use DNA polymerase i (Klenow sheetSection) fill remaining breach, utilize T4 ligase to connect described construct. The specific embodiment of the method is described inMorinagaet al. (1984), Biotechnology2, p.646-639. United States Patent (USP) 4,760,025 discloses by expressingThe minor alteration of box is introduced the oligonucleotides of the multiple sudden changes of coding. But, can by Morinaga method any one timeBetween introduce a greater variety of sudden changes because can introduce many oligonucleotides of different length.
The another kind of method that sudden change is incorporated in coding for alpha-diastatic DNA sequence dna is described in Nelsonand Long,(1989), Analytical Biochemistry180, p.147-151. It relates to 3 steps of the PCR fragment that comprises required sudden changeProduce, wherein the DNA chain of chemical synthesis is introduced to required sudden change as one of them primer in PCR reaction. Can lead toCross with restriction enzyme enzymatic lysis and reinserted in expression plasmid and the fragment of producing from PCR separate carry described prominentThe DNA fragmentation becoming.
Localized random mutagenesis
Random mutagenesis can advantageously be confined to a part for discussed parent's AMS. For example,, when identifyingThe specific region that goes out enzyme particular importance and expection for the specified characteristic of enzyme can produce and have the characteristic of improvement while modificationVariation time, this may be favourable. Under normal circumstances, when having illustrated the merit of the tertiary structure of parent enzyme and itself and enzymeCan be correlated with time, can identify these regions.
Use induced-mutation technique that PCR as above causes or any other suitable technology known in the art easilyImplement localization or regiospecificity random mutagenesis. Or, the DNA of a part for the DNA sequence dna that can separate encodes will modifySequence, for example, by being inserted in suitable carrier, can be used any method of mutagenesis discussed above to described part subsequentlyCarry out mutagenesis.
The variant of heterozygote or wild-type enzyme
The wild type that contains carbohydrate binding modules (" CBM ") and AMS catalytic module or heterozyme are at starchPerformance in biodegrading process can be improved by protein engineering, as passed through direct mutagenesis (site-directedMutagenesis), pass through localized random mutagenesis (localized randommutagenesis), pass through to prepare with synthetic methodThe new variant of parent's wild-type enzyme or parent's heterozyme or by any other suitable protein engineering.
Can utilize traditional protein engineering to produce described variant.
The expression of polypeptide in host cell
The nucleotide sequence being introduced in host cell DNA can be incorporated in nucleic acid construct to described nucleic acid structureBuild body and comprise the nucleotide sequence that is operably connected to one or more control sequences, described control sequence guiding coded sequenceUnder the condition compatible with control sequence, in suitable host cell, express.
Can be by the nucleotide sequence of several different methods operate coding polypeptide so that expression of polypeptides. Depend on that described expression carriesBody, in described nucleotide sequence is inserted into carrier before, to its operation may be need or essential. Utilize recombinant DNAThe technology of method modified nucleotide sequence is well known in the art.
Described control sequence can be suitable promoter sequence, and promoter sequence is identified to express core by host cellThe nucleotide sequence of nucleotide sequence. Described promoter sequence comprises transcriptional control sequence, the expression of its mediation polypeptide. Described startupSon can be any nucleotide sequence that shows transcriptional activity in selected host cell, comprise sudden change, brachymemma andThe promoter of heterozygosis, can be by the born of the same parents of coding and host cell homology or non-homology in outer or born of the same parents the gene of polypeptide obtain.
Guide nucleic acid construct of the present invention to transcribe, especially in the suitable promoter of bacterial host cell transcriptionExample is from Escherichia coli lactose operon, streptomyces coelicolor (Streptomycescoelicolor) agarase gene(dagA), bacillus subtilis levansucrase (levansucrase) gene (sacB), bacillus licheniformis (BacillusLicheniformis) alpha-amylase gene (amyL), bacillus stearothermophilus (BacillusStearothermophilus) produce maltogenic amylase (maltogenicamylase) gene (amyM), bacillus amyloliquefaciens(Bacillus amyloliquefaciens) alpha-amylase gene (amyQ), bacillus licheniformis penicillinase gene(penP) promoter (Villa-that, bacillus subtilis xylA and xylB gene and prokaryotes beta-lactamase gene obtain Kamaroff et al.，1978，Proceedings of the National Academy of Sciences USA75：3727-3731), and tac promoter (DeBoer et al., 1983, Proceedings of the NationalAcademy of SciencesUSA80:21-25). More multiple promoter is described in Scientific American, and 1980,242:" Useful proteins from recombinant bacteria " in 74-94; With Sambrook et al., 1989,With upper.
For guiding the example of nucleic acid construct of the present invention in the suitable promoter of filamentous fungal host cell transcriptionSon is by aspergillus oryzae TAKA amylase, rhizomucor miehei (Rhizomucor miehei) aspartic protease, aspergillus niger neutralityAMS, stable AMS, aspergillus niger or aspergillus awamori glucoamylase (glaA), the rhizomucor miehei fat of aspergillus niger acidFat enzyme, aspergillus oryzae alkali protease, aspergillus oryzae phosphotriose isomerase, aspergillus nidulans acetamidase and Fusarium oxysporum pancreas eggThe promoter that the gene of white enzyme sample protease (WO 96/00787) obtains, and NA2-tpi promoter is (from aspergillus niger neutralityThe heterozygote of the promoter of the gene of AMS and aspergillus oryzae phosphotriose isomerase) and sudden change, brachymemma and assortedThe promoter of closing.
In yeast host, useful promoter is by saccharomyces cerevisiae (Saccharomyces cerevisiae) enolase(ENO-1), saccharomyces cerevisiae galactokinase (GAL1), Ethanol in Saccharomyces cerevisiae dehydrogenase/glyceraldehyde-3-phosphate dehydrogenase (ADH2/GAP) and the kinase whose gene of saccharomyces cerevisiae 3-phoshoglyceric acid obtain. Romanos et al., 1992, Yeast8423-488 retouchesState the promoter that other can be used for yeast host cell.
Described control sequence can be also suitable tanscription termination subsequence, and described tanscription termination subsequence is by host cellIdentification is transcribed with termination. Described terminator sequence is operably connected to 3 ' end of the nucleotide sequence of coded polypeptide. AppointWhere in selected host cell, there is the terminator of function to may be used to the present invention.
Be used for the preferred terminator of filamentous fungal host cell from aspergillus oryzae TAKA amylase, aspergillus niger glucose starchEnzyme, aspergillus nidulans o-amino benzoyl acid synthase, aspergillus niger alpha-glucosidase and Fusarium oxysporum trypsin-like proteaseGene obtains.
For preferred terminator home-brewed yeast enolase, the brewing yeast cell pigment C of yeast host cell(CYC1) and the gene of saccharomyces cerevisiae glyceraldehyde-3-phosphate dehydrogenase obtain. Romanos et al., 1992, the same descriptionFor other useful terminator of yeast host cell.
Described control sequence can be also suitable targeting sequencing, and described targeting sequencing is for being undertaken by host cellTranslation is the untranslated region of important mRNA. Described targeting sequencing is operably connected to the nucleotides sequence of coded polypeptide5 ' end of row. Any have the terminator of function to may be used to the present invention in selected host cell.
Be used for the preferred targeting sequencing of filamentous fungal host cell by aspergillus oryzae TAKA amylase and aspergillus nidulans phosphoric acidThe gene of triose isomerase obtains.
Be used for the suitable targeting sequencing of yeast host cell by saccharomyces cerevisiae enolase (ENO-1), saccharomyces cerevisiae 3-Phosphoglyceric kinase, saccharomyces cerevisiae α-factor and Ethanol in Saccharomyces cerevisiae dehydrogenase/glyceraldehyde-3-phosphate dehydrogenase (ADH2/GAP) gene obtains.
Described control sequence can also be Polyadenylation sequence, and Polyadenylation sequence is operably connected to core3 ' end of nucleotide sequence, in the time transcribing, it is identified by host cell, adds poly adenosine residue as the mRNA to transcribingSignal. Any Polyadenylation sequence that has function in selected host cell may be used to the present invention.
Be used for the preferred Polyadenylation sequence of filamentous fungal host cell by aspergillus oryzae TAKA amylase, aspergillus nigerGlucoamylase, aspergillus nidulans o-amino benzoyl acid synthase, Fusarium oxysporum trypsin-like protease and aspergillus niger α-grapeThe gene of glycosidase obtains.
Guo and Sherman, 1995, Molecular Cellular Biology15:5983-5990 has described availableIn the Polyadenylation sequence of yeast host cell.
Described control sequence also can be encoded and is connected to the aminoterminal amino acid sequence of polypeptide and by coded manyPeptide is directed to the signal peptide coding region in the secretory pathway of cell. 5 ' end of the coded sequence of nucleotide sequence itself can wrapContaining signal peptide coding region, its in translation reading frame with natural being connected of code area fragment of coding secrete polypeptide. Or, code sequence5 ' end of row can comprise the signal peptide coding region for external source concerning coded sequence. Described coded sequence does not comprise letter natively, may need external source signal peptide coding region when number the peptide-coding region. Or external source signal peptide coding region can be replaced natural simplySignal peptide coding region to strengthen the secretion of polypeptide. But, any by expressed polypeptide be directed to selected host cell pointThe signal peptide coding region of secreting approach may be used to the present invention.
To the effective signal peptide coding region of bacterial host cell be by bacillus NCIB11837 produce maltogenic amylase,Bacillus stearothermophilus alpha-amylase, bacillus licheniformis subtilisin, bacillus licheniformis beta-lactamase, thermophilic fatThe signal peptide coding that the gene of fat bacillus neutral proteinase (nprT, nprS, nprM) and bacillus subtilis prsA obtainsDistrict. Simonen and Palva, 1993, Microbiological Reviews57:109-137 has described more signalPeptide.
By aspergillus oryzae TAKA amylase, the neutral shallow lake of aspergillus niger to the effective signal peptide coding region of filamentous fungal host cellPowder enzyme, aspergillus niger glucoamylase, rhizomucor miehei aspartic protease, special humic mould (Humicola insolens)The signal peptide coding region that the gene of cellulase and pubescence humicola lanuginosa (Humicola lanuginose) lipase obtains.
