Stress Resistant Plants

Abstract

Stress tolerance in plants and plant cells is achieved by using nucleotide sequences encoding enzymes involved in the NAD salvage synthesis pathway and/or the NAD de novo synthesis pathway from fungal or yeast like organisms other than Saccharomyces cereviseae, e.g., for overexpression in plants.

Description

[0001] Methods are provided for increasing the stress resistance in plants and plant cells whereby enzymes involved in the NAD salvage synthesis pathway and/or the NAD de novo synthesis pathway originating from fungal organisms or yeasts,

BACKGROUND ART

[0002] Tolerance of plants to adverse growing conditions, including drought, high light intensities, high temperatures, nutrient limitations, saline growing conditions and the like, is a very desired property for crop plants, in view of the never-ending quest to ultimately increase the actual yield of these plants.

[0003] Various ways of achieving that goal of improving what is commonly known as the stress resistance or stress tolerance of plants have been described. Since different abiotic stress conditions frequently result in the generation of harmful reactive oxygen species ("ROS") such as superoxides or hydrogen peroxides, initial attempts to improve stress resistance in plants focused on prevention of the generation of the ROS or the removal thereof. Examples of these approaches are overexpression of ROS scavenging enzymes such as catalases, peroxidases, superoxide dismutases etc. or even increasing the amount of ROS scavenging molecules such as ascorbic acid, glutathione etc. These approaches and other attempts to engineer stress tolerant plants are reviewed e.g. in Wang et al. 2003, Planta 218:1-14.

[0004] Stress tolerance in plant cells and plants can also be achieved by reducing the activity or the level of the endogenous poly-ADP-ribose polymerases (ParP) or poly(ADP-ribose) glycohydrolases (ParG) as described in WO00/04173 and PCT/EP2004/003995, respectively. It is thought that in this way, fatal NAD and ATP depletion in plant cells subject to stress conditions, resulting in traumatic cell death, can be avoided or sufficiently postponed for the stressed cells to survive and acclimate to the stress conditions.

[0005] Uchimiya et al. (2002) et al. describe the isolation of a rice gene denoted YK1, as well as use of a chimeric YK1 gene to increase the tolerance of transgenic rice plants harboring that gene to rice blast and several abiotic stresses such as NaCl, UV-C, submergence, and hydrogen peroxide. (Uchimiya et al., 2002, Molecular breeding 9: 25-31).

[0006] Uchimiya et al. further published a poster abstract describing that overexpression of a NAD dependent reductase gene (YK1) in rice cells also promoted the level of NAD(P)(H) through up-regulating NAD synthetase activities, and concluded that this modification in turn generated a pool of redox substances needed for ROS stress resistance (Uchimiya et al. 2003 Keystone symposium on Plant biology: Functions and control of cell death, Snowbird Utah April 10-15, 2003).

[0007] NAD synthetase from yeast has been well characterized and is the last enzyme in both the NAD de novo synthesis pathway and the NAD salvage. In the de novo pathway, quinolate is the precursor for NAD synthesis and is generated as a product of tryptophan degradation. In the salvage pathway, nicotinamide (which is a degradation product of NAD, generated through the action of various enzymes such as PARP, NAD-dependent deacetylases or other NAD glycohydrolases) is the precursor molecule. In a first step, nicotinamide is deamidated to nicotinic cid by a nicotinamidase. The nicotinic acid is transferred to 5-phosphoribosyl-1-pyrophosphate by the enzyme nicotinate phosphoribosyl transferase to yield nicotinic acid mononucleotide. This compound is shared between the de novo and the salvage pathway. Hence, further conversion of this compound by NAD+ pyrophosphorylase and NAD synthetase is achieved as in the de novo pathway.

[0008] In yeast, overexpression of PNC1 (encoding nicotinamidase) has been correlated with life span extension by calorie restriction and low-intensity stress (Anderson et al., 2003 Nature 423: p181-185; Gallo et al., 2004, Molecular and Cellular Biology 24: 1301-1312).

[0009] WO2004/016726 describes methods and compositions for modulating the life span of eukaryotic and prokaryotic cells and for protecting cells against certain stresses. One method comprises modulating the flux of the NAD+salvage pathway in the cell, e.g. by modulating the level or activity of one or more proteins selected from the group consisting of PNC1, NMA1, NPT1 and NMA2.

[0010] Little is known about the respective enzymes of the NAD biosynthesis pathways in plants. Hunt et al., 2004 describe the use of the available genomic information from Arabidopsis to identify the plant homologues of these enzymes (Hunt et al. , 2004, New Phytologist 163(1): 31-44). The identified DNA sequences have the following Accession numbers: for nicotinamidase: At5g23220; At5g23230 and At3g16190; for nicotinate phosphoribosyltransferase: At4g36940, At2g23420, for nicotinic acid mononucleotide adenyltransferase: At5g55810 and for NAD synthetase: At1g55090 (all nucleotide sequences are incorporated herein by reference).

[0011] PCT/EP 2005/010168 describes methods for increasing the stress resistance in plants and plant cells whereby enzymes involved in the NAD salvage synthesis pathway and/or the NAD de novo synthesis pathway are expressed in plants.

[0012] Alternative methods for increasing stress tolerance in plants are still required and the embodiments described hereinafter, including the claims, provide such methods and means.

SUMMARY OF THE INVENTION

[0013] In one embodiment of the invention, a method is provided for obtaining a plant with increased stress resistance comprising introducing a chimeric gene into a cells of a plant to obtain transgenic cells whereby the chimeric gene comprises the following operably linked DNA fragments: [0014] i. A plant-expressible promoter; [0015] ii. A DNA region coding for a plant-functional enzyme of the nicotinamide adenine dinucleotide salvage synthesis pathway selected from nicotinamidase, nicotinate phosphoribosyltransferase, nicotinic acid mononucleotide adenyl transferase or nicotinamide adenine dinucleotide synthetase [0016] iii. A 3'end region involved in transcription termination and polyadenylation, followed by regenerating the transgenic cells to obtain a population of transgenic plants; and selecting a plant from the population of transgenic plants which exhibits increased stress resistance or selecting a plant which exhibits a reduced level of reactive oxygen species or maintains a high level of NADH under stress conditions when compared to a similar non-transgenic plant wherein said method is characterized in that the amino acid sequence of the plant-functional enzyme encoded by the DNA region comprises one of the following: the amino acid sequence of accession number XP.sub.--444840 (Candida glabrata), the amino acid sequence of accession number XP.sub.--456073 (Kluyveromyces lactis), the amino acid sequence of accession number NP.sub.--986013 (Eremothecium gossypii), the amino acid sequence of accession number XP.sub.--888958 (Candida albicans), the amino acid sequence of accession number XP500320 (Yarrowia lipolytica), the amino acid sequence of accession number XP389372 (Giberella zeae), the amino acid sequence of accession number XP.sub.--749509 (Aspergillus fumigatus), the amino acid sequence of accession number XP.sub.--712112 (Candida albicans), the amino acid sequence of accession number BAE56421 (Aspergillus oryzae), the amino acid sequence of accession number XP.sub.--567125 (Cryptococcus neofomans),the amino acid sequence of accession number XP.sub.--964547 (Neurospora crassa), the amino acid sequence of accession number XP.sub.--712135 (Candida albicans), the amino acid sequence of accession number XP.sub.--448179 (Candida glabrata), the amino acid sequence of accession number XP.sub.--453643 (Kluyveromyces lactis), the amino acid sequence of accession number NP.sub.--987024 (Eremothecium gossypii), the amino acid sequence of accession number XP.sub.--500272 (Yarrowia lipolytica), the amino acid sequence of accession number XP.sub.--722371 (Candida albicans), the amino acid sequence of accession number XP.sub.--456405 (Debaromyces hansenii), the amino acid sequence of accession number BAE61562 (Aspergillus oryzae), the amino acid sequence of accession number XP.sub.--759702 (Ustilago maydis), the amino acid sequence of accession number EAL18079 (Cryptococcus neoformans), the amino acid sequence of accession number NP.sub.--587771 (Schizosaccharomyces pombe), the amino acid sequence of accession number XP.sub.--681472 (Aspergillus nidulans), the amino acid sequence of accession number XP.sub.--959191 (Neurospora crassa), the amino acid sequence of accession number XP.sub.--567726 (Cryptococcus neoformans), the amino acid sequence of accession number EAQ90706 (Chaetomium globosum), the amino acid sequence of accession number XP.sub.--387574 (Giberella zeae), the amino acid sequence of accession number XP.sub.--748008 (Aspergillus fumigatus), the amino acid sequence of accession number XP.sub.--361704 (Magnaporthe grisea), the amino acid sequence of accession number Q06178, the amino acid sequence of accession number XP.sub.--444815 (Candida glabrata), the amino acid sequence of accession number NP.sub.--986687 ((Eremothecium gossypii), the amino acid sequence of accession number XP.sub.--453005 (Kluyveromyces lactis), the amino acid sequence of accession number XP.sub.--458184(Debaromyces hansenii), the amino acid sequence of accession number XP.sub.--718656 (Candida albicans), the amino acid sequence of accession number XP.sub.--504391 (Yarrowia lipolytica), the amino acid sequence of accession number NP.sub.--592856 (Schizosaccharomyces pombe), the amino acid sequence of accession number XP.sub.--762639 (Ustilago maydis), the amino acid sequence of accession number XP.sub.--571297 (Cryptococcus neoformans), the amino acid sequence of accession number BAE57070 (Aspergillus oryzae), the amino acid sequence of accession number XP.sub.--750776 (Aspergillus fumigatus), the amino acid sequence of accession number XP.sub.--659349 (Aspergillus nidulans), the amino acid sequence of accession number XP.sub.--389652 (Giberella zeae), the amino acid sequence of accession number XP.sub.--957634 (Neurospora crassa), the amino acid sequence of accession number XP.sub.--363364 (Magnaporthe grisea), the amino acid sequence of accession number XP.sub.--758179 (Ustilago maydis), the amino acid sequence of accession number EAQ85219 ((Chaetomium globosum), the amino acid sequence of accession number CAA85352 (Saccharomyces cerevisae), the amino acid sequence of accession number XP.sub.--448893 (Candida glabrata), the amino acid sequence of accession number XP.sub.--453357 (Kluyveromyces lactis), the amino acid sequence of accession number NP.sub.--983562 (Eremothecium gossypii), the amino acid sequence of accession number XP.sub.--462577 (Debaromyces hansenii), the amino acid sequence of accession number XP .sub.--889008 (Candida albicans), the amino acid sequence of accession number XP .sub.--500338 (Yarrowia lipolytica), the amino acid sequence of accession number XP .sub.--746744 (Aspergillus fumigatus), the amino acid sequence of accession number BAE64333 (Aspergillus oryzae), the amino acid sequence of accession number XP.sub.--965789 (Neurospora crassa), the amino acid sequence of accession number EAQ93453 (Chaetomium globosum), the amino acid sequence of accession number XP.sub.--682385 (Aspergillus nidulans), the amino acid sequence of accession number AAN74808 (Gibberella moniliformis), the amino acid sequence of accession number Q9UTK3, the amino acid sequence of accession number XP.sub.--361075 (Magnaporthe grisea), the amino acid sequence of accession number EAL18922 (Cryptococcus neoformans), the amino acid sequence of accession number XP.sub.--568039 (Cryptococcus neoformans), the amino acid sequence of accession number XP.sub.--760597 (Ustilago maydis), the amino acid sequence of accession number NP.sub.--011524,the amino acid sequence of accession number XP.sub.--444815 (Candida glabrata), the amino acid sequence of accession number NP.sub.--986687 ((Eremothecium gossypii), the amino acid sequence of accession number XP.sub.--453005 (Kluyveromyces lactis), the amino acid sequence of accession number XP.sub.--458184 (Debaromyces hansenii), the amino acid sequence of accession number XP.sub.--718656 (Candida albicans), the amino acid sequence of accession number XP.sub.--504391 (Yarrowia lipolytica), the amino acid sequence of accession number NP.sub.--592856 (Schizosaccharomyces pombe), the amino acid sequence of accession number XP.sub.--762639 (Ustilago maydis), the amino acid sequence of accession number XP.sub.--571297 (Cryptococcus neoformans), the amino acid sequence of accession number BAE57070 (Aspergillus oryzae), the amino acid sequence of accession number XP.sub.--750776 (Aspergillus fumigatus), the amino acid sequence of accession number XP.sub.--659349 (Aspergillus nidulans), the amino acid sequence of accession number XP.sub.--389652 (Giberella zeae), the amino acid sequence of accession number XP.sub.--957634 (Neurospora crassa), the amino acid sequence of accession number XP.sub.--363364 (Magnaporthe grisea), the amino acid sequence of accession number XP.sub.--758179 (Ustilago maydis) or the amino acid sequence of accession number EAQ85219 (Chaetomium globosum).

[0017] In another embodiment, the invention relates to the chimeric genes as described herein, plant cells comprising these chimeric genes, and plants consisting essentially of plant cells comprising these chimeric genes, and seeds of such plants. These plants and plant cells may be characterized in that they have a lower level of reactive oxygen species under stress conditions than a similar plant not comprising such a chimeric gene.

[0018] In yet another embodiment, the invention relates to the use of the described chimeric genes to increase the stress resistance of a plant or to decrease the level of reactive oxygen species in a plant or a plant cell under stress conditions.

[0019] The invention further provides the use of one of the mentioned DNA sequence encoding a plant functional enzyme of the nicotinamide adenine dinucleotide salvage synthesis pathway selected from nicotinamidase, nicotinate phosphoribosyltransferase, nicotinic acid mononucleotide adenyl transferase or nicotinamide adenine dinucleotide synthetase which are from fungal or yeast-like origin to increase the stress resistance of a plant or to decrease the level of reactive oxygen species or maintain the level of NADH in a plant or a plant cell under stress conditions.

DETAILED DESCRIPTION

[0020] The current invention is based on the finding that DNA sequences encoding plant-functional enzymes from the NAD salvage pathway in yeasts could be used to obtain transgenic plants which were more resistant to stress, particularly abiotic stress, than plants not comprising these DNA sequences. The transgenic plants also exhibited a significantly reduced level of reactive oxygen species ("ROS") and maintained a high level of NADH, when put under stress conditions, compared to control plants

[0021] Thus in one embodiment of the invention, a method is provided to obtain a plant with increased stress resistance, whereby the method comprises the steps of [0022] introducing a stress resistant chimeric gene as herein described into cells of a plant to obtain cells comprising the stress resistant chimeric gene; [0023] regenerating these cells comprising the stress resistant chimeric gene to obtain a population of plants comprising the stress resistant chimeric gene; and [0024] selecting a plant from the population of these plants which exhibits increased stress resistance and/or decreased ROS level under stress conditions and/or maintains a high level of NADH, when compared to a similar non-transgenic plant.

[0025] The stress resistant chimeric gene thereby comprises a plant-expressible promoter operably linked to a DNA region coding for a plant-functional enzyme of the nicotinamide adenine dinucleotide salvage synthesis pathway selected from nicotinamidase, nicotinate phosphoribosyltransferase, nicotinic acid mononucleotide adenyl transferase or nicotinamide adenine dinucleotide synthetase from fungal or yeast like origin and a 3'end region involved in transcription termination and polyadenylation.

[0026] As used herein, "a plant-functional enzyme of the nicotinamide adenine dinucleotide salvage synthesis pathway" is an enzyme which when introduced into plants, linked to appropriate control elements such as plant expressible promoter and terminator region, can be transcribed and translated to yield a enzyme of the NAD salvage synthesis pathway functional in plant cells. Included are the enzymes (and encoding genes) from the NAD salvage synthesis, which are obtained from a yeast or fungus different from Saccharomyces cerevisae.

[0027] The latter proteins are very suitable for the methods according to the invention, since these are less likely to be subject to the enzymatic feedback regulation etc. to which similar plant-derived enzymes may be subject.

[0028] Enzymes involved in the NAD salvage synthesis pathway comprise the following [0029] Nicotinamidase (EC 3.5.1.19) catalyzing the hydrolysis of the amide group of nicotinamide, thereby releasing nicotinate and NH3. The enzyme is also known as nicotinamide deaminase, nicotinamide amidase, YNDase or nicotinamide amidohydrolase [0030] Nicotinate phophoribosyltransferase (EC 2.4.2.11) also known as niacin ribonucleotidase, nicotinic acid mononucleotide glycohydrolase; nicotinic acid mononucleotide pyrophosphorylase; nicotinic acid phosphoribosyltransferase catalyzing the following reaction

[0030] Nicotinate-D-ribonucleotide+diphosphate=nicotinate+5-phospho-.alp- ha.-D-ribose 1-diphosphate [0031] Nicotinate-nucleotide adenylyltransferase, (EC 2.7.7.18) also known as deamido-NAD+pyrophosphorylase; nicotinate mononucleotide adenylyltransferase; deamindonicotinamide adenine dinucleotide pyrophsophorylase; NaMT-ATase; nicotinic acid mononucleotide adenylyltransferase catalyzing the following reaction

[0031] ATP+nicotinate ribonucleotide=diphosphate+deamido-NAD.sup.+ [0032] NAD-synthase (EC 6.3.1.5) also known as NAD synthetase; NAD.sup.+synthase;

[0033] nicotinamide adenine dinucleotide synthetase; diphosphopyridine nucleotide synthetase, catalyzing the following reaction

Deamido-NAD.sup.++ATP+NH3=AMP+diphosphate+NAD.sup.+

[0034] In one embodiment of the invention, the coding regions encoding the different enzymes of the NAD salvage pathway comprise a nucleotide sequence encoding proteins with the amino acid sequences as set forth hereinafter.

[0035] Suitable nucleotide sequences encoding a nicotinamidase similar to PNC1 from Saccharomyces cerevisiae but from fungal or yeast-like origin include a nucleotide sequence encoding a nicotineamidase comprising an amino acid sequence selected from:

[0036] the amino acid sequence of accession number XP.sub.--444840 (Candida glabrata)

[0037] the amino acid sequence of accession number XP.sub.--456073 (Kluyveromyces lactis)

[0038] the amino acid sequence of accession number NP.sub.--986013 (Eremothecium gossypii)

[0039] the amino acid sequence of accession number XP.sub.--888958 (Candida albicans)

[0040] the amino acid sequence of accession number XP500320 (Yarrowia lipolytica)

[0041] the amino acid sequence of accession number XP389372 (Giberella zeae)

[0042] the amino acid sequence of accession number XP.sub.--749509 (Aspergillus fumigatus)

[0043] the amino acid sequence of accession number XP.sub.--712112 (Candida albicans)

[0044] the amino acid sequence of accession number BAE56421 (Aspergillus oryzae)

[0045] the amino acid sequence of accession number XP.sub.--567125 (Cryptococcus neofomans)

[0046] the amino acid sequence of accession number XP.sub.--964547 (Neurospora crassa)

[0047] the amino acid sequence of accession number XP.sub.--712135 (Candida albicans)

[0048] Suitable nucleotide sequences encoding an NAD(+) synthetase similar to Qns1 from Saccharomyces cerevisiae but from fungal origin include a nucleotide sequence encoding a NAD(+) synthetase comprising an amino acid sequence selected from:

[0049] the amino acid sequence of accession number XP.sub.--448179 (Candida glabrata)

[0050] the amino acid sequence of accession number XP.sub.--453643 (Kluyveromyces lactis)

[0051] the amino acid sequence of accession number NP.sub.--987024 (Eremothecium gossypii)

[0052] the amino acid sequence of accession number XP.sub.--500272 (Yarrowia lipolytica)

[0053] the amino acid sequence of accession number XP.sub.--722371 (Candida albicans)

[0054] the amino acid sequence of accession number XP.sub.--456405 (Debaromyces hansenii)

[0055] the amino acid sequence of accession number BAE61562 (Aspergillus oryzae)

[0056] the amino acid sequence of accession number XP.sub.--759702 (Ustilago maydis)

[0057] the amino acid sequence of accession number EAL18079 (Cryptococcus neoformans)

[0058] the amino acid sequence of accession number NP.sub.--587771 (Schizosaccharomyces pombe)

[0059] the amino acid sequence of accession number XP.sub.--681472 (Aspergillus nidulans)

[0060] the amino acid sequence of accession number XP.sub.--959191 (Neurospora crassa)

[0061] the amino acid sequence of accession number XP.sub.--567726 (Cryptococcus neoformans)

[0062] the amino acid sequence of accession number EAQ90706 (Chaetomium globosum)

[0063] the amino acid sequence of accession number XP.sub.--387574 (Giberella zeae)

[0064] the amino acid sequence of accession number XP.sub.--748008 (Aspergillus fumigatus)

[0065] the amino acid sequence of accession number XP.sub.--361704 (Magnaporthe grisea)

[0066] Suitable nucleotide sequences encoding an Nicotinic acid mononucleotide adenylyltransferase similar to NMA1 from Saccharomyces cerevisiae but from fungal origin include a nucleotide sequence encoding a acid mononucleotide adenylyltransferase comprising an amino acid sequence selected from:

[0067] the amino acid sequence of accession number Q06178

[0068] the amino acid sequence of accession number XP.sub.--444815 (Candida glabrata)

[0069] the amino acid sequence of accession number NP.sub.--986687 ((Eremothecium gossypii)

[0070] the amino acid sequence of accession number XP.sub.--453005 (Kluyveromyces lactis)

[0071] the amino acid sequence of accession number XP.sub.--458184(Debaromyces hansenii)

[0072] the amino acid sequence of accession number XP.sub.--718656 (Candida albicans)

[0073] the amino acid sequence of accession number XP.sub.--504391 (Yarrowia lipolytica)

[0074] the amino acid sequence of accession number NP .sub.--592856 (Schizosaccharomyces pombe)

[0075] the amino acid sequence of accession number XP.sub.--762639 (Ustilago maydis)

[0076] the amino acid sequence of accession number XP.sub.--571297 (Cryptococcus neoformans)

[0077] the amino acid sequence of accession number BAE57070 (Aspergillus oryzae)

[0078] the amino acid sequence of accession number XP.sub.--750776 (Aspergillus fumigatus)

[0079] the amino acid sequence of accession number XP.sub.--659349 (Aspergillus nidulans)

[0080] the amino acid sequence of accession number XP.sub.--389652 (Giberella zeae)

[0081] the amino acid sequence of accession number XP.sub.--957634 (Neurospora crassa)

[0082] the amino acid sequence of accession number XP.sub.--363364 (Magnaporthe grisea)

[0083] the amino acid sequence of accession number XP.sub.--758179 (Ustilago maydis)

[0084] the amino acid sequence of accession number EAQ85219 ((Chaetomium globosum)

[0085] Suitable nucleotide sequences encoding a nicotinate phosphoribosyltransferase similar to NPT1 from Saccharomyces cerevisiae but from fungal or yeast-like origin include a nucleotide sequence encoding nicotinate phosphoribosyltransferase comprising an amino acid sequence selected from:

[0086] the amino acid sequence of accession number CAA85352 (Saccharomyces cerevisae)

[0087] the amino acid sequence of accession number XP.sub.--448893 (Candida glabrata)

[0088] the amino acid sequence of accession number XP.sub.--453357 (Kluyveromyces lactis)

[0089] the amino acid sequence of accession number NP.sub.--983562 (Eremothecium gossypii)

[0090] the amino acid sequence of accession number XP.sub.--462577 (Debaromyces hansenii)

[0091] the amino acid sequence of accession number XP.sub.--889008 (Candida albicans)

[0092] the amino acid sequence of accession number XP.sub.--500338 (Yarrowia lipolytica)

[0093] the amino acid sequence of accession number XP.sub.--746744 (Aspergillus fumigatus)

[0094] the amino acid sequence of accession number BAE64333 (Aspergillus oryzae)

[0095] the amino acid sequence of accession number XP.sub.--965789 (Neurospora crassa)

[0096] the amino acid sequence of accession number EAQ93453 (Chaetomium globosum)

[0097] the amino acid sequence of accession number XP.sub.--682385 (Aspergillus nidulans)

[0098] the amino acid sequence of accession number AAN74808 (Gibberella moniliformis)

[0099] the amino acid sequence of accession number Q9UTK3

[0100] the amino acid sequence of accession number XP.sub.--361075 (Magnaporthe grisea)

[0101] the amino acid sequence of accession number EAL18922 (Cryptococcus neoformans)

[0102] the amino acid sequence of accession number XP.sub.--568039 (Cryptococcus neoformans)

[0103] the amino acid sequence of accession number XP.sub.--760597 (Ustilago maydis)

[0104] Suitable nucleotide sequences encoding an Nicotinic acid mononucleotide adenylyltransferase similar to NMA2 from Saccharomyces cerevisiae but from fungal or yeast like origin include a nucleotide sequence encoding a acid mononucleotide adenylyltransferase comprising an amino acid sequence selected from:

[0105] the amino acid sequence of accession number NP.sub.--011524

[0106] the amino acid sequence of accession number XP.sub.--444815 (Candida glabrata)

[0107] the amino acid sequence of accession number NP.sub.--986687 ((Eremothecium gossypii)

[0108] the amino acid sequence of accession number XP.sub.--453005 (Kluyveromyces lactis)

[0109] the amino acid sequence of accession number XP.sub.--458184 (Debaromyces hansenii)

[0110] the amino acid sequence of accession number XP.sub.--718656 (Candida albicans)

[0111] the amino acid sequence of accession number XP.sub.--504391 (Yarrowia lipolytica)

[0112] the amino acid sequence of accession number NP.sub.--592856 (Schizosaccharomyces pombe)

[0113] the amino acid sequence of accession number XP.sub.--762639 (Ustilago maydis)

[0114] the amino acid sequence of accession number XP.sub.--571297 (Cryptococcus neoformans)

[0115] the amino acid sequence of accession number BAE57070 (Aspergillus oryzae)

[0116] the amino acid sequence of accession number XP.sub.--750776 (Aspergillus fumigatus)

[0117] the amino acid sequence of accession number XP.sub.--659349 (Aspergillus nidulans)

[0118] the amino acid sequence of accession number XP.sub.--389652 (Giberella zeae)

[0119] the amino acid sequence of accession number XP.sub.--957634 (Neurospora crassa)

[0120] the amino acid sequence of accession number XP.sub.--363364 (Magnaporthe grisea)

[0121] the amino acid sequence of accession number XP.sub.--758179 (Ustilago maydis)

[0122] the amino acid sequence of accession number EAQ85219 ((Chaetomium globosum)

[0123] All amino acid sequences referred to by their accession numbers are herein incorporated by reference.

[0124] However, it will be clear that variants of these sequences, including insertions, deletions and substitutions thereof may be also be used to the same effect. Variants of the described sequence will have a sequence identity which is preferably at least about 80%, or 85 or 90% or 95% with identified sequences of enzymes from the NAD salvage pathway,. Preferably, these variants will be functional proteins with the same enzymatic activity as the enzymes from the NAD salvage pathway. For the purpose of this invention, the "sequence identity" of two related nucleotide or amino acid sequences, expressed as a percentage, refers to the number of positions in the two optimally aligned sequences which have identical residues (.times.100) divided by the number of positions compared. A gap, i.e. a position in an alignment where a residue is present in one sequence but not in the other, is regarded as a position with non-identical residues. The alignment of the two sequences is performed by the Needleman and Wunsch algorithm (Needleman and Wunsch 1970). The computer-assisted sequence alignment above, can be conveniently performed using standard software program such as GAP which is part of the Wisconsin Package Version 10.1 (Genetics Computer Group, Madision, Wis., USA) using the default scoring matrix with a gap creation penalty of 50 and a gap extension penalty of 3.

[0125] Homologous nucleotide sequence from other fungi or yeast-like organisms may also be identified and isolated by hybridization under stringent conditions using as probes identified nucleotide sequences encoding enzymes from the NAD salvage pathway.

[0126] "Stringent hybridization conditions" as used herein means that hybridization will generally occur if there is at least 95% and preferably at least 97% sequence identity between the probe and the target sequence. Examples of stringent hybridization conditions are overnight incubation in a solution comprising 50% formamide, 5.times.SSC (150 mM NaCl, 15 mM trisodium citrate), 50 mM sodium phosphate (pH 7.6), 5.times.Denhardt's solution, 10% dextran sulfate, and 20 .mu.g/ml denatured, sheared carrier DNA such as salmon sperm DNA, followed by washing the hybridization support in 0.1.times.SSC at approximately 65.degree. C., preferably twice for about 10 minutes. Other hybridization and wash conditions are well known and are exemplified in Sambrook et al, Molecular Cloning: A Laboratory Manual, Second Edition, Cold Spring Harbor, N.Y. (1989), particularly chapter 11.

[0127] The methods of the invention can be used to obtain plants tolerant to different kinds of stress-inducing conditions, particularly abiotic stress conditions including submergence, high light conditions, high UV radiation levels, increased hydrogen peroxide levels, drought conditions, high or low temperatures, increased salinity conditions. The methods of the invention can also be used to reduce the level of ROS in the cells of plants growing under adverse conditions, particularly abiotic stress conditions including submergence, high light conditions, high UV radiation levels, increased hydrogen peroxide levels, drought conditions, high or low temperatures, increased salinity conditions etc. The level of ROS or the level of NADH can be determined using the methods known in the art, including those described in Example 3.

[0128] Using the methods described herein, plants may be obtained wherein the level of ROS is equal to or lower than in control plants under non-stressed conditions, such as but not limited to low light. In these plants, under non-stressed conditions, the level of ROS may range from 50% to 100% of the level of control plants under low light conditions, more particularly from about 60% to about 85%. The level of the ROS in these plants under stress conditions is about 50% to 80% of the level of ROS in control plants under stress conditions, corresponding to about 60 to 80% of the level of ROS in control plants under non-stressed conditions. Similarly, the NADH level in these plants is equal to or higher than in control plants under non-stressed conditions, such as but not limited to low light. In these plants, under non-stressed conditions, the level of NADH may range from 100% to 160% of the level of NADH in control plants under low light conditions, more particularly from about 120% to about 140%. The level of NADH in these plants under stress conditions is about 200 to 300% of the level of NADH in control plants under stress conditions, corresponding to about 100 to 160% of the level of ROS in control plants under non-stressed conditions.