The signal peptide useful to yeast host cell obtained by saccharomyces cerevisiae α-factor and saccharomyces cerevisiae invertase gene.Romanos et al., 1992, the same other useful signal peptide coding region of having described.
Described control sequence can also be the front peptide-coding region that coding is positioned at the aminoterminal amino acid sequence of polypeptide. GainedPolypeptide is called as proenzyme (proenzyme) or front polypeptide (propolypeptide) (is called proenzyme in some occasions(zymogen)). Normally non-activity of front polypeptide, can be by catalysis or the autocatalysis cracking of the propetide from front polypeptideChange ripe active peptides into. Front peptide-coding region can be by bacillus subtilis alkali proteinase (aprE), bacillus subtilisNeutral proteinase (nprT), saccharomyces cerevisiae α-factor, rhizomucor miehei aspartic protease and thermophilic fungus destroyed wireThe gene of (Myceliophthora thermophila) laccase (WO95/33836) obtains.
When signal peptide and pre-peptide region are all present in the amino terminal of polypeptide, pre-peptide region is positioned at the amino end of adjacent polypeptideThe position of end, signal peptide region is positioned at the aminoterminal position of adjacent pre-peptide region.
Adding with respect to the growth of host cell allows to regulate the adjusting sequence of expression of polypeptides also may need. RegulateThe example of system is to cause the expression response chemistry of gene or physical stimulation thing to comprise regulating the existence of compound and beat and open or closeThose that close. Regulating system in prokaryotic system comprises lac, tac and trp operon system. In yeast, can useADH2 system or GAL1 system. In filamentous fungi, TAKA AMS promoter, aspergillus niger glucoamylase promoter andAspergillus oryzae glucoamylase promoter can be with making adjustments sequence. Other example that regulates sequence is that of permission gene magnificationA bit. In eukaryotic system, these are included in methotrexate (MTX) and have the dihydrofolate reductase gene of lower amplification and follow heavy metalAnd the metallothionein gene of amplification. In these examples, the nucleotide sequence of coded polypeptide can operate and be connected with adjusting sequence.
Above-mentioned multiple nucleotides and control sequence can be linked together to prepare recombinant expression carrier, it can compriseOne or more restriction sites are easily listed in the insertion in these sites or get with the nucleotides sequence that allows coding said polypeptideGeneration. Or, can be by the nucleotide sequence that comprises described sequence or nucleic acid construct be inserted to the suitable carrier for expressingIn express nucleotide sequence of the present invention. In construction of expression vector process, described coded sequence is placed in to carrier, so thatDescribed coded sequence is operationally linked together for expressing with suitable control sequence.
Described recombinant expression carrier can be any carrier (for example, plasmid or virus), can use it for easily heavilyGroup DNA process also can cause the expression of described nucleotide sequence. The selection of carrier typically depends on described carrier and this yearThe compatibility of body host cell to be imported. Described carrier can be plasmid linear or closed ring.
Described carrier can be autonomously replicationg vector, that is, the carrier existing as the outer entity of chromosome, it copies and is independent ofChromosome replication, for example, plasmid, extra-chromosomal element, minichromosome or artificial chromosome.
Described carrier can comprise any mode for guaranteeing self-replacation. Or described carrier can be when importingTo in host cell time, be incorporated into the carrier copying together with the one or more chromosomes that are integrated in genome and with it.In addition, can use comprise to import the single carrier of all DNA in host cell gene group or plasmid or two orMultiple carriers or plasmid, or transposons.
Carrier of the present invention preferably comprises one or more can selected marker, and it is thin that it allows to select easily to transformBorn of the same parents. Selectable mark is gene, and its product provides antiseptic or virus resistance, heavy metal resistance, prototrophy to auxotrophyType, etc.
Appropriate flags for yeast host cell is ADE2, HIS3, LEU2, LYS2, MET3, TRP1 and URA3. Be used forFilamentous fungal host cell can selected marker include but not limited to that (ornithine carbamyl turns for amdS (acetamidase), argBMove enzyme), bar (careless ammonium phosphinothricin acetyl based transferase), hygB (hygromix phosphotransferase), niaD (nitrate reductase), pyrG (breastClear glycosides-5 '-phosphate decarboxylase), sC (sulfate adenylyl transferase), trpC (o-amino benzoyl acid synthase) and equivalent thereof.
What be preferred for aspergillus cell is amdS and pyrG gene and the streptomyces hygroscopicus of aspergillus nidulans or aspergillus oryzaeBar gene.
Carrier of the present invention preferably comprise allow described carrier stable integration in host cell gene group or allow instituteState carrier and in cell, be independent of genome and one or more elements of self-replicating.
In order to be incorporated in host cell gene group, described carrier may rely on the nucleotide sequence of coded polypeptide or forCarrier by homology or non-homogeneous restructuring stable integration to any other carrier element in genome. Or described carrier canTo comprise extra nucleotide sequence, described extra nucleotide sequence is used in reference to conducting and crosses homologous recombination to host cell geneDirectional integration in group. Described extra nucleotide sequence make described carrier can be incorporated in host cell gene group one orOne or more exact positions in multiple chromosome. In order to increase the possibility that is integrated in exact position, described integrated elementShould preferably comprise the nucleotides of enough numbers, as 100 to 1,500 base-pairs, preferably 400 to 1,500 base-pairs, optimumSelect 800 to 1,500 base-pairs, itself and corresponding target sequence height homology, to increase the probability of homologous recombination. Described integration is firstPart can be the sequence of the target sequence homology in any and host cell gene group. In addition, described integrated element can be non-volumeCode or coding nucleotide sequence. On the other hand, described carrier can pass through the genome of non-homogeneous recombination and integration to host cellIn.
For self-replicating, described carrier can further comprise replication origin, and described replication origin makes described carrier energyEnough self-replicatings in discussed host cell. Bacterium replication origin example be to allow the matter that copies in Escherichia coliThe replication origin of grain pBR322, pUC19, pACYC177 and pACYC184, the pUB110 that allows to copy in bacillus,The replication origin of pE194, pTA1060 and pAM β 1. The example that is used for the replication origin of yeast host cell is 2 microns(2micron) combination of the combination of replication origin, ARS1, ARS4, ARS1 and CEN3 and ARS4 and CEN6. Replication origin canTo be the replication origin with sudden change, described sudden change make its in host cell, play temperature sensitivity effect (referring to, for example, Ehrlich，1978，Proceedings of the NationalAcademy of Sciences USA75：1433)。
The nucleotide sequence of the present invention that exceedes a copy can be inserted in host cell to increase gene outcomeProduction. Can be by least one additional copy of sequence is incorporated in host cell gene group, or by expandingIncrease can selected marker gene be included in nucleotide sequence together with, and obtain the increase of nucleotide sequence copy numbers; Wherein logicalCross cultured cell under suitable can selective reagent existence, and select to comprise can selected marker gene amplification copy, alsoThereby the cell of the additional copy that comprises nucleotide sequence.
Those skilled in the art for connecting said elements to build the method for recombinant expression carrier of the present inventionKnow (referring to, for example, Sambrook et al., 1989, the same).
Host cell:The invention still further relates to restructuring fermentation fungi, or the host who comprises nucleic acid construct of the present invention is thinBorn of the same parents, it is advantageously used in (on site) on the spot recombinant production of polypeptide. The carrier that comprises nucleotide sequence of the present invention is introduced intoIn host cell so as described carrier as chromosome composition part or as before the self-replacation sex chromosome describedOuter carrier exists.
Described host cell is fungal cell. " fungi " used herein comprises Ascomycota (Ascomycota), basidiomycetesDoor (Basidiomycota), chytrid door (Chytridiomycota) and Zygomycota (Zygomycota) are (as HawksworthEt al., at Ainsworth and Bisby ' s Dictionary ofThe Fungi, the 8th edition, 1995, CABInternational, University Press, Cambridge, defines in UK) and oomycetes subphylum (Oomycota) (asHawksworth et al., 1995, the same, quote for 171 pages) and all mitospore fungi (HawksworthEt al., 1995, the same).
In a more preferred embodiment, described fungal host cells is filamentous fungal cells. " filamentous fungi " comprises veryThe all thread form (as Hawksworth et al., 1995, the same definition) of bacterium and oomycetes subphylum. Described filamentous fungiTaking the mycelia body wall that formed by chitin, cellulose, glucan, chitosan, mannosan and other complex polysaccharide asFeature. Extend into by mycelia that row is nourished and grown and carbon catabolism is strict aerobic.
In preferred embodiments, filamentous fungal host cell is thermophilic or the cell of heat-resisting fungi, for example sac fungusSpecies in subphylum (Ascomycotina), Basidiomycotina (Basidiomycotina), Zygomycota or chytrid door, special(as too auspicious by Chaetomium (Chaetomium), Thermoascus, Malbranchea or the mould genus of shuttle spore shell (Thielavia)This shuttle spore shell mould (Thielavia terrestris)) or the group of Peziza (Trichophaea) composition in species. MorePreferred described host cell is that Trichophaeasaccata or humic are mould as Humicola insolens bacterial strain.
Fungal cell can form in a manner known way protoplast by relating to, transform protoplast and regenerationThe method of cell membrane transforms. Be described in EP 238 023 and Yelton for the suitable method that transforms aspergillus host cell et al.，1984，Proceedings of the National Academyof Sciences USA81：1470-1474。Malardier et al., 1989, Gene 78:147-156 and WO 96/00787 have described for transforming the mould species of reaping hookSuitable method. Can utilize Beckerand Guarente, In Abelson, J.N.and Simon, M.I., editors, Guide to Yeast Geneticsand Molecular Biology，Methods in Enzymology，Volume 194，pp182-187，Academic Press，Inc.，New York；Ito et al.，1983，Journal of Bacteriology 153：163；and Hinnen et al.，1978，Proceedings of the NationalMethod transformed yeast described in Academy of SciencesUSA 75:1920.
The expression of enzyme in plant
Can be as described below in genetically modified plants, transform and express coding polypeptide of interest as heterozyme of the present invention orThe variant of wild-type enzyme or the DNA sequence dna of heterozygote.
Described genetically modified plants can be dicots or monocotyledonous, are called for short dicotyledon or monocotyledon. SingleThe example of cotyledon plant is grass, as meadow grass (blue grass, Poa L. (Poa)), and fodder grasses, as sheep lance (Festuca),Rye (Lolium), temperate zone grass (temperate grass), as Agrostis (Agrostis), and cereal, for example, wheat, swallowWheat, rye, barley, rice, Chinese sorghum and maize (corn).
The example of dicotyledon is tobacco, legume (as lupin), potato, beet, pea, soya bean (bean)And soybean (soybean), and crucifer (Cruciferae (Brassicaceae)), as cauliflower, rape and closely phaseThe model organism arabidopsis (Arabidopsis thaliana) closing.
The example of plant part is stem, callus, leaf, root, fruit, seed and stem tuber (tuber) and comprises theseThe independent body of part, for example, epidermis, mesophyll, interstitial tissue (parenchyme), vascular tissue, separate living tissue. Upper and lower at thisWen Zhong, specific plant cell cell, as chloroplaset, apoplast, mitochondria, vacuole, peroxisome and cytoplasm are also recognizedFor being plant part. In addition, no matter any plant cell, organize what origin is, is all considered to plant part. Equally, plantThing part, as separated so that the particular organization of utilization of the present invention and cell are also considered to plant part, for example, embryo, embryoBreast, aleuron and seed coat.
The offspring of these plants, plant part and plant cell is also included within scope of the present invention.
Can be according to genetically modified plants or the plant cell of methods known in the art construction expression polypeptide of interest. SimplyGround is said by one or more expression construct of coding polypeptide of interest are incorporated in plant host genome and by gainedThe plant through transformation or plant cell breeding build plant or plant cell for genetically modified plants or plant cell.
Expediently, described expression construct is DNA construct, and it comprises coding adjusting order polypeptide of interest and suitableRow can operative association gene, described adjusting sequence is that described gene is expressed required in selected plant or plant part. ThisOutward, described expression construct can comprise the mark selected that has been incorporated into host cell wherein for the identification of expression constructNote and described construct is imported to DNA sequence dna essential in discussed plant (the latter depends on that the DNA that will use importsMethod).
For example according to described enzyme require when, where and how to express and determine that regulating and controlling sequence is (as promoter and endOnly subsequence and optional signals or transit sequence) selection. For example, the encode expression of gene of enzyme of the present invention can be groupMoulding or derivable, or can be growth, stage or tissue-specific, and gene outcome can be directed to spyDetermine cell cell, tissue or plant part as seed or leaf. As Tague et al, Plant Phys., retouches in 86,506,1988State regulating and controlling sequence.
In order to carry out constructive expression, can use 35S-CaMV, maize ubiquitin 1 and rice actin 1 promoter (Franck et al.1980.Cell21：285-294，Christensen AH，SharrockRA and Quail 1992.Maize polyubiquitin genes：structure，thermal perturbationof 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 activity in transgenicRiceplants.Plant Cell 3,1155-1165). Organ specific promoters can be for example from thesaurus(storage sink) tissue as seed, potato tubers and fruit (Edwards & Coruzzi,1990.Annu.Rev.Genet.24:275-303), or from metabolic pool (metabolic sink) tissue as separate living tissueThe promoter of (Ito et al., 1994, Plant Mol.Biol.24:863-878), seed specific promoters is as from waterPaddy albumen, alcohol soluble protein, globulin or albuminous promoter (Wu et al., Plantand Cell Physiology Vol.39，No.8pp.885-889(1998))，Conrad U.et al，Journalof Plant PhysiologyVol.152, No.6, the legumin B4 from broad bean (Viciafaba) and unknown seed that pp.708-711 (1998) describesThe broad bean promoter of albumen, from promoter (Chen et al., the Plant and Cell of seed oil body proteinPhysiology, Vol.39, No.9, pp.935-941 (1998), from the storage of cabbage type rape (Brassica napus)Albumen napA promoter, or any other seed specific promoters known in the art, for example, described in WO91/14772. In addition, described promoter can be that leaf specificity promoter from paddy rice or tomato is as rbcs promoter (KyozukaEtal., Plant Physiology, Vol.102, No.3, pp.991-1000 (1993), chlorella virus adenine methyl turnsMove enzyme gene promoter (Mitra, A.and Higgins, DW, Plant Molecular Biology, Vol.26, No.1,Pp.85-93 (1994), or from aldP gene promoter (Kagaya et al., the Molecular and General of paddy riceGenetics, Vol.248, No.6, pp.668-674 (1995) or wound inducible promoter are as potato pin2 promoter(Xu et al, Plant Molecular Biology, Vol.22, No.4, pp.573-588 (1993). Equally, described startupSon can be induced as temperature, arid or salinity change by abiotic processing, or the activation applying by outsideThe material of promoter, for example, ethanol, estrogen, plant hormone sample ethene, abscisic acid and gibberellic acid and heavy metal are induced.
Promoter enhancer element is used in the higher expression of enzymes of acquisition in plant. For example, described promoter enhancerAssembly can be the introne between promoter and the nucleotide sequence of codase. For example, Xu et al.opcit is openRice actin 1 gene First Intron strengthen express purposes.
Can selectable marker gene and any other parts of expression construct can existingly from this area select those.
Described DNA construct is incorporated in Plant Genome according to conventional art known in the art, comprises Agrobacterium(Agrobacterium) conversion of mediation, virus-mediated conversion, microinjection, particle bombardment, Bombardment-Mediated Transformation and electricity are wornHole (Gasser et al, Science, 244,1293; Potrykus, Bio/Techn.8,535,1990; Shimamoto et al，Nature，338,274，1989)。
At present, the transgenosis of Agrobacterium tumefaciems (Agrobacterium tumefaciens) mediation is to turn in order to produce(summary is referring to Hooykas & Schilperoort, 1992, Plant for Gene Double cotyledon plant and the method selectedMol.Biol., 19:15-38), also can be for transforming monocots, although conventionally use turning of other for these plantsChange method. The desirable monocotyledonous method of production transgenosis of at present, Agrobacterium means being supplemented is to embryo callusParticle bombardment (with the coated micro-gold of transforming DNA or tungsten particle) (Christou, 1992, the Plant of tissue or developmental embryo J.，2：275-281；Shimamoto，1994，Curr.Opin.Biotechnol.，5：158-162；Vasil et al.，1992, Bio/Technology 10:667-674). Be used for the alternative of transforming monocots with Omirulleh S, etAl., PlantMolecular Biology, Vol.21, No.3, the described protoplast transformation of pp.415-428 (1993) is basePlinth.
After conversion, select to have mixed the transformant of described expression construct and according to method breeding well known in the art beComplete plant. Conventionally described method for transformation is designed for regeneration period or after production in utilize for example use twoIndividual independently T-DNA construct carries out cotransformation or carries out the locus specificity excision of Select gene by specificity recombinaseSelective removal Select gene.
Starch processing
First, the polypeptide of second and/or the 3rd aspect can, in the method for liquefying starch, wherein be situated between at waterIn matter, process gelatinization or pearl starch substrate with described heterozyme. First, the polypeptide of second and/or the 3rd aspect alsoCan be in the method for saccharifying of liquefying starch substrate. Preferred purposes is in fermentation process, starch substrates in the methodAt first, liquefaction and/or saccharification are suitable for by fermenting organism to produce under the existence of polypeptide aspect second and/or the 3rdPreferred yeast is converted into glucose and/or the maltose of tunning. These fermentation process comprise produces fuel ethanol or drinkBy the method for ethanol (portable alcohol), the method for preparation of drinks, the method for producing required organic compound, as lemonAcid, itaconic acid, lactic acid, gluconic acid, gluconic acid sodium salt, calcium gluconate, potassium gluconate, gluconic acid Δ lactone or sodium isoascorbate;Ketone; Amino acid, as glutamic acid (monosodium glutamate (sodium monoglutaminate)), is difficult to by synthetic method raw in additionThe more complex compounds that produce are as antibiotic, as penicillin, tetracycline; Enzyme; Vitamin, as riboflavin, B12, beta carotene;Hormone.
Starch to be processed can be highly refined starch quality, preferably at least 90%, at least 95%, at least 97%Or at least 99.5% is pure, or it can be the starch-containing material of the thicker whole grain that comprises grinding, and it comprises non-starchPart is as plumule residue and fiber. Raw material are polished to open tissue as complete grain, thereby can further process. According to thisIt is preferred inventing two kinds of polishings: wet-milling and dry grinding. Also can apply maize pulp, preferably the maize pulp through grinding.
Except starch, dry also will comprise a large amount of non-starch carbohydrates through grinding grain. When passing through sprayPenetrate boiling (jet cooking) while processing this heterogeneous material, conventionally only reach the part gelatinization of starch. Due to of the present inventionPolypeptide has the high activity for non-gelatinized starch, thereby advantageously described polypeptide is applied to and comprises through jet cookingDry and through grind that starch liquefies and/or the method for saccharification in.
In addition, due to the superior hydrolysing activity of the polypeptide of first aspect, the need to glucoamylase during saccharification stepAsk greatly and reduce. This permission is carried out saccharification under extremely low glucoamylase activity level, and preferred glucoamylase activityDisappearance or if present, be no more than or even less than 0.5AGU/g DS, more preferably no more than or even fewIn 0.4AGU/g DS, be more preferably be no more than or even less than 0.3AGU/g DS, be most preferably less than 0.1AGU/g DS, asBe no more than or exist even less than the amount of 0.05AGU/gDS starch substrates. What represent with mg zymoprotein has a glucoamylaseActive enzyme or disappearance, or be no more than or even less than 0.5mg EP/g DS, more preferably no more than or even fewIn 0.4mg EP/g DS, be more preferably be no more than or even less than 0.3mg EP/g DS, be most preferably not exceeding or evenBe less than 0.1mg EP/g DS, be for example no more than or even less than 0.05mg EP/g DS or be no more than or even less thanThe amount of 0.02mg EP/g DS starch substrates exists. Described glucoamylase can preferably derive from the bacterial classification, basket of aspergillusBacterial strain in the bacterial classification of the bacterial classification of Pseudomonas, the bacterial classification of Pachyktospora or Trametes, more preferably comes from aspergillus niger, Ai Mosen is basketBacterium (Talaromyces emersonii), lobe ring bolt bacterium or the large decorative pattern spore of papery (Pachykytospora papyracea).