[0129] Methods to obtain transgenic plants are not deemed critical for the current invention and any transformation method and regeneration suitable for a particular plant species can be used. Such methods are well known in the art and include Agrobacterium-mediated transformation, particle gun delivery, microinjection, electroporation of intact cells, polyethyleneglycol-mediated protoplast transformation. electroporation of protoplasts, liposome-mediated transformation, silicon-whiskers mediated transformation etc. The transformed cells obtained in this way may then be regenerated into mature fertile plants.

[0130] The obtained transformed plant can be used in a conventional breeding scheme to produce more transformed plants with the same characteristics or to introduce the chimeric gene according to the invention in other varieties of the same or related plant species, or in hybrid plants. Seeds obtained from the transformed plants contain the chimeric genes of the invention as a stable genomic insert and are also encompassed by the invention.

[0131] It will be clear that the different stress resistant chimeric genes described herein, with DNA regions encoding different enzymes from the NAD salvage pathway can be combined within one plant cell or plant, to further enhance the stress tolerance of the plants comprising the chimeric genes. Thus, in one embodiment of the invention, plant cells and plants are provided which comprise at least two stress resistant chimeric genes each comprising a different coding region.

[0132] The transgenic plant cells and plant lines according to the invention may further comprise chimeric genes which will reduce the expression of endogenous PARP and/or PARG genes as described in WO 00/04173 and PCT/EP2004/003995. These further chimeric genes may be introduced e.g. by crossing the transgenic plant lines of the current invention with transgenic plants containing PARP and/or PARG gene expression reducing chimeric genes. Transgenic plant cells or plant lines may also be obtained by introducing or transforming the chimeric genes of the invention into transgenic plant cells comprising the PARP or PARG gene expression reducing chimeric genes or vice versa.

[0133] For the purpose of the invention, the promoter is a plant-expressible promoter. As used herein, the term "plant-expressible promoter" means a DNA sequence which is capable of controlling (initiating) transcription in a plant cell. This includes any promoter of plant origin, but also any promoter of non-plant origin which is capable of directing transcription in a plant cell, i.e., certain promoters of viral or bacterial origin such as the CaMV35S (Harpster et al., 1988 Mol. Gen. Genet. 212, 182-190), the subterranean clover virus promoter No 4 or No 7 (WO9606932), or T-DNA gene promoters but also tissue-specific or organ-specific promoters including but not limited to seed-specific promoters (e.g., WO89/03887), organ-primordia specific promoters (An et al., 1996, The Plant Cell 8, 15-30), stem-specific promoters (Keller et al., 1988, EMBO J. 7, 3625-3633), leaf specific promoters (Hudspeth et al., 1989, Plant Mol Biol 12, 579-589), mesophyl-specific promoters (such as the light-inducible Rubisco promoters), root-specific promoters (Keller et al., 1989, Genes Devel. 3, 1639-1646), tuber-specific promoters (Keil et al., 1989, EMBO J. 8, 1323-1330), vascular tissue specific promoters (Peleman et al., 1989, Gene 84, 359-369), stamen-selective promoters (WO 89/10396, WO 92/13956), dehiscence zone specific promoters (WO 97/13865) and the like.

[0134] The chimeric genes of the inventions may also be equipped with a nuclear localization signal ("NLS") functional in plants, operably linked to the DNA region encoding an enzyme of the NAD salvage pathway such as the SV40 NLS.

[0135] Having read this document, a person skilled in the art will immediately realize that similar effects with regard to increased stress resistance can be obtained whenever natural variants of plants are obtained wherein the endogenous genes coding for NAD salvage pathway enzymes are more active or expressed at a higher level. Such variant plants can be obtained by subjecting a population of plants to mutagenesis, such as, but not limited to EMS mutagenesis, followed by a screening for an increased activity of any one of the NAD salvage pathway enzymes, or a combination thereof.

[0136] It will also be immediately clear that a population of different varieties or cultivars can be screened for increased tolerance to the above mentioned stress conditions in general or particular selected abiotic stresses, followed by a correlation of the increased tolerance to stress conditions with the presence of a particular allele of any of the endogenous genes encoding an enzyme of the NAD salvage pathway enzyme. Such alleles can than be introduced into a plant of interest by crossing, if the species are sexually compatible, or they may be identified using conventional techniques as described herein (including hybridization or PCR amplification) and introduced using recombinant DNA technology. Introduction of particularly desired alleles using breeding techniques may be followed using molecular markers specific for the alleles of interest.

[0137] The methods and means described herein are believed to be suitable for all plant cells and plants, both dicotyledonous and monocotyledonous plant cells and plants including but not limited to cotton, Brassica vegetables, oilseed rape, wheat, corn or maize, barley, sunflowers, rice, oats, sugarcane, soybean, vegetables (including chicory, lettuce, tomato), tobacco, potato, sugarbeet, papaya, pineapple, mango, Arabidopsis thaliana, but also plants used in horticulture, floriculture or forestry.

[0138] As used herein "comprising" is to be interpreted as specifying the presence of the stated features, integers, steps or components as referred to, but does not preclude the presence or addition of one or more features, integers, steps or components, or groups thereof. Thus, e.g., a nucleic acid or protein comprising a sequence of nucleotides or amino acids, may comprise more nucleotides or amino acids than the actually cited ones, i.e., be embedded in a larger nucleic acid or protein. A chimeric gene comprising a DNA region which is functionally or structurally defined, may comprise additional DNA regions etc.

[0139] The following non-limiting Examples describe the construction of chimeric genes to increase stress resistance in plant cells and plants and the use of such genes.

[0140] Unless stated otherwise in the Examples, all recombinant DNA techniques are carried out according to standard protocols as described in Sambrook et al. (1989) Molecular Cloning: A Laboratory Manual, Second Edition, Cold Spring Harbor Laboratory Press, NY and in Volumes 1 and 2 of Ausubel et al. (1994) Current Protocols in Molecular Biology, Current Protocols, USA. Standard materials and methods for plant molecular work are described in Plant Molecular Biology Labfax (1993) by R. D. D. Croy, jointly published by BIOS Scientific Publications Ltd (UK) and Blackwell Scientific Publications, UK. Other references for standard molecular biology techniques include Sambrook and Russell (2001) Molecular Cloning: A Laboratory Manual, Third Edition, Cold Spring Harbor Laboratory Press, NY, Volumes I and II of Brown (1998) Molecular Biology LabFax, Second Edition, Academic Press (UK). Standard materials and methods for polymerase chain reactions can be found in Dieffenbach and Dveksler (1995) PCR Primer: A Laboratory Manual, Cold Spring Harbor Laboratory Press, and in McPherson at al. (2000) PCR--Basics: From Background to Bench, First Edition, Springer Verlag, Germany.

[0141] Throughout the specification reference is made to the following entries in the Sequence listing:

[0142] SEQ ID No. 1: XP.sub.--444840 (Candida glabrata)

[0143] SEQ ID No. 2: XP.sub.--456073 (Kluyveromyces lactis)

[0144] SEQ ID No. 3: NP.sub.--986013 (Eremothecium gossypii)

[0145] SEQ ID No. 4: XP.sub.--888958 (Candida albicans)

[0146] SEQ ID No. 5: XP500320 (Yarrowia lipolytica)

[0147] SEQ ID No. 6: XP389372 (Giberella zeae)

[0148] SEQ ID No. 7: XP.sub.--749509 (Aspergillus fumigatus)

[0149] SEQ ID No. 8: XP.sub.--712112 (Candida albicans)

[0150] SEQ ID No. 9: BAE56421 (Aspergillus oryzae)

[0151] SEQ ID No. 10: XP.sub.--567125 (Cryptococcus neofomans)

[0152] SEQ ID No. 11: XP.sub.--964547 (Neurospora crassa)

[0153] SEQ ID No. 12: XP.sub.--712135 (Candida albicans)

[0154] SEQ ID No. 13: XP.sub.--448179 (Candida glabrata)

[0155] SEQ ID No. 14: XP.sub.--453643 (Kluyveromyces lactis)

[0156] SEQ ID No. 15: NP.sub.--987024 (Eremothecium gossypii)

[0157] SEQ ID No. 16: XP.sub.--500272 (Yarrowia lipolytica)

[0158] SEQ ID No. 17: XP.sub.--722371 (Candida albicans)

[0159] SEQ ID No. 18: XP 456405 (Debaromyces hansenii)

[0160] SEQ ID No. 19: BAE61562 (Aspergillus oryzae)

[0161] SEQ ID No. 20: XP.sub.--759702 (Ustilago maydis)

[0162] SEQ ID No. 21: EAL18079 (Cryptococcus neoformans)

[0163] SEQ ID No. 22: NP.sub.--587771 (Schizosaccharomyces pombe)

[0164] SEQ ID No. 23: XP.sub.--681472 (Aspergillus nidulans)

[0165] SEQ ID No. 24: XP.sub.--959191 (Neurospora crassa)

[0166] SEQ ID No. 25: XP.sub.--567726 (Cryptococcus neoformans)

[0167] SEQ ID No. 26: EAQ90706 (Chaetomium globosum)

[0168] SEQ ID No. 27: XP.sub.--387574 (Giberella zeae)

[0169] SEQ ID No. 28: XP.sub.--748008 (Aspergillus fumigatus)

[0170] SEQ ID No. 29: XP.sub.--361704 (Magnaporthe grisea)

[0171] SEQ ID No. 30: Q06178

[0172] SEQ ID No. 31: XP.sub.--444815 (Candida glabrata)

[0173] SEQ ID No. 32: NP.sub.--986687 ((Eremothecium gossypii)

[0174] SEQ ID No. 33: XP.sub.--453005 (Kluyveromyces lactis)

[0175] SEQ ID No. 34: XP 458184(Debaromyces hansenii)

[0176] SEQ ID No. 35: XP.sub.--718656 (Candida albicans)

[0177] SEQ ID No. 36: XP.sub.--504391 (Yarrowia lipolytica)

[0178] SEQ ID No. 37: NP.sub.--592856 (Schizosaccharomyces pombe)

[0179] SEQ ID No. 38: XP.sub.--762639 (Ustilago maydis)

[0180] SEQ ID No. 39: XP.sub.--571297 (Cryptococcus neoformans)

[0181] SEQ ID No. 40: BAE57070 (Aspergillus oryzae)

[0182] SEQ ID No. 41: XP.sub.--750776 (Aspergillus fumigatus)

[0183] SEQ ID No. 42: XP.sub.--659349 (Aspergillus nidulans)

[0184] SEQ ID No. 43: XP.sub.--389652 (Giberella zeae)

[0185] SEQ ID No. 44: XP.sub.--957634 (Neurospora crassa)

[0186] SEQ ID No. 45: XP.sub.--363364 (Magnaporthe grisea)

[0187] SEQ ID No. 46: XP.sub.--758179 (Ustilago maydis)

[0188] SEQ ID No. 47: EAQ85219 ((Chaetomium globosum)

[0189] SEQ ID No. 48: CAA85352 (Saccharomyces cerevisae)

[0190] SEQ ID No. 49: XP.sub.--448893 (Candida glabrata)

[0191] SEQ ID No. 50: XP.sub.--453357 (Kluyveromyces lactis)

[0192] SEQ ID No. 51: NP.sub.--983562 (Eremothecium gossypii)

[0193] SEQ ID No. 52: XP.sub.--462577 (Debaromyces hansenii)

[0194] SEQ ID No. 53: XP.sub.--889008 (Candida albicans)

[0195] SEQ ID No. 54: XP.sub.--500338 (Yarrowia lipolytica)

[0196] SEQ ID No. 55: XP.sub.--746744 (Aspergillus fumigatus)

[0197] SEQ ID No. 56: BAE64333 (Aspergillus oryzae)

[0198] SEQ ID No. 57: XP.sub.--965789 (Neurospora crassa)

[0199] SEQ ID No. 58: EAQ93453 (Chaetomium globosum)

[0200] SEQ ID No. 59: XP.sub.--682385 (Aspergillus nidulans)

[0201] SEQ ID No. 60: AAN74808 (Gibberella moniliformis)

[0202] SEQ ID No. 61: Q9UTK3

[0203] SEQ ID No. 62: XP.sub.--361075 (Magnaporthe grisea)

[0204] SEQ ID No. 63: EAL18922 (Cryptococcus neoformans)

[0205] SEQ ID No. 64: XP.sub.--568039 (Cryptococcus neoformans)

[0206] SEQ ID No. 65: XP.sub.--760597 (Ustilago maydis)

[0207] SEQ ID No. 66 :NP 011524

[0208] All amino acid sequences referred to by their accession numbers are herein incorporated by reference.

EXAMPLES

Example 1

[0209] Assembly of stress resistant chimeric genes and introduction into plants.

[0210] To increase the stress resistance in plants, a chimeric gene is constructed using conventional techniques comprising the following DNA fragments in order: [0211] A promoter region from Cauliflower Mosaic Virus (CaMV 35S); [0212] A DNA fragment of about 60 by corresponding to the untranslated leader Cab22L; [0213] A DNA fragment as mentioned herein elsewhere encoding a NAD salvage pathway enzyme from fungal or yeast-like origin, different from PNC1, NMA1, NMA2 or NPT1 from Saccharomyces cereviseae. [0214] A fragment of the 3' untranslated end from the 35 S transcript of CaMV (3' 35S)

[0215] This chimeric gene is introduced in a T-DNA vector, between the left and right border sequences from the T-DNA, together with a selectable marker gene.

[0216] The T-DNA vectors are introduced into Agrobacterium strains comprising a helper Ti-plasmid using conventional methods. The chimeric genes are introduced into plants using a conventional transformation method. Transgenic plants exhibit a higher stress resistance than their counterpart plants without transgenes.

Sequence CWU 1

1

661211PRTCandida glabrata 1Met Lys Thr Leu Leu Val Ile Asp Val Gln Asn Asp Phe Ile Thr Pro 1 5 10 15 Asp His Ser Met Tyr Val Pro Gln Gly Glu Glu Val Val Ser Pro Ile 20 25 30 Val Glu Leu Met Lys Asp Pro Gln Trp His Arg Val Val Val Ser Arg 35 40 45 Asp Trp His Pro Gln Asn His Ile Ser Phe Ala Lys Asn His Gly Val 50 55 60 Glu Asp Tyr Thr Glu Thr Thr Tyr Lys Ser Pro Arg Pro Gly Asp Asp 65 70 75 80 Ser Thr Gln Pro Ala Thr Leu Trp Pro Val His Cys Val Gln Asn Thr 85 90 95 Arg Gly Ala Gln Leu Ala Pro Asp Ile Leu Glu Leu Val Asn Ser Lys 100 105 110 His Ile Lys Ile Val Asp Lys Gly Tyr Leu Ser Asn Cys Glu Tyr Tyr 115 120 125 Ser Ala Phe Asn Asp Thr Trp Glu Trp His Lys Thr Glu Leu Asp Glu 130 135 140 Tyr Leu Lys Lys His His Thr Thr Glu Val Tyr Val Val Gly Leu Ala 145 150 155 160 Leu Asp Phe Cys Val Lys Asn Thr Ala Ile Ser Ala Ala Lys Leu Gly 165 170 175 Tyr Asp Thr Thr Ile Leu Lys Asp Tyr Thr Lys Pro Ile Tyr Thr Asp 180 185 190 Glu Asp His Gln Gln Gln Leu Glu Lys Asp Leu Lys Glu His Asn Val 195 200 205 Lys Val Lys 210 2218PRTKluyveromyces lactis 2Met Gly Ala Arg Ala Leu Leu Val Ile Asp Ile Gln Asn Asp Phe Leu 1 5 10 15 Pro Pro Lys Gly Ser Leu Ala Val Gln Asp Gly Asp Thr Ile Ile Asp 20 25 30 Pro Val Ile Gln Leu Leu Gln Asp Gln Asp Trp Asp Cys Val Ala Met 35 40 45 Thr Lys Asp Trp His Pro Pro Asp His Ile Ser Phe Ala Lys Asn His 50 55 60 Gly Leu Pro Asp Phe Ser Ser Phe Thr Tyr Asp Ser Pro Val Pro Gly 65 70 75 80 Ser Thr Glu Lys Gln Ser Ala Thr Leu Trp Pro Val His Cys Val Gln 85 90 95 Glu Thr Trp Gly Ser Glu Val Pro Glu Lys Leu Leu Ala Glu Ile Leu 100 105 110 Lys Leu Lys Val Pro His Lys Ile Val Asn Lys Gly Tyr Leu Ser Asp 115 120 125 Arg Glu Tyr Tyr Ser Gly Phe Asn Asp Ile Trp Asn Asp His His Thr 130 135 140 Glu Leu Asp Ala Phe Phe Lys Glu Asn Asp Val Thr Glu Ile Tyr Val 145 150 155 160 Val Gly Leu Ala Phe Asp Phe Cys Val Lys Asn Ser Ala Ile Ser Ala 165 170 175 Ala Asn Leu Gly Tyr His Val Thr Ile Leu Lys Asp Tyr Thr Lys Ala 180 185 190 Ile Ala Asn Asp Leu Gln Ser Ile Glu Ser Phe Ile Gln Glu Leu Ala 195 200 205 Lys Asn Glu Val Ser Val Gln Glu Ser Ile 210 215 3218PRTEremothecium gossypii 3Met Ser Lys Ala Leu Ile Val Val Asp Val Gln Asn Asp Phe Ala Asp 1 5 10 15 Ala Arg Gly Ala Leu Ala Val Pro Gly Ala His Glu Ile Val Gln Pro 20 25 30 Leu Ala Glu Leu Ala Gln Asp Pro Arg Trp Ala Tyr Val Ala Met Thr 35 40 45 Arg Asp Trp His Pro Pro Asp His Val Ser Phe Ala Asp Thr His Gly 50 55 60 Arg Pro Pro Phe Ser Pro Tyr Met Tyr His Pro Pro Pro Gly Val Arg 65 70 75 80 Ala Pro Pro Gln Ala Gly Thr Leu Trp Pro Thr His Cys Val Gln Gly 85 90 95 Ser Trp Gly Ala Gln Leu Ala Pro Gln Leu Ala Ala Ala Arg Ser Leu 100 105 110 Pro His Ser Val Val Asp Lys Gly Val Trp Pro Asp Arg Glu Cys Tyr 115 120 125 Ser Ala Phe Glu Asp Ile Trp Ala Asp Arg Ser Ser Gly Leu Asp Gly 130 135 140 Leu Leu Arg Ser His Gly Val Lys His Val Tyr Val Ala Gly Leu Ala 145 150 155 160 Leu Asp Tyr Cys Val Lys Ser Thr Ala Ile Ser Ala Ala Arg Leu Gly 165 170 175 Tyr Thr Thr Thr Ile Leu Leu Asp Tyr Thr Arg Ala Ile Ala Ala Asp 180 185 190 Ala Gln Ser Met Ala Arg Leu Ser Ser Asp Leu Ala Gly His Gln Val 195 200 205 Ala Leu Cys Glu Gly Ala Glu Pro Leu Pro 210 215 4244PRTCandida albicans 4Met Lys Lys Thr Ala Leu Ile Val Val Asp Leu Gln Glu Asp Phe Leu 1 5 10 15 Pro Pro Asn Gly Ser Leu Ala Ile Lys Asn Gly Arg Ser Val Ile Pro 20 25 30 Lys Ile Asn Gln Leu Leu Pro Ser Gln Asp Asn His Ser Lys Phe Asp 35 40 45 Trp Ser Leu Ile Val Ala Thr Gln Asp Trp His Pro Pro Asn His Thr 50 55 60 Ser Phe Ala Ser Gln His Glu Asn Val Ala Pro Phe Thr Glu Ile Glu 65 70 75 80 Phe Ile His Pro Glu Lys Lys Leu Asp Pro Lys Thr Asn Gln Pro Ile 85 90 95 Val Met Asn Gln Ile Val Trp Pro Asp His Cys Val Gln Gly Thr Lys 100 105 110 Gly Ala Gln Leu Glu Pro Ser Phe Ala Asn Gln Phe Glu Lys Leu Thr 115 120 125 Lys Gln Asp Asp Asn Asn Thr Ala Pro Cys Lys Ile Val Lys Lys Gly 130 135 140 Tyr Leu Pro Asp Arg Glu Tyr Tyr Ser Cys Phe Gln Asp Cys Trp Gly 145 150 155 160 Leu His His Thr Glu Leu Ile Asp Leu Leu His Glu Tyr Asp Ile Glu 165 170 175 Asn Val Val Phe Val Gly Leu Ala Tyr Asp Phe Cys Val Leu Ser Ser 180 185 190 Ala Ile Asp Ser Ala Lys Asn Gly Phe Lys Thr Phe Val Leu Lys Asn 195 200 205 Tyr Cys Glu Ser Val Tyr Pro Glu Lys Ile Asn Asp Thr Asp Lys Leu 210 215 220 Phe Ile Asp Asn Gly Val Thr Ile Val Asp Asn Asp Glu Lys Phe Asp 225 230 235 240 Ser Leu Phe Lys 5203PRTYarrowia lipolytica 5Met Ala Ala Leu Ile Ile Val Asp Leu Gln Asn Asp Phe Leu Pro Gly 1 5 10 15 Gly Ser Leu Ala Val Val Asp Gly Asn Asp Ile Ile Pro Ile Val Gln 20 25 30 Lys Leu Ala Asp Ser Gly Lys Tyr Lys Phe Val Val Ala Thr Lys Asp 35 40 45 Ser His Pro Gln Asp His Thr Ser Phe Ala Ala Asn His Gly Ala Glu 50 55 60 Pro Phe Thr Ser Ile Thr Phe Lys His Pro Asn Ser Asp Lys Gln Val 65 70 75 80 Asp His Thr Val Trp Pro Val His Cys Val Glu Gly Thr Ser Gly Ala 85 90 95 Asp Tyr Pro Pro Ser Phe Asp Ser Ser Asn Val Gln Ala Leu Val Arg 100 105 110 Lys Gly Tyr Leu Gln Asp Arg Glu Tyr Tyr Ser Gly Phe Glu Asp Val 115 120 125 Trp Gly Ile His Lys Thr Glu Leu His Asp Leu Leu Gln Gln Asn Gly 130 135 140 Val Thr Glu Val Asp Val Val Gly Leu Ala Phe Asp Tyr Cys Val Phe 145 150 155 160 Asn Thr Ala Lys Asp Ala Ala Lys Arg Gly Tyr Lys Thr Thr Val Ile 165 170 175 Arg Glu Ala Thr Lys Pro Val Asp Pro Ser Ser Glu Lys Lys Ile Val 180 185 190 Ala Ser Leu Glu Glu Ala Gly Val His Val Val 195 200 6223PRTGiberella zeae 6Met Thr Ser Gln Lys Ser Phe Lys Pro Ala Leu Ile Ile Val Asp Phe 1 5 10 15 Gln Glu Asp Phe Cys Pro Pro Asn Gly Ser Leu Ala Val Pro Glu Gly 20 25 30 Arg Thr Ile Ala Pro Thr Ile Asn Thr Leu Thr Ala Leu Pro Phe His 35 40 45 Leu Ile Leu Ala Thr Lys Asp Phe His Pro Pro Ser His Ile Ser Phe 50 55 60 Ala Ser Asn His Pro Ser Ser Thr Pro Tyr Thr Ser Thr Thr Thr Ile 65 70 75 80 Thr His Pro Arg Asp Ser Ser Arg Ser Tyr Thr Thr Thr Leu Trp Pro 85 90 95 Thr His Cys Val Gln Gly Thr Pro Gly Ala Asp Leu Val Pro Glu Leu 100 105 110 Asp Val Ser Arg Leu His Ala Val Ile Glu Lys Gly Gln Asp Lys Arg 115 120 125 Val Glu Met Tyr Ser Ala Phe Tyr Asp Pro Phe Arg Val Ser Asp Ser 130 135 140 Gly Leu Ala Gly Met Leu Gly Glu Gln Asn Val Thr Asp Val Phe Val 145 150 155 160 Val Gly Leu Ala Ala Asp Phe Cys Val Lys Ala Thr Ala Glu Asp Ala 165 170 175 Val Lys Glu Gly Tyr Ser Thr Trp Ile Val Asn Glu Gly Thr Lys Pro 180 185 190 Val Met Pro Asp Lys Trp Asp Glu Cys Arg Lys Gly Met Glu Asp Met 195 200 205 Gly Ile Lys Phe Thr Ser Val Ala Asn Ala Val Asp Lys Phe Lys 210 215 220 7235PRTAspergillus fumigatus 7Met Lys Ala Ala Leu Ile Val Val Asp Met Gln Glu Asp Phe Cys Pro 1 5 10 15 Pro Asp Gly Ser Leu Ala Val Gln Gly Ala Arg Ser Ile Ala Pro Leu 20 25 30 Ile Asn Ser Leu Leu Ala Asn Pro Gly Phe Val Ile Arg Val Ala Ser 35 40 45 Gln Asp Tyr His Pro Arg Asp His Val Ser Phe Ala Ser Asn His Pro 50 55 60 Glu Pro Asn Asn Arg Pro Phe Glu Ser Val Ile Gln Met Asn Asn Pro 65 70 75 80 Ala Pro Gly Lys Glu Ser Glu Thr Lys Glu Gln Arg Leu Trp Pro Val 85 90 95 His Cys Val Gly Gly Thr Lys Gly Ala Thr Ile Ile Pro Glu Ile Asp 100 105 110 Ser Ser Lys Ile Asp Leu His Val Lys Lys Gly Met Asp Ser Arg Val 115 120 125 Glu Met Tyr Ser Ala Phe Ser Asp Ala Phe Gly Asn Leu Asp Pro Ala 130 135 140 Val His Thr Gln Ser Val Asp Val Asp Leu Lys Ala Val Leu Ala Glu 145 150 155 160 Arg Gly Ile Thr His Val Phe Ser Ala Gly Ile Ala Gly Asp Tyr Cys 165 170 175 Val Lys Tyr Thr Ala Met Asp Ala Ala Arg Ala Gly Phe Lys Ser Phe 180 185 190 Leu Val Glu Asp Ala Thr Arg Ser Val Asp Ser Gly Ala Gly Trp Glu 195 200 205 Glu Ala Arg Arg Glu Cys Glu Ala Ala Gly Val Ser Ile Ile Gln Ser 210 215 220 Asp Gly Pro Glu Ile Ala Ala Leu Thr Ala Ser 225 230 235 8165PRTCandida albicans 8Met Lys Lys Thr Ala Leu Ile Val Val Asp Leu Gln Glu Asp Phe Leu 1 5 10 15 Pro Pro Asn Gly Ser Leu Ala Ile Lys Asn Gly Arg Ser Val Ile Pro 20 25 30 Lys Ile Asn Gln Leu Leu Pro Ser Gln Asp Asn His Ser Lys Phe Asp 35 40 45 Trp Ser Leu Ile Val Ala Thr Gln Asp Trp His Pro Pro Asn His Thr 50 55 60 Ser Phe Ala Ser Gln His Glu Asn Val Ala Pro Phe Thr Glu Ile Glu 65 70 75 80 Phe Ile His Pro Glu Lys Lys Leu Asp Pro Lys Thr Asn Gln Pro Ile 85 90 95 Val Met Asn Gln Ile Val Trp Pro Asp His Cys Val Gln Gly Thr Lys 100 105 110 Gly Ala Gln Leu Glu Pro Ser Phe Ala Asn Gln Phe Glu Lys Leu Thr 115 120 125 Lys Gln Asp Asp Asn Asn Thr Ala Pro Cys Lys Ile Val Lys Lys Gly 130 135 140 Tyr Leu Pro Asp Arg Glu Tyr Tyr Ser Cys Phe Gln Asp Cys Trp Gly 145 150 155 160 Tyr Ile Ile Ser Asn 165 9234PRTAspergillus oryzae 9Met Lys Ala Ala Leu Val Val Val Asp Met Gln Glu Asp Phe Cys Pro 1 5 10 15 Pro Asn Gly Val Leu Pro Val Gln Glu Gly Arg Ala Ile Ala Pro Ile 20 25 30 Ile Asn Glu Leu Leu Ala His Gln Gly Phe Ala Val Arg Val Ala Thr 35 40 45 Gln Asp Tyr His Pro Val Asp His Ile Ser Phe Ala Asn Ser His Pro 50 55 60 Arg Pro Asn Asn Arg Pro Phe Glu Ser Val Ile Thr Val Asn Asn Pro 65 70 75 80 Ala Pro Gly Lys Glu His Glu Thr Lys Pro Gln Asn Leu Trp Pro Ala 85 90 95 His Cys Val Gly Glu Thr Arg Gly Ala Glu Ile Ile Pro Glu Ile Gln 100 105 110 Thr Asp Asn Ile Asp Leu Tyr Val Lys Lys Gly Met His Ser Gln Val 115 120 125 Glu Met Tyr Ser Ala Phe Ala Asp Ala Phe Gly Asn Val Asp Pro Ser 130 135 140 Ile Thr Asp Gln Ser Val Asp Ala Asp Leu Lys Asp Phe Leu Ala Ser 145 150 155 160 Lys Gly Val Thr Asp Val Phe Val Val Gly Leu Ala Gly Asp Tyr Cys 165 170 175 Val Lys His Thr Ala Ile Asp Ala Ala Arg Val Gly Phe Lys Ser Tyr 180 185 190 Val Val Glu Asn Ala Ile Arg Cys Val Val Pro Gly Ser Gly Trp Asp 195 200 205 Gly Ala Lys Arg Glu Leu Arg Glu Ala Gly Val Ser Ile Ile Gln Ser 210 215 220 Asn Gly Pro Glu Ile Ser Gly Leu Ala Ile 225 230 10225PRTCryptococcus neoformans 10Met Ala Ser Met Pro Ala Ser Thr Ala Leu Ile Ile Val Asp Val Gln 1 5 10 15 Asn Asp Phe Leu Pro Pro Thr Gly Ser Leu Ala Val Pro Asn Gly Arg 20 25 30 Glu Val Leu Pro Val Ile Thr Gly Leu Leu Asp Arg Lys Trp Asp Trp 35 40 45 Ala Val Val Val Val Ser Gln Asp Tyr His Pro Lys Gly His Ile Ser 50 55 60 Phe Ala Ser Ala His Pro Pro Asn Gln Ala Tyr Thr Gln Leu Pro Leu 65 70 75 80 Val Asn Ala His Gly Glu Ser Tyr Ile Gln Thr Leu Trp Pro Asp His 85 90 95 Cys Ile Gln Gly Thr Ala Gly Ala Asp Leu Glu Ser Gly Leu Ala Glu 100 105 110 Val Leu Ala Lys Arg Gly Asp Gly Ile His Ser Lys Leu Glu Ala Tyr 115 120 125 Ser Ala Phe Gln Glu Ile Val Pro Pro Lys Thr Ser Glu Leu Ala Glu 130 135 140 Phe Leu Leu Ala Gln Gly Val Asn Lys Val Val Ile Ala Gly Val Ala 145 150 155 160 Thr Asp Phe Cys Val Leu Gln Thr Ala Leu Ser Ser Ile Ser Ser Ser 165 170 175 Phe Pro Thr Leu Leu Ile Ala Pro Ala Met Arg Ala Ile Ser Pro Glu 180 185 190 Tyr Glu Ala Lys Thr Phe Glu Ala Val Glu Ser Leu Gly Gly Val Ile 195 200 205 Leu Gly Arg Asn Gly Glu Glu Trp Lys Thr Lys Leu Ala Glu Trp Ile 210 215 220 Arg 225 11297PRTNeurospora crassa 11Met Gly Phe Leu Glu Trp Leu Met Pro Pro Ser Ile Phe Asn Val Phe 1 5 10 15 Gln Thr Arg Leu Leu Glu Asn Gly Gln Gly Ala Gln Pro Glu Pro Asp 20 25 30 Phe Arg Pro Ala Leu Leu Val Val Asp Met Gln Glu Asp Phe Cys Pro 35 40 45 Pro Asn Gly Thr Leu Ala Val Thr Gly Gly Arg Ser Ile Thr Pro Leu 50 55 60 Ile Asn Thr Leu Leu Ser Ser Pro Leu Phe Val Leu Arg Ile Ala Thr 65 70 75 80 Lys Asp Trp His Pro Pro Asn His Ile Ser Phe Ala Ser Asn His Asn 85 90