Same due to the superior hydrolysing activity of the polypeptide of first aspect, in liquefaction and/or saccharification step to AMSDemand greatly reduce. The polypeptide of first aspect representing with mg zymoprotein can be no more than or even less than 0.5mgEP/g DS, more preferably no more than or even less than 0.4mg EP/gDS, be more preferably and be no more than or even less than 0.3mgEP/g DS, be most preferably not exceeding or even less than 0.1mg EP/g DS, for example, be no more than or even less than 0.05mgEP/gDS or be no more than or even less than the amount preparation of 0.02mg EP/g DS starch substrates. The polypeptide of first aspect canWith with 0.05 to 10.0AFAU/g DS, preferably 0.1 to 5.0AFAU/g DS, more preferably 0.25 to 2.5AFAU/g DS starchAmount preparation. Described method can comprise: a) by starch substrates with comprise catalytic module and the carbon aquation with alpha-amylase activityThe polypeptide of compound binding modules, for example, the polypeptide contact of first aspect; B) in being enough at least 90% or at least 92%, extremelyAt the bottom of described starch few 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99.5%w/wThing is converted in the temperature and time of fermentable sugars, and described starch substrates is hatched together with described polypeptide; C) fermenting and producing is sent outFerment product, d) optionally reclaims tunning. At treatment step b) and/or c), have glucoamylase activity enzyme orDisappearance, or with 0.001 to 2.0AGU/gDS, 0.01 to 1.5AGU/g DS, 0.05 to 1.0AGU/gDS, 0.01 to 0.5AGU/The amount of g DS exists. Preferably there is enzyme or the disappearance of glucoamylase activity, or to be no more than or to be even less than0.5AGU/g DS, more preferably no more than or be even less than 0.4AGU/g DS, be preferably no more than or be even less than again0.3AGU/gDS, be most preferably not exceeding or be even less than 0.1AGU, forming sediment as being no more than or being even less than 0.05AGU/g DSThe amount of foundation cream thing exists. The enzyme with glucoamylase activity or the disappearance that represent with mg zymoprotein, or being no more than orPerson even less than 0.5mgEP/g DS, more preferably no more than or even less than 0.4mg EP/g DS, be more preferably be no more than orPerson even less than 0.3mg EP/g DS, be most preferably not exceeding or even less than 0.1mg EP/g DS, be for example no more than orEven less than 0.05mg EP/g DS or be no more than or exist even less than the amount of 0.02mg EP/g DS starch substrates. ?In described method, step a, b, c and/or d can carry out individually or simultaneously.
Described method can comprise on the other hand: a) connect by starch substrates and through the yeast cells transforming to express polypeptideTouch, described polypeptide comprises catalytic module and the carbohydrate binding modules with alpha-amylase activity, for example, first and/Or the polypeptide of second aspect; B) in be enough to by the described starch substrates of 90%w/w be at least converted into fermentable sugars temperature andIn time, described starch substrates is hatched together with described yeast; C) fermentation is to produce ethanol; D) optionally reclaim ethanol. Step a,B and c can carry out separately or simultaneously.
The hydrolysis, particularly pearl starch that described in another aspect, method comprises gelatinization or pearl starch slurry is lower than instituteState at the temperature of initial gelatinization point of pearl starch and be hydrolyzed to soluble starch hydrolysate. Except thering is α-shallow lake with comprisingThe polypeptide of the catalytic module of powder enzymatic activity and carbohydrate binding modules, for example, outside the polypeptide contact of first aspect, instituteStating starch can also contact with the enzyme that is selected from lower group: fungal alpha-amylase (EC3.2.1.1), beta amylase (E.C.3.2.1.2),And glucoamylase (E.C.3.2.1.3). Can further add in embodiments bacterialα-amylase or debranching enzyme, for exampleIsoamylase (E.C.3.2.1.68) or amylopectase (E.C.3.2.1.41). Bacterium alphalise starch in the context of the present inventionEnzyme be as in WO99/19467 the 3rd page the 18th walk to the 6th page of the 27th defined AMS of row.
Described method is implemented at the temperature lower than initial gelatinization point in embodiments. While preferably implementing described methodTemperature be at least 30 DEG C, at least 31 DEG C, at least 32 DEG C, at least 33 DEG C, at least 34 DEG C, at least 35 DEG C, at least 36 DEG C, at least 37DEG C, at least 38 DEG C, at least 39 DEG C, at least 40 DEG C, at least 41 DEG C, at least 42 DEG C, at least 43 DEG C, at least 44 DEG C, at least 45 DEG C, extremelyFew 46 DEG C, at least 47 DEG C, at least 48 DEG C, at least 49 DEG C, at least 50 DEG C, at least 51 DEG C, at least 52 DEG C, at least 53 DEG C, at least 54DEG C, at least 55 DEG C, at least 56 DEG C, at least 57 DEG C, at least 58 DEG C, at least 59 DEG C or preferably at least 60 DEG C. While implementing described methodPH can be 3.0 to 7.0, preferably 3.5 to 6.0 or more preferably within the scope of 4.0-5.0. In preferred embodiments, described sideMethod for example comprises at approximately 32 DEG C, as the temperature of 30 to 35 DEG C with culture propagation for example to produce ethanol.
In another preferred embodiment, described method for example comprises at 30 to 35 DEG C, for example the temperature of approximately 32 DEG C withTime saccharification and fermentation, for example with yeast to produce ethanol, or required organic to produce with the suitable fermenting organism of another kindCompound.
In above-mentioned fermentation process, ethanol content reaches at least 7%, at least 8%, at least 9%, at least 10%, at least11%, at least 12%, at least 13%, at least 14%, at least 15%, as at least 16% ethanol.
Can there is the dry solids shape starch of 20-55% for the starch slurry of above-mentioned either side, preferably 25-40% dry solids shape starch, more preferably the dry solids shape starch of 30-35%. There is AMS with comprisingActive catalytic module and the polypeptide of carbohydrate binding modules, for example, after the polypeptide contact of first aspect, graininess is formed sedimentThe drying solid of powder 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%Be converted into soluble starch hydrolysate.
In another preferred embodiment, catalytic module and the carbohydrate combination with alpha-amylase activity will be comprisedThe polypeptide of module, for example, the polypeptide of first aspect is for liquefaction, the method for saccharifying of gelatinized starch, such as but not limited to logicalCross the gelatinization that jet cooking carries out. Described method can comprise that fermentation is to produce such as ethanol of tunning. This from starch-containingMaterial comprises by the method for fermentative production of ethanol: (i) with comprising catalytic module and the carbon hydrate with alpha-amylase activityThe polypeptide of thing binding modules, for example, the described starch-containing material of polypeptide liquefaction of first aspect; (ii) liquefaction that saccharification obtainsWine with dregs; (iii) there is at fermenting organism the material obtaining in bottom fermentation step (ii). Optional described method further comprises recovery secondAlcohol. Saccharification and fermentation can be used as synchronous glycosylation and fermentation process (SSF method) is implemented. Between yeast phase, ethanol content reaches at least7%, at least 8%, at least 9%, at least 10%, at least 11%, at least 12%, at least 13%, at least 14%, at least 15% as extremelyFew 16% ethanol.
Especially, in the method aspect above-mentioned, starch to be processed can be from stem tuber, root, stem, legume, paddyThing or whole grain obtain. More particularly, pearl starch can be from corn, corncob (cobs), wheat, barley, rye, buy sieveJowar, sago, cassava, tapioca, Chinese sorghum, paddy rice, pea, soya bean (bean), banana or potato obtain. Special consideration is glutinousType and non-glutinous type corn and barley.
The invention still further relates to the composition of the polypeptide that comprises first and/or second aspect. In particularly preferred enforcementThe polypeptide that composition described in scheme comprises first aspect, described polypeptide be selected from 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、The group of V057, V059, V060, V061, V063, V064, V065, V066, V067, V068 and V069. Described composition can enterOne step comprises the enzyme that is selected from lower group: fungal alpha-amylase (EC3.2.1.1), beta amylase (E.C.3.2.1.2), glucoamylaseAnd amylopectase (E.C.3.2.1.41) (E.C.3.2.1.3). Described glucoamylase can preferably come from the bacterium of aspergillusKind bacterial strain as aspergillus niger or come from the bacterial classification of Talaromyces, particularly come from the bacterium of Talaromyces leycettanusStrain, as United States Patent (USP) Re.32, disclosed glucoamylase in 153, come from Talaromyces duponti and/orTalaromyces thermopiles, as United States Patent (USP) 4,587, disclosed glucoamylase in 215, and more preferably come fromTalaromyces emersonii. Most preferably described glucoamylase derives from Talaromyces emersonii bacterial strain CBS 793.97 and/or hasIn WO99/28448 as the disclosed sequence of SEQ ID NO:7. More preferably have with aforementioned amino acid sequence and have at least 50%, at least60%, the glucose starch of the amino acid sequence of at least 70%, at least 80%, at least 90% or even at least 95% homologyEnzyme. The basket bacterium glucose starch of business enzyme preparation is supplied by Novozymes A/S, is called Spirizyme Fuel.
For comprising first and/or the polypeptide of second aspect and the composition of glucoamylase, also preferably there is PortugalThe polypeptide of the bacterial strain that comes from Trametes, preferred lobe ring bolt bacterium of saccharogenic amylase activity. More preferably there is glucoamylase activity alsoAnd with U.S. Patent application No.60/650, in 612 the amino acid of the mature polypeptide amino acid/11 to 575 of SEQ ID NO:5 have toThe polypeptide of few 50%, at least 60%, at least 70%, at least 80%, at least 90% or even at least 95% homology.
For comprising first and/or the polypeptide of second aspect and the composition of glucoamylase, also preferably there is PortugalSaccharogenic amylase activity come from Pachyktospora, preferably the large decorative pattern spore of papery bacterial strain or come from and be deposited in DSMZ and protectThe polypeptide of the coli strain of Tibetan DSM17105. More preferably there is glucoamylase activity and and U.S. Patent applicationNo.60/650, in 612 the amino acid of the mature polypeptide amino acid/11 to 556 of SEQ ID NO:2 have at least 50%, at least 60%,The polypeptide of at least 70%, at least 80%, at least 90% or even at least 95% homology.
Above-mentioned composition can be used for liquefaction and/or saccharification gelatinization or granular starch, and the starch of part gelatinization.The starch of part gelatinization refers to a certain extent by the starch of gelatinization, wherein partial starch irreversibly expansion and gelatinization andPartial starch still exists with graininess state.
Above-mentioned composition can preferably comprise with 0.01 to 10AFAU/g DS, preferably 0.1 to 5AFAU/gDS, more preferably0.5 to 3AFAU/g DS, the acid alpha-amylase that most preferably amount of 0.3 to 2AFAU/g DS exists. Can be by described compositionBe applied in above-mentioned arbitrary starch process.
Materials and methods
The mensuration of acid alpha-amylase activity
When time used according to the invention, can measure any acid alphalise starch with AFAU (acid fungal alpha-amylase unit)The activity of enzyme, it is with respect to enzyme standard test. 1AFAU is defined as degraded per hour under the standard conditions of mentioning belowThe amount of the enzyme of 5.260mg starch dry matter.
Acid alpha-amylase, i.e. sour stable AMS, a kind of inscribe-AMS (Isosorbide-5-Nitrae-α-D-glucan-grapeGlycosyl-hydrolase (Isosorbide-5-Nitrae-alpha-D-glucan-glucano-hydrolase), E.C.3.2.1.1), at starch moleculeInterior zone hydrolyzing alpha-Isosorbide-5-Nitrae-glycosidic bond is to form dextrin and the oligosaccharides with different chain length. With iodine form color intensity withThe concentration of starch is directly proportional. Amylase activity under the analysis condition of specifying with the reverse colorimetric method of the reduction of starch concentration(reverse colorimetry), measures.
Indigo plant/purple t=23 discolors second
Standard conditions/reaction condition:
Substrate: soluble starch, about 0.17g/L
Buffer solution: citrate, about 0.03M
Iodine (I2): 0.03g/L
CaCl2： 1.85mM
pH： 2.50±0.05
Incubation temperature: 40 DEG C
Reaction time: 23 seconds
Wavelength: 590nm
Enzyme concentration: 0.025AFAU/mL
Enzyme working range: 0.01-0.04AFAU/mL
The brochure of this analytical method is described in more detailEB-SM-0259.02/01Can be to NovozymesA/S, Denmark's ropeGet, this brochure is added as a reference herein.
Glucoamylase activity
Can measure glucoamylase activity with amyloglucosidase unit (AGU). AGU be defined as 37 DEG C,PH4.3, substrate: maltose 23.2mM, buffer solution: hydrolysis per minute under acetate 0.1M, the standard conditions in 5 minutes reaction timeThe amount of the enzyme of 1 micromole's maltose.
Can use automatic analysis instrument system. In GDH reagent, add mutarotase, so that existingWhat alpha-D-glucose is all converted into β-D-Glucose. In above-mentioned reaction, GDH is anti-with β-D-Glucose specificallyShould form NADH, utilize photometer to measure NADH at 340nm place, as measuring of initial glucose concentration.
AMG is hatched:
Substrate: maltose 23.2mM
Buffer solution: acetate 0.1M
Ph： 4.30±0.05
Incubation temperature: 37 DEG C ± 1
Reaction time: 5 minutes
Enzyme working range: 0.5-4.0AGU/mL
Color reaction:
GlucDH： 430U/L
Mutarotase: 9U/L
NAD： 0.21mM
Buffer solution: phosphate 0.12M; 0.15M NaCl
pH： 7.60±0.05
Incubation temperature: 37 DEG C ± 1
Reaction time: 5 minutes
Wavelength: 340nm
The brochure (EB-SM-0131.02/01) of describing in more detail this analytical method can be to Novozymes A/S, pelletWheat is asked for, and this brochure is added as a reference herein.
Bacterial strain and plasmid
Escherichia coli DH12S (can be obtained by Gibco BRL) is for yeast plasmid rescue (rescue).
PLA1 is saccharomyces cerevisiae and the shuttle vehicle under the control of TPI promoter, in WO 01/92502Having described it builds from pJC039. Acid black aspergillus AMS burst, acid black aspergillus α-shallow lake are wherein insertedPowder enzyme gene (SEQ ID NO:1) and comprise joint (SEQ ID NO:67) and part sieve ear of CBM (SEQ ID NO:91)Ah too bacterium glucoamylase gene sequence. In SEQ ID NO:103, provide the complete sequence of described plasmid. Alpha-amylase geneFor from 5029 to 6468 sequence, joint is from 6469 to 6501 sequence, and CBM is from 6502 to 6795 sequence. Described yearBody builds for AMS CBM heterozygote.
Saccharomyces cerevisiae YNG318:MATa Dpep4[cir+] ura3-52, leu2-D2, his4-539 is used to AMSVariant is expressed. Its description is shown in to J.Biol.Chem.272 (15), pp9720-9727,1997.
Culture medium and substrate
10X base soln:Containing amino acid whose yeast nitrogen base (DIFCO) 66.8g/l, succinate (salt) 100g/l, NaOH60g/l。
SC-glucose:20% glucose (, final concentration=2g/100ml of 2%)) 100ml/l, 5% threonine 4ml/L, 1% tryptophan 10ml/l, 20% casamino acid 25ml/l, 10X base soln 100ml/l. Solution is micro-with aperture 0.20The filter sterilised of rice. Agar and H2O (about 761ml) autoclaving together, and the SC-glucose solution of independent sterilizing is addedTo described agar solution.
YPD：Bacto peptone 20g/l, yeast extract 10g/l, 20% glucose 100ml/l.
PEG/LiAc solution:40%PEG400050ml, 5M lithium acetate 1ml.
DNA operation
Except as otherwise noted, DNA operation and conversion adopt Sambrook et al. (1989) MolecularCloning:A Laboratory Manual，Cold Spring Harbor Lab.，Cold Spring Harbor，NY；Ausubel， F.M.et al.(eds.)″Current Protocols in Molecular Biology″，JohnWiley and Sons，1995; Harwood, C.R.and Cutting, the standard molecular biological method described in S.M. (eds.) is carried out.
Yeast conversion
By lithium acetate method enforcement yeast conversion. By the carrier of 0.5 μ L (digesting by restriction endonuclease) and 1 μ LPCR fragment mix. YNG318 competent cell thaws on ice. In 12ml polypropylene test tube (Falcon2059), mixThe carrier DNA (Clontech) of cell, DNA mixture and the 10 μ L of 100 μ L. Add 0.6ml PEG/LiAc solution mixed gentlyClose. 30 DEG C, 200rpm are hatched 30min. Hatch 30min (heat shock) for 42 DEG C. Transfer to eppendorf pipe also centrifugal 5 seconds. RemoveSupernatant is also dissolved in 3ml YPD. Hatch described cell suspension 45min for 200rpm30 DEG C. Pour described suspension into SC-grapeSugar is dull and stereotyped and hatch 3 days to produce bacterium colony in 30 DEG C. Use Nucleic AcidsResearch, Vol.20, No.14 (1992)Robzyk and Kassir ' the s method of describing in 3790 is extracted the total DNA of yeast.
DNA sequencing
Implement Escherichia coli by electroporation (BIO-RAD Gene impulse generator) and transform, for DNA sequencing. Use alkaline process(molecular cloning, Cold Spring Harbor) or usePlasmid kit is prepared DNA plasmid. Use QiagenGel extraction kit reclaims DNA fragmentation from Ago-Gel. With PTC-200 DNA Engine enforcement PCR. ABI PRISMTM310 Genetic Analyzer are for the mensuration of all dna sequences.
Table 2
Embodiment 1: coding Rhizomucor pusillus (Rhizomucor pusillus) alpha amylase and Luo Eratai bacteriumThe structure of the nucleotide sequence V019 of (Athelia rolfsii) glucoamylase CBM
With suitable restriction endonuclease digested vector pLAl, to cut away coding aspergillus niger AMS catalytic structureThe region in territory. With primer P001 (SEQ ID NO:104) and P002 (SEQ IDNO:105) pcr amplification Rhizomucor pusillus alphalise starchEnzyme gene, the fragment of amplification is as shown in SEQ ID NO:19.
Reclaim DNA fragmentation from Ago-Gel by Qiagen gel extraction kit. Purifying fragment and the carrier of gained disappearCompound is mixed together. The solution of mixing is imported in saccharomyces cerevisiae, to pass through recombination to construct expression plasmid pLAV019 in body.
Embodiment 2: the huge bracket fungus of encoding (Meripilus giganteus) alpha amylase and Luo Eratai bacterium glucose form sedimentThe structure of the nucleotide sequence V022 of powder enzyme CBM
With primer P003 (SEQ ID NO:106) and the huge bracket fungus alphalise starch of P004 (SEQ ID NO:107) pcr amplificationEnzyme gene.
Reclaim DNA fragmentation from Ago-Gel by Qiagen gel extraction kit. By the purifying fragment of gained with closingSuitable restriction endonuclease digestion and the carrier pLAl that cut away coding aspergillus niger AMS catalyst structure domain mixes. WillThe solution mixing imports in saccharomyces cerevisiae, to pass through recombination to construct expression plasmid pLAV022 in body.