95 His Ala Ser Ser Pro Ser Pro Cys Cys Pro Asp Ser Ser Gly Lys Ala 100 105 110 Ala Ile Pro Phe Leu Ser Thr Thr Thr Val His Asn Pro His Asn Pro 115 120 125 Ser Glu Ser Tyr Thr Thr Arg Leu Trp Pro Ser His Cys Ile Ala Asp 130 135 140 Thr Pro Gly Ala Ser Leu Ile Pro Glu Leu Asp Val Ser Lys Ile Asp 145 150 155 160 Gln Ile Leu Glu Lys Gly Thr Asn Arg Leu Val Glu Met Tyr Ser Ala 165 170 175 Phe Tyr Asp Pro Phe Thr Ser Pro Arg Val Ser Asp Ser Gly Leu Ala 180 185 190 His Met Leu Arg Glu Ala Lys Val Thr His Val Tyr Val Val Gly Leu 195 200 205 Ala Ala Asp Tyr Cys Val Trp Ser Thr Ala Met Asp Ala His Asn Glu 210 215 220 Gly Phe Glu Thr Val Val Val Glu Glu Ala Thr Lys Pro Val Asp Glu 225 230 235 240 Asp Gly Trp Arg Arg Cys Lys Glu Ala Leu Val Gly Glu Pro Gly Val 245 250 255 Arg Val Val Arg Trp Glu Gly Glu Glu Val Arg Arg Leu Phe Pro Gly 260 265 270 Gly Leu Val Thr Thr Thr Val Gly Ala Gly Asn Asp Glu Glu Val Val 275 280 285 Glu Glu Glu Glu Glu Glu Glu Lys Ile 290 295 12121PRTCandida albicans 12Met Lys Lys Thr Ala Leu Ile Val Val Asp Leu Gln Glu Asp Phe Leu 1 5 10 15 Pro Pro Asn Gly Ser Leu Ala Ile Lys Asn Gly Arg Ser Val Ile Pro 20 25 30 Lys Ile Asn Gln Leu Leu Pro Ser Gln Asp Asn His Ser Lys Phe Asp 35 40 45 Trp Ser Leu Ile Val Ala Thr Gln Asp Trp His Pro Pro Asn His Thr 50 55 60 Ser Phe Ala Ser Gln His Glu Asn Val Ala Pro Phe Thr Glu Ile Glu 65 70 75 80 Phe Ile His Pro Glu Lys Lys Leu Asp Pro Lys Thr Asn Gln Pro Ile 85 90 95 Val Met Asn Gln Ile Val Trp Pro Asp His Cys Val Gln Gly Thr Lys 100 105 110 Gly Ala Gln Leu Glu Pro Ser Phe Ala 115 120 13713PRTCandida glabrata 13Met Ser His Leu Val Thr Leu Ala Thr Cys Ser Leu Asn Gln Trp Ala 1 5 10 15 Leu Asp Phe Glu Gly Asn Arg Asp Arg Ile Leu Glu Ser Ile Arg Ile 20 25 30 Ala Lys Glu Arg Gly Ala Arg Leu Arg Val Gly Pro Glu Leu Glu Ile 35 40 45 Ser Gly Tyr Gly Cys Leu Asp His Phe Leu Glu Asn Asp Val Cys Leu 50 55 60 His Ser Trp Glu Met Tyr Ala Gln Ile Leu Lys Asn Pro Glu Thr His 65 70 75 80 Gly Leu Ile Leu Asp Ile Gly Met Pro Leu Leu His Lys Asn Val Arg 85 90 95 Tyr Asn Cys Arg Leu Leu Ser Leu Asp Gly Lys Ile Leu Phe Ile Arg 100 105 110 Pro Lys Ile Trp Leu Ala Asn Asp Gly Asn Tyr Arg Glu Met Arg Phe 115 120 125 Phe Thr Pro Trp Met Lys Pro Gly Val Val Glu Glu Leu Thr Leu Pro 130 135 140 Pro Met Ile Gln Lys Ile Thr Gly Gln Lys Lys Val Pro Phe Gly Asp 145 150 155 160 Ala Val Ile Asn Thr Leu Asp Thr Cys Ile Gly Ala Glu Thr Cys Glu 165 170 175 Glu Val Phe Thr Pro Gln Ser Pro His Ile Ala Met Ser Leu Asp Gly 180 185 190 Val Glu Ile Ile Thr Asn Ser Ser Gly Ser His His Glu Leu Arg Lys 195 200 205 Leu Asn Lys Arg Leu Glu Leu Ile Leu Asn Gly Thr Gly Arg Cys Gly 210 215 220 Gly Val Tyr Leu Tyr Ala Asn Gln Lys Gly Cys Asp Gly Asp Arg Leu 225 230 235 240 Tyr Tyr Asp Gly Cys Ala Leu Ile Ala Ile Asn Gly Lys Ile Leu Ala 245 250 255 Gln Gly Lys Gln Phe Ser Leu Asp Asp Val Glu Val Val Thr Ala Thr 260 265 270 Val Asp Leu Glu Glu Val Arg Asn His Arg Ala Asn Val Met Ser Arg 275 280 285 Gly Leu Gln Ser Ser Leu Ala Asp Leu Lys Tyr Glu His Ile Asp Val 290 295 300 Glu Ile Glu Leu Ala Pro Arg Gly Ser Arg Phe Asn Pro Lys Ile Thr 305 310 315 320 Pro Thr Lys Ser Arg Asp Val Thr Tyr His Thr Pro Glu Glu Glu Ile 325 330 335 Ala Leu Gly Pro Ala Cys Trp Leu Trp Asp Tyr Ile Arg Arg Cys Asn 340 345 350 Gly Thr Gly Tyr Phe Leu Pro Leu Ser Gly Gly Ile Asp Ser Cys Ala 355 360 365 Thr Ala Met Ile Ile His Ser Met Cys Arg Leu Val His Lys Ala Cys 370 375 380 His Glu Gly Asn Asp Leu Val Leu Lys Asp Ile Arg Arg Ile Thr Arg 385 390 395 400 Ser Pro Asp Asp Trp Ile Pro Glu Asn Pro Gln Glu Ile Ala Asn Lys 405 410 415 Met Phe His Thr Cys Phe Met Gly Thr Glu Asn Ser Ser Val Glu Thr 420 425 430 Arg Ser Arg Ser Lys Gln Leu Ala Glu Lys Ile Gly Ser Tyr His Val 435 440 445 Asp Leu Asn Met Asp Gly Leu Val Ser Ser Val Val Ser Leu Phe Glu 450 455 460 Val Ala Thr Gly Arg Lys Pro Ile Phe Lys Ile Phe Gly Gly Ser Gln 465 470 475 480 Ile Glu Asn Leu Ala Leu Gln Asn Ile Gln Ala Arg Leu Arg Met Val 485 490 495 Leu Ala Tyr Leu Phe Ala Gln Leu Leu Pro Trp Val Arg Gly Ile Pro 500 505 510 Asn Ser Gly Gly Leu Leu Val Leu Gly Ser Ala Asn Val Asp Glu Cys 515 520 525 Leu Arg Gly Tyr Leu Thr Lys Tyr Asp Cys Ser Ser Ala Asp Val Asn 530 535 540 Pro Ile Gly Gly Ile Ser Lys Thr Asp Leu Lys Gly Phe Ile Lys Tyr 545 550 555 560 Ala Ser Glu Glu Tyr Asp Met Pro Ile Leu Asp Glu Phe Leu Asn Ala 565 570 575 Thr Pro Thr Ala Glu Leu Glu Pro Ile Thr Lys Asp Tyr Val Gln Ser 580 585 590 Asp Glu Arg Asp Met Gly Met Thr Tyr Glu Glu Leu Ser Val Phe Gly 595 600 605 Tyr Leu Arg Lys Val Glu Lys Cys Gly Pro Tyr Ser Met Phe Leu Lys 610 615 620 Leu Leu His Glu Trp Thr Pro Arg Leu Thr Pro Ala Gln Val Ala Glu 625 630 635 640 Lys Val Lys Arg Phe Phe Phe Phe Tyr Ala Ile Asn Arg His Lys Gln 645 650 655 Thr Val Leu Thr Pro Ser Tyr His Ala Glu Gln Tyr Ser Pro Asp Asp 660 665 670 Asn Arg Phe Asp Leu Arg Pro Phe Leu Ile Asn Pro Arg Phe Pro Trp 675 680 685 Ala Ser Lys Lys Ile Asp Glu Val Val Lys Gln Cys Glu Gly His Ser 690 695 700 Ser Glu Ile Asp Phe Met Thr Ile Asp 705 710 14714PRTKluyveromyces lactis 14Met Ser Gln Leu Ile Thr Val Ala Thr Cys Asn Leu Asn Gln Trp Ala 1 5 10 15 Leu Asp Phe Glu Gly Asn Arg Asp Arg Ile Phe Glu Ser Ile Lys Ile 20 25 30 Ala Lys Glu Arg Gly Ala Lys Leu Arg Val Gly Pro Glu Leu Glu Ile 35 40 45 Thr Gly Tyr Gly Cys Leu Asp His Phe Leu Glu Asp Asp Val Phe Leu 50 55 60 His Ser Trp Glu Met Tyr Gly Gln Ile Ile Lys Arg Pro Glu Thr His 65 70 75 80 Gly Ile Leu Leu Asp Ile Gly Met Pro Val Met His Arg Asn Val Arg 85 90 95 Tyr Asn Cys Arg Ile Leu Ser Leu Asp Gly Lys Ile Leu Phe Ile Arg 100 105 110 Pro Lys Ile Trp Leu Ala Asn Asp Gly Asn Tyr Arg Glu Met Arg Phe 115 120 125 Phe Thr Pro Trp Met Lys Ala Ala His Thr Glu Glu Tyr Leu Leu Pro 130 135 140 Pro Met Ile Gln Lys Leu Thr Gly Gln Tyr Arg Ile Pro Phe Gly Asp 145 150 155 160 Ala Val Ile Ser Thr Leu Asp Thr Cys Ile Gly Ala Glu Thr Cys Glu 165 170 175 Glu Leu Phe Thr Pro Gln Ser Pro His Ile Ala Met Ser Leu Asp Gly 180 185 190 Val Glu Ile Phe Thr Asn Ser Ser Gly Ser His His Glu Leu Arg Lys 195 200 205 Leu Asp Lys Arg Leu Asp Leu Ile Met Ser Ala Thr Arg Arg Cys Gly 210 215 220 Gly Val Tyr Leu Tyr Ala Asn Gln Arg Gly Cys Asp Gly Asp Arg Leu 225 230 235 240 Tyr Tyr Asp Gly Cys Ala Leu Ile Cys Val Asn Gly Ser Ile Val Ala 245 250 255 Gln Gly Ser Gln Phe Cys Leu Lys Asp Val Glu Val Val Thr Ala Thr 260 265 270 Val Asp Leu Glu Gln Val Arg Ser Tyr Arg Ser Thr Val Met Ser Arg 275 280 285 Gly Leu Gln Ala Ser Leu Thr Glu Thr Lys Phe Lys Arg Ile Asp Val 290 295 300 Glu Val Glu Leu Ala Thr Leu Asp Asp Arg Phe Asp Ser Thr Leu Val 305 310 315 320 Pro Glu Lys Pro Arg Lys Ala Phe Tyr His Ile Pro Ser Glu Glu Ile 325 330 335 Ala Leu Gly Pro Ala Cys Trp Leu Trp Asp Tyr Leu Arg Arg Cys Asn 340 345 350 Gly Thr Gly Tyr Phe Leu Pro Leu Ser Gly Gly Ile Asp Ser Cys Ala 355 360 365 Thr Ala Val Ile Val His Ser Met Cys Arg Leu Val Val Lys Glu Ala 370 375 380 Ala Glu Gly Asn Gln Gln Val Ile Lys Asp Val Arg Arg Leu Ala Arg 385 390 395 400 Met Asn Asp Glu Trp Ile Pro Lys Thr Pro Gln Glu Leu Ala Asn Lys 405 410 415 Ile Phe Asn Thr Cys Phe Met Gly Thr Glu Asn Ser Ser Lys Glu Thr 420 425 430 Arg Ser Arg Ala Lys Lys Leu Ala Glu His Ile Gly Ala Tyr His Val 435 440 445 Asp Leu Asn Met Asp Ser Leu Val Ser Ser Met Val Thr Leu Phe Glu 450 455 460 Val Thr Thr Gly Lys Arg Pro Ile Phe Lys Ile Phe Gly Gly Ser Gln 465 470 475 480 Thr Glu Asn Leu Ala Leu Gln Asn Ile Gln Ala Arg Leu Arg Met Val 485 490 495 Leu Ala Tyr Leu Phe Ala Gln Leu Leu Pro Trp Val Arg Ser Ile Pro 500 505 510 Asn Ala Gly Gly Leu Leu Val Leu Gly Ser Ala Asn Val Asp Glu Cys 515 520 525 Leu Arg Gly Tyr Leu Thr Lys Tyr Asp Cys Ser Ser Ala Asp Ile Asn 530 535 540 Pro Ile Gly Gly Ile Ser Lys Thr Asp Leu Lys Lys Phe Ile Ala Tyr 545 550 555 560 Ala Ser Lys Glu Phe Asp Leu Pro Ile Leu Glu Glu Phe Leu Asn Ala 565 570 575 Thr Pro Thr Ala Glu Leu Glu Pro Ile Thr Lys Asn Tyr Val Gln Ser 580 585 590 Asp Glu Ile Asp Met Gly Met Thr Tyr Glu Glu Leu Ser Val Phe Gly 595 600 605 Tyr Leu Arg Lys Val Glu Lys Cys Gly Pro Phe Ser Met Tyr Leu Lys 610 615 620 Leu Leu His Glu Trp Thr Pro Lys Leu Thr Pro Ala Gln Val Ala Glu 625 630 635 640 Lys Val Lys Lys Phe Phe Phe Phe Tyr Ala Ile Asn Arg His Lys Gln 645 650 655 Thr Val Leu Thr Pro Ser Tyr His Ala Glu Gln Tyr Ser Pro Asp Asp 660 665 670 Asn Arg Phe Asp Leu Arg Pro Phe Leu Ile Asn Pro Arg Phe Pro Trp 675 680 685 Ala Phe Lys Lys Ile Asp Asp Ala Val Ala Gln Ser Glu Gly Thr Leu 690 695 700 Ser Gly Ala Leu Asp Val Met Thr Val Glu 705 710 15715PRTEremothecium gossypii 15Met Ser His Leu Ile Thr Leu Ala Thr Cys Asn Leu Asn Gln Trp Ala 1 5 10 15 Leu Asp Phe Glu Gly Asn Arg Asp Arg Ile Leu Glu Ser Ile Arg Ile 20 25 30 Ala Lys Glu Lys Asn Ala Lys Leu Arg Val Gly Pro Glu Leu Glu Val 35 40 45 Ser Gly Tyr Gly Cys Leu Asp His Phe Leu Glu Asp Asp Val Tyr Leu 50 55 60 His Ser Trp Glu Met Tyr Ala Gln Ile Leu Lys Asp Glu Lys Thr His 65 70 75 80 Gly Ile Leu Leu Asp Ile Gly Met Pro Val Val His Lys Asn Val Arg 85 90 95 Tyr Asn Cys Arg Val Leu Ser Leu Asp Gly His Ile Leu Phe Ile Arg 100 105 110 Pro Lys Leu Trp Leu Ala Asn Asp Gly Asn Tyr Arg Glu Met Arg Phe 115 120 125 Phe Thr Pro Trp Met Lys Pro Thr Val Val Glu Glu Phe Gln Leu Pro 130 135 140 Pro Val Ile Gln Lys Ile Thr Gly Gln His Ile Ile Pro Phe Gly Asp 145 150 155 160 Ala Val Ile Arg Thr Leu Asp Thr Cys Ile Gly Ala Glu Thr Cys Glu 165 170 175 Glu Leu Phe Thr Pro Gln Ser Pro Asn Ile Ala Met Ser Leu Asp Gly 180 185 190 Val Glu Ile Ile Thr Asn Ser Ser Gly Ser His His Glu Leu Arg Lys 195 200 205 Leu His Lys Arg Leu Asp Leu Ile Leu Gly Ala Thr Gly Arg Cys Gly 210 215 220 Gly Val Tyr Leu Tyr Ala Asn Gln Arg Gly Cys Asp Gly Asp Arg Leu 225 230 235 240 Tyr Tyr Asp Gly Cys Ala Leu Ile Ala Val Asn Gly Arg Val Val Ala 245 250 255 Gln Gly Ser Gln Phe Ser Leu Arg Asp Val Glu Val Val Thr Ala Thr 260 265 270 Val Asp Leu Gln Glu Val Arg Asp Tyr Arg Met Ser Val Met Ser Arg 275 280 285 Gly Leu Gln Ala Val Ser Asn Asn Val Thr Phe Glu Arg Ile Gln Val 290 295 300 Pro Val Glu Leu Ala Ala Met Gln Asp Arg Phe Asn Pro Thr Ile Asn 305 310 315 320 Leu Thr Lys Ala Lys Ala Pro Tyr Tyr His Ser Pro Glu Glu Glu Ile 325 330 335 Ala Leu Gly Pro Ala Cys Trp Leu Trp Asp Tyr Leu Arg Arg Cys Arg 340 345 350 Gly Thr Gly Tyr Phe Leu Pro Leu Ser Gly Gly Ile Asp Ser Cys Ala 355 360 365 Thr Ala Val Ile Val His Ser Met Cys Arg Met Val Val Lys Glu Ala 370 375 380 Ser Glu Gly Asn Leu Gln Val Ile Ala Asp Ala Arg Arg Leu Ala Arg 385 390 395 400 Ala Ser Asp Asp Trp Ile Pro Thr Asp Ala Arg Glu Phe Ala Asn Met 405 410 415 Ile Phe His Thr Cys Phe Met Gly Thr Ala Asn Ser Thr Asn Glu Thr 420 425 430 Arg Ser Arg Ala Lys Lys Leu Ala Glu His Leu Gly Ala Tyr His Val 435 440 445 Asp Leu Asn Met Asp Ser Val Val Lys Ser Val Val Thr Leu Phe Glu 450 455 460 Val Thr Thr Gly Lys Arg Pro Ile Phe Lys Val Phe Gly Gly Ser Asn 465 470 475 480 Ile Glu Asn Leu Ala Leu Gln Asn Ile Gln Ala Arg Leu Arg Met Val 485 490 495 Leu Ala Tyr Leu Phe Ala Gln Leu Leu Pro Trp Val Arg Ser Ile Lys 500 505 510 Asn Ser Gly Gly Leu Leu Val Leu Gly Ser Ala Asn Val Asp Glu Cys 515 520 525 Leu Arg Gly Tyr Leu Thr Lys Tyr Asp Cys Ser Ser Ala Asp Ile Asn 530