Embodiment 3. expresses the amylase with CBM in aspergillus oryzae
Comprising of describing in embodiment 1 and 2 being respectively used to construction expression with the construct of the alpha amylase gene of CBM carriesBody pAspV019 and pAspV022. These two plasmids of pAspV019 and pAspV022 are made up of expression cassette, described expression cassette based onAspergillus niger neutral starch enzyme II promoter and aspergillus niger starch glycosidase (amyloglycosidase) terminator (Tamg), described inNeutral starch enzyme II promoter is blended in the targeting sequencing (Pna2/tpi) of aspergillus nidulans phosphotriose isomerase untranslated. DescribedOn plasmid, also have the aspergillus selected marker amdS from aspergillus nidulans, it allows on the acetamide as only nitrogen sourceGrowth. As Lassen et al. (2001), Applied and Environmental Micorbiology, 67,4701-Described in 4707, expression plasmid pAspV019 and pAspV022 are transformed in aspergillus. The transformant of expressing V019 and V022 is dividedFrom, purifying and be incubated in shaking flask. Sent out by aspergillus oryzae with protein affinity purification method (Biochem.J. (2003) 372,905-910) purifyingThe fluid nutrient medium that ferment obtains, described aspergillus oryzae is expressed the amylase with CBM.
Embodiment 4. is with the amylase of CBM
Produce polypeptide of the present invention; The catalyst structure domain of selection is blended in to connecing of Luo Eratai bacterium glucoamylaseHead-CBM region, is attached to C003 aspergillus oryzae catalyst structure domain (Fungamyl PE variant) by the CBM region of selection.
Because the CBM+ joint from Trichophaea saccata AMS is positioned at N-end, so be inserted inBetween SP288 signal and aspergillus oryzae catalyst structure domain. Other CBM is placed in C-end.
Variant V008 had both comprised the Luo Eratai bacterium glucoamylase joint and the CBM region that are placed in C end, also comprised and was placed inJoint+the CBM from Trichophaea saccata AMS of N-end.
The catalyst structure domain variant of the CBM variant of aspergillus oryzae AMS and Luo Eratai bacterium glucoamylase CBM respectivelyList in table 3 and 4. Other polypeptide that the present invention produces is listed in table 5 and 6.
Described variant, for starch, especially has the activity of improvement for pearl starch.
Table 3
Table 4
Table 5
Table 6
Embodiment 5
In fermenting on a small scale, use Talaromyces emersonii (Talaromyces emersonii) glucose starch of various doseThe performance of enzyme assessment polypeptide V019. By starch substrates, the crushing maize of 583.3g is added in 912.2g running water. To this mixingIn thing, supplement the 1g/L penicillin solution of 4.5ml. Use 40%H2SO4The pH of these slurries is adjusted to 5.0. The duplicate DS water of measuringPut down is 34.2 ± 0.8%. This about 5g slurries are added in 20ml phial. Each phial according to dosage adds appropriateEnzyme, adds 200 μ L yeast propagation thing/5g slurries afterwards. Actual dose taking the accurate weight of corn slurries in each phial asBasis. Phial is in 32 DEG C of insulations. After fermentation, pass in time and measure the loss in weight. 70 hours time, stop fermentation, and prepareHPLC analyzes. The preparation of HPLC comprises the 40%H by adding 50 μ L2SO4Cessation reaction, centrifugal and by 0.45 micronFilter filters. Wait for that the sample of HPLC analysis is in 4 DEG C of storages.
Table 7
Embodiment 6
By will be with heat-staple bacterialα-amylase (LIQUOZYME XTM, Novozymes A/S) liquefaction corn form sedimentDE11 maltodextrin prepared by powder is dissolved in Milli-QTMIn water, and dry solids content (DS) is adjusted to 30%,And for the preparation of the substrate of saccharification. Under 60 DEG C, the condition of initial pH4.3, prolonged agitation, in the 2ml glass vial of sealingIn carry out mashing test. Utilizing 0.35AGU/g DS Talaromyces emersonii glucoamylase and 0.04AFAU/g DS aspergillus nigerAfter the standard of acid alpha-amylase is processed, apply CBM AMS V019 or the V022 of two kinds of various dose at once.
In official hour interval sampling, and in boiling water, heat 15 minutes, with by enzyme-deactivating. After cooling, divide at HPLCAnalyse front by Sample Dilution to 5%DS and filter (Sartorius MINISARTTMNML0.2 micron). In following table 8, provide withThe glucose level that the percentage of total soluble-carbohydrate represents.
Table 8
Embodiment 7
In fermenting on a small scale, the raw starch SSF of assessment processes. Mix 410g fine grinding corn, 590ml running water, 3.0ml1g/L penicillin and 1g urea, the pearl starch that obtains 35%DS is starched. The pH of slurries is adjusted to 4.5 with 5N NaOH, by 5g sampleBe assigned in 20ml phial. Quantitatively add appropriate enzyme, to inoculation yeast in phial. Phial is in 32 DEG C of insulations. Every kindProcessing is in nonuplicate fermented. Select to come in triplicate the analysis as 24 hours, 48 hours and 70 hours points. In24, vortex phial 48 and 70 hours time. Time point analysis comprises weighs and prepares for the sample of HPLC phial. For enteringRow HPLC, by adding 50 μ L40%H2SO4Cessation reaction, centrifugal, and by 0.45 μ m filter filter. To wait for that HPLC analyzesSample in 4 DEG C of storages.
Embodiment 7a
Enzyme and the amount using are as shown in the table. A-AMG is aspergillus niger glucose starch enzymatic compositions.
Table 9
In the aspergillus niger AMG of 1.7-85.5AGU/AFAU and the ratio ranges of V019, observe 70 hours fermentation after veryGood alcohol yied, shows that the mixture of aspergillus niger AMG and V019 is having excellent performance within the scope of activity ratio widely.
Table 10
Embodiment 7b
Enzyme and the amount using are as shown in the table. A-AMG is Talaromyces emersonii glucose starch enzymatic compositions.
Table 11
In the Talaromyces emersonii AMG and V019 ratio ranges of 10-216AGU/AFAU, observe after fermentation in 70 hoursWell ethanol production, has shown the scope of activity ratio widely of the mixture of Talaromyces emersonii AMG and V019.
Table 12
Biomaterial preservation
Following biomaterial is deposited in Deutsche Sammmlung according to budapest treaty vonMicroorganismen und Zellkulturen GmbH(DSMZ)，Mascheroder Weg 1b，D-38124Braunschweig DE, and given following preserving number:
Preservation preserving number preservation date
Escherichia coli NN049798 DSM17106 on February 2nd, 2005
Escherichia coli NN049797 DSM17105 on February 2nd, 2005
Described bacterial strain is ensureing that patent and trademark committee member determines that according to 37C.F.R. § 1.14 and 35U.S.C. § 122 it has moneyThe people of lattice can obtain under the condition of this culture by preservation during present patent application is undecided. Described preserved material is by being protectedHide the pure culture substantially of bacterial strain. Submitting the correspondence application of described application or the foreign country that its son is applied for to, can be as thisThe described preserved material of the desired acquisition of Patent Law of a little countries. But, it should be understood that and can obtain this preserved material, do not formIn the patent right process of being authorized by action by government in infringement, implement license of the present invention.
<110>Novozymes Company (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>enzyme of processing for starch
<130>10729.500-US
<160>179
<170>PatentIn version 3.3
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Tyr Phe Leu Leu Thr Asp Arg Phe Gly Arg Thr Asp Asn Ser Thr Thr
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Ala Thr Cys Asp Thr Gly Asp Gln Ile Tyr Cys Gly Gly Ser Trp Gln
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Asn Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln His Tyr Ala
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Asp Gly Ser Gln Ile Val Thr Ile Leu Ser Asn Lys Gly Ala Ser Gly
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Asp Ser Tyr Thr Leu Ser Leu Ser Gly Ala Gly Tyr Thr Ala Gly Gln
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Gln Leu Thr Glu Val Ile Gly Cys Thr Thr Val Thr Val Gly Ser Asp
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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 Gly Arg
465 470 475 480
<210>4
<211>480
<212>PRT
<213>aspergillus oryzae (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 Gly Arg
465 470 475 480
<210>5
<211>1434
<212>DNA
<213>aspergillus oryzae (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 (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 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 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 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 Thr Ser 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 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 gac ctg agc 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 agc 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 agcgga 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 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 aae 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 age 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 Gln Ile Cys Val Gln Leu Ser Ser Gly G1y 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 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 (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 (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 A1a 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>bacterial classification (Acremonium sp.) of the mould genus of branch top spore
<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 G1u 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>bacterial classification (Acremonium sp.) of the mould genus of branch top spore
<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 (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 G1n 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 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 (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 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 Ser
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>huge bracket fungus (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 Val 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 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 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 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>huge bracket fungus (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 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 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>bacterial classification of Stereum (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 aec att gga gag 672
Phe Trp Pro Asp Phe Ala 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 acg 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 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>bacterial classification of Stereum (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 G1n 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 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 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>bacterial classification of Trametes (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 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>bacterial classification of Trametes (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 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>salmon shellfish leather covers bacterium (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 Mct 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 acg 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>salmon shellfish leather covers bacterium (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>bacterial classification (Dinemasporium sp.) of thorn shell bistrichiasis Pseudomonas
<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>bacterial classification (Dinemasporium sp.) of thorn shell bistrichiasis Pseudomonas
<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 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 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
G1u 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
<21l>1428
<212>DNA
<213>bacterial classification (Coniochaeta sp.) of cone Chaetomium
<220>
<221>GDS
<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 Ile 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 cea 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>bacterial classification (Coniochaeta sp.) of cone Chaetomium
<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 Ile 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>bacterial classification of look two spore Pseudomonas (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 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>bacterial classification of look two spore Pseudomonas (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>bacterial classification (Nectria sp.) of the red shell Pseudomonas of clump
<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 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 Asn 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>bacterial classification (Nectria sp.) of the red shell Pseudomonas of clump
<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 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>bacterial classification of Gliocladium (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>bacterial classification of Gliocladium (Gliocladium sp.)
<400>42
Ala Asp Thr A1a 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 agc 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 acg 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>the large decorative pattern spore of papery (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>the large decorative pattern spore of papery (Pachykytospora papayracea)
<400>46
Gly Asn Ala Gly Pro Ser
1 5
<210>47
<211>21
<212>DNA
<213>lobe ring bolt bacterium (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>lobe ring bolt bacterium (Trametes cingulata)
<400>48
Gly Ser Gly Gly Ala Gly Thr
1 5
<210>49
<211>33
<212>DNA
<213>leucopaxillus giganteus (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 giganteus (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 Ser 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 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 Asn 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 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 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 acg tcc acc tcg acc gcc tcc tgc gcc gcc acc 45
Thr Thr Thr Lys Thr Ser Thr 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 Thr Ala Ser Cys Ala Ala Thr
1 5 10 15
<210>57
<211>78
<212>DNA
<213>bacterial classification (Acremonium sp.) of the mould genus of branch top spore
<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>bacterial classification (Acremonium sp.) of the mould genus of branch top spore
<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>huge bracket fungus (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>huge bracket fungus (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 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 Ser 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 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>Luo Eratai bacterium (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>Luo Eratai bacterium (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 albicans (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 Ala Ala Ala Thr Thr Ser Ser Ser
20 25 30
<210>70
<211>31
<212>PRT
<213>aspergillus albicans (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 Ala Ala Ala Thr Thr Ser Ser Ser
20 25 30
<210>71
<211>111
<212>DNA
<213>aspergillus niger (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 agc 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 (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>bacterial classification (Coniochaeta sp.) of cone Chaetomium
<220>
<221>CDS
<222>(1)..(96)
<400>73
acc acg aca aca gct acg acg aag acg 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 Cys Thr Ala Thr Ala
20 25 30
<210>74
<211>32
<212>PRT
<213>bacterial classification (Coniochaeta sp.) of cone Chaetomium
<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 Cys Thr Ala Thr Ala
20 25 30
<210>75
<211>285
<212>DNA
<213>the large decorative pattern spore of papery (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>the large decorative pattern spore of papery (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>lobe ring bolt bacterium (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>lobe ring bolt bacterium (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 giganteus (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 giganteus (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 ValArg Ile Thr Ser A sp 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
<21l>294
<212>DNA
<213>bacterial classification (Acremonium sp.) of the mould genus of branch top spore
<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>bacterial classification (Acremonium sp.) of the mould genus of branch top spore
<400>86
Val Asn 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>huge bracket fungus (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 Glv 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 Ash Arg Gln Ala
65 70 75 80
acc gcg ccc gcg tcc ggt 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>huge bracket fungus (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)..(26l)
<400>89
acc gtt tgg gga caa aat gta tac gtt gtc ggg aat att tcg cag ctg 48
Thr Val Trp 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 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>Luo Eratai bacterium (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
65707580
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
859095
tct tag 294
Ser
<210>92
<211>97
<212>PRT
<213>Luo Eratai bacterium (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 albicans (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 Thr 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 albicans (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 (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 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 tcg 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 (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 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>bacterial classification (Coniochaeta sp.) of cone Chaetomium
<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 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>bacterial classification (Coniochaeta sp.) of cone Chaetomium
<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 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>heterozygote that comprises Fungamyl variant CD and Luo Eratai bacterium (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 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 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 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 construct
<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 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>with Rhizomucor pusillus (Rhizomucor pusillus) amylase of joint with from Luo Eratai bacterium (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 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>huge bracket fungus (Meripilus giganteus) amylase and Luo Eratai bacterium (A.rolfsii) SBD's is assortedFit
<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 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 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
yal 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 Thr 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>for building the plasmid of heterozygote
<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 acccacaccg ggtgtcataa 2160
tcaaccaatc gtaaccttca tctcttccac ccatgtctct ttgagcaata aagccgataa 2220
caaaatcttt gtcgctcttc gcaatgtcaa cagtaccctt 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 cagatttacg 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 taactacccc 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
atttttcttt tttttctgta cagacgcgtg tacgcatgta acattatact 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 gccccaacag c 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>bacterial classification (Thermoascus sp.) that Thermoascus belongs to
<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 Glu 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
<2l1>476
<212>PRT
<213>bacterial classification (Thermoascus sp.) that Thermoascus belongs to
<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 Val 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>bacterial classification (Coniocheata sp.) of cone Chaetomium
<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 Asn 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 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>bacterial classification (Coniocheata sp.) of cone Chaetomium
<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 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
385 390 395 400
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>bacterial classification (Nectria sp.) of the red shell Pseudomonas of clump
<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 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>bacterial classification (Nectria sp.) of the red shell Pseudomonas of clump
<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 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>bacterial classification of Fusarium (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
370375380
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>bacterial classification of Fusarium (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>gauffer bolt bacterium (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 ggc 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 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 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>gauffer bolt bacterium (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 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 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>bacterial classification of Penicillium (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>bacterial classification of Penicillium (Penicillium sp.)
<400>121
Ala Glu Trp Arg Ser Gln Set 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
Set 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 Ile 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>thermophilic ascomycete (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>thermophilic ascomycete (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 chrysosporium (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 tac 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 gtc ttc gtc acg atc cac gac acg 816
Trp Val Pro Gly Thr Ser Ala Asn Val Phe Val Thr Ile 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 Val Gly Ala Lys Gly Thr Ala
435 440 445
ggc 1347
Gly
<210>127
<211>449
<212>PRT
<213>Phanerochaete chrysosporium (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 (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 rle 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 aoa 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 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 (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 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
145 150 155 160
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 Lcu Lys Asp Gly Leu Pro Ala Leu Phc Val Pro Ser Ser
435 440 445
<210>132
<211>1305
<212>DNA
<213>pappus colter mould (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>pappus colter mould (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 (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 (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 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
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>bacterial classification (Coniochaeta sp.) of cone Chaetomium
<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 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>bacterial classification (Coniochaeta sp.) of cone Chaetomium
<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 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>gauffer bolt bacterium (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 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
ttt 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>gauffer bolt bacterium (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 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
1 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>bacterial classification of Penicillium (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>bacterial classification of Penicillium (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>bacterial classification (Coniochaeta sp.) of cone Chaetomium
<220>
<221>CDS
<222>(1)..(123)
<400>144
acg acg tcg acg agt acg ggg acg agc tcg acc acg 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 acg tcc acg aag act acg gcg tcg acg acg acg acg aag 96
Thr Leu Thr Thr Ser Thr Lys Thr Thr Ala Ser Thr Thr Thr Thr Lys
20 25 30
agc agc agt tcc tgc acc gcc aaca gca 123
Ser Ser Ser Ser Cys Thr Ala Thr Ala
35 40
<210>145
<211>41
<212>PRT
<213>bacterial classification (Coniochaeta sp.) of cone Chaetomium
<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 Cys Thr Ala Thr Ala
35 40
<210>146
<211>30
<212>DNA
<213>gauffer bolt bacterium (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>gauffer bolt bacterium (Trameres 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 A1a 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>bacterial classification of Penicillium (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 Ser Thr Thr Ser Lys Thr Thr Thr
20 25 30
tcc act aca tcc acg agc tgc aca cag gct act gca 132
Ser Thr Thr Ser Thr Ser Cys Thr Gln Ala Thr Ala
35 40
<210>151
<211>44
<212>PRT
<213>bacterial classification of Penicillium (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 Ser Thr Thr Ser Lys Thr Thr Thr
20 25 30
Ser Thr Thr 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>mud streptomycete (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>mud streptomycete (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
180 185 190
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>pappus colter mould (Absidia cristata)
<220>
<221>CDS
<222>(1)..(1443)
<220>
<221>sig_peptide
<222>(1)..(120)
<220>
<221>misc_feature
<222>(121)..(1443)
<223>catalyst structure 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
Phe Ala Gly Gly Gly Asp Cys Ser Asp Leu Ser Asp Tyr Cys Gly Gly
65 70 75 80
aat tat aaa gge 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>pappus colter mould (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
165 170 175
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>bacterial classification (Acremonium sp.) of the mould genus of branch top spore
<220>
<221>CDS
<222>(1)..(1878)
<220>
<221>sig_peptide
<222>(1)..(63)
<220>
<221>misc_feature
<222>(64)..(1506)
<223>catalyst structure domain
<220>
<221>misc_feature
<222>(1507)..(1584)
<223>joint
<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 cca gtg gtc aag cag gtg gaa ggc aat 288
Phe Thr Ala Val Trp Ile Ser Pro Val Val Lys Gln Val Glu Gly Ash
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 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 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>bacterial classification (Acremonium sp.) of the mould genus of branch top spore
<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 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 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>bacterial classification (Coniochaeta sp.) of cone Chaetomium
<220>
<22l>CDS
<222>(1)..(1890)
<220>
<221>sig_peptide
<222>(1)..(69)
<220>
<221>misc_feature
<222>(70)..(1497)
<223>catalyst structure domain
<220>
<221>misc_feature
<222>(1498)..(1596)
<223>joint
<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 tct tgc acc 1584
Thr Thr Ser Thr Thr Thr Thr Ser Thr Lys Thr Ser Ser Ser Cys Thr
515 520 525
gcc acc gcg gta gca atc acc ttc 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>bacterial classification (Coniochacta sp.) of cone Chaetomium
<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 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>huge bracket fungus (Meripilus giganteus)
<220>
<221>CDS
<222>(1)..(1806)
<220>
<221>sig_peptide
<222>(1)..(78)
<220>
<221>misc_feature
<222>(79)..(1476)
<223>catalyst structure domain
<220>
<221>misc_feature
<222>(1477)..(1521)
<223>joint
<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 Ile 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 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 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 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 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>huge bracket fungus (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 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 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>bacterial classification of Penicillium (Penicillium sp.)