535 540 Pro Ile Gly Gly Ile Ser Lys Lys Asp Leu Lys Asn Phe Ile Ser Tyr 545 550 555 560 Ala Ser Lys Glu Phe Asp Leu Pro Ile Leu Arg Glu Phe Val Glu Ala 565 570 575 Thr Pro Thr Ala Glu Leu Glu Pro Ile Thr Glu Asp Tyr Val Gln Ser 580 585 590 Asp Glu Arg Asp Met Gly Met Thr Tyr Glu Glu Leu Ser Val Phe Gly 595 600 605 Tyr Leu Arg Lys Val Glu Lys Cys Gly Pro Tyr Ser Met Phe Leu Lys 610 615 620 Leu Leu His Glu Trp Thr Pro Arg Leu Thr Pro Ser Glu Val Ala Glu 625 630 635 640 Lys Val Lys Arg Phe Phe Tyr Phe Tyr Ala Ile Asn Arg His Lys Gln 645 650 655 Thr Val Leu Thr Pro Ser Tyr His Ala Glu Gln Tyr Ser Pro Asp Asp 660 665 670 Asn Arg Phe Asp Leu Arg Pro Phe Leu Ile Asp Pro Arg Phe Ser Trp 675 680 685 Ala Ser Lys Lys Ile Asp Leu Val Val Lys Gln Cys Glu Gly Gly Pro 690 695 700 Ser Thr Thr Gln Leu Asp Val Met Ser Val Asp 705 710 715 16705PRTYarrowia lipolytica 16Met Gly His Tyr Val Thr Leu Ala Thr Cys Asn Leu Asn Gln Trp Ala 1 5 10 15 Leu Asp Phe Glu Gly Asn Arg Asp Arg Ile Leu Glu Ser Ile Arg Glu 20 25 30 Ala Lys Arg Gln Gly Ala Ser Leu Arg Val Gly Pro Glu Leu Glu Ile 35 40 45 Thr Gly Tyr Gly Cys Leu Asp His Phe Leu Glu Gly Asp Leu Tyr Leu 50 55 60 His Ser Trp Glu Val Tyr Ala Glu Ile Leu Glu His Pro Asp Thr Ser 65 70 75 80 Asp Ile Ile Leu Asp Ile Gly Met Pro Val Met His Lys Asn Val Lys 85 90 95 Tyr Asn Cys Arg Val Ile Ser Tyr Asn Arg Glu Ile Leu Leu Ile Arg 100 105 110 Pro Lys Leu Ser Leu Ala Asn Asp Gly Asn Tyr Arg Glu Met Arg Tyr 115 120 125 Phe Thr Pro Trp Pro Lys Ala Arg Tyr Val Glu Asp Tyr Thr Leu Pro 130 135 140 Arg Phe Val Gln Asn Val Cys Ala Asn Glu Ser Ala Ile Val Pro Phe 145 150 155 160 Gly Asp Cys Val Leu Ser Thr Lys Asp Ala Val Ile Gly Phe Glu Thr 165 170 175 Cys Glu Glu Leu Phe Thr Pro Gln Ser Pro His Ile Gly Met Ser Leu 180 185 190 Asp Gly Val Glu Ile Phe Thr Asn Ser Ser Gly Ser His His Glu Leu 195 200 205 Arg Lys Leu Asn Thr Arg Met Glu Leu Ile Arg Glu Ala Thr Ala Lys 210 215 220 Cys Gly Gly Ile Tyr Leu Tyr Ala Asn Gln Arg Gly Cys Asp Gly Asp 225 230 235 240 Arg Leu Tyr Tyr Asp Gly Cys Ala Val Ile Ala Val Asn Gly Glu Val 245 250 255 Val Ala Gln Gly Ser Gln Phe Ser Leu Asp Asp Val Glu Val Val Ser 260 265 270 Ala Thr Leu Asp Leu Glu Ala Val Arg Ser Tyr Arg Ala Ser Lys Ile 275 280 285 Ser Gln Cys Met Gln Ala Ala Asn Ser Pro Cys Tyr Ala Arg Val Thr 290 295 300 Cys Lys Ala Glu Leu Ser Pro Ser Ser Val Thr Phe Asp Ser Glu Val 305 310 315 320 Tyr Pro Thr Pro Thr Arg Glu Ile Arg Tyr His Ser Pro Glu Glu Glu 325 330 335 Ile Ala Leu Gly Pro Ala Cys Trp Met Trp Asp Tyr Val Arg Arg Cys 340 345 350 Arg Ala Ala Gly Phe Phe Val Pro Leu Ser Gly Gly Ile Asp Ser Cys 355 360 365 Ala Thr Ala Thr Ile Val Tyr Ser Met Cys Val Leu Val Ala Asp Ala 370 375 380 Ala Asn Asn Gly Asn Glu Gln Val Ile Lys Asp Ala Arg Val Val Thr 385 390 395 400 Gly Asp Pro Asp Phe Val Pro Thr Asp Pro Lys Glu Leu Cys Asn Arg 405 410 415 Ile Phe His Thr Cys Phe Met Gly Thr Glu Asn Ser Ser Lys Asp Thr 420 425 430 Arg Ser Arg Ala Lys Asp Leu Ala Ala Ala Ile Gly Ala Tyr His Thr 435 440 445 Asp Leu Asn Met Asp Ser Val Val Ser Ala Val Arg Gly Leu Phe Glu 450 455 460 Thr Val Thr Gly Lys Arg Pro Ile Phe Lys Val His Gly Gly Ser Ala 465 470 475 480 Thr Glu Asn Leu Ala Leu Gln Asn Ile Gln Ala Arg Leu Arg Met Val 485 490 495 Leu Ala Tyr Leu Phe Ala Gln Leu Leu Pro Trp Cys Arg Gly Arg Ala 500 505 510 Gly Gly Leu Leu Val Leu Gly Ser Ala Asn Val Asp Glu Thr Leu Arg 515 520 525 Gly Tyr Leu Thr Lys Tyr Asp Cys Ser Ser Ala Asp Ile Asn Pro Ile 530 535 540 Gly Gly Ile Ser Lys Thr Asp Leu Lys Lys Phe Ile Ala Tyr Ala Glu 545 550 555 560 His Lys Phe Asp Leu Pro Ile Leu Asn Asp Phe Leu Thr Ala Val Pro 565 570 575 Thr Ala Glu Leu Glu Pro Ile Thr Lys Asp Tyr Val Gln Ser Asp Glu 580 585 590 Val Asp Met Gly Met Thr Tyr Asp Glu Leu Ser Val Phe Gly Arg Leu 595 600 605 Arg Lys Val Glu Lys Cys Gly Pro Tyr Ser Met Phe Ile Lys Leu Tyr 610 615 620 His Glu Trp Thr Pro Arg Leu Ser Ala Glu Gln Ile Ala Ala Lys Val 625 630 635 640 Lys Arg Phe Phe Trp Phe Tyr Ala Val Asn Arg His Lys Thr Thr Val 645 650 655 Leu Thr Pro Ser Tyr His Ala Glu Gln Tyr Ser Pro Asp Asp Asn Arg 660 665 670 Phe Asp Leu Arg Pro Phe Leu Ile Asn Pro Gly Phe Ser Trp Ala Ser 675 680 685 Lys Lys Ile Asp Ala Ile Val Lys Ser Leu Glu Thr Lys Lys Lys Glu 690 695 700 Asp 705 17714PRTCandida albicans 17Met Gly Asn Tyr Ile Thr Val Ala Thr Cys Asn Leu Asn Gln Trp Ala 1 5 10 15 Leu Asp Phe Glu Gly Asn Arg Asp Arg Ile Phe Glu Ser Ile Lys Glu 20 25 30 Ala Lys Arg Gln Gly Ala Lys Leu Arg Val Gly Pro Glu Leu Glu Val 35 40 45 Cys Gly Tyr Gly Cys Leu Asp His Phe Ala Glu Asn Asp Leu Tyr Arg 50 55 60 His Ser Trp Glu Val Tyr Gly Glu Ile Leu Ser Asn Pro Glu Thr His 65 70 75 80 Gly Ile Leu Leu Asp Ile Gly Ile Pro Ile Ile His Lys Ser Ile Lys 85 90 95 Tyr Asn Cys Arg Ile Ile Ser Tyr Asn Gly Lys Ile Leu Leu Ile Arg 100 105 110 Pro Lys Ile Tyr Leu Ala Asn Asp Gly Asn Tyr Arg Glu Met Arg Tyr 115 120 125 Phe Thr Gly Trp Asn Arg Pro Lys Tyr His Glu Glu Tyr Gln Leu Pro 130 135 140 Lys Phe Ile Ser Lys Ile Thr Gly Gln Ala Arg Val Pro Phe Gly Asp 145 150 155 160 Cys Ile Val Gln Thr Leu Glu Thr Arg Leu Gly Cys Glu Thr Cys Glu 165 170 175 Glu Leu Phe Thr Pro Glu Ser Pro His Ile Ala Met Ala Leu Asp Gly 180 185 190 Val Glu Ile Phe Thr Asn Ser Ser Gly Ser His His Glu Leu Arg Lys 195 200 205 Leu Asp Thr Arg Leu Lys Leu Ile Thr Glu Ala Thr Lys Lys Cys Gly 210 215 220 Gly Ile Tyr Leu Tyr Ala Asn Gln Lys Gly Cys Asp Gly Asp Arg Leu 225 230 235 240 Tyr Tyr Asp Gly Cys Ala Ser Ile Ile Val Asn Gly Asn Val Leu Ala 245 250 255 Gln Ala Ser Gln Phe Ser Leu Lys Asp Val Glu Val Ile Ser Ala Thr 260 265 270 Val Asp Leu Asp Asp Val Arg Ala Tyr Arg Asn Gln Lys Ser Ala Ser 275 280 285 Val Gln Ala Val Asn Gln Ser Glu Lys Phe Lys Val Ile Tyr Thr Asp 290 295 300 Val Glu Leu Ser Pro Ser Asp Tyr Val Phe Asp His Ser Ile Ile Pro 305 310 315 320 Ser Lys Pro Gln Pro Ile Lys Tyr His Thr Pro Glu Glu Glu Ile Ala 325 330 335 Leu Gly Pro Ala Cys Trp Leu Trp Asp Tyr Leu Arg Arg Ser Lys Cys 340 345 350 Gly Gly Tyr Phe Leu Pro Leu Ser Gly Gly Ile Asp Ser Cys Ala Thr 355 360 365 Ala Val Ile Val His Ser Met Cys Arg Leu Val Val Glu Ala Ile Pro 370 375 380 Asn Asp Glu Gln Val Leu Lys Asp Ile Gln Ala Ile Thr His Asp Glu 385 390 395 400 Gly Phe Val Pro Lys Thr Pro Gln Asp Ile Ala Gln Arg Ile Phe Tyr 405 410 415 Thr Ser Phe Met Gly Thr Glu Asn Ser Ser Lys Glu Thr Arg Ser Arg 420 425 430 Ser Lys Glu Leu Ala Ser Lys Ile Gly Ser Tyr His Val Asp Leu Asn 435 440 445 Met Asp Asn Leu Val Thr Ser Val Val Ser Leu Phe Glu Val Ala Thr 450 455 460 Gly Lys Lys Pro Ile Phe Lys Ile Phe Gly Gly Ser Asn Thr Glu Asn 465 470 475 480 Leu Ala Leu Gln Asn Ile Gln Ala Arg Leu Arg Met Val Leu Ser Tyr 485 490 495 Leu Phe Ala Gln Leu Leu Pro Trp Thr Arg Gly Lys Asn Val Pro Gly 500 505 510 Leu Leu Val Leu Gly Ser Ala Asn Val Asp Glu Cys Leu Arg Gly Tyr 515 520 525 Leu Thr Lys Tyr Asp Cys Ser Ser Ala Asp Ile Asn Pro Ile Gly Gly 530 535 540 Ile Ser Lys Thr Asp Leu Lys Arg Phe Ile Ala Trp Ala Glu Lys Asn 545 550 555 560 Phe Asp Leu Pro Ile Leu His Glu Phe Leu Thr Ala Thr Pro Thr Ala 565 570 575 Glu Leu Glu Pro Ile Thr Lys Asp Tyr Val Gln Ser Asp Glu Ile Asp 580 585 590 Met Gly Met Thr Tyr Asp Glu Leu Ser Arg Phe Gly Thr Leu Arg Lys 595 600 605 Val Asp Lys Cys Gly Pro Leu Ala Met Phe Ile Lys Leu Tyr His Glu 610 615 620 Trp Ser Gln Pro Pro Tyr Asn Leu Ser Ala Lys Gln Ile Ala Glu Lys 625 630 635 640 Val Lys Arg Phe Trp Phe Phe Tyr Ala Ile Asn Arg His Lys Met Thr 645 650 655 Thr Met Thr Pro Ala Tyr His Ala Glu Gln Tyr Ser Pro Asp Asp Asn 660 665 670 Arg Phe Asp Leu Arg Pro Phe Leu Ile Asn Pro Arg Phe Pro His Ala 675 680 685 Ser Lys Lys Ile Asp Glu Leu Val Glu Glu Ile Glu Lys Arg Gln His 690 695 700 Glu Ile Asp Ser Ser Asn Lys Ser Val Asp 705 710 18716PRTDebaryomyces hansenii 18Met Gly His Tyr Ile Thr Leu Ala Thr Cys Asn Leu Asn Gln Trp Ala 1 5 10 15 Leu Asp Phe Glu Gly Asn Arg Asp Arg Ile Ile Thr Ser Ile Ile Glu 20 25 30 Ala Lys Lys Leu Gly Ala Thr Leu Arg Val Gly Pro Glu Leu Glu Ile 35 40 45 Cys Gly Tyr Gly Cys Leu Asp His Phe Leu Glu Asn Asp Leu Tyr Asp 50 55 60 His Ser Trp Glu Met Tyr Gly His Ile Leu Thr Asn Pro Asn Thr Gln 65 70 75 80 Asp Ile Leu Leu Asp Val Gly Met Pro Ile Ile His Lys Ser Ile Lys 85 90 95 Tyr Asn Cys Arg Leu Leu Ser Tyr Asn Gly Lys Ile Leu Leu Ile Arg 100 105 110 Pro Lys Leu Tyr Leu Ala Asn Asp Gly Asn Tyr Arg Glu Met Arg Tyr 115 120 125 Phe Thr Pro Trp Asn Arg Pro Lys Tyr Tyr Glu Ser Phe Gln Leu Pro 130 135 140 Lys Asn Ile Ser Ser Val Thr Gly Gln Ser Asn Val Thr Phe Gly Asp 145 150 155 160 Cys Val Ile Gln Thr Leu Glu Thr Thr Leu Gly Ala Glu Thr Cys Glu 165 170 175 Glu Leu Phe Thr Pro Gln Ser Pro His Ile Ser Met Ala Leu Asp Gly 180 185 190 Val Glu Ile Phe Thr Asn Ser Ser Gly Ser His His Glu Leu Arg Lys 195 200 205 Leu Asp Thr Arg Leu Gln Leu Ile Thr Gly Ala Thr Lys Lys Cys Gly 210 215 220 Gly Val Tyr Leu Tyr Ala Asn Gln Lys Gly Cys Asp Gly Asp Arg Leu 225 230 235 240 Tyr Tyr Asp Gly Cys Ala Cys Ile Ile Val Asn Gly Lys Val Val Ala 245 250 255 Gln Ala Ser Gln Phe Ser Leu Arg Asp Val Glu Val Val Ser Ala Thr 260 265 270 Ile Asp Leu Asp Asp Val Arg Ser Tyr Arg Asn Gln Lys Leu Ser Ala 275 280 285 Phe Gln Ser Val Ser Gln Ser Asp Ser Thr Val Tyr His His Ile Pro 290 295 300 Thr Asp Ile Glu Leu Ser Pro Asn Ser Asn Val Phe Asn Pro Asn Val 305 310 315 320 Lys Pro Ser Pro Tyr Arg Asp Ile Arg Tyr His Leu Pro Glu Glu Glu 325 330 335 Ile Ala Leu Gly Pro Ala Cys Trp Leu Trp Asp Tyr Leu Arg Arg Ser 340 345 350 Lys Cys Ala Gly Tyr Phe Leu Pro Leu Ser Gly Gly Ile Asp Ser Cys 355 360 365 Ala Thr Ala Val Ile Val His Leu Met Cys Arg Leu Val Val Lys Ser 370 375 380 Cys Glu Glu Gly Asp Lys Gln Val Ile Ser Asp Ile Gln Ser Leu Thr 385 390 395 400 His Asp Pro Glu Phe Val Pro Lys Thr Pro Gln Glu Val Ala Gly Arg 405 410 415 Leu Phe Tyr Thr Ser Phe Met Gly Thr Glu Asn Ser Ser Lys Glu Thr 420 425 430 Arg Ser Arg Ala Lys Glu Leu Ser Glu Lys Val Gly Ser His His Ile 435 440 445 Asp Met Asn Met Asp Ser Leu Val Ser Ala Val Val Ser Val Phe Glu 450 455 460 Val Ala Thr Gly Lys Lys Pro Ile Phe Lys Ile Phe Gly Gly Ser Gln 465 470 475 480 Thr Glu Asn Leu Ala Leu Gln Asn Ile Gln Ala Arg Leu Arg Met Val 485 490 495 Leu Ser Tyr Leu Phe Ala Gln Leu Leu Pro Trp Thr Arg Asn Ile Ser 500 505 510 Gly Gly Leu Leu Val Leu Gly Ser Ala Asn Val Asp Glu Cys Leu Arg 515 520 525 Gly Tyr Leu Thr Lys Tyr Asp Cys Ser Ser Ala Asp Ile Asn Pro Ile 530 535 540 Gly Gly Ile Ser Lys Thr Asp Leu Lys Arg Phe Ile Asp Trp Ala Asp 545 550 555 560 Lys Asn Phe Glu Leu Pro Ile Leu His Asp Phe Leu Thr Ala Thr Pro 565 570 575 Thr Ala Glu Leu Glu Pro Ile Thr Gln Asn Tyr Val Gln Ser Asp Glu 580 585 590 Val Asp Met Gly Met Thr Tyr Asp Glu Leu Ser Arg Phe Gly Arg Leu 595 600 605 Arg Lys Val Asp Lys Cys Gly Pro Met Ala Met Phe Ile Lys Leu Tyr 610 615 620 His Glu Trp Ser Gln Pro Pro Leu Asn Leu Thr Ala Glu Gln Val Ala 625 630 635 640 Glu Lys Val Lys Arg Phe Trp Phe Phe Tyr Ala Ile Asn Arg His Lys 645 650 655 Met Thr Thr Met Thr Pro Ser Tyr His Ala Glu Gln Tyr Ser Pro Asp 660 665 670 Asp Asn Arg Phe Asp Leu Arg Pro Phe Leu Ile Asn Pro Arg Phe Pro 675 680 685 Trp Ala Ser Lys Lys Ile Asp Glu Ala Val Asp Ile Ile Asn Gln Arg 690

695 700 Thr Glu Glu Ile Lys Arg Ala Asn Leu Ser Val Asp 705 710 715 19749PRTAspergillus oryzae 19Met Gly His Leu Val Thr Leu Ala Thr Cys Ser Leu Asn Gln Trp Ala 1 5 10 15 Leu Asp Phe Glu Gly Asn Cys Glu Arg Ile Ile Glu Ser Ile Arg Gln 20 25 30 Ala Lys Lys Ala Gly Ala Thr Leu Arg Val Gly Pro Glu Leu Glu Ile 35 40 45 Thr Gly Tyr Gly Val Leu Asp Gly Phe Leu Glu Gly Asp Thr Phe Leu 50 55 60 His Ser Trp Glu Met Leu Ala Arg Ile Ile Asp His Ala Asp Cys Gln 65 70 75 80 Asp Ile Val Val Asp Val Gly Met Pro Val Arg His Arg Asn Val Arg 85 90 95 Tyr Asn Cys Arg Val Ile Phe Tyr Asn Arg Lys Ile Ile Leu Ile Arg 100 105 110 Pro Lys Met Trp Leu Ala Asn Asp Gly Asn Tyr Arg Glu Met Arg Tyr 115 120 125 Phe Thr Pro Trp Gln Arg Pro Gln Glu Ile Glu Asp Tyr Tyr Leu Glu 130 135 140 Ser Ile Val Gly Lys Ile Thr Gly Gln Tyr Lys Val Pro Phe Gly Asp 145 150 155 160 Ala Val Ile Ser Thr Arg Asp Thr Cys Leu Gly Leu Glu Thr Cys Glu 165 170 175 Glu Leu Phe Thr Pro Asn Gly Tyr Ala Leu Gln Leu Arg Asn Cys Asp 180 185 190 Tyr His Ala Asn Ile Tyr Val Gly Leu Ile Phe Leu Met Val Leu Pro 195 200 205 Val Trp Pro Ser Leu Gln Asp Arg Pro Leu Thr Ser Pro Ile Gly Val 210 215 220 Glu Ile Ile Ser Asn Ser Ser Gly Ser His His Glu Leu Arg Lys Leu 225 230 235 240 Asp Thr Arg Ile Asn Leu Val Thr Gln Ala Thr Lys Leu Ser Gly Gly 245 250 255 Ile Tyr Leu Tyr Ala Asn Gln Gln Gly Cys Asp Gly Asp Arg Leu Tyr 260 265 270 Tyr Asp Gly Cys Ala Met Ile Val Val Asn Gly Asn Ile Val Ala Gln 275 280 285 Gly Ser Gln Phe Ser Leu Asn Asp Val Glu Val Val Thr Ala Thr Val 290 295 300 Asp Ile Glu Glu Val Arg Thr Tyr Arg Ser Ser Ala Ser Arg Gly Met 305 310 315 320 Gln Ala Ser Lys Gln Thr Pro Phe Val Arg Leu Asp Leu Asp Met Arg 325 330 335 Leu Ser Arg Gln Asn Glu Glu Ala Asp Pro Gly Leu Ala Pro Ser Glu 340 345 350 Ala Ile Ala Pro Arg Tyr His Ala Pro Glu Glu Glu Val Ala Leu Gly 355 360 365 Pro Ala Cys Trp Leu Trp Asp Tyr Leu Arg Arg Ser Gly Ala Ala Gly 370 375 380 Phe Phe Leu Pro Leu Ser Gly Gly Ile Asp Ser Cys Ala Thr Ala Ile 385 390 395 400 Ile Val His Ser Met Cys Arg Glu Val Ile Lys Ala Val Ser Glu Gly 405 410 415 Asn Glu Gln Val Ile Lys Asp Val Arg Arg Leu Cys Ala Glu Pro Ala 420 425 430 Asp Ser Thr Trp Leu Pro Thr Thr Ser Gln Glu Val Cys Asn Arg Ile 435 440 445 Phe His Thr Ser Tyr Met Gly Thr Gln Asn Ser Ser Lys Glu Thr Arg 450 455 460 Asp Arg Ser Lys Arg Leu Ser Thr Asp Ile Gly Ser Tyr His Val Asp 465 470 475 480 Phe Asn Phe Asp Thr Val Val Thr Ser Leu Thr Asn Leu Phe Thr Met 485 490 495 Val Thr Asn Phe Gln Pro Lys Phe Lys Val His Gly Gly Ser Arg Ala 500 505 510 Glu Asn Gln Ala Leu Gln Asn Val Gln Ala Arg Leu Arg Met Val Leu 515 520 525 Ser Tyr Leu Phe Ala Ser Leu Leu Pro Thr Val Arg Gln Arg Pro Gly 530 535 540 Gly Gly Gly Leu Leu Val Leu Ala Ser Ser Asn Val Asp Ala Glu Cys 545 550 555 560 Leu Arg Gly Tyr Leu Thr Lys Tyr Asp Ala Ser Ser Ala Asp Leu Asn 565 570 575 Pro Ile Gly Ser Ile Ser Lys Val Asp Leu Lys Lys Phe Ile Ala Trp 580 585 590 Ser Arg Asp Ser Phe Glu Leu Pro Ile Leu His Glu Phe Leu Asn Ala 595 600 605 Thr Pro Thr Ala Glu Leu Glu Pro Ile Thr Ser Thr Tyr Val Gln Ser 610 615 620 Asp Glu Ala Asp Met Gly Val Thr Tyr Ala Glu Leu Ser Thr Phe Gly 625 630 635 640 Tyr Leu Arg Lys Ile Ala Lys Leu Gly Pro Trp Ser Met Tyr Glu Arg 645 650 655 Leu Leu His Val Trp Gly Asn Glu Tyr Ser Pro Arg Glu Ile Tyr Glu 660 665 670 Lys Thr Arg His Phe Phe Tyr Asn Tyr Ala Ile Asn Arg His Lys Met 675 680 685 Thr Val Leu Thr Pro Ser Tyr His Ala Glu Gln Tyr Ser Pro Asp Asp 690 695 700 Asn Arg His Asp Leu Arg Gln Phe Leu Tyr Pro Ser Phe Thr Trp Ala 705 710 715 720 Tyr Lys Lys Met Glu Asp Ser Val Lys Tyr Trp Glu Ser Lys Gly Trp 725 730 735 Thr Ala Gly Lys Ala Gln Lys Lys Asn Val Lys Ala Asp 740 745 20767PRTUstilago maydis 20Met Gly Leu Pro Val Thr Val Ser Thr Cys Ser Leu Asn Gln Trp Ala 1 5 10 15 Leu Asp Phe Asp Gly Asn Arg Asp Arg Ile Leu Glu Ser Ile Arg Leu 20 25 30 Ala Lys Ser Val Gly Ser Arg Leu Arg Val Gly Pro Glu Leu Glu Ile 35 40 45 Pro Gly Tyr Gly Cys Phe Asp His Phe Leu Glu Pro Asp Thr Val Leu 50 55 60 His Ser Trp Gln Val Leu Ala Glu Ile Leu Ser Ser Asp Ala Thr Asn 65 70 75 80 Gly Ile Leu Cys Asp Val Gly Met Pro Val Leu His Arg Ser Thr Leu 85 90 95 Tyr Asn Cys Arg Val Leu Leu Leu Asp Gly Lys Ile Leu His Ile Arg 100 105 110 Pro Lys Met Trp Leu Ala Asn Asp Gly Asn Tyr Arg Glu Met Arg Tyr 115 120 125 Phe Ser Pro Trp Thr Arg Thr Asn His Thr Asp Ser Phe Pro Leu Pro 130 135 140 Arg Ile Val Ser Ser Ile Thr Asp Gln His Glu Val Pro Phe Gly Asp 145 150 155 160 Ala Val Val Lys Thr Arg Asp Thr Val Leu Gly Val Glu Leu Cys Glu 165 170 175 Glu Leu Phe Thr Pro Asn Ser Pro His Ile Arg Gln Gly Leu Asp Gly 180 185 190 Val Glu Ile Phe Thr Asn Ser Ser Ala Ser His His Glu Leu Arg Lys 195 200 205 Leu Tyr Arg Arg Val Glu Leu Ile Lys Glu Ala Thr Leu Lys Leu Gly 210 215 220 Gly Ile Tyr Leu Tyr Ala Asn Gln Gln Gly Cys Asp Gly Asp Arg Leu 225 230 235 240 Tyr Tyr Asp Gly Cys Pro Leu Ile Ala Val Asn Gly Ser Ile Val Ala 245 250 255 Gln Gly Ser Gln Phe Ser Leu Asp Asp Val Gln Val Val Ser Ala Thr 260 265 270 Val Asp Leu Asp Asp Val Arg Ala His Arg Ser Ala Lys Ser Arg Gly 275 280 285 Met Gln Ala Val Ser His Ser Leu Gly Ser Gly Tyr Pro Arg Ile His 290 295 300 Val Asp Phe Glu Val Gly Glu Ser Glu Glu Tyr Ser Ser Lys Thr Pro 305 310 315 320 Gly Thr Ser Thr Pro Val Ala Val Gly Ser Ala Val Ala Pro Val Asp 325 330 335 Gly Gln Arg Asp Asp Ala Glu Arg Leu Tyr Lys Arg Tyr Leu Thr Pro 340 345 350 Leu Ser Gln Pro Ile Glu Val His Tyr His Ser Pro Glu Gln Glu Ile 355 360 365 Ala Leu Gly Pro Ala Cys Trp Leu Trp Asp Tyr Leu Arg Arg Ser Arg 370 375 380 Thr Gln Gly Tyr Phe Val Pro Leu Ser Gly Gly Ile Asp Ser Cys Ala 385 390 395 400 Thr Ala Thr Ile Val Phe Ser Met Cys Arg Leu Val Ile Ala Ala Ile 405 410 415 Asp Ala Pro Ser Ser Ser Ser Pro Ala Ser Lys Ala Thr Ser Ser Leu 420 425 430 Thr Thr Asp Thr Arg Thr Gln Val Leu Gln Asp Val Arg Arg Ile Cys 435 440 445 Asn Glu Lys Pro Ser Ser Thr Trp Ile Pro Ala Ser Pro Gln Glu Leu 450 455 460 Cys Asn Arg Ile Phe Val Thr Cys Tyr Met Gly Thr Glu Asn Ser Ser 465 470 475 480 Ala Glu Thr Arg Gln Arg Ala Lys Asp Leu Ala Ala Asp Ile Gly Ala 485 490 495 Tyr His Ile Asp Leu Asn Met Asp Ile Val Val Arg Ala Ile Ile Ala 500 505 510 Leu Phe Ser Thr Val Thr Gly Ser Thr Pro Arg Phe Arg Val His Gly 515 520 525 Gly Thr Pro Ala Glu Asn Leu Ala Leu Gln Asn Ile Gln Ala Arg Leu 530 535 540 Arg Met Leu Leu Ala Tyr Met Phe Ala Gln Leu Thr Pro Trp Val Arg 545 550 555 560 Gly Ser Trp Gly Gly Leu Leu Val Leu Gly Ser Ala Asn Val Asp Glu 565 570 575 Ser Leu Arg Gly Tyr Leu Thr Lys Tyr Asp Cys Ser Ser Ala Asp Ile 580 585 590 Asn Pro Ile Gly Gly Ile Ser Lys Thr Asp Leu Lys Ala Phe Ile Ala 595 600 605 Tyr Ala Arg Asp Ala Phe Ser Leu Pro Ile Leu His Ser Phe Leu Thr 610 615 620 Ala Val Pro Thr Ala Glu Leu Glu Pro Ile Thr Glu Ser Tyr Val Gln 625 630 635 640 Ala Asp Glu Ala Asp Met Gly Met Thr Tyr Asp Glu Leu Ser Val Phe 645 650 655 Gly Arg Leu Arg Lys Asn Leu Lys Cys Gly Pro Tyr Ser Met Phe Asn 660 665 670 Lys Leu Leu Gln Gln Trp Gly Pro Thr Met Gly Pro Glu Arg Val Ala 675 680 685 Glu Lys Val Lys Leu Phe Trp Phe Glu Tyr Ala Arg Asn Arg His Lys 690 695 700 Met Thr Thr Leu Thr Pro Ser Tyr His Ala Glu Ser Tyr Ser Pro Asp 705 710 715 720 Asp Asn Arg Phe Asp Leu Arg Pro Phe Leu Tyr Pro Ser Arg Phe Pro 725 730 735 Phe Gln Phe Arg Lys Ile Asp Glu Leu Val Lys Arg Leu Gln Ala Phe 740 745 750 Gln Ala Ile Pro Pro Pro Ser Arg Asp Glu Asn Arg Lys Gln Val 755 760 765 21706PRTCryptococcus neoformans 21Met His Leu Val Thr Val Ala Thr Cys Gln Leu Arg Gln Trp Ser Leu 1 5 10 15 Asp Phe Glu Gly Asn Cys Glu Arg Ile Leu Arg Ser Ile Ala Ile Ala 20 25 30 Lys Ser Arg Gly Ala Thr Leu Arg Val Gly Pro Glu Leu Glu Val Pro 35 40 45 Gly Tyr Gly Cys Asp Thr Met Leu His Ser Trp Glu Val Leu Ala Lys 50 55 60 Ile Leu Gln Ser Glu Glu Ala Lys Gly Ile Val Cys Asp Ile Gly Met 65 70 75 80 Pro Leu Glu His Lys Asn Asn Asn Tyr Asn Cys Arg Val Ile Ile Phe 85 90 95 Asn Gly Lys Ile Leu Leu Ile Arg Pro Lys Met Trp Met Ala Asn Asp 100 105 110 Gly Asn Tyr Arg Glu Leu Arg His Phe Thr Pro Trp His Lys His Arg 115 120 125 Gln Val Glu Lys His Ser Leu Pro His Met Ile Arg Ile Val Thr Gly 130 135 140 Gln Thr Tyr Val Pro Phe Gly Asp Ala Val Ile Ala Thr Glu Asp Thr 145 150 155 160 Val Ile Gly Val Glu Leu Cys Glu Glu Leu Phe Thr Pro Ala Ser Pro 165 170 175 His Ile Leu Met Gly Leu Asp Gly Val Glu Ile Phe Thr Asn Ser Ser 180 185 190 Gly Ser His His Glu Leu Arg Lys Leu Asn Arg Arg Val Glu Leu Ile 195 200 205 Lys Glu Ala Thr Met Lys Leu Gly Gly Ile Tyr Leu Tyr Ala Asn Gln 210 215 220 Gln Gly Cys Asp Gly Asp Arg Leu Tyr Tyr Asp Gly Ala Cys Leu Ile 225 230 235 240 Ala Met Asn Gly Gln Ile Leu Ala Gln Gly Pro Gln Phe Ser Leu Ser 245 250 255 Glu Val Glu Val Val Ser Ala Thr Val Asp Leu Arg Ala Val Arg Ala 260 265 270 His Arg Thr Thr Ser Ser Arg Arg Met Gln Ser Ala Gln Ala Glu Ala 275 280 285 Tyr Glu Arg Val Val Ala Asp Thr Arg Leu Asp Gly Gly Glu Gln Ile 290 295 300 Lys Val Gly Leu Arg Glu Thr Lys Gly Ser Met Asp Val Arg Tyr His 305 310 315 320 Thr Pro Glu Glu Glu Ile Ala Leu Gly Pro Ala Cys Trp Leu Trp Asp 325 330 335 Tyr Leu Arg Arg Ser Arg Thr Gln Gly Tyr Phe Leu Pro Leu Ser Gly 340 345 350 Gly Ile Asp Ser Cys Ala Thr Ala Ile Ile Val His Ser Met Cys Arg 355 360 365 Leu Val Val Glu Ala Ala Ala Lys Gly Asp Glu Gln Val Ile Thr Asp 370 375 380 Ala Arg Arg Ile Thr Asn Glu Pro Glu Asp Ser Thr Tyr Ile Pro Glu 385 390 395 400 Asp Pro Arg Glu Phe Ala Gly Arg Ile Phe His Thr Cys Tyr Met Gly 405 410 415 Thr Glu Asn Ser Ser Ser Glu Thr Arg Glu Arg Ala Lys Asn Leu Ala 420 425 430 Asp Ala Ile Gly Ala Tyr His Val Asp Leu Asn Met Asp Thr Ala Val 435 440 445 Ser Ala Val Lys Gly Ile Phe Ser Phe Val Thr Gly Lys Thr Pro Gln 450 455 460 Phe Lys Ala His Gly Gly Thr Asn Ala Glu Asn Leu Ala Leu Gln Asn 465 470 475 480 Ile Gln Ala Arg Leu Arg Met Val Val Ser Tyr Met Phe Ala Gln Leu 485 490 495 Leu Pro Trp Val Arg Gly Lys Asn Gly Gly Leu Leu Val Leu Gly Ser 500 505 510 Ala Asn Val Asp Glu Ser Leu Arg Gly Tyr Phe Thr Lys Tyr Asp Cys 515 520 525 Ser Ser Ala Asp Val Asn Pro Ile Gly Gly Ile Ser Lys Val Asp Leu 530 535 540 Lys Arg Phe Ile Ala Trp Ala Gln Val Lys Phe Asp Leu Pro Ile Leu 545 550 555 560 Tyr Asn Phe Leu His Ala Val Pro Thr Ala Glu Leu Ile Pro Ile Gly 565 570 575 Pro Asp Asn Ile Ile Gln Ser Asp Glu Ile Glu Met Gly Met Thr Tyr 580 585 590 Asp Glu Leu Ser Val Tyr Gly Arg Leu Arg Lys Val Glu Lys Cys Gly 595 600 605 Pro Phe Ser Met Phe Gly Lys Leu Val Gln Glu Trp Gly Ser Phe Leu 610 615 620 Ser Pro Lys Glu Ile Ala Glu Lys Val Lys His Phe Phe Phe Met Tyr 625 630 635 640 Ala Ile Asn Arg His Lys Met Thr Thr Ile Thr Pro Ser Val His Met 645 650 655 Glu Ser Tyr Ser Pro Asp Asp Asn Arg Phe Asp Leu Arg Pro Phe Leu 660 665 670 Tyr Pro Ser Gln Phe Thr His Gln Phe Arg Lys Ile Asp Glu Leu Ala 675 680 685 Gly Lys Leu Pro Asp Met Ala Gln Lys Pro Lys Val Asp Thr Asn Glu 690 695 700 Val Asp 705 22700PRTSchizosaccharomyces pombe 22Met Glu Arg Tyr Val Thr Ile Ala Ser Cys Gln Leu Asn Gln Trp Ala 1 5 10 15 Met Asp Phe Glu Gly Asn Arg Leu Arg Ile Ile Asp Ser Ile Lys Glu 20 25 30 Ala Lys Arg Gln Asn Ala Ser Leu Arg Val Gly Pro Glu Leu Glu Val 35 40 45 Thr Gly Tyr Gly

Cys Glu Asp His Phe Leu Glu Ser Asp Thr Tyr Tyr 50 55 60 His Ser Trp Glu Met Leu Cys Ser Ile Ile His Asp Pro Asp Cys Gln 65 70 75 80 Asp Ile Leu Leu Asp Ile Gly Met Pro Val Met His Lys Ala Met Arg 85 90 95 His Asn Cys Arg Ile Leu Ala Leu Asn Gly Lys Ile Leu Leu Ile Arg 100 105 110 Pro Lys Ile Trp Leu Cys Asp Asp Gly Asn Phe Arg Glu Ser Arg Trp 115 120 125 Phe Thr Pro Trp Leu Arg Pro Arg Val Val Glu Thr His Tyr Leu Pro 130 135 140 Thr Phe Val Ala Lys Ser Leu Asn Gln Thr Thr Val Pro Ile Gly Asp 145 150 155 160 Ala Ile Leu Gln Cys Asn Glu Thr Val Val Gly Val Glu Thr Cys Glu 165 170 175 Glu Leu Phe Thr Pro Asn Ser Pro His Ile Asp Met Ala Leu Asp Gly 180 185 190 Val Glu Ile Phe Ile Asn Ala Ser Gly Ser His His Glu Leu Arg Lys 195 200 205 Leu Thr Thr Arg Val Asn Leu Ile Gln Asn Ala Thr Glu Lys Cys Gly 210 215 220 Gly Ile Tyr Leu Tyr Ser Asn Gln Arg Gly Cys Asp Gly Gly Arg Leu 225 230 235 240 Tyr Tyr Asp Gly Ser Ser Met Ile Phe Ala Asn Gly Lys Met Leu Ala 245 250 255 Gln Gly His Gln Phe Ser Leu Lys Asp Val Glu Val Ile Ser Ala Thr 260 265 270 Val Asp Val Asp Thr Val Arg Ser Tyr Arg Phe Gln Pro Ser His Gly 275 280 285 Ile Gln Gly Val Thr Arg Pro Ser Tyr Glu Arg Ile His Val Asn Phe 290 295 300 Ser Leu Ser Ser Tyr Gln Gln Asp Tyr Asp Ile Tyr Arg Lys Pro Thr 305 310 315 320 Asp Pro Ile Glu Val Thr Ile Pro Leu Pro Glu Glu Glu Ile Thr Phe 325 330 335 Gly Pro Ala Cys Trp Leu Trp Asp Tyr Leu Arg Arg Ser His Ala Ala 340 345 350 Gly Phe Phe Leu Pro Leu Ser Gly Gly Leu Asp Ser Cys Ser Thr Ala 355 360 365 Val Leu Val Tyr Ser Met Cys Arg Ile Val Cys Lys Ala Met Glu Glu 370 375 380 Asp Asp Ala Gln Val Leu Ser Asp Val Arg Arg Ile Val Gly Asp Pro 385 390 395 400 Ser Tyr Ser Ser Thr Asp Pro Lys Lys Leu Leu Asn His Leu Phe Tyr 405 410 415 Thr Ala Phe Met Gly Ser Glu His Ser Ser Lys Glu Thr Arg Ser Arg 420 425 430 Ala Lys Glu Leu Ser Ser Leu Ile Gly Ser Tyr His Thr Asp Val Asn 435 440 445 Ile Asp Thr Met Thr Ser Ala Val Val Lys Leu Phe Ala Leu Val Thr 450 455 460 Gly Lys Thr Pro Gln Phe Arg Ser Asn Gly Gly Thr Asn Ala Glu Asn 465 470 475 480 Leu Ala Leu Gln Asn Ile Gln Ala Arg Ser Arg Met Leu Leu Gly Tyr 485 490 495 Leu Phe Ala Gln Leu Leu Pro Trp Val Arg Gly Tyr Ser Gly Ser Leu 500 505 510 Leu Val Leu Gly Ser Ser Asn Val Asp Glu Cys Leu Arg Gly Tyr Leu 515 520 525 Thr Lys Tyr Asp Cys Ser Ser Ala Asp Ile Asn Pro Ile Gly Gly Ile 530 535 540 Ser Lys Thr Asp Leu Lys Ser Phe Leu Arg Tyr Ala Lys Glu Ala Leu 545 550 555 560 Asp Leu Pro Ile Leu Gln Glu Phe Leu Asp Ala Thr Pro Thr Ala Glu 565 570 575 Leu Glu Pro Thr Thr Glu Ser Tyr Val Gln Ser Asp Glu Ala Asp Met 580 585 590 Gly Met Thr Tyr Ala Glu Leu Ser Val Phe Gly Arg Leu Arg Lys Ile 595 600 605 Ser Lys Cys Gly Pro Tyr Ser Met Phe Thr Gln Leu Met His Gln Trp 610 615 620 Gly Asp Arg Leu Ser Pro Ser Gln Val Ala Glu Lys Val Lys Arg Phe 625 630 635 640 Phe His Tyr Tyr Gly Ile Asn Arg His Lys Met Thr Thr Leu Thr Pro 645 650 655 Ser Tyr His Ala Glu Thr Tyr Gly Val Asp Asp Asn Arg Tyr Asp Leu 660 665 670 Arg Gln Phe Leu Tyr Pro Ser Trp Thr Trp Gln Asn Lys Lys Ile Asp 675 680 685 Ala Leu Ala Ser Lys Phe Glu Gln His Gln Arg Lys 690 695 700 23678PRTAspergillus nidulans 23Met Gly Arg Leu Ile Thr Leu Ala Thr Cys Ser Leu Asn Gln Trp Ala 1 5 10 15 Leu Asp Trp Glu Gly Asn Cys Glu Arg Ile Ile Glu Ser Ile Arg Gln 20 25 30 Ala Lys Ala Ala Gly Ala Thr Leu Arg Val Gly Pro Glu Leu Glu Ile 35 40 45 Thr Gly Tyr Gly Val Leu Asp Gly Phe Leu Glu Gly Asp Thr Phe Leu 50 55 60 His Ser Trp Glu Met Leu Ala Arg Ile Ile Asp His Pro Asp Cys Gln 65 70 75 80 Asp Ile Val Val Asp Val Asp Gly Asn Tyr Arg Glu Met Arg His Phe 85 90 95 Thr Pro Trp Gln Arg Pro Arg Glu Val Glu Asp Tyr Tyr Leu Glu Gln 100 105 110 Ile Val Gly Lys Ile Thr Gly Gln Tyr Lys Val Pro Phe Gly Asp Ala 115 120 125 Val Ile Ser Thr Arg Asp Thr Cys Leu Gly Leu Glu Thr Cys Glu Glu 130 135 140 Leu Phe Thr Pro Asn Gly Pro His Ile Pro Tyr Ser Leu Ala Gly Val 145 150 155 160 Glu Ile Ile Ser Asn Ser Ser Gly Ser His His Glu Leu Lys Lys Leu 165 170 175 Asp Thr Arg Val Asn Leu Ile Thr Gln Ala Thr Lys Leu Ser Gly Gly 180 185 190 Ile Tyr Leu Tyr Ala Asn Gln Gln Gly Cys Asp Gly Asp Arg Leu Tyr 195 200 205 Tyr Asp Gly Cys Ala Met Ile Val Ile Asn Gly Asn Ile Val Ala Gln 210 215 220 Gly Ser Gln Phe Ser Leu Asn Asp Val Glu Val Val Thr Ala Thr Val 225 230 235 240 Asp Ile Glu Glu Val Arg Thr Tyr Arg Ala Ser Thr Ser Arg Asn Met 245 250 255 Gln Ala Ser Arg Gln Pro Pro Phe Val Arg Leu Asp Leu Asp Thr Arg 260 265 270 Leu Ser Arg Ser Asp Glu Asp Ala Asp Pro Gly Ile Ala Pro Ser Glu 275 280 285 Thr Leu Ile Pro Arg Tyr His Ala Pro Glu Glu Glu Ile Ala Leu Gly 290 295 300 Pro Ala Cys Trp Leu Trp Asp Tyr Leu Arg Arg Ser Gly Ala Ala Gly 305 310 315 320 Phe Phe Leu Pro Leu Ser Gly Gly Ile Asp Ser Cys Ala Thr Ala Val 325 330 335 Ile Val His Ser Met Cys Arg Glu Val Ile Lys Ala Val Gln Gln Gly 340 345 350 Asn Glu Gln Val Ile Lys Asp Val Arg Arg Leu Cys Ala Glu Pro Ala 355 360 365 Gly Ser Thr Trp Leu Pro Thr Thr Ser Gln Glu Val Cys Asn Phe Met 370 375 380 Gly Thr Gln Asn Ser Ser Lys Glu Thr Arg Asp Arg Ala Lys Glu Leu 385 390 395 400 Ala Ala Glu Ile Gly Ser Tyr His Ile Asp Phe Asn Phe Asp Thr Val 405 410 415 Val Thr Ala Leu Met Asn Leu Phe Thr Val Val Thr Asn Phe Gln Pro 420 425 430 Arg Phe Lys Val His Gly Gly Ser Arg Ala Glu Asn Gln Ala Leu Gln 435 440 445 Asn Ile Gln Ala Arg Leu Arg Met Val Leu Ser Tyr Leu Phe Ala Ser 450 455 460 Leu Leu Pro Thr Val Arg Gln Arg Pro Gly Gly Gly Gly Leu Leu Val 465 470 475 480 Leu Ala Ser Ser Asn Val Asp Glu Cys Leu Arg Gly Tyr Leu Thr Lys 485 490 495 Tyr Asp Ala Ser Ser Ala Asp Leu Asn Pro Ile Gly Ser Ile Ser Lys 500 505 510 Val Asp Leu Lys Lys Phe Ile Gly His Cys Ala Thr Ser Phe Asp Met 515 520 525 Pro Ile Leu Thr Ser Phe Leu Asn Ala Thr Pro Thr Ala Glu Leu Glu 530 535 540 Pro Ile Thr Ala Thr Tyr Val Gln Ser Asp Glu Ala Asp Met Gly Val 545 550 555 560 Thr Tyr Ala Glu Leu Gly Thr Phe Gly Tyr Leu Arg Lys Val Ser Lys 565 570 575 Leu Gly Pro Trp Ser Met Tyr Glu Arg Leu Leu His Met Trp Gly Asn 580 585 590 Glu Tyr Ser Pro Arg Glu Ile Tyr Glu Lys Thr Arg His Phe Phe Tyr 595 600 605 Asn Tyr Ala Ile Asn Arg His Lys Met Thr Val Ile Thr Pro Ser Tyr 610 615 620 His Ala Glu Gln Tyr Ser Pro Asp Asp Asn Arg His Asp Leu Arg Gln 625 630 635 640 Phe Leu Tyr Pro Pro Phe Thr Trp Ala Tyr Lys Lys Met Glu Glu Ser 645 650 655 Val Lys Tyr Trp Glu Glu Arg Gly Trp Thr Thr Gly Lys Ala Gln Lys 660 665 670 Lys Ser Val Lys Ala Asp 675 24729PRTNeurospora crassa 24Met Gly Gly His Leu Val Thr Val Ala Thr Cys Ser Leu Asn Gln Trp 1 5 10 15 Val Leu Asp Trp Glu Gly Asn Leu Gln Arg Ile Val Glu Ser Ile His 20 25 30 Leu Ala Lys Lys Ala Gly Ala Arg Leu Arg Val Gly Pro Glu Leu Glu 35 40 45 Ile Cys Gly Tyr Ser Ser Leu Asp His Phe His Glu Leu Asp Val Tyr 50 55 60 Thr His Ser Leu Glu Met Leu Arg Lys Leu Leu Glu Asp Glu Ser Cys 65 70 75 80 His Asp Ile Leu Ile Asp Val Gly Leu Pro Ile Leu His Arg Asn Ile 85 90 95 Arg Tyr Asn Ala Arg Ala Ile Leu Leu Asn Gly Lys Ile Leu Leu Ile 100 105 110 Arg Pro Lys Met Trp Leu Ala Asn Asp Gly Asn Tyr Arg Glu Met Arg 115 120 125 His Phe Thr Pro Trp Met Arg Pro Arg Glu Thr Glu Leu Phe His Leu 130 135 140 Pro Lys Ile Leu Gln Glu Ile Gln Gly Glu Thr His Val Leu Phe Gly 145 150 155 160 Asp Ala Val Ile Ser Thr Pro Glu Thr Ala Phe Gly Ala Glu Thr Cys 165 170 175 Glu Glu Leu Phe Thr Pro Lys Ala Pro His Ile Asp Met Ala Leu Asp 180 185 190 Gly Val Glu Ile Ile Thr Asn Ser Ser Gly Ser His Phe Thr Leu Gln 195 200 205 Lys Leu Asp Val Arg Leu Gln Leu Ile Met Glu Ala Thr Arg Lys Ser 210 215 220 Gly Gly Val Tyr Leu Tyr Ala Asn Gln Gln Gly Cys Asp Gly Glu Arg 225 230 235 240 Leu Tyr Phe Asp Gly Cys Ala Met Ile Ile Val Asn Gly Asn Ile Val 245 250 255 Ala Gln Gly Ser Gln Phe Ser Leu Asn Asp Val Glu Val Val Thr Ala 260 265 270 Thr Val Asp Leu Glu Glu Val Arg Ala Tyr Arg Ser Ser Ile Ser Arg 275 280 285 Gly Leu Gln Ala Ala Thr Ser Asn Ala Lys Tyr Gln Arg Ile Gln Thr 290 295 300 Ser Phe Glu Leu Ser Pro Glu Asp Glu Asp Thr Asp Ile Trp Lys Lys 305 310 315 320 Pro Thr Leu Pro Arg Pro Pro Arg Tyr His Ser Val Glu Glu Glu Ile 325 330 335 Ala Leu Cys Gly Gly Cys Tyr Leu Trp Asp Tyr Leu Arg Arg Ser Gly 340 345 350 Thr Ala Gly Tyr Leu Val Pro Leu Ser Gly Gly Ile Asp Ser Cys Ala 355 360 365 Thr Ala Thr Leu Val Phe Ser Met Cys Arg Ile Val Ile Gln Ala Ile 370 375 380 Glu Asp Gly Asn Gln Gln Val Ile Asp Asp Val Arg Cys Ile Cys Lys 385 390 395 400 Tyr Gly Lys Glu Gly Glu Leu Pro Lys Thr Pro Gln Glu Leu Cys Asn 405 410 415 Gln Val Phe Thr Thr Ile Tyr Met Gly Met Ser Lys Gln Ser Ser Ala 420 425 430 Glu Thr Arg Gly Arg Ala Lys Glu Leu Ser Asp Ala Ile Gly Ser Tyr 435 440 445 His Val Asn Leu Asp Ile Asp Asp Val Tyr Glu Ala Gln Lys Lys Leu 450 455 460 Ile Val Gln Thr Thr Asn Phe Glu Pro Arg Phe Lys Val His Gly Gly 465 470 475 480 Thr Val Gln Glu Asn Leu Thr Leu Gln Cys Leu Gln Ala Arg Ile Arg 485 490 495 Met Val Thr Ala Tyr Glu Phe Gly Gln Ile Leu Pro Thr Ala Arg Gly 500 505 510 Arg Pro Gly Gly Gly Ser Leu Leu Val Leu Gly Ser Ala Asn Val Gly 515 520 525 Glu Ser Leu Arg Gly Tyr Leu Thr Lys Tyr Asp Cys Ser Ser Ala Asp 530 535 540 Ile Asn Pro Ile Gly Ser Ile Asp Lys Ala Asp Leu Lys Arg Phe Ile 545 550 555 560 Ala Trp Ala Glu Lys Lys Phe Asp Leu Pro Cys Leu His Gly Phe Leu 565 570 575 Thr Ala Val Pro Thr Ala Glu Leu Glu Pro Ile Thr Gln Glu Tyr Val 580 585 590 Gln Ser Asp Glu Ala Asp Met Gly Met Thr Tyr Ala Glu Leu Thr Val 595 600 605 Phe Gly Arg Leu Arg Lys Leu Asn Lys Leu Gly Pro Tyr Ala Met Phe 610 615 620 Gln Arg Leu Val His Asp Trp Ser Ala Asp Arg Glu Lys Val Glu Gly 625 630 635 640 Asp Glu Ala Pro Phe Tyr Thr Pro Arg Gln Val Ala Glu Lys Val Lys 645 650 655 Arg Phe Phe His Phe Tyr Ala Ile Asn Arg His Lys Met Thr Thr Leu 660 665 670 Thr Pro Ala Leu His Cys Asn Asp Tyr Ser Pro Asp Asp Asn Arg Phe 675 680 685 Asp Leu Arg Pro Phe Leu Tyr Pro Pro Phe Trp Lys Ser Trp Ser Phe 690 695 700 Lys Arg Ile Asp Met Glu Leu Glu Arg Ile Glu Lys Lys Arg Glu Glu 705 710 715 720 Arg Ala Gly Lys Gly Lys Glu Thr Ala 725 25652PRTCryptococcus neoformans 25Met Leu His Ser Trp Glu Val Leu Ala Lys Ile Leu Gln Ser Glu Glu 1 5 10 15 Ala Lys Gly Ile Val Cys Asp Ile Gly Met Pro Leu Glu His Lys Asn 20 25 30 Asn Asn Tyr Asn Cys Arg Val Ile Ile Phe Asn Gly Lys Ile Leu Leu 35 40 45 Ile Arg Pro Lys Met Trp Met Ala Asn Asp Gly Asn Tyr Arg Glu Leu 50 55 60 Arg His Phe Thr Pro Trp His Lys His Arg Gln Val Glu Lys His Ser 65 70 75 80 Leu Pro His Met Ile Arg Ile Val Thr Gly Gln Thr Tyr Val Pro Phe 85 90 95 Gly Asp Ala Val Ile Ala Thr Glu Asp Thr Val Ile Gly Val Glu Leu 100 105 110 Cys Glu Glu Leu Phe Thr Pro Ala Ser Pro His Ile Leu Met Gly Leu 115 120 125 Asp Gly Val Glu Ile Phe Thr Asn Ser Ser Gly Ser His His Glu Leu 130 135 140 Arg Lys Leu Asn Arg Arg Val Glu Leu Ile Lys Glu Ala Thr Met Lys 145 150 155 160 Leu Gly Gly Ile Tyr Leu Tyr Ala Asn Gln Gln Gly Cys Asp Gly Asp 165 170 175 Arg Leu Tyr Tyr Asp Gly Ala Cys Leu Ile Ala Met Asn Gly Gln Ile 180 185 190 Leu Ala Gln Gly Pro Gln Phe Ser Leu Ser Glu Val Glu Val Val Ser 195 200 205 Ala Thr Val Asp Leu Arg Ala Val Arg Ala His Arg Thr Thr Ser Ser 210 215 220 Arg Arg Met Gln Ser Ala Gln Ala Glu Ala Tyr Glu Arg Val Val Ala 225 230

235 240 Asp Thr Arg Leu Asp Gly Gly Glu Gln Ile Lys Val Gly Leu Arg Glu 245 250 255 Thr Lys Gly Ser Met Asp Val Arg Tyr His Thr Pro Glu Glu Glu Ile 260 265 270 Ala Leu Gly Pro Ala Cys Trp Leu Trp Asp Tyr Leu Arg Arg Ser Arg 275 280 285 Thr Gln Gly Tyr Phe Leu Pro Leu Ser Gly Gly Ile Asp Ser Cys Ala 290 295 300 Thr Ala Ile Ile Val His Ser Met Cys Arg Leu Val Val Glu Ala Ala 305 310 315 320 Ala Lys Gly Asp Glu Gln Val Ile Thr Asp Ala Arg Arg Ile Thr Asn 325 330 335 Glu Pro Glu Asp Ser Thr Tyr Ile Pro Glu Asp Pro Arg Glu Phe Ala 340 345 350 Gly Arg Ile Phe His Thr Cys Tyr Met Gly Thr Glu Asn Ser Ser Ser 355 360 365 Glu Thr Arg Glu Arg Ala Lys Asn Leu Ala Asp Ala Ile Gly Ala Tyr 370 375 380 His Val Asp Leu Asn Met Asp Thr Ala Val Ser Ala Val Lys Gly Ile 385 390 395 400 Phe Ser Phe Val Thr Gly Lys Thr Pro Gln Phe Lys Ala His Gly Gly 405 410 415 Thr Asn Ala Glu Asn Leu Ala Leu Gln Asn Ile Gln Ala Arg Leu Arg 420 425 430 Met Val Val Ser Tyr Met Phe Ala Gln Leu Leu Pro Trp Val Arg Gly 435 440 445 Lys Asn Gly Gly Leu Leu Val Leu Gly Ser Ala Asn Val Asp Glu Ser 450 455 460 Leu Arg Gly Tyr Phe Thr Lys Tyr Asp Cys Ser Ser Ala Asp Val Asn 465 470 475 480 Pro Ile Gly Gly Ile Ser Lys Val Asp Leu Lys Arg Phe Ile Ala Trp 485 490 495 Ala Gln Val Lys Phe Asp Leu Pro Ile Leu Tyr Asn Phe Leu His Ala 500 505 510 Val Pro Thr Ala Glu Leu Ile Pro Ile Gly Pro Asp Asn Ile Ile Gln 515 520 525 Ser Asp Glu Ile Glu Met Gly Met Thr Tyr Asp Glu Leu Ser Val Tyr 530 535 540 Gly Arg Leu Arg Lys Val Glu Lys Cys Gly Pro Phe Ser Met Phe Gly 545 550 555 560 Lys Leu Val Gln Glu Trp Gly Ser Phe Leu Ser Pro Lys Glu Ile Ala 565 570 575 Glu Lys Val Lys His Phe Phe Phe Met Tyr Ala Ile Asn Arg His Lys 580 585 590 Met Thr Thr Ile Thr Pro Ser Val His Met Glu Ser Tyr Ser Pro Asp 595 600 605 Asp Asn Arg Phe Asp Leu Arg Pro Phe Leu Tyr Pro Ser Gln Phe Thr 610 615 620 His Gln Phe Arg Lys Ile Asp Glu Leu Ala Gly Lys Leu Pro Asp Met 625 630 635 640 Ala Gln Lys Pro Lys Val Asp Thr Asn Glu Val Asp 645 650 26677PRTChaetomium globosum 26Met Gly His Leu Val Thr Val Ala Thr Cys Ser Leu Asn Gln Trp Val 1 5 10 15 Leu Asp Trp Glu Gly Asn Leu Gly Arg Ile Ile Glu Ser Ile His Gln 20 25 30 Ala Lys Ala Ala Gly Ala Arg Leu Arg Val Gly Pro Glu Leu Glu Ile 35 40 45 Cys Gly Tyr Ser Ser Leu Asp His Phe His Glu Leu Asp Val Tyr Thr 50 55 60 His Ser Leu Glu Met Leu Ala Gln Leu Leu Gln Asp Lys Ser Thr His 65 70 75 80 Gly Ile Leu Leu Asp Val Gly Val Pro Ile Leu His Arg Asn Leu Arg 85 90 95 Tyr Asn Cys Arg Val Ile Cys Leu Asp Gly Lys Ile Leu Leu Ile Arg 100 105 110 Pro Lys Met Trp Leu Ala Asn Asp Gly Asn Tyr Arg Glu Met Arg His 115 120 125 Phe Thr Pro Trp Met Arg Pro Arg Glu Thr Glu Leu Phe His Leu Pro 130 135 140 Lys Ile Leu Ala Glu Leu Gln Gly Glu Thr His Val Leu Phe Gly Asp 145 150 155 160 Ala Val Ile Ser Thr Pro Glu Thr Ala Phe Gly Ala Glu Thr Cys Glu 165 170 175 Glu Leu Phe Thr Pro Lys Ala Pro His Ile Asp Met Ala Leu Asp Gly 180 185 190 Val Glu Ile Ile Thr Asn Ser Ser Gly Ser His Phe Thr Leu Arg Lys 195 200 205 Leu Asp Thr Arg Leu Gln Leu Ile Met Glu Ala Thr Arg Lys Ser Gly 210 215 220 Gly Val Tyr Leu Tyr Ala Asn Gln Gln Gly Cys Asp Gly Glu Arg Leu 225 230 235 240 Tyr Phe Asp Gly Cys Ala Met Ile Ile Val Asn Gly Asp Val Val Ala 245 250 255 Gln Gly Ser Gln Phe Ser Leu Asn Asp Val Glu Val Val Thr Ala Thr 260 265 270 Val Asp Leu Glu Glu Val Arg Ser Tyr Arg Ala Ala Ile Ser Arg Gly 275 280 285 Leu Gln Ala Ala Ala Ser Thr Ala Lys Tyr Gln Arg Ile Gln Thr Pro 290 295 300 Phe Glu Leu Ser Ser Glu Asp Gly Asp Ala Asp Val Thr Val Ala Pro 305 310 315 320 Thr Leu Leu Ile Gln Pro Arg Tyr His Ser Val Glu Glu Glu Ile Ala 325 330 335 Leu Ser Gly Gly Cys Tyr Leu Trp Asp Tyr Leu Arg Arg Ser Gly Thr 340 345 350 Ala Gly Tyr Leu Val Pro Leu Ser Gly Gly Ile Asp Ser Cys Ala Thr 355 360 365 Ala Gly Ile Val Tyr Ser Leu Cys Arg Ile Val Met Gly Gly Leu Gly 370 375 380 Glu Gly Asn Lys Gln Val Leu Glu Glu Val Gln Arg Ile Pro Lys Tyr 385 390 395 400 Gly Gly Glu Gly Val Phe Thr Thr Thr Pro Gln Glu Leu Cys Lys Pro 405 410 415 Gly Phe Ser Pro Ile Tyr Met Gly Met Lys Lys Gln Ser Ser Arg Glu 420 425 430 Thr Pro Gln Arg Ala Gln Asp Leu Ser Glu Ala Ile Gly Ser Tyr His 435 440 445 Val Asn Leu Asp Ile Asp Asp Glu Val Gly Gln Met Leu Ser Thr Ala 450 455 460 Arg Gln Arg Pro Gly Gly Gly Ser Leu Leu Val Leu Gly Ser Ala Asn 465 470 475 480 Val Gly Glu Ser Leu Arg Gly Tyr Leu Thr Lys Tyr Asp Cys Ser Ser 485 490 495 Ala Asp Ile Asn Pro Ile Gly Ser Ile Asp Lys Ala Asp Leu Lys Arg 500 505 510 Phe Ile Ala Trp Ala Glu Lys Asn Phe Asp Leu Pro Cys Leu His Glu 515 520 525 Phe Leu Thr Ala Val Pro Thr Ala Glu Leu Glu Pro Ile Thr Glu Asp 530 535 540 Tyr Val Gln Ser Asp Glu Ala Asp Met Gly Met Thr Tyr Gln Glu Leu 545 550 555 560 Thr Ile Phe Gly Arg Leu Arg Lys Leu Asn Lys Leu Gly Pro Phe Gly 565 570 575 Met Phe Gln Arg Leu Val His Asp Trp Ser Ile Asp Arg Val Arg Lys 580 585 590 Pro Asp Asp Asp Ala Pro Tyr Tyr Thr Pro Thr Gln Val Ala Glu Lys 595 600 605 Val Lys Lys Phe Phe His Phe Tyr Ala Ile Asn Arg His Lys Met Thr 610 615 620 Thr Leu Thr Pro Ala Leu His Cys Asn Asp Tyr Ser Pro Asp Asp Asn 625 630 635 640 Arg Phe Asp Leu Arg Pro Phe Leu Tyr Pro Pro Phe Trp Lys Ser Trp 645 650 655 Ser Phe Lys Arg Ile Asp Met Glu Leu Glu Lys Ile Glu Arg Lys Arg 660 665 670 Ala Ser Arg Lys Gln 675 27689PRTGiberella zeae 27Met Ala Asp Leu Ile Thr Leu Ala Thr Cys Ser Leu Asn Gln Trp Val 1 5 10 15 Leu Asp Trp Glu Gly Asn Leu Gly Arg Ile Arg Lys Ser Ile Ile Leu 20 25 30 Ala Lys Glu Ala Gly Ala Thr Leu Arg Thr Gly Pro Glu Leu Glu Ile 35 40 45 Thr Gly Tyr Gly Cys Leu Asp His Phe Leu Glu Ala Asp Val Tyr Asp 50 55 60 His Ser Leu Glu Ser Leu Leu Ala Ile Leu Thr Asp Thr Glu Leu His 65 70 75 80 Gly Ile Leu Ile Asp Val Gly Leu Pro Leu Met His Arg Gly Cys Arg 85 90 95 Tyr Asn Cys Arg Ala Ile Ile Leu Asp Gly Lys Leu Leu Cys Leu Arg 100 105 110 Pro Lys Ile Tyr Leu Ala Asn Asp Gly Asn Phe Arg Glu Asn Arg Phe 115 120 125 Phe Thr Pro Trp Asn Arg Pro Arg Tyr Val Glu Gln Tyr Asn Leu Pro 130 135 140 Pro Ala Leu Gln Lys His Gln Gly Val Arg Gln Val Pro Ile Gly Asp 145 150 155 160 Val Ile Leu Ser Leu Asn Asp Thr Thr Val Ala Ala Glu Thr Cys Glu 165 170 175 Glu Leu Phe Thr Pro Gln Ala Pro His Ile Asn Met Ala Leu Asn Gly 180 185 190 Val Glu Ile Phe Thr Asn Ser Ser Gly Ser His His Thr Leu Arg Lys 195 200 205 Leu Asn Glu Arg Leu Ala Leu Ile Ser Glu Ala Thr Arg Lys Ser Gly 210 215 220 Gly Val Tyr Leu Tyr Ala Asn Gln Ser Gly Ser Asp Gly Asp Arg Leu 225 230 235 240 Leu Tyr Asp Gly Ser Ser Leu Ile Met Val Asn Gly Asn Ile Val Ala 245 250 255 Gln Gly Ser Gln Phe Ser Leu Asp Asp Val Glu Val Ile Thr Ala Thr 260 265 270 Val Asp Leu Glu Glu Val Arg Ala Tyr Arg Phe Ala Pro Ser Arg Asn 275 280 285 Phe Gln Ala Val Gln Ala Pro Val Tyr Glu Arg Ile Glu Val Asp Phe 290 295 300 Ser Leu Gly Val Glu Asp Leu Asp Leu Leu Arg Ala Pro Thr Pro Pro 305 310 315 320 Arg Pro Ala Arg Tyr His Val Pro Glu Glu Glu Ile Ala Leu Val Leu 325 330 335 Val Arg Arg Ser Lys Ala Ser Gly Tyr Leu Val Pro Leu Ser Gly Gly 340 345 350 Ile Asp Ser Cys Ala Thr Ala Thr Ile Val Phe Ser Met Cys Arg Leu 355 360 365 Val Val Ala Ala Ile Lys Ala Gly Asn Glu Glu Val Ile Ala Asp Val 370 375 380 Lys Arg Ile Ala Val Tyr Ser Asp Lys Leu Pro Glu Thr Ala Glu Glu 385 390 395 400 Phe Cys Asn Gln Ile Phe His Thr Val Tyr Met Gly Met Glu Lys Gln 405 410 415 Ser Ser Lys Glu Thr Arg Gln Arg Ala Lys Asp Leu Ser Ala Arg Ile 420 425 430 Gly Ser Tyr His Thr Asp Met Asn Ile Asp Asp Thr Phe Asn Ala Thr 435 440 445 Lys Asn Leu Leu Thr Gln Ala Thr Gly Phe Glu Pro Lys Phe Lys Val 450 455 460 His Gly Gly Ser Ala Thr Glu Asn Leu Ala Leu Gln Asn Ile Gln Ala 465 470 475 480 Arg Ser Arg Met Val Val Ala Tyr Tyr Tyr Ala Gln Met Leu Pro Thr 485 490 495 Val Arg Gln Arg Pro Gly Gly Gly Ser Leu Leu Val Leu Gly Ser Ser 500 505 510 Asn Val Asp Glu Cys Leu Arg Gly Tyr Leu Thr Lys Tyr Asp Cys Ser 515 520 525 Ser Ala Asp Val Asn Pro Ile Gly Ser Val Ser Lys Thr Asp Leu Lys 530 535 540 Arg Phe Ile Ala Trp Ser Ala Lys Ser Phe Asn Met Pro Ile Leu Glu 545 550 555 560 Glu Phe Ile His Ala Thr Pro Asp Met Gly Met Thr Tyr Asp Glu Leu 565 570 575 Ser Arg Phe Gly Arg Leu Arg Lys Glu Ser Lys Leu Gly Pro Tyr Gly 580 585 590 Met Phe Leu Arg Leu Leu Glu Glu Trp Gly Gly Glu Gly Lys Met Thr 595 600 605 Pro Arg Asp Val Ala Thr Lys Val Lys Arg Phe His Gly Phe His Tyr 610 615 620 Ile Asn Arg His Lys Gln Ala Val Ala Thr Pro Ala Val His Val Glu 625 630 635 640 Asn Tyr Ser Pro Asp Asp His Arg Phe Asp Leu Arg Pro Leu Val Tyr 645 650 655 Pro Ser Pro Trp Asn Ser Trp Ser Phe Glu Lys Ile Asp Lys Arg Val 660 665 670 Glu Ala Ile Glu Arg Ala Met Glu Lys Lys Lys Lys Thr Glu Ile Ser 675 680 685 Lys 28674PRTAspergillus fumigatus 28Met Leu Ala Arg Ile Ile Asp His Pro Asp Cys Gln Asp Ile Val Val 1 5 10 15 Asp Val Gly Met Pro Val Arg His Arg Asn Val Arg Tyr Asn Cys Arg 20 25 30 Val Ile Phe Tyr Asn Arg Lys Ile Ile Leu Ile Arg Pro Lys Met Trp 35 40 45 Leu Ala Asn Gly Ile Leu Phe Ser Leu Ala Val Ile Phe Leu Pro Thr 50 55 60 Ser Val Gln Leu Phe Thr Asn His Val Ala Ala Arg Ser Asp Gly Asn 65 70 75 80 Tyr Arg Glu Leu Arg His Phe Ser Pro Trp Gln Arg Pro Arg Glu Ile 85 90 95 Glu Asp Tyr Tyr Leu Glu Gln Ile Val Gly Lys Ile Thr Gly Gln Tyr 100 105 110 Lys Val Pro Phe Gly Asp Ala Val Ile Ser Thr Arg Asp Thr Cys Ile 115 120 125 Gly Leu Glu Thr Cys Glu Glu Leu Phe Thr Pro Asn Gly Pro His Ile 130 135 140 Pro Tyr Gly Leu Ala Gly Val Glu Ile Ile Ser Asn Ser Ser Gly Ser 145 150 155 160 His His Glu Leu Lys Lys Leu Asp Thr Arg Val Asn Leu Ile Thr Gln 165 170 175 Ala Thr Lys Leu Ser Gly Gly Ile Tyr Leu Tyr Ala Asn Gln Gln Gly 180 185 190 Cys Asp Gly Asp Arg Leu Tyr Tyr Asp Gly Cys Ala Met Ile Val Ile 195 200 205 Asn Gly Asn Ile Val Ala Gln Gly Ser Gln Phe Ser Leu Lys Asp Val 210 215 220 Glu Val Ile Thr Ala Thr Val Asp Ile Glu Glu Val Arg His Pro Val 225 230 235 240 Arg Thr Tyr Arg Ala Ser Ser Ser Arg Asn Met Gln Ala Thr Arg Gln 245 250 255 Pro Pro Phe Val Arg Leu Asp Leu Asp Val Arg Leu Ser Arg Leu Asp 260 265 270 Asp Asp Ala Glu Pro Gly Leu Val Pro Ser Glu Pro Ile Ser Ala Lys 275 280 285 Tyr His Ala Pro Glu Glu Glu Ile Ser Leu Gly Pro Ala Cys Trp Leu 290 295 300 Trp Asp Tyr Leu Arg Arg Ser Gly Ala Ala Gly Phe Phe Leu Pro Leu 305 310 315 320 Ser Gly Gly Ile Asp Ser Cys Ala Thr Ala Ile Ile Val His Ser Met 325 330 335 Cys Arg Glu Val Val Lys Ala Val Ser Glu Gly Asn Gln Gln Val Ile 340 345 350 Lys Asp Val Arg Arg Leu Cys Ala Glu Pro Glu Gly Ser Thr Trp Leu 355 360 365 Pro Arg Thr Ser Gln Glu Val Cys Asn Arg Ile Phe His Thr Ser Phe 370 375 380 Met Gly Thr Gln Asn Ser Ser Lys Glu Thr Arg Glu Arg Ala Lys Ala 385 390 395 400 Leu Ser Thr Glu Ile Gly Ser Tyr His Ile Asp Phe Asn Phe Asp Thr 405 410 415 Val Val Thr Ala Ile Thr Asn Leu Phe Thr Val Ile Thr Asn Phe Gln 420 425 430 Pro Arg Phe Lys Val His Gly Gly Thr Gly Ala Glu Asn Ala Ala Leu 435 440 445 Gln Asn Val Gln Ala Arg Leu Arg Met Val Leu Ser Tyr Leu Phe Ala 450 455 460 Ser Leu Leu Pro Thr Val Arg Gln Arg Pro Gly Gly Gly Gly Leu Leu 465 470 475 480 Val Leu Ala Ser Ser Asn Val Asp Asp Leu Lys Lys Phe Ile Ala Trp 485 490 495 Ala Arg Asp Ser Phe Asp Leu Pro Ile Leu His Asp Phe Leu Thr Ala 500 505 510 Thr Pro Thr Ala Glu Leu Glu Pro

Ile Thr Ala Thr Tyr Val Gln Ser 515 520 525 Asp Glu Ala Asp Met Gly Val Thr Tyr Ala Glu Leu Gly Thr Phe Gly 530 535 540 Tyr Leu Arg Lys Val Ala Lys Leu Gly Pro Trp Ser Met Tyr Glu Lys 545 550 555 560 Leu Leu His Val Trp Gly Asn Glu Tyr Ser Pro Arg Glu Ile Tyr Glu 565 570 575 Lys Thr Arg His Phe Phe Tyr His Tyr Ala Ile Asn Arg His Lys Met 580 585 590 Thr Val Leu Thr Pro Ser Tyr His Ala Glu Gln Tyr Ser Pro Glu Asp 595 600 605 Asn Arg His Asp Leu Arg Gln Phe Leu Cys Gln Leu Leu Ser Ser Thr 610 615 620 Asp Gly Leu Leu Ala Arg Val Asn Ala Asp Leu Cys Leu Leu Asp Pro 625 630 635 640 Pro Phe Thr Trp Ala Tyr Lys Lys Met Glu Glu Ser Val Lys Tyr Trp 645 650 655 Glu Ser Lys Gly Trp Thr Ala Gly Lys Ala Gln Lys Lys Ser Val Lys 660 665 670 Ala Asp 291315PRTMagnaporthe grisea 29Met Arg Phe Val Thr Val Ala Ala Ala Thr Leu Pro Ser Val Pro Leu 1 5 10 15 Asp Phe Glu Gly Asn Arg Asp Arg Ile Leu Glu Ser Ile Lys Leu Ala 20 25 30 Lys Glu Lys Gly Ala Thr Leu Arg Thr Gly Pro Glu Leu Glu Ile Pro 35 40 45 Gly Tyr Gly Cys Leu Asp His His Leu Glu Gly Asp Thr Glu Leu His 50 55 60 Ser Trp Glu Val Leu Ala Glu Ile Ile Ser Asp Pro Val Cys Lys Asp 65 70 75 80 Met Leu Val Asp Leu Gly Leu Gly Val Lys Thr Arg Asn Val Gln Tyr 85 90 95 Asn Cys Arg Val Leu Cys Thr Tyr Lys Lys Ile Tyr Ala Ile Arg Ala 100 105 110 Lys Gln Ala Leu Ala Gly Asp Gly Leu Tyr Arg Glu Pro Arg His Phe 115 120 125 Thr Ala Trp Val Lys Glu Arg Gln Val Glu Thr His Lys Leu His Lys 130 135 140 Val Val Arg Asp Val Thr Gly Gln Thr Thr Val Pro Ile Gly Asp Phe 145 150 155 160 Ile Leu Glu Thr Pro Asp Thr Ser Val Thr Cys Glu Thr Cys Glu Glu 165 170 175 Leu Phe Val Pro Arg Asn Pro Ser Ile Phe Ser Gly Leu Asn Gly Ala 180 185 190 Glu Ile Ile Leu Asn Ser Ser Ala Ser His Ala Glu Leu Arg Lys Leu 195 200 205 Gly Thr Arg Leu Asn Leu Ile Ser Asn Ser Thr Arg Ser Asn Gly Gly 210 215 220 Leu Tyr Val Tyr Ala Asn Ala Ser Gly Ile Asp Gly Glu Ala Arg Met 225 230 235 240 Leu Phe Asp Gly Ser Ser Met Ile Ile Gln Asn Gly Glu Val Leu Ala 245 250 255 Gln Ser Ser Gln Phe Ser Leu Leu Pro Val Glu Val Thr Val Ala Thr 260 265 270 Val Asp Leu Glu Arg Val Arg Ser Tyr Arg Thr Ser Ala Ser Arg Asn 275 280 285 Val Gln Ala Ala Arg Gln Pro Glu Tyr Pro Arg Ile Asp Cys Asp Ile 290 295 300 Glu Leu Ala Arg Pro Ser Glu Glu Ile Phe Arg Ser Asn Lys Val Ile 305 310 315 320 Ala Met Glu Ile Pro Ile Arg Ile Leu Asp Pro Met Glu Glu Ile His 325 330 335 Met Ala Thr Ser Val Tyr Leu Trp Gln Tyr Leu Val Arg Ser Ser Gly 340 345 350 Ala Gly Phe Phe Leu Ala Leu Ser Gly Gly Leu Asp Ser Ser Ser Val 355 360 365 Ala Leu Phe Val Tyr Gly Met Ala Lys Leu Val Leu Leu Ser Ile Lys 370 375 380 Asn Gly Glu Glu Asn Thr Leu Asn Asp Leu Arg Lys Val Thr Gly Ile 385 390 395 400 Asn Asp Tyr Val Pro Glu Ser Pro Glu Glu Ile Val Gly Lys Leu Leu 405 410 415 His Thr Cys Phe Met Gly Thr Val Asn Ser Ser Asp Glu Thr Arg Ser 420 425 430 Arg Ala Lys Arg Leu Ala Glu Arg Leu Gly Ala Tyr His Thr Asp Ile 435 440 445 Asn Ile Asp Asn Ala Val Gln Ala His Glu Ser Ile Ile Glu Ser Ala 450 455 460 Leu Gly Gly Phe Lys Pro Lys Tyr Ala Val Glu Gly Gly Thr Asn Ser 465 470 475 480 Glu Asn Leu Ala Lys Gln Asn Ile Gln Ala Arg Asn Arg Leu Val Val 485 490 495 Ser Tyr Glu Leu Ala Gln Leu Ser Thr Gln Ala Arg Gly Leu Pro Arg 500 505 510 Ala Gly Ala Ser Leu Leu Val Leu Gly Ser Gly Asn Val Asp Glu Asn 515 520 525 Leu Arg Gly Tyr Tyr Thr Lys Tyr Asp Ala Ser Ser Ala Asp Leu Ala 530 535 540 Pro Leu Gly Ser Ile Ser Lys Asn Asp Ala Lys Asp Phe Gln Arg Trp 545 550 555 560 Ala Arg Asp Asn Trp Asp Leu Ser Ile Met Ser Glu Phe Ile Asp Ala 565 570 575 Ile Pro Ser Ala Glu Leu Leu Pro Leu Ser Ala Gly Val Gln Ala Asp 580 585 590 Glu Val Glu Met Gly Leu Thr Tyr Ser Glu Leu Ser Asp Phe Gly Ile 595 600 605 Leu Arg Lys Val Asp Lys Leu Gly Pro Trp Ser Ala Tyr Leu Arg Leu 610 615 620 Leu Ser Gln Trp Lys Glu Arg Pro Gly Phe Gly Pro Arg Glu Ile Ala 625 630 635 640 Glu Lys Val Phe Leu Phe Phe Arg Phe Tyr Ala Ile Asn Arg His Lys 645 650 655 Ala Thr Ile Ile Thr Pro Ser Val His Leu Ser Ala Tyr Asn Pro Asp 660 665 670 Asp Asn Arg His Asp Asp Asn Asn Arg Glu Lys Lys Ser Ile Ala Ser 675 680 685 Ile Trp Gln Ser Gln Ala Phe Ser Ala Thr Gly Asp Leu Pro Thr Leu 690 695 700 Leu Leu Ala Gly Ala Lys Leu Pro Lys Ile Asn Pro Ser Leu Arg Arg 705 710 715 720 Lys Cys Asp Ser Arg Leu Asp Ser Asn Gly Lys Arg Arg Cys Pro Ser 725 730 735 Gly Val Thr Pro Asn Phe Gln Pro Gln Pro Ala His Leu Gln Val Leu 740 745 750 Thr Pro Ser Thr Ser Asn Arg Leu Glu Ile Asp Ala Thr Ser Arg Ala 755 760 765 His Phe Ile Gly Trp Leu Cys Gly Ser Leu Leu Ala Thr Ala Val Ser 770 775 780 Ala Thr Asn Phe Ala Asn Cys Tyr His Leu Ala Phe Glu Glu Phe Arg 785 790 795 800 Asn Gly Thr His Pro Met Arg Asp Ser Phe Phe Trp Lys Glu Lys Asp 805 810 815 Pro Leu Ile Gly Leu Lys Asn Gln Ser Ala Arg Pro Glu Ile Val Leu 820 825 830 Thr Arg Ala Gly Cys Glu His Phe Cys Ser Ile Tyr Pro Gln Tyr Asn 835 840 845 Asn Val Ile Asp Ala Phe Gln Ile Leu Thr Thr Trp Val Leu Pro Ala 850 855 860 Ile Ala Leu Met Ser Gln Leu Pro Tyr Glu Ser Leu Ser Val Arg Trp 865 870 875 880 Arg Lys Asn Leu Ala Ala Phe Gly Asn Trp Val Gly Ala Pro Ala Ala 885 890 895 Ala Met Thr Thr Thr Phe Trp Asn Ile Val Leu Ile His Glu Cys Ser 900 905 910 Val Lys Phe Gly Leu Phe Arg Leu Pro Glu Thr Arg Glu Glu Ile Arg 915 920 925 Asp Ala Leu Phe Ile Leu Ser Cys Val Asn Gln Tyr Glu Tyr Pro Arg 930 935 940 Arg Glu Gln Val Gly Arg Asp Leu Arg Arg Asp Ser Ala Leu Leu Lys 945 950 955 960 Gly Ile Leu Tyr Pro Tyr Phe Lys Asp Gly Ile Ser Glu Arg Gln Arg 965 970 975 Arg Thr Leu Ala Asn Phe Asn Gln His Leu Ala Phe Gln Leu Arg Leu 980 985 990 Gln Arg Arg Lys Gly Val Tyr Pro Ile Phe Ile Ser Ile Gly Trp Phe 995 1000 1005 Gly Met Ala Phe Ala Phe Ser Ile Val Ile Ser Phe Ala Ala Leu 1010 1015 1020 Gly Asp Asn Thr Thr Ala His Ser Leu Ala Leu Gly Leu Leu Leu 1025 1030 1035 Ser Trp Val Pro Val Met Leu Phe Ala Thr Val Ile Asp Arg Asn 1040 1045 1050 Pro Thr Ser Ala Thr Arg Cys Ser Glu Leu Ile Gln Arg Trp Leu 1055 1060 1065 Phe Asn Ile Asp Arg Leu Leu Pro Ala Thr Asp Leu Ser Ser Leu 1070 1075 1080 Pro Pro Lys Phe Trp Gln Ala His His Gly Gly Gln Lys His Ala 1085 1090 1095 Asp Thr Thr Glu Glu Phe Asp Ile Gly Glu Tyr Met Gly Gln Gly 1100 1105 1110 Arg Thr Leu Arg Tyr Cys Gly Val Ala Asp Thr Val Leu Asp Met 1115 1120 1125 Ile Lys Asn Pro Ser Glu Ala Thr Leu Asp Val Pro Asp Leu Ser 1130 1135 1140 Val Gly Lys Lys His Ala Lys Phe Ser Asp Arg Ser Asp Glu Ala 1145 1150 1155 Thr Val Gly Met Gly Gly Gly Val Ala His Gln Pro Gly His Cys 1160 1165 1170 Asp His Gln Leu Arg His Gly Leu His Gly Val Val Gln His Ala 1175 1180 1185 Asn Ala Gly Ser Gly Leu Ser Leu Ala Ala Leu Pro Leu Leu Val 1190 1195 1200 Ala Pro Gly Ser Ala Leu Val Ala Asp Pro Gly Ser Leu Ser Gly 1205 1210 1215 Ala Gln His Gln Met Gln Ser Phe Gly Gly Leu Asn Ser Cys Leu 1220 1225 1230 Cys Lys Thr Ser Val Phe Gly Leu Pro Pro Phe Gly Arg Tyr Met 1235 1240 1245 Asp Phe Glu Asn Ala Glu Phe Tyr Lys Glu Tyr Tyr Tyr Val Glu 1250 1255 1260 Ala Phe Trp Gly Ser Ala Thr Gly Ile Gly Gly Ala Thr Met Ala 1265 1270 1275 Ile Ser Val Ser Trp Leu Ala Trp Lys Trp His Lys Ser Ser Ala 1280 1285 1290 Leu Trp Arg Val Thr Glu Asp Thr Thr Val Arg Val Glu Asp Asp 1295 1300 1305 Val Ser Leu Asp Trp Leu Thr 1310 1315 30401PRTSaccharomyces cereviseae 30Met Asp Pro Thr Arg Ala Pro Asp Phe Lys Pro Pro Ser Ala Asp Glu 1 5 10 15 Glu Leu Ile Pro Pro Pro Asp Pro Glu Ser Lys Ile Pro Lys Ser Ile 20 25 30 Pro Ile Ile Pro Tyr Val Leu Ala Asp Ala Asn Ser Ser Ile Asp Ala 35 40 45 Pro Phe Asn Ile Lys Arg Lys Lys Lys His Pro Lys His His His His 50 55 60 His His His Ser Arg Lys Glu Gly Asn Asp Lys Lys His Gln His Ile 65 70 75 80 Pro Leu Asn Gln Asp Asp Phe Gln Pro Leu Ser Ala Glu Val Ser Ser 85 90 95 Glu Asp Asp Asp Ala Asp Phe Arg Ser Lys Glu Arg Tyr Gly Ser Asp 100 105 110 Ser Thr Thr Glu Ser Glu Thr Arg Gly Val Gln Lys Tyr Gln Ile Ala 115 120 125 Asp Leu Glu Glu Val Pro His Gly Ile Val Arg Gln Ala Arg Thr Leu 130 135 140 Glu Asp Tyr Glu Phe Pro Ser His Arg Leu Ser Lys Lys Leu Leu Asp 145 150 155 160 Pro Asn Lys Leu Pro Leu Val Ile Val Ala Cys Gly Ser Phe Ser Pro 165 170 175 Ile Thr Tyr Leu His Leu Arg Met Phe Glu Met Ala Leu Asp Ala Ile 180 185 190 Ser Glu Gln Thr Arg Phe Glu Val Ile Gly Gly Tyr Tyr Ser Pro Val 195 200 205 Ser Asp Asn Tyr Gln Lys Gln Gly Leu Ala Pro Ser Tyr His Arg Val 210 215 220 Arg Met Cys Glu Leu Ala Cys Glu Arg Thr Ser Ser Trp Leu Met Val 225 230 235 240 Asp Ala Trp Glu Ser Leu Gln Pro Ser Tyr Thr Arg Thr Ala Lys Val 245 250 255 Leu Asp His Phe Asn His Glu Ile Asn Ile Lys Arg Gly Gly Val Ala 260 265 270 Thr Val Thr Gly Glu Lys Ile Gly Val Lys Ile Met Leu Leu Ala Gly 275 280 285 Gly Asp Leu Ile Glu Ser Met Gly Glu Pro Asn Val Trp Ala Asp Ala 290 295 300 Asp Leu His His Ile Leu Gly Asn Tyr Gly Cys Leu Ile Val Glu Arg 305 310 315 320 Thr Gly Ser Asp Val Arg Ser Phe Leu Leu Ser His Asp Ile Met Tyr 325 330 335 Glu His Arg Arg Asn Ile Leu Ile Ile Lys Gln Leu Ile Tyr Asn Asp 340 345 350 Ile Ser Ser Thr Lys Val Arg Leu Phe Ile Arg Arg Ala Met Ser Val 355 360 365 Gln Tyr Leu Leu Pro Asn Ser Val Ile Arg Tyr Ile Gln Glu His Arg 370 375 380 Leu Tyr Val Asp Gln Thr Glu Pro Val Lys Gln Val Leu Gly Asn Lys 385 390 395 400 Glu 31411PRTCandida glabrata 31Met Asp Pro Thr Arg Asp Pro Asp Phe Lys Pro Arg Asp Pro Asp Ala 1 5 10 15 Lys Leu Leu Pro Pro Pro Asp Pro Thr Ser Lys Ile Pro Lys Ser Gly 20 25 30 Pro Ile Thr Pro Tyr Val Leu Ala Asp Tyr Asn Ala Ser Ile Asp Ala 35 40 45 Pro Leu Gln Met Lys Lys Asn Thr Thr His Leu Pro His Ser Gln Gly 50 55 60 Asn His Gln Arg Ile Pro Leu Asn Lys Ser Glu Phe Gln Pro Leu Ser 65 70 75 80 Thr Thr Gly Ser Ser Glu Glu Asp Phe Glu Leu Asp Asp Glu Asn Met 85 90 95 Asp Ser Asp Ser Gly Ser Lys Arg Glu Ser Leu Gly Gln Leu Ser Gly 100 105 110 His Gly Ile Gly Ile Gly Val His Lys Asn Gln Ile Ala Asp Leu Glu 115 120 125 Glu Val Pro His Gly Ile Val Arg Gln Ala Arg Phe Leu Glu Asp Tyr 130 135 140 Glu Phe Pro Thr His Arg Leu Ala Asn Arg Leu Gln Asp Pro Asn Lys 145 150 155 160 Met Pro Leu Val Ile Val Ala Cys Gly Ser Phe Ser Pro Ile Thr Tyr 165 170 175 Leu His Leu Arg Met Phe Glu Met Ala Leu Asp Ala Ile Ser Glu Met 180 185 190 Thr Arg Phe Glu Val Val Gly Gly Tyr Tyr Ser Pro Val Ser Asp Asn 195 200 205 Tyr Lys Lys Gln Gly Leu Ala Pro Ser Tyr His Arg Val Arg Met Cys 210 215 220 Glu Leu Ala Cys Glu Arg Thr Ser Ser Trp Leu Met Val Asp Ala Trp 225 230 235 240 Glu Ser Leu Gln Pro Ser Tyr Thr Arg Thr Ala Lys Val Leu Asp His 245 250 255 Phe Asn His Glu Ile Asn Val Lys Arg Gly Gly Ile Thr Val His Glu 260 265 270 Lys Lys Arg Asn Ala Asp Asn Ser Gly Tyr His Met Glu Glu His Lys 275 280 285 Arg Gly Val Lys Ile Met Leu Leu Ala Gly Gly Asp Leu Ile Glu Ser 290 295 300 Met Gly Glu Pro Gly Val Trp Ala Asp Glu Asp Leu His His Ile Leu 305 310 315 320 Gly Asn Tyr Gly Cys Leu Ile Val Glu Arg Thr Gly Ser Asp Val Arg 325 330 335 Ser Phe Leu Leu Ser His Asp Ile Met Tyr Glu His Arg Arg Asn Val 340 345 350 Leu Val Ile Lys Gln Leu Ile Tyr Asn Asp Ile Ser Ser Thr Lys Val 355 360 365 Arg Leu Phe Ile Arg Arg Asn Met Ser Val Gln Tyr Leu Leu Pro Asn 370 375 380 Ser Val Ile Arg Tyr Ile Gln Glu His Lys Leu Tyr Ile Asn Gln Ser 385 390 395 400 Glu Pro Val Lys Gln Val Leu Ser Gly Lys Glu 405

410 32400PRTEremothecium gossypii 32Met Asp Pro Thr Arg Ala Pro Asp Phe Lys Pro Leu Gln Gly Asp Asp 1 5 10 15 Lys Pro Glu Pro Pro Leu Ala Pro Asp Ser Glu Ile Pro Glu Asn Gly 20 25 30 Pro Ile Met Pro Phe Val Leu Ala Asp Tyr Asn Thr Ser Ile Asp Ala 35 40 45 Pro Ile His Pro Lys Ser Tyr Lys Lys Ser Met Lys Arg Asn Ser Ser 50 55 60 Gln Pro Ser Asn Cys Ser Lys Gly Arg Gly Gly Ser Gly Ser Ile Pro 65 70 75 80 Leu Lys Arg Ser Gly Leu Glu Pro Phe Ser Asn Asp Val Ser Ser Glu 85 90 95 Ser Glu Cys Gly Glu Glu Asp Glu Gln Gln Gly Glu Ser His Ala Ala 100 105 110 Asp Ala Asn Ser Ser Lys Leu Arg Ser Met Val Gln Asn Ile Ala Asp 115 120 125 Leu Glu Glu Val Pro Cys Gly Ile Ile Arg Gln Ala Arg Ile Leu Glu 130 135 140 Asp Tyr Glu Phe Pro Thr His Arg Leu Lys Thr Thr Leu His Asn Ala 145 150 155 160 Asn Lys Leu Pro Leu Val Ile Val Ala Cys Gly Ser Phe Leu Pro Ile 165 170 175 Thr His Leu His Leu Arg Met Phe Glu Met Ala Met Asp Ala Ile Val 180 185 190 Glu Gln Thr Arg Phe Glu Val Val Gly Gly Tyr Tyr Ser Pro Val Ser 195 200 205 Asp Asn Tyr Asn Lys Pro Gly Leu Ala Ser Ala Thr His Arg Val Arg 210 215 220 Met Cys Glu Leu Ala Cys Glu Arg Thr Ser Ser Trp Leu Met Val Asp 225 230 235 240 Ala Trp Glu Ser Leu Gln Pro Gln Tyr Thr Arg Thr Ala Lys Val Leu 245 250 255 Asp His Phe Asn Asp Glu Ile Asn Val Lys Arg Gly Gly Ile Lys Thr 260 265 270 Ser Thr Gly Asp Arg Ile Gly Val Lys Ile Met Leu Leu Ala Gly Gly 275 280 285 Asp Leu Ile Glu Ser Met Gly Glu Pro Asn Val Trp Ala Asp Ala Asp 290 295 300 Leu His His Ile Leu Gly Asn Tyr Gly Cys Leu Ile Val Glu Arg Thr 305 310 315 320 Gly Ser Asp Val Arg Ser Phe Leu Leu Ser His Asp Ile Met Tyr Glu 325 330 335 His Arg Arg Asn Ile Leu Val Ile Lys Gln Met Ile Tyr Asn Asp Ile 340 345 350 Ser Ser Thr Lys Val Arg Leu Phe Ile Arg Arg Gly Met Ser Val Gln 355 360 365 Tyr Leu Leu Pro Asn Ser Val Ile Arg Tyr Ile Gln Glu Tyr Gly Leu 370 375 380 Tyr Val Asn Glu His Glu Pro Val Gln Gln Val Ile Ser Asn Lys Asp 385 390 395 400 33449PRTKluyveromyces lactis 33Met Asp Pro Thr Arg Asp Pro Asn Phe Lys Ser Pro Gln Glu Leu Asp 1 5 10 15 Ser Glu Ala Leu Gln Ser Ser Thr Asp Ile Pro Lys Ile Gly Pro Ile 20 25 30 Ile Pro Tyr Val Leu Ala Asp Tyr Asn Thr Ala Ile Asp Lys Pro Ile 35 40 45 Arg Pro Arg Lys Tyr Lys Lys Asn Ala Ile Lys Arg Lys Leu Ala Ser 50 55 60 Ser Met Thr Ser Thr Ser Asp Asp Ser Asn Glu Gln Gln His Leu Ser 65 70 75 80 Ala Asn Ser Asn Asn Gly Phe Ile Pro Leu Lys Gln Arg Glu Leu Gln 85 90 95 Pro Val Ser Ala Glu Thr Ser Gly Asp Ser Glu Ser Glu Ser Glu Ser 100 105 110 Pro Ala Glu Pro Ala Asn Val Asp Leu Asp Ile Asp Pro Asn Pro Glu 115 120 125 Ser Asp Glu Val Met Ala Ser Ala Pro Val Ala His Ala Ser Gly Ser 130 135 140 Val Ser Gly Pro Ser Gly Met Ala Ala Ala Ala Ala Ala Ala Ala Ser 145 150 155 160 Leu Asp Gln Glu Ile Thr Ser Arg Ile His Lys Phe Gln Ile Ala Asp 165 170 175 Leu Glu Glu Val Pro His Gly Ile Val Arg Gln Ala Asn Asn Trp Lys 180 185 190 Asp Tyr Gln Phe Pro Ala His Arg Leu Lys Gln Arg Leu Arg Asn Ser 195 200 205 Asn Lys Leu Pro Leu Val Ile Val Ala Cys Gly Ser Phe Ser Pro Ile 210 215 220 Thr Tyr Leu His Leu Arg Met Phe Glu Met Ala Leu Asp Ala Ile Ser 225 230 235 240 Glu Gln Thr Arg Phe Glu Val Ile Gly Gly Tyr Tyr Ser Pro Val Ser 245 250 255 Asp Asn Tyr Lys Lys Pro Gly Leu Ala Pro Ala His His Arg Val Arg 260 265 270 Met Cys Glu Leu Gly Cys Glu Arg Thr Ser Ser Trp Leu Met Val Asp 275 280 285 Ala Trp Glu Ser Leu Gln Pro Thr Tyr Thr Arg Thr Ala Met Val Leu 290 295 300 Asp His Phe Asn Glu Glu Ile Asn Val Lys Arg Lys Gly Val Ile Lys 305 310 315 320 Asn Asp Ala Gly Glu Arg Met Gly Val Lys Ile Met Leu Leu Ala Gly 325 330 335 Gly Asp Leu Ile Glu Ser Met Gly Glu Pro Asn Val Trp Ala Asp Tyr 340 345 350 Asp Leu His His Ile Leu Gly Asn Tyr Gly Cys Leu Ile Val Glu Arg 355 360 365 Thr Gly Ser Asp Val Arg Ser Phe Leu Leu Ser His Asp Ile Met Tyr 370 375 380 Glu His Arg Arg Asn Ile Leu Val Ile Lys Gln Leu Ile Tyr Asn Asp 385 390 395 400 Ile Ser Ser Thr Lys Val Arg Leu Phe Ile Arg Arg Arg Met Ser Val 405 410 415 Gln Tyr Leu Leu Pro Asn Ser Val Ile Arg Tyr Ile Gln Glu His Gly 420 425 430 Leu Tyr Val Asn Gln Thr Glu Pro Val Lys Gln Val Ile Gly Asn Lys 435 440 445 Asp 34400PRTDebyaromyces hansenii 34Met Asp Pro Thr Arg Ala Pro Asp Phe Lys Pro Leu Gln Gly Asp Asp 1 5 10 15 Lys Pro Glu Pro Pro Leu Ala Pro Asp Ser Glu Ile Pro Glu Asn Gly 20 25 30 Pro Ile Met Pro Phe Val Leu Ala Asp Tyr Asn Thr Ser Ile Asp Ala 35 40 45 Pro Ile His Pro Lys Ser Tyr Lys Lys Ser Met Lys Arg Asn Ser Ser 50 55 60 Gln Pro Ser Asn Cys Ser Lys Gly Arg Gly Gly Ser Gly Ser Ile Pro 65 70 75 80 Leu Lys Arg Ser Gly Leu Glu Pro Phe Ser Asn Asp Val Ser Ser Glu 85 90 95 Ser Glu Cys Gly Glu Glu Asp Glu Gln Gln Gly Glu Ser His Ala Ala 100 105 110 Asp Ala Asn Ser Ser Lys Leu Arg Ser Met Val Gln Asn Ile Ala Asp 115 120 125 Leu Glu Glu Val Pro Cys Gly Ile Ile Arg Gln Ala Arg Ile Leu Glu 130 135 140 Asp Tyr Glu Phe Pro Thr His Arg Leu Lys Thr Thr Leu His Asn Ala 145 150 155 160 Asn Lys Leu Pro Leu Val Ile Val Ala Cys Gly Ser Phe Leu Pro Ile 165 170 175 Thr His Leu His Leu Arg Met Phe Glu Met Ala Met Asp Ala Ile Val 180 185 190 Glu Gln Thr Arg Phe Glu Val Val Gly Gly Tyr Tyr Ser Pro Val Ser 195 200 205 Asp Asn Tyr Asn Lys Pro Gly Leu Ala Ser Ala Thr His Arg Val Arg 210 215 220 Met Cys Glu Leu Ala Cys Glu Arg Thr Ser Ser Trp Leu Met Val Asp 225 230 235 240 Ala Trp Glu Ser Leu Gln Pro Gln Tyr Thr Arg Thr Ala Lys Val Leu 245 250 255 Asp His Phe Asn Asp Glu Ile Asn Val Lys Arg Gly Gly Ile Lys Thr 260 265 270 Ser Thr Gly Asp Arg Ile Gly Val Lys Ile Met Leu Leu Ala Gly Gly 275 280 285 Asp Leu Ile Glu Ser Met Gly Glu Pro Asn Val Trp Ala Asp Ala Asp 290 295 300 Leu His His Ile Leu Gly Asn Tyr Gly Cys Leu Ile Val Glu Arg Thr 305 310 315 320 Gly Ser Asp Val Arg Ser Phe Leu Leu Ser His Asp Ile Met Tyr Glu 325 330 335 His Arg Arg Asn Ile Leu Val Ile Lys Gln Met Ile Tyr Asn Asp Ile 340 345 350 Ser Ser Thr Lys Val Arg Leu Phe Ile Arg Arg Gly Met Ser Val Gln 355 360 365 Tyr Leu Leu Pro Asn Ser Val Ile Arg Tyr Ile Gln Glu Tyr Gly Leu 370 375 380 Tyr Val Asn Glu His Glu Pro Val Gln Gln Val Ile Ser Asn Lys Asp 385 390 395 400 35401PRTCandida albicans 35Met Asp Pro Thr Asn Asp Pro Asn Phe Thr Pro Pro Ser Leu Asn Lys 1 5 10 15 Asn Ile Glu Pro Thr Ala Pro Ser Asp Lys Ile Pro Ser Ile Met Pro 20 25 30 Ile Gln Pro Phe Val Leu Glu Glu Leu Gly Glu Gly Val Asp Gly Pro 35 40 45 Val Pro His Pro Ala Ser Ser Ser Arg Pro Thr Pro Thr Thr Ala Arg 50 55 60 Ser Tyr Asp Ala Ser His Ala Ser Asp Thr Glu Ser Lys Tyr His Ser 65 70 75 80 Lys Ile Pro Arg Lys His Thr Glu Leu Ile Ser Ser Ser Ser Ser Asp 85 90 95 Glu Glu Asn Glu Pro Leu Ser Pro Lys Pro Glu Ile Ile Pro Pro Lys 100 105 110 Lys Glu Ile Leu Pro Pro Ser Ile Lys Val Arg Ser Ser Gln Ile Ala 115 120 125 Asp Leu Glu Glu Val Pro His Gly Ile Gln Arg Gln Ala Leu Lys Leu 130 135 140 Glu Asp Tyr His Phe Pro Thr His Arg Leu Ala Thr Thr Leu Thr Asp 145 150 155 160 Asp Ser Lys His Pro Leu Val Ile Val Ala Cys Gly Ser Phe Ser Pro 165 170 175 Ile Thr Tyr Leu His Leu Arg Met Phe Glu Met Ala Leu Asp Ala Ile 180 185 190 Thr Glu Gln Thr Arg Phe Glu Val Ile Gly Gly Tyr Tyr Ser Pro Val 195 200 205 Ser Ser Asn Tyr Lys Lys Gln Gly Leu Ala Pro Ala His His Arg Val 210 215 220 Arg Met Cys Glu Leu Ala Cys Glu Arg Thr Ser Ser Trp Leu Met Val 225 230 235 240 Asp Ala Trp Glu Ser Leu Gln Pro Lys Tyr Thr Arg Thr Ala Leu Val 245 250 255 Leu Asp His Phe Asn Glu Glu Ile Asn Ile Lys Gln Gly Gly Ile Met 260 265 270 Thr Arg Ser Gly Glu Lys Arg Gly Val Lys Ile Met Leu Leu Ala Gly 275 280 285 Gly Asp Leu Ile Glu Ser Met Gly Glu Pro Asp Val Trp Ala Asp Gln 290 295 300 Asp Leu His His Ile Leu Gly Lys Tyr Gly Cys Leu Ile Val Glu Arg 305 310 315 320 Thr Gly Ser Asp Val Arg Ser Phe Leu Leu Ser His Asp Ile Leu Tyr 325 330 335 Glu His Arg Lys Asn Ile Leu Val Ile Lys Gln Leu Ile Tyr Asn Asp 340 345 350 Ile Ser Ser Thr Lys Ile Arg Leu Phe Ile Arg Arg Gly Met Ser Val 355 360 365 Gln Tyr Leu Leu Pro Asn Ser Val Ile Arg Tyr Ile Gln Gln His Asn 370 375 380 Leu Tyr Gly Asp Ser Glu Pro Val Lys Gln Val Met Ser Asp Arg Ala 385 390 395 400 Asp 36470PRTYarrowia lipolytica 36Met Asp Pro Lys Leu Ala Pro Asn Phe Val Arg Pro Ser Asp Lys Arg 1 5 10 15 Pro Thr Ala Tyr Arg Ser Pro Ala Pro Ala Gln Ala Ser Leu Ile Pro 20 25 30 Asn Ile Ala Pro Ile Gln Pro Tyr Val Leu Glu Asp Ser Gln His Glu 35 40 45 Ile Asp Leu Pro Gln Asp Ser Pro Arg Leu Leu Pro Ser Arg Thr Asn 50 55 60 Ser Arg Asp Ser Leu Val Gly Leu Glu Gln Ile Ala Leu Thr Leu Lys 65 70 75 80 His His Ser Lys His Asn Pro Lys Asp Ser Asn Tyr His Pro Ala Pro 85 90 95 Val Asn Ile Pro Arg Ile His Ser Glu Leu Asn Met Ser Asp Ser Ser 100 105 110 Pro Asp Arg Cys Glu Lys Ile Asp Glu Val Asp Leu Glu Val Ser Pro 115 120 125 Asn Glu Ile Gln Thr Asn Phe Ser Lys Phe Ser Leu Gly Asp Gln Ala 130 135 140 Leu Pro Pro Thr Thr Val Glu Glu Ala Met Ala Pro Thr Ser Pro Lys 145 150 155 160 Ser Pro Lys Glu Pro Gln Val His Thr Glu Thr Gly Thr Ala Asp Ser 165 170 175 Ser Ser Arg Thr Pro Pro Tyr Leu Leu Asp Asn Ser Gly Leu Arg Pro 180 185 190 Ile Ile Gln Ser Ala Asp Leu Glu Glu Val Pro Ile Gly Val Ser Arg 195 200 205 Gln Ala Arg Asp Leu Asp His Tyr Lys Phe Pro Thr His Arg Leu Ser 210 215 220 Glu Val Met Ile Glu Glu Thr Lys Ser Pro Leu Val Ile Val Ala Cys 225 230 235 240 Gly Ser Phe Ser Pro Ile Thr Tyr Leu His Leu Arg Met Phe Glu Met 245 250 255 Ala Met Asp Ser Ile Arg Glu Gln Thr Arg Phe Glu Val Ile Gly Gly 260 265 270 Tyr Tyr Ser Pro Val Ser Asp Asn Tyr Asn Lys Pro Gly Leu Ala Pro 275 280 285 Ala His His Arg Val Arg Met Cys Glu Leu Ala Cys Glu Arg Thr Ser 290 295 300 Ser Trp Leu Met Val Asp Ala Trp Glu Ser Leu Gln Pro Thr Tyr Gln 305 310 315 320 Arg Thr Ala Thr Val Leu Asp His Phe Asn Glu Glu Ile Asn Ile Lys 325 330 335 Arg Gly Gly Ile Lys Thr Val Ser Gly Lys Arg Lys Gly Val Lys Ile 340 345 350 Met Leu Leu Ala Gly Gly Asp Leu Ile Glu Ser Met Gly Glu Pro Asn 355 360 365 Val Trp Glu Glu Arg Asp Leu His His Ile Leu Gly Arg Tyr Gly Cys 370 375 380 Leu Ile Val Glu Arg Thr Gly Ala Asp Val Arg Ser Phe Leu Leu Ser 385 390 395 400 His Asp Ile Met Tyr Glu His Arg Arg Asn Val Leu Val Ile Lys Gln 405 410 415 Leu Ile Tyr Asn Asp Ile Ser Ser Thr Lys Val Arg Leu Phe Ile Arg 420 425 430 Arg Gly Met Ser Val Gln Tyr Leu Ile Pro Asn Ser Val Ile Arg Tyr 435 440 445 Ile Gln Glu His Arg Leu Tyr Val Gly Glu Thr Glu Pro Val Lys Gln 450 455 460 Val Leu Tyr Asp Arg Glu 465 470 37365PRTSchizosaccharomyces pombe 37Met Asn Gly Asp Asn Phe Ala Asn Ser Phe Pro Lys Asn Pro Leu Leu 1 5 10 15 Ser Arg Asn Ser Ser Ser Ser Asn Val Ile Gln Tyr Ser Asp Glu Phe 20 25 30 Ser Pro Asp Glu Asp Trp Leu Asn Glu His Ala Ala Lys Glu His Glu 35 40 45 Glu Arg Ile Arg Arg Pro Ser Val Asn Arg Ala Trp Gln Lys Asn Ser 50 55 60 Thr Ser Gly Gly Pro Ser Val Ser Leu Glu Lys Arg Glu Ala Asp Val 65 70 75 80 Ala Ser Leu Gly Glu Val Met Asp Leu Glu Glu Val Pro Arg Gly Ile 85 90 95 Thr Arg Gln Ala Arg Gln Leu Asn Glu Tyr Ile Phe Pro Lys His Arg 100 105 110 Phe Arg Asn His Leu Val Asp Glu Gly Lys Ile Pro Leu Val Leu Val 115 120 125 Ala Cys Gly Ser Phe Ser Pro Ile Thr Tyr Leu His Leu Arg Met Phe 130 135 140 Glu Met Ala Thr Asp Thr Ile Gln Glu Gln Thr Asn Met Glu Leu Val 145 150 155

160 Ala Gly Tyr Phe Ser Pro Val Asn Asp His Tyr Lys Lys Glu Gly Leu 165 170 175 Ala Pro Ala Tyr His Arg Val Arg Met Cys Glu Leu Ala Cys Glu Arg 180 185 190 Thr Ser Ser Trp Leu Met Val Asp Ala Trp Glu Ser Leu Gln Pro Ser 195 200 205 Tyr Thr Cys Thr Ala Arg Val Leu Asp His Phe Asp Glu Glu Ile Asn 210 215 220 Gln Lys Arg Gly Gly Ile Thr Leu Ser Asp Gly Thr Lys Arg Pro Cys 225 230 235 240 Lys Ile Met Leu Leu Ala Gly Gly Asp Leu Ile Ala Ser Met Gly Glu 245 250 255 Pro Gly Val Trp Ser Asp Lys Asp Leu His His Ile Leu Gly Lys Phe 260 265 270 Gly Cys Cys Ile Val Glu Arg Thr Gly Ser Asp Val Trp Ala Phe Leu 275 280 285 Leu Ala His Asp Ile Met Phe Ala Tyr Arg Gly Asn Ile Leu Val Ile 290 295 300 Lys Gln Leu Ile Tyr Asn Asp Ile Ser Ser Thr Lys Val Arg Leu Phe 305 310 315 320 Ile Arg Arg Gly Met Ser Ile Arg Tyr Leu Leu Pro Asn Ser Val Ile 325 330 335 Gln Tyr Ile Glu Arg Tyr Ala Leu Tyr Arg Asp Ala Glu Pro Val Lys 340 345 350 Thr Ile Phe Tyr Gln Ser Pro Phe Val Arg Met Glu Pro 355 360 365 38584PRTUstilago maydis 38Met Pro Arg Met Thr Asp Ser Gln Ala Gly Pro Gly Gly Pro Ser Ser 1 5 10 15 Leu Lys Phe Ala Ala Leu Ser Val Gln Ser Phe His Leu Asp Ser Pro 20 25 30 Pro Phe Thr Gly Ala Ala Val Gly Gly Ala Gly Pro Leu Asp Glu Ala 35 40 45 Gly Lys Arg Leu Ala Ser His Asp Ala Asp Pro Ala Tyr His Ser Leu 50 55 60 Asp Ser Gly Tyr Ser Gln His Gln Pro Gln Ser Pro Ala Cys Asn Asp 65 70 75 80 Arg Gln Ser Arg Arg Pro Gly Gly Ser Ser Pro Leu Ser Lys Ala Ile 85 90 95 Ser Val Thr Ser Ser Gly Glu Asp His Asp Pro Tyr Arg Arg Ser Met 100 105 110 Ser Gln Thr Arg Pro Pro Ser Gln Ser Gln Thr Leu Arg Ser Gln Asp 115 120 125 Arg Gln His Asn Thr Asp Val Lys Ser Ser Met Ala Gln Pro Gln Ser 130 135 140 Leu Pro Pro Asn Gly Met Thr Thr Ser Glu Asp Ala Pro Ser Ala Ser 145 150 155 160 Asn His Ser Asp Pro His Arg Ser Asn Asp Ser Asn Gly His Leu Glu 165 170 175 Ser Arg Phe Asp Arg Asp Val Pro His Trp Asp Leu Asp Glu Lys Leu 180 185 190 Ser Ser Arg Gln Ala Ser Ser Ala Ser Leu Ala Thr Leu Ser Pro Asp 195 200 205 Lys Pro Ile Met Arg Leu Ser Ser Thr Glu Thr Ser Ser Ala Val Asp 210 215 220 Arg Pro Gly Thr Arg Arg Ser Asp Asp Phe Gln Thr Gly Ser Asn Arg 225 230 235 240 Glu Thr Leu Ile Ala Pro Asn Pro Ser Ser His Arg Thr Asn Ser Asn 245 250 255 Ser Thr Ser Asn Ser Arg Thr Leu Ser Phe Ser Ala Val Leu Asp Glu 260 265 270 Arg Pro Ser Tyr Ser Gln Phe Ser Glu Asp Leu Asp Ala Gln Glu Asp 275 280 285 Ala Ala Ser Ser Ala Ala Asp Arg Asp Glu Glu Val Asp Gly Pro Glu 290 295 300 Gly Leu Ser Ala Glu Phe Arg Leu Arg Asp Arg Arg Val Pro Gln Gln 305 310 315 320 Gly Gln Thr Gln Glu Asp Tyr Ser Phe Pro Arg His Arg Leu Pro Thr 325 330 335 Arg Met Arg Asp Glu Ser Lys Thr Pro Leu Val Val Val Ala Cys Gly 340 345 350 Ser Phe Ser Pro Pro Thr Tyr Leu His Met Arg Ile Phe Glu Met Ala 355 360 365 Lys Asp Gln Ile Ile Glu Ser Gly Lys Tyr Glu Leu Leu Ala Gly Tyr 370 375 380 Tyr Ser Pro Val Ser Asp Tyr Tyr Lys Lys Glu Gly Leu Ala Lys Ala 385 390 395 400 Thr His Arg Val Arg Met Cys Glu Leu Ala Val Glu Lys Thr Ser Thr 405 410 415 Trp Leu Met Val Asp Ala Trp Glu Ser Leu Gln Asp Glu Tyr Gln Arg 420 425 430 Thr Ala Val Val Leu Asp His Phe His Asp Glu Ile Asn Gly Ser Ser 435 440 445 Asn Gly Gly Val Leu Leu Gly Asp Gly Thr Arg Lys Asn Val Lys Ile 450 455 460 Met Leu Leu Ala Gly Gly Asp Leu Ile Gln Ser Met Gly Glu Pro Gly 465 470 475 480 Val Trp Ala Thr Ala Asp Leu His His Ile Leu Gly Gln Tyr Gly Cys 485 490 495 Leu Ile Val Glu Arg Thr Gly Ala Asp Val Trp Ser Phe Leu Leu Ser 500 505 510 His Asp Leu Leu Trp Lys Tyr Arg Arg Asn Leu Lys Ile Val Lys Gln 515 520 525 Thr Ile Tyr Asn Asp Ile Ser Ser Ser Lys Ile Arg Leu Phe Val Arg 530 535 540 Arg Gly Gln Ser Ile Lys Tyr Leu Leu Pro Asn Ser Val Ile Gln Tyr 545 550 555 560 Ile Glu Lys Glu Gly Leu Tyr Arg Leu Pro Pro Asp Glu Asp Leu Lys 565 570 575 Ser Asp Ser Glu His Ala Asn Trp 580 39537PRTCryptococcus neoformans 39Met Thr Arg Val Ser Ile Leu Ser Leu Leu Ser Ser Leu Leu Thr Leu 1 5 10 15 Leu Ser Pro Pro Phe Gly Gly Thr Ala Thr Ser Glu Met Pro Asp Val 20 25 30 Pro Ser Leu Ser Leu Glu Pro Gln Gln His Ser Arg Pro Val Leu Ser 35 40 45 Thr Asn Pro Ser Ala Arg Gln Gln Gly Pro Ala Arg Thr Ala Ser Asn 50 55 60 Thr Ser Gln Thr Ile Ser Asn Pro Glu Pro Val Ser Ser Gly Thr Arg 65 70 75 80 Glu Thr Pro Ser Lys Ala Ile Ser Ser Leu Lys Ser Ile Gln Pro Pro 85 90 95 Thr Pro Pro Val Pro Ile Thr Ser Asp Asp Glu Leu Ser Ser Thr Arg 100 105 110 Ser Arg Arg Leu Ile Ser Gly Tyr Leu Phe Gly Asn Pro Pro Ser Pro 115 120 125 Thr Cys Thr Gly Pro Glu Thr Ser Pro Val Thr Ala Ala Ser His Thr 130 135 140 Ser Thr Ala Glu Glu Ser Arg Asp Pro Met Met Ser Arg Lys Phe Ser 145 150 155 160 Pro Thr Leu Glu Lys Ala Arg Asp Val Glu Asn Arg Met Ala Glu Glu 165 170 175 Leu Asp Ser Pro Pro Leu Thr Asp Asp Ser Gln Ile Asp Pro Arg Asp 180 185 190 Ala Leu Glu Met Asp Ser Thr Pro Pro Pro Pro Ser Leu Glu Ser Pro 195 200 205 Lys Pro Ala Asn Ser Asp Leu Val Ser Met Asn Glu Pro Leu Ser Ser 210 215 220 Asp Val Gly Ala Gly Glu Ala Lys Val Lys Gly Arg Lys Ser Glu Arg 225 230 235 240 Ala Arg Lys Arg Glu Thr Gly Tyr Asp Ala Leu Glu Gly Arg Asn Asp 245 250 255 Gly Glu Ala Asp Leu Asp Leu Asn Ala Pro Gln Ala Glu Gly Gly Gly 260 265 270 Ser Gly Ala Tyr Leu Ala Gly Lys Ala Glu Tyr Arg Phe Pro Arg His 275 280 285 Arg Leu Arg Thr Lys Met His Asp Glu Asn Lys Ile Pro Leu Val Ile 290 295 300 Val Ala Cys Gly Ser Phe Ser Pro Pro Thr Tyr Leu His Leu Arg Met 305 310 315 320 Phe Glu Met Ala Lys Asp Glu Ile Val Glu Ser Gln Thr Tyr Glu Ile 325 330 335 Met Ala Gly Tyr Tyr Ser Pro Val Ser Ser Tyr Tyr Lys Lys Ser Gly 340 345 350 Leu Ala Pro Ala Pro His Arg Val Arg Met Cys Glu Leu Ala Val Glu 355 360 365 His Thr Ser Thr Trp Leu Met Val Asp Pro Trp Glu Ala Gly Gln Pro 370 375 380 Glu Tyr Gln Arg Thr Ala Phe Val Leu Asp His Phe Asp Glu Met Leu 385 390 395 400 Asn Gly Gly Glu His Gly Lys Gly Gly Leu Val Met Arg Asp Gly Thr 405 410 415 Arg Arg Arg Tyr Lys Ile Met Leu Leu Ala Gly Gly Asp Leu Ile Glu 420 425 430 Ser Phe Gly Glu Pro Gly Val Trp Ser Glu Pro Asp Leu His Val Ile 435 440 445 Leu Gly Arg Phe Gly Cys Leu Ile Val Glu Arg Ala Gly Ser Asp Val 450 455 460 Trp Ala Phe Leu Leu Ser His Asp Ile Leu Tyr His His Arg Arg Asn 465 470 475 480 Val Val Val Ile Lys Gln Leu Ile Tyr Asn Asp Ile Ser Ser Thr Lys 485 490 495 Val Arg Leu Phe Val Arg Arg Gly Met Ser Ile Lys Tyr Leu Leu Pro 500 505 510 Asn Ser Val Ile Gln Tyr Ile Gln Asp Asn Lys Leu Tyr His Gly Ser 515 520 525 Asp Pro Lys Gly Met Ile Gly Lys His 530 535 40287PRTAspergillus oryzae 40Met Thr Asp Ile Thr Gly Gly His Gly Glu Asp Val His Gln Pro Pro 1 5 10 15 Ala His Ile Pro Pro Ala Pro Met Glu Asp Tyr Gln Phe Pro Glu Leu 20 25 30 Arg Leu Lys Arg Lys Met Asp Asp Pro Glu Lys Thr Pro Leu Leu Leu 35 40 45 Val Ala Cys Gly Ser Phe Ser Pro Ile Thr Tyr Leu His Leu Arg Met 50 55 60 Phe Glu Met Ala Ala Asp Tyr Val Lys Phe Ser Ser Asn Phe Glu Leu 65 70 75 80 Ile Gly Gly Tyr Leu Ser Pro Val Ser Asp Ala Tyr Arg Lys Ala Gly 85 90 95 Leu Ala Ala Ala Glu His Arg Val Ala Met Cys Gln Leu Ala Val Glu 100 105 110 Gln Thr Ser Asp Trp Leu Met Val Asp Thr Trp Glu Pro Met Gln Lys 115 120 125 Ala Tyr Gln Pro Thr Ala Val Val Leu Asp His Phe Asp His Glu Ile 130 135 140 Asn Thr Val Arg Glu Gly Ile Glu Ala Ala Asp Gly Thr Arg Lys His 145 150 155 160 Val Arg Ile Ala Leu Leu Ala Gly Ala Asp Leu Ile His Thr Met Ser 165 170 175 Thr Pro Gly Val Trp Ser Glu Lys Asp Leu Asp His Ile Leu Gly Lys 180 185 190 Tyr Gly Ser Phe Ile Val Glu Arg Ser Gly Thr Asp Ile Asp Glu Ala 195 200 205 Leu Ala Ala Leu Gln Pro Trp Lys Asp Asn Ile His Val Ile Gln Gln 210 215 220 Leu Ile Gln Asn Asp Val Ser Ser Thr Lys Ile Arg Leu Phe Leu Arg 225 230 235 240 Arg Glu Met Ser Val Arg Tyr Leu Ile Pro Val Pro Val Ile Arg Tyr 245 250 255 Ile Glu Gln His Arg Leu Tyr Gly Asp Asp Asn Thr Thr Ala Asn Ser 260 265 270 Thr Ser Asp Lys Gly Lys Gly Lys Gln Glu Pro Ser Lys Ser Gly 275 280 285 41288PRTAspergillus fumigatus 41Met Thr Asp Met Val Gly Gly Gln Ser Asp Asp Val His Gln Val Pro 1 5 10 15 Pro Pro Leu Pro Pro Ala Pro Met Glu Asn Tyr Thr Phe Pro Glu His 20 25 30 Arg Leu Lys Arg Lys Met Asp Asp Pro Glu Lys Thr Pro Leu Leu Leu 35 40 45 Val Ala Cys Gly Ser Phe Ser Pro Ile Thr Tyr Leu His Leu Arg Met 50 55 60 Phe Glu Met Ala Ala Asp Tyr Val Lys Phe Ser Thr Asp Phe Glu Leu 65 70 75 80 Ile Gly Gly Tyr Leu Ser Pro Val Ser Asp Ala Tyr Arg Lys Ala Gly 85 90 95 Leu Ala Ser Ala Glu His Arg Val Ala Met Cys Gln Leu Ala Val Asp 100 105 110 Gln Thr Ser Asn Trp Leu Met Val Asp Thr Trp Glu Pro Met Gln Lys 115 120 125 Glu Tyr Gln Pro Thr Ala Val Val Leu Asp His Phe Asp Tyr Glu Ile 130 135 140 Asn Val Val Arg Glu Gly Ile Asp Ala Gly Asn Gly Thr Arg Lys Pro 145 150 155 160 Val Arg Val Ala Leu Leu Ala Gly Ala Asp Leu Ile His Thr Met Ser 165 170 175 Thr Pro Gly Val Trp Ser Glu Lys Asp Leu Asp His Ile Leu Gly Lys 180 185 190 Tyr Gly Ser Phe Ile Val Glu Arg Ser Gly Thr Asp Ile Asp Glu Ala 195 200 205 Leu Ala Ala Leu Gln Pro Trp Lys Asp Asn Ile Tyr Val Ile Gln Gln 210 215 220 Leu Ile Gln Asn Asp Val Ser Ser Thr Lys Ile Arg Leu Phe Leu Arg 225 230 235 240 Arg Glu Met Ser Val Arg Tyr Leu Ile Pro Val Pro Val Ile His Tyr 245 250 255 Ile Glu Gln His His Leu Tyr Glu Asp Asp Ser Thr Thr Thr Ala Ser 260 265 270 Ser Ser Ala Asp Lys Gly Lys Glu Pro Ser Gln Pro Gly Lys Ser Gly 275 280 285 42285PRTAspergillus nidulans 42Met Thr Glu Ser Thr Gln Glu Gln Gly Asn Asp Gly Gln Arg Met Pro 1 5 10 15 Pro Ala Pro Ala Thr Pro Val Glu Asp Tyr Val Phe Pro Glu Tyr Arg 20 25 30 Leu Lys Arg Val Met Asp Asp Pro Glu Lys Thr Pro Leu Leu Leu Ile 35 40 45 Ala Cys Gly Ser Phe Ser Pro Ile Thr Phe Leu His Leu Arg Met Phe 50 55 60 Glu Met Ala Ala Asp Tyr Val Lys Leu Ser Thr Asp Phe Glu Ile Ile 65 70 75 80 Gly Gly Tyr Leu Ser Pro Val Ser Asp Ala Tyr Arg Lys Ala Gly Leu 85 90 95 Ala Ser Ala Asn His Arg Ile Ala Met Cys Gln Arg Ala Val Asp Gln 100 105 110 Thr Ser Asp Trp Met Met Val Asp Thr Trp Glu Pro Met His Lys Glu 115 120 125 Tyr Gln Pro Thr Ala Ile Val Leu Asp His Phe Asp Tyr Glu Ile Asn 130 135 140 Thr Val Arg Lys Gly Ile Asp Thr Gly Lys Gly Thr Arg Lys Arg Val 145 150 155 160 Gln Val Val Leu Leu Ala Gly Ala Asp Leu Val His Thr Met Ser Thr 165 170 175 Pro Gly Val Trp Ser Glu Lys Asp Leu Asp His Ile Leu Gly Gln Tyr 180 185 190 Gly Thr Phe Ile Val Glu Arg Ser Gly Thr Asp Ile Asp Glu Ala Leu 195 200 205 Ala Ala Leu Gln Pro Trp Lys Lys Asn Ile His Val Ile Gln Gln Leu 210 215 220 Ile Gln Asn Asp Val Ser Ser Thr Lys Ile Arg Leu Phe Leu Arg Arg 225 230 235 240 Asp Met Ser Val Arg Tyr Leu Ile Pro Asp Pro Val Ile Glu Tyr Ile 245 250 255 Tyr Glu Asn Asn Leu Tyr Met Asp Asp Gly Thr Thr Gln Pro Thr Ala 260 265 270 Asp Lys Gly Lys Thr Arg Glu Glu Pro Ala Pro Ser Asn 275 280 285 43276PRTGiberella zeae 43Met Ala Cys Asp Tyr Gln Tyr Val Lys Glu His Thr Arg Glu Asp Tyr 1 5 10 15 Val Phe Pro Ser His Arg Phe Gln Arg Ser Cys Ser Pro Asp Lys Thr 20 25 30 Pro Leu Cys Leu Val Ala Cys Gly Ser Phe Ser Pro Ile Thr Phe Leu 35 40 45 His Leu Arg Met Phe Pro Met Ala Arg Asp His Ala Arg Asn Glu Asp 50 55 60 Phe Glu Val Val Ala Gly Val Leu Ser Pro Val Ser Asp Ala Tyr Lys 65 70 75 80 Lys Lys Gly Leu Ala Pro Ala His His Arg Ile Glu Met Cys Arg Leu 85 90 95 Ala Thr Glu Asn Thr Ser Lys Trp Leu Met

Val Asp Pro Trp Glu Ala 100 105 110 Glu Ser Pro Thr Tyr Ile Pro Thr Ala Lys Val Leu Asp His Phe Asp 115 120 125 Tyr Glu Ile Asn Glu Val Met Gly Gly Val Glu Cys Thr Asp Gly Thr 130 135 140 Arg Lys Arg Cys Arg Ile Val Leu Leu Ala Gly Leu Asp Leu Ile Gln 145 150 155 160 Thr Met Ser Thr Pro Gly Val Trp Asp Glu Arg Asp Leu Asp His Ile 165 170 175 Leu Gly Asn Tyr Gly Val Phe Ala Leu Glu Arg Thr Gly Thr Glu Ile 180 185 190 Asp Ser Thr Leu Ala Asn Leu Lys Gln Trp Glu Lys Asn Ile His Ile 195 200 205 Ile Arg Gln Val Val Thr Asn Asp Ile Ser Ser Thr Lys Ile Arg Leu 210 215 220 Leu Leu Lys Arg Asn Met Ser Ile Asp Phe Leu Ile Pro Asp Asp Val 225 230 235 240 Ile Ser Tyr Ile Tyr Glu His Asn Leu Tyr Arg Asp Leu Asp Met Pro 245 250 255 Asp Ser Lys Gly Lys Glu Lys Ala Leu Thr Asn Gly Pro Asp Ala Gly 260 265 270 Thr Ser Thr Gly 275 44317PRTNeurospora crassa 44Met Ser Ser Gln Thr Ser Thr Gly Met Ala Thr Pro Val Thr Tyr Pro 1 5 10 15 Pro Pro Glu Gln Ala Ser Thr Gly Asn Thr Thr Val Pro Tyr Thr Phe 20 25 30 Pro Gln Ala Lys Leu Lys Leu Gln Gln Thr Gln Pro Gly Arg Thr Pro 35 40 45 Leu Val Leu Val Ala Cys Gly Ser Phe Ser Pro Ile Thr Phe Leu His 50 55 60 Leu Arg Met Phe Glu Met Ala Ser Asp Phe Val Arg Phe Asn Thr Asn 65 70 75 80 Phe Glu Val Cys Gly Gly Tyr Leu Ser Pro Val Ser Asp Ala Tyr Lys 85 90 95 Lys Ala Gly Leu Ala Pro Gly His His Arg Val Glu Met Cys Ser Arg 100 105 110 Ala Val Glu His Ser Ser Trp Leu Met Val Asp Pro Phe Glu Thr Val 115 120 125 Asn Cys Asp Glu Asn Gly Glu Pro Ala Tyr Val Pro Thr Ala Arg Val 130 135 140 Leu Arg His Phe Asp His Glu Ile Asn Thr Val Leu Gly Gly Ile Glu 145 150 155 160 Gly Thr Asp Gly Val Arg Arg Lys Ala Lys Ile Ala Leu Leu Ala Gly 165 170 175 Ala Asp Leu Val Met Ser Met Gly Glu Pro Gly Leu Trp Ser Pro Val 180 185 190 Asp Leu Gly Val Ile Leu Gly Glu Tyr Gly Ala Phe Ile Ile Glu Arg 195 200 205 Ser Gly Thr Asp Ile Asp Glu Ala Leu Ala Thr Leu Arg Gln Tyr Glu 210 215 220 Asp Asn Ile Trp Val Ile Ser Gln Val Ile Gln Asn Asp Ile Ser Ser 225 230 235 240 Thr Lys Val Arg Leu Phe Leu Lys Lys Asp Leu Ser Val Arg Tyr Leu 245 250 255 Ile Pro Asp Pro Val Val Glu Tyr Ile Glu Glu His Gly Leu Phe Gln 260 265 270 Asp Glu Gln Ser Ser Lys Lys Lys Asn Asn Asp Thr Ser Ser Thr Gly 275 280 285 Gly Lys Asp Lys Glu Lys Glu Lys Pro Thr Thr Ala Asp Gly Thr Ser 290 295 300 Thr Pro Ser Ser Ser Thr Glu Glu Thr Thr Gln Gln Ser 305 310 315 45292PRTMagnaporthe grisea 45Met Ser Asn Ala Thr Ser Pro Thr Pro Gln Phe Pro Pro Thr Thr Pro 1 5 10 15 Gly Tyr Thr Phe Pro Val Asp Lys Leu Arg Thr Arg Gln Thr Gln Asn 20 25 30 Glu Arg Thr Pro Leu Val Leu Val Ala Cys Gly Ser Phe Ser Pro Ile 35 40 45 Thr Tyr Leu His Leu Arg Met Phe Glu Met Ala Arg Ala Gly Pro Ala 50 55 60 Asp Asn Arg Thr Gly Asp His Cys Ser Leu Asn Thr Asn Phe Glu Val 65 70 75 80 Val Gly Gly Tyr Ile Ser Pro Val Ser Asp Ala Tyr Lys Lys Ala Gly 85 90 95 Leu Ala Pro Ala His His Arg Ile Asn Met Cys Lys Leu Ser Leu Ala 100 105 110 Ser Ser Ser Trp Ile Met Val Asp Glu Tyr Glu Thr Ser Val Arg Asn 115 120 125 Pro Thr Thr Asn Glu Pro Ala Tyr Thr Pro Thr Ala Gln Val Leu Ala 130 135 140 Lys Leu Asp His Glu Ile Asn Thr Val Leu Gly Gly Ile Gln Ser Ala 145 150 155 160 Asp Asp Pro Asn Lys Arg Thr Arg Ala Arg Ile Cys Leu Leu Ala Gly 165 170 175 Gly Asp Leu Val Leu Thr Met Ser Thr Pro Gly Leu Trp Ala Pro Ser 180 185 190 Asp Leu Asp Val Ile Leu Gly Pro Lys Phe Gly Ala Phe Ile Val Glu 195 200 205 Arg Ser Gly Thr Asp Thr Glu Glu Ala Leu Ala Ser Leu Gln Arg Tyr 210 215 220 Lys Asp Asn Ile Trp Val Ile Pro Gln Val Ile Gln Asn Asp Val Ser 225 230 235 240 Ser Thr Lys Ile Arg Leu Phe Leu Lys Lys Asn Leu Ser Ile Arg Tyr 245 250 255 Leu Ile Pro Asp Pro Val Val Arg Tyr Ile Glu Glu His Gly Leu Phe 260 265 270 Asn Gly Glu Phe Ser Gly Ala Ser Ser Ser Lys Glu Ala Glu Pro Ser 275 280 285 Pro Ser Thr Ala 290 46120PRTUstilago maydis 46Met Leu Leu Ala Gly Gly Asp Leu Ile Gln Ser Met Gly Glu Pro Gly 1 5 10 15 Val Trp Ala Thr Ala Asp Leu His His Ile Leu Gly Gln Tyr Gly Cys 20 25 30 Leu Ile Val Glu Arg Thr Gly Ala Asp Val Trp Ser Phe Leu Leu Ser 35 40 45 His Asp Leu Leu Trp Lys Tyr Arg Arg Asn Leu Lys Ile Val Lys Gln 50 55 60 Thr Ile Tyr Asn Asp Ile Ser Ser Ser Lys Ile Arg Leu Phe Val Arg 65 70 75 80 Arg Gly Gln Ser Ile Lys Tyr Leu Leu Pro Asn Ser Val Ile Gln Tyr 85 90 95 Ile Glu Lys Glu Gly Leu Tyr Arg Leu Pro Pro Asp Glu Asp Leu Lys 100 105 110 Ser Asp Ser Glu His Ala Asn Trp 115 120 47225PRTChaetomium globosum 47Met Thr Ala Gly Thr Ile Asn Ser Asp Thr Gln Thr Pro Thr Ala Met 1 5 10 15 Gly Pro Ala Val Asp Gly Ala Gln Ala Pro Tyr Asn Phe Pro Thr Gln 20 25 30 Lys Leu Lys Arg Gln Met Thr Gln Pro Gly Lys Thr Pro Leu Val Leu 35 40 45 Val Ala Cys Gly Ser Phe Ser Pro Ile Thr Tyr Leu His Leu Arg Met 50 55 60 Phe Glu Met Ala Gly Asp Phe Val Arg Phe Asn Thr Asp Phe Glu Val 65 70 75 80 Cys Ala Gly Tyr Leu Ser Pro Val Ser Asp Ala Tyr Lys Lys Val Gly 85 90 95 Leu Ala Pro Gly Ser His Arg Val Asn Met Cys Gly Arg Ala Val Glu 100 105 110 Gln Ser Pro Trp Leu Met Val Asp Pro Phe Glu Thr Val Asn Cys Asp 115 120 125 Glu Asn Gly Glu Pro Gln Tyr Val Pro Thr Ala Lys Val Leu Arg His 130 135 140 Phe Asp His Glu Ile Asn Thr Val Leu Gly Gly Ile Glu Ala Pro Asp 145 150 155 160 Gly Gln Met Lys Lys Ala Arg Ile Ala Leu Leu Ala Gly Ala Asp Leu 165 170 175 Val Met Ser Met Gly Gly Phe Asp Thr Gly Ser Arg Val Ser Asn Val 180 185 190 Lys Leu Thr Cys Thr Arg Gly Ala Trp Ala Leu Gly Ser Lys Gly Ser 195 200 205 Gly His Asp Pro Arg Val Val Arg Arg Phe His His Arg Ala Leu Gly 210 215 220 Asp 225 48426PRTSaccharomyces cerevisae 48Met Ser Glu Pro Val Ile Lys Ser Leu Leu Asp Thr Asp Met Tyr Lys 1 5 10 15 Ile Thr Met His Ala Ala Val Phe Thr Asn Phe Pro Asp Val Thr Val 20 25 30 Thr Tyr Lys Tyr Thr Asn Arg Ser Ser Gln Leu Thr Phe Asn Lys Glu 35 40 45 Ala Ile Asn Trp Leu Lys Glu Gln Phe Ser Tyr Leu Gly Asn Leu Arg 50 55 60 Phe Thr Glu Glu Glu Ile Glu Tyr Leu Lys Gln Glu Ile Pro Tyr Leu 65 70 75 80 Pro Ser Ala Tyr Ile Lys Tyr Ile Ser Ser Ser Asn Tyr Lys Leu His 85 90 95 Pro Glu Glu Gln Ile Ser Phe Thr Ser Glu Glu Ile Glu Gly Lys Pro 100 105 110 Thr His Tyr Lys Leu Lys Ile Leu Val Ser Gly Ser Trp Lys Asp Thr 115 120 125 Ile Leu Met Arg Ser Leu Thr Val Leu Ile Ser Glu Ala Tyr Leu Ile 130 135 140 Val Thr Ser Thr Gly Leu Arg Asn His Arg Gln Ala Glu Lys Lys Ala 145 150 155 160 Glu Thr Leu Phe Asp Asn Gly Ile Arg Phe Arg Ile His Gly Thr Arg 165 170 175 Arg Arg Arg Ser Leu Lys Ala Gln Asp Leu Ile Met Gln Gly Ile Met 180 185 190 Lys Ala Val Asn Gly Asn Pro Asp Arg Asn Lys Ser Leu Leu Leu Gly 195 200 205 Thr Ser Asn Ile Leu Phe Ala Lys Lys Tyr Gly Val Lys Pro Ile Gly 210 215 220 Thr Val Ala His Glu Trp Val Met Gly Val Ala Ser Ile Ser Glu Leu 225 230 235 240 Asp Tyr Leu His Ala Asn Lys Asn Ala Met Asp Cys Trp Ile Asn Thr 245 250 255 Phe Gly Ala Lys Asn Ala Gly Leu Ala Leu Thr Asp Thr Phe Gly Thr 260 265 270 Asp Asp Phe Leu Lys Ser Phe Arg Pro Pro Tyr Ser Asp Ala Tyr Val 275 280 285 Gly Val Arg Gln Asp Ser Gly Asp Pro Val Glu Tyr Thr Lys Lys Ile 290 295 300 Ser His His Tyr His Asp Val Leu Lys Leu Pro Lys Phe Ser Lys Ile 305 310 315 320 Ile Cys Tyr Ser Asp Ser Leu Asn Val Glu Lys Ala Ile Thr Tyr Ser 325 330 335 His Ala Ala Lys Glu Asn Gly Met Leu Ala Thr Phe Gly Ile Gly Thr 340 345 350 Asn Phe Thr Asn Asp Phe Arg Lys Lys Ser Glu Pro Gln Val Lys Ser 355 360 365 Glu Pro Leu Asn Ile Val Ile Lys Leu Leu Glu Val Asn Gly Asn His 370 375 380 Ala Ile Lys Ile Ser Asp Asn Leu Gly Lys Asn Met Gly Asp Pro Ala 385 390 395 400 Thr Val Lys Arg Val Lys Glu Glu Leu Gly Tyr Thr Glu Arg Ser Trp 405 410 415 Ser Gly Asp Asn Glu Ala His Arg Trp Thr 420 425 49431PRTCandida glabrata 49Met Ser Ser Met Thr Pro Ala Ile Thr Ser Leu Leu Asp Thr Asp Met 1 5 10 15 Tyr Lys Ile Thr Met His Ala Ala Val Phe Thr Asn Phe Pro Asp Ala 20 25 30 Arg Val Val Tyr Lys Phe Thr Asn Arg Thr Ala Gln Phe His Phe Asn 35 40 45 Lys Arg Ala Val Asp Trp Ile Lys Glu Gln Phe Arg Leu Leu Gly Asp 50 55 60 Leu Thr Phe Thr His Asp Asp Val Glu Tyr Leu Ala Arg Glu Ile Pro 65 70 75 80 Phe Leu Pro Ala Lys Tyr Leu His Tyr Ile Glu Asn Gly Phe Thr Leu 85 90 95 Lys Pro Asp Glu Gln Ile Glu Leu Asp Cys Gln Glu Ile Lys Gly Lys 100 105 110 Glu Asp Gln Tyr Asp Leu His Ile Leu Val Lys Gly Leu Trp Ile Asp 115 120 125 Thr Ile Leu Tyr Glu Ile Pro Ile Leu Ala Leu Leu Ser Glu Ala Tyr 130 135 140 Phe Lys Phe Val Asp Thr Asp Trp Asp Tyr Glu Asn Gln Leu Ser Asn 145 150 155 160 Ala Lys Glu Lys Ala Leu Arg Leu Phe Glu Asn Asn Leu Ser Phe Ser 165 170 175 Glu Phe Gly Thr Arg Arg Arg Arg Ser Phe Lys Thr Gln Asp Leu Val 180 185 190 Met Glu Gly Ile Met Gln Ala Val Lys Glu Asn Pro Glu Lys Tyr Arg 195 200 205 Pro Leu Leu Leu Gly Thr Ser Asn Ile Leu Phe Ala Lys Lys Tyr Gly 210 215 220 Val Lys Pro Ile Gly Thr Val Ala His Glu Trp Ile Met Gly Ile Ala 225 230 235 240 Ser Ile Thr Gly Asp Tyr Pro Glu Thr Asn Arg Ile Ala Met Asp Tyr 245 250 255 Trp Ile Lys Thr Phe Gly Lys Glu His Ala Gly Leu Ala Leu Thr Asp 260 265 270 Thr Phe Gly Thr Asp Asp Phe Leu Lys Ser Phe Lys Pro Pro Tyr Ser 275 280 285 Asp Tyr Tyr Ile Gly Val Arg Gln Asp Ser Gly Asp Pro Ile Lys Tyr 290 295 300 Thr Glu Lys Ile Ala His His Phe His Asp Val Leu Lys Leu Pro Lys 305 310 315 320 Phe Ser Lys Phe Ile Cys Tyr Ser Asp Ser Leu Asn Ile Asp Lys Ala 325 330 335 Ile Glu Tyr Gly Lys Val Ala Glu Ala His Gly Ile Lys Ser Thr Phe 340 345 350 Gly Ile Gly Thr Asn Phe Thr Asn Asp Phe His Lys Lys Ser Asp Pro 355 360 365 Ser Val Lys Ser Ala Pro Leu Asn Ile Val Ile Lys Leu Leu Glu Val 370 375 380 Asn Gly Asn His Ser Ile Lys Ile Ser Asp Asn Ala Gly Lys Asn Met 385 390 395 400 Gly Asp Pro Asp Thr Val Lys Lys Val Lys Glu Gln Leu Gly Tyr Val 405 410 415 Glu Arg Gln Trp Ala Gly Gly Asn Glu Ala His Arg Ser Ala Ala 420 425 430 50427PRTKluyveromyces lactis 50Met Glu Pro Val Ile Thr Ser Phe Leu Asp Thr Asp Met Tyr Lys Leu 1 5 10 15 Thr Met His Ala Ala Val Tyr Thr His Phe Lys Asp Val Lys Val Lys 20 25 30 Tyr Lys Tyr Thr Asn Arg Ser Pro Gln Met Thr Phe Asn Lys Glu Ala 35 40 45 Val Glu Trp Leu Lys Gly Gln Phe Leu Leu Leu Ala Asn Ile Arg Leu 50 55 60 Thr Thr Glu Glu Leu Lys Tyr Ile Lys Glu Ala Ile Pro Tyr Leu Pro 65 70 75 80 Ala Glu Tyr Leu Glu Phe Ile Ser Asn Gly Gly Phe Glu Val Asn Pro 85 90 95 Lys Asp Glu Ile Lys Phe Glu Ala Arg Glu Ile Glu Gly Glu Pro Gly 100 105 110 His Tyr Glu Leu Asp Ile Ser Ile Glu Gly Leu Trp Ile Lys Thr Ile 115 120 125 Trp Tyr Glu Ile Pro Val Leu Ala Leu Val Ser Glu Ala Tyr Phe Lys 130 135 140 Phe Val Asp Thr Asp Trp Thr Tyr Asp Gly Gln Val Glu Lys Ala Tyr 145 150 155 160 Ala Lys Ala Lys Lys Leu Leu Asp His Asp Ile Val Phe Ser Glu Phe 165 170 175 Gly Thr Arg Arg Arg Arg Ser Phe Lys Thr Gln Asp Leu Val Met Gln 180 185 190 Gly Ile Ile Asn Ala Ala Lys Asp Cys Asp Lys Ser Lys Tyr Val Leu 195 200 205 Gly Thr Ser Asn Val Leu Phe Ala Lys Lys Tyr Asn Val Asn Pro Ile 210 215 220 Gly Thr Val Ala His Glu Trp Met Met Gly Ile Ala Ser Ile Thr Asn 225 230 235 240 Asp Tyr Leu Asn Ala Asn Lys Asn Ala Met Asp Tyr Trp Ile Glu Thr 245 250 255 Phe Gly Met Glu Asn Ala Gly Leu Ala Leu Thr Asp Thr Phe Gly Thr 260 265 270 Asp Ser Phe Leu Lys Ser Phe Tyr Pro Pro Tyr Ser Asp Ala Tyr Ile 275 280 285 Gly Val Arg Gln Asp Ser Gly Asp Pro Ile Leu Tyr Thr

Glu Lys Ile 290 295 300 Ala His His Tyr Asn Asp Val Leu Lys Leu Pro Lys Phe Ser Lys Ile 305 310 315 320 Ile Cys Tyr Ser Asp Ser Leu Asn Pro Asp Arg Ala Ile Glu Tyr Ala 325 330 335 Gln Val Ala His Lys His Gly Leu Lys Ala Thr Phe Gly Ile Gly Thr 340 345 350 Asn Phe Thr Asn Asp Phe Gln Arg Lys Ser Asp Val Ser Val Lys Ser 355 360 365 Glu Pro Leu Asn Ile Val Ile Lys Leu Leu Glu Val Asn Gly Asn His 370 375 380 Ala Ile Lys Ile Ser Asp Asn Leu Gly Lys Asn Met Gly Asp Pro Glu 385 390 395 400 Thr Val Arg Arg Val Lys Glu Glu Leu Gly Tyr Val Glu Arg Lys Tyr 405 410 415 Ala Gly Asp Asn Glu Ala His Arg Trp Ala Ala 420 425 51430PRTEremothecium gossypii 51Met Thr Ser Glu Glu Ala Ala Ile Lys Ser Leu Leu Asp Thr Asp Met 1 5 10 15 Tyr Lys Leu Thr Met His Ala Ala Val Tyr Val Asn Phe Pro Asp Thr 20 25 30 Glu Val Val Tyr Lys Tyr Thr Asn Arg Ser Ala Gly Leu Ser Phe Asn 35 40 45 Lys Ala Ala Ile Val Trp Leu Glu Asp Gln Val Ser Lys Leu Ala Thr 50 55 60 Leu Arg Phe Thr Ala Glu Glu Val Ala Tyr Leu Lys Glu Thr Leu Pro 65 70 75 80 Phe Leu Pro Ala Gln Tyr Ile Asp Tyr Ile Ser Ser Pro Glu Cys Arg 85 90 95 Met Asp Pro Ala Thr Gln Val Gln Leu Leu His Glu Gln Arg Glu Gly 100 105 110 Glu Glu Arg Tyr Asp Leu Asn Ile Thr Val Thr Gly Leu Trp Lys Asp 115 120 125 Thr Ile Leu Tyr Glu Ile His Met Leu Ala Leu Ile Ser Glu Ala Tyr 130 135 140 Phe Lys Phe Val Asp Thr Asp Trp Val Leu Asp Gly Gln Val Glu Gln 145 150 155 160 Ala Tyr Arg Lys Thr Arg Leu Leu Leu Asp Asn Gly Leu Val Phe Ser 165 170 175 Glu Phe Gly Thr Arg Arg Arg Arg Ser Leu Leu Val Gln Asp Leu Val 180 185 190 Leu Gln Gly Ile Ala Glu Ala Val Ala Asp Ser Gly Thr Gly Asp Thr 195 200 205 Gln Phe Ile Gly Thr Ser Asn Val Tyr Phe Ala Lys Lys Tyr Gly Val 210 215 220 Lys Pro Val Gly Thr Val Ala His Glu Trp Tyr Met Gly Ile Ala Ala 225 230 235 240 Leu Thr Asp Asp Tyr Arg Asn Ala Asn Lys Asn Ala Met Asp Phe Trp 245 250 255 Leu Asn Thr Phe Gly Ser Glu Gln Ala Gly Leu Val Leu Thr Asp Thr 260 265 270 Phe Gly Thr Asp Thr Phe Leu Pro Met Phe Arg Pro Pro Tyr Ser Asp 275 280 285 Val Tyr Asp Gly Val Arg Gln Asp Ser Gly Asp Pro Ala Val Phe Thr 290 295 300 Glu Lys Val Ala His His Tyr Leu Asn Val Leu His Tyr Pro Arg Phe 305 310 315 320 Ser Lys Val Ile Cys Tyr Ser Asp Ser Leu Asn Pro Glu Lys Ala Leu 325 330 335 Gln Tyr Ala Glu Val Ala Arg Ala His Gly Met Arg Ala Ser Phe Gly 340 345 350 Ile Gly Thr Asn Phe Thr Asn Asp Phe Arg Arg His Ser Ala Pro Asp 355 360 365 Ala Lys Ser Glu Pro Leu Asn Ile Val Phe Lys Leu Leu Thr Val Asn 370 375 380 Gly Arg Pro Ala Ile Lys Ile Ser Asp Asp Leu Gly Lys Thr Met Gly 385 390 395 400 Asp Pro Glu Lys Val Glu Glu Val Lys Arg Glu Leu Gly Tyr Ile Glu 405 410 415 Arg Thr Trp Glu Gly Ser Asp Glu Ala His Arg Trp Lys Asp 420 425 430 52422PRTDebaromyces hansenii 52Met Thr Thr Asp Ile Pro Ile Ile Thr Ser Ile Leu Asp Thr Asp Leu 1 5 10 15 Tyr Lys Leu Thr Met His Ala Ala Val Val Lys His Phe Pro Asn Ile 20 25 30 Pro Val Val Tyr Arg Tyr Thr Asn Arg Thr Pro Ser Met Val Leu Asn 35 40 45 Lys Glu Ala Ile Asp Trp Leu Lys Tyr Gln Ile Ser Lys Leu Ser Asp 50 55 60 Leu Arg Val Ser Ser Glu Glu Leu Glu Tyr Leu Arg Lys Ala Leu Pro 65 70 75 80 Gln Met Pro Glu Val Tyr Leu Lys Tyr Leu Glu Thr Phe Gln Leu Phe 85 90 95 Pro Asp Lys Gln Ile Lys Tyr Phe Asn Asp Glu Ser Asn Phe Glu Glu 100 105 110 Phe Glu Ile Glu Met Lys Gly Lys Trp Asp Glu Thr Met Leu Tyr Glu 115 120 125 Ile Pro Leu Leu Ala Leu Ile Ser Glu Ala Tyr Phe Lys Phe Val Asp 130 135 140 Thr Asp Trp Asn Tyr Asp Gly Gln Ala Glu Arg Ala Glu Asp Lys Cys 145 150 155 160 Ala Gln Leu Phe Lys Asn Glu Cys Thr Phe Ser Glu Phe Gly Thr Arg 165 170 175 Arg Arg Arg Ser Phe Lys Thr Gln Asp Leu Val Val Lys Asn Leu Cys 180 185 190 Asp Phe Ala Gly Lys Asn Pro Asp Lys Lys His Phe Leu Gly Thr Ser 195 200 205 Asn Val Leu Leu Ala Lys Lys Tyr Asn Thr Thr Pro Ile Gly Thr Val 210 215 220 Ala His Glu Trp Phe Met Gly Ile Ala Ser Ile Thr Gln Asp Tyr Thr 225 230 235 240 Asn Ala Asn Lys Leu Ala Met Asp Tyr Trp Leu Asp Thr Phe Gly Pro 245 250 255 Glu His Ala Gly Leu Ala Leu Thr Asp Thr Phe Gly Thr Asp Ala Tyr 260 265 270 Leu Lys Val Phe Thr Lys Pro Tyr Thr Asp Tyr Tyr Thr Gly Val Arg 275 280 285 Gln Asp Ser Gly Asp Pro Glu Leu Phe Ala Glu Lys Leu Ala Asp His 290 295 300 Tyr Lys Lys Gln Gly Tyr Pro Asp Phe Ser Lys Ile Ile Cys Phe Ser 305 310 315 320 Asp Ser