<220>
<221>CDS
<222>(1)..(1929)
<220>
<221>sig_peptide
<222>(1)..(60)
<220>
<221>misc_feature
<222>(61)..(1488)
<223>catalyst structure domain
<220>
<221>misc_feature
<222>(1489)..(1617)
<223>joint
<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 Ser Thr Thr Ser Lys 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 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>bacterial classification of Penicillium (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 Met Ile Asn 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 Ser Thr Thr Ser Lys Thr Thr Thr
515 520 525
Ser Thr Thr 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 Asn 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>mud streptomycete (Streptomyces limosus)
<220>
<221>CDS
<222>(1)..(1698)
<220>
<221>sig_peptide
<222>(1)..(84)
<220>
<221>misc_feature
<222>(85)..(1503)
<223>catalyst structure domain
<220>
<221>misc_feature
<222>(1504)..(1701)
<223>joint+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 Tyr Asp 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 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>mud streptomycete (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
l45 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 A1a 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 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>catalyst structure domain
<220>
<221>misc_feature
<222>(1462)..(1536)
<223>joint
<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 tae 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 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 Gly Gly Ser Gly 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 Gly Gly Ser Gly 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 (Syncephalastrum racemosum)
<220>
<221>CDS
<222>(1)..(1389)
<220>
<221>sig_peptide
<222>(1)..(60)
<220>
<221>misc_feature
<222>(61)..(1389)
<223>catalyst structure 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 Ash 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 (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>gauffer bolt bacterium (Trametes corrugata)
<220>
<221>CDS
<222>(1)..(1764)
<220>
<221>sig_peptide
<222>(1)..(60)
<220>
<221>misc_feature
<222>(61)..(1431)
<223>catalyst structure domain
<220>
<221>misc_feature
<222>(1432)..(1473)
<223>joint
<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 agc ctg gtc agc tct gct cat gcg aag ggc ata tat gtg 384
Asp Leu Lys Ser Leu Val 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>gauffer bolt bacterium (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 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>joint+CBM (N-end)
<220>
<221>misc_feature
<222>(862)..(2322)
<223>catalyst structure 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 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 Thr Ser Thr Ala Thr 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 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 Thr Ser Ala Thr Ser Thr Thr Lys Ser
130 135 140
Ser Thr Thr Ser Thr Ser Thr Ala Thr Ser Thr Ser Val Ala Thr Ser
145 150 155 160
Ser Leu Pro Ala Ile Ile 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>catalyst structure domain
<220>
<221>misc_feature
<222>(1414)..(1458)
<223>joint
<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 tcc 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 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 Ash 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>catalyst structure domain
<220>
<221>misc_feature
<222>(1411)..(1443)
<223>joint
<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 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 G1y
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 G1n 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 (52)

1. a peptide species, described polypeptide is by the first amino acid sequence, the joint sequence that contain catalyst structure domain and contain carbon aquationThe second amino acid sequence composition of compound binding modules, described joint sequence is present in described first and described the second amino acid orderPosition between row, described catalyst structure domain is the catalysis knot of the Rhizomucor pusillus AMS shown in SEQ ID NO:20Structure territory, described carbohydrate binding modules is Luo Eratai bacterium (Athelia rolfsii) glucose in SEQ ID NO:92Amylase CBM.
2. the polypeptide of claim 1, wherein said joint sequence is selected from lower group: 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。
3. according to the polypeptide of claim 1, wherein said polypeptide is by the catalytic structure domain amino acid shown in SEQ ID NO:20Carbohydrate binding modules ammonia shown in joint sequence shown in sequence, SEQ ID NO:68 and SEQ ID NO:92Base acid sequence composition.
4. the purposes for liquefying according to the polypeptide of claims 1 to 3 any one.
5. the purposes for saccharification according to the polypeptide of claims 1 to 3 any one.
6. be used for the purposes of the method that comprises fermentation according to the polypeptide of claims 1 to 3 any one.
7. the purposes in starch method for transformation according to the polypeptide of claims 1 to 3 any one.
8. the purposes in the method for producing oligosaccharides according to the polypeptide of claims 1 to 3 any one.
9. the purposes in the method for producing maltodextrin or glucose syrup according to the polypeptide of claims 1 to 3 any one.
10. the purposes in the method for producing fuel or drinking alcohol according to the polypeptide of claims 1 to 3 any one.
11. according to the polypeptide of claims 1 to 3 any one the purposes in the method for preparation of drinks.
12. according to the polypeptide of claims 1 to 3 any one the purposes in the fermentation process for the production of organic compound.
13. according to the purposes of claim 12, and wherein said organic compound is citric acid, ascorbic acid, lysine or paddy ammoniaAcid.
The method of 14. starch saccharifications, wherein uses according to the polypeptide of claims 1 to 3 any one and processes starch.
15. according to the method for claim 14, comprises and changes starch into contain dextrose and/or maltose syrup.
16. according to the method for claims 14 or 15, and wherein said starch is starch gelatinization or granular.
17. according to the method for claims 14 or 15, wherein the starch of saccharification is contacted to produce tunning with fermenting organism.
18. according to the method for claim 17, and wherein said fermenting organism is yeast, and described tunning is ethanol.
19. 1 kinds of methods, comprising:
(a) by starch and according to the polypeptide that comprises catalytic module and carbohydrate binding modules of claim 1-3 any oneContact, described catalytic module has alpha-amylase activity;
(b) described starch is incubated together with described polypeptide;
(c) fermentation, to produce tunning,
(d) optionally reclaim described tunning,
Wherein there is enzyme or the disappearance of glucoamylase activity, or deposit with the amount that is no more than 0.5 AGU/g DS starch substrates.
The method of 20. claims 19, wherein has the enzyme of glucoamylase activity with at the bottom of being no more than 0.4 AGU/g DS starchThe amount of thing exists.
The method of 21. claims 20, wherein has the enzyme of glucoamylase activity with at the bottom of being no more than 0.3 AGU/g DS starchThe amount of thing exists.
The method of 22. claims 21, wherein has the enzyme of glucoamylase activity with at the bottom of being no more than 0.1 AGU/g DS starchThe amount of thing exists.
The method of 23. claims 22, wherein has the enzyme of glucoamylase activity with at the bottom of being no more than 0.05 AGU/g DS starchThe amount of thing exists.
24. 1 kinds of methods, comprising:
(a) starch substrates is contacted with yeast cells, described yeast cells is converted to express any one in claim 1-3The polypeptide that comprises catalytic module and carbohydrate binding modules, described catalytic module has alpha-amylase activity;
(b) described starch substrates is preserved together with described yeast;
(c) fermentation is to produce ethanol;
(d) optionally reclaim ethanol.
25. by fermenting by the method for amyloid manufacture of materials ethanol, and described method comprises:
(i) use according to catalytic module and the carbohydrate knot comprising of claim 1-3 any one with alpha-amylase activityThe described starch-containing material of polypeptide liquefaction of compound module;
(ii) liquefied fermented glutinous rice that saccharification obtains;
(iii) there is at fermenting organism the material obtaining in bottom fermentation step (ii).
26. according to the method for claim 25, further comprises recovery ethanol.
27. according to the method for claim 25 or 26, wherein said saccharification and fermentation real as saccharification and fermentation process simultaneouslyExecute.
28. according to the method for claim 25 or 26, and wherein during step I ii, ethanol content reaches at least 7% ethanol.
29. according to the method for claim 28, and wherein during step I ii, ethanol content reaches at least 11% ethanol.
30. according to the method for claim 29, and wherein during step I ii, ethanol content reaches at least 16% ethanol.
31. according to the method for claim 25, and wherein said polypeptide is acid alpha-amylase.
32. according to the method for claim 31, and wherein said acid alpha-amylase exists with the amount of 0.01 to 10 AFAU/g DS.
33. according to the method for claim 32, and wherein said acid alpha-amylase exists with the amount of 0.1 to 5 AFAU/g DS.
34. according to the method for claim 33, and wherein said acid alpha-amylase exists with the amount of 0.3 to 2 AFAU/g DS.
35. according to the method for claim 31, and wherein said acid alpha-amylase and glucoamylase are with 0.1 to 10 AGU/The ratio of AFAU is added.
36. according to the method for claim 35, and wherein said acid alpha-amylase and glucoamylase are with 0.30 to 5 AGU/The ratio of AFAU is added.
37. according to the method for claim 36, and wherein said acid alpha-amylase and glucoamylase are with 0.5 to 3 AGU/AFAURatio add.
38. codings are according to the DNA sequence dna of the polypeptide of claims 1 to 3 any one.
39. comprise according to the DNA construct of the DNA sequence dna of claim 38.
40. carry according to the recombinant expression carrier of the DNA construct of claim 39.
The host cell that 41. use transform according to the DNA construct of claim 39 or according to the carrier of claim 40.
42. according to the host cell of claim 41, and it is microorganism.
43. according to the host cell of claim 42, and it is bacterium or fungal cell.
44. according to the host cell of claim 41, and it is yeast.
45. according to the host cell of claim 41 or 42, its be from the bacterial strain of aspergillus, from the bacterial strain of Talaromyces,Or from the bacterial strain of trichoderma.
46. according to the host cell of claim 45, and the wherein said bacterial strain from aspergillus is aspergillus niger, described from basketThe bacterial strain of Pseudomonas is Talaromyces emersonii.
47. comprise according to the composition of the polypeptide of claims 1 to 3 any one.
48. according to the composition of claim 47, and described composition further comprises glucoamylase.
49. according to the composition of claim 48, and wherein said glucoamylase derives from bacterial classification, the Eurotium of TalaromycesBacterial classification, the bacterial classification of Trametes or the bacterial classification of Pachyktospora in bacterial strain.
50. according to the composition of claim 49, and wherein said glucoamylase derives from the species that are selected from lower group: aspergillus niger,Talaromyces leycettanus, Talaromyces duponti, Talaromyces emersonii, lobe ring bolt bacterium and the large decorative pattern of paperySpore.
51. according to the composition of claim 47 to 50 any one for making the liquefaction of gelatinization or pearl starch and/or saccharificationPurposes.
52. are used for that part gelatinized starch is liquefied and/or the purposes of saccharification according to the composition of claim 47 to 50 any one.
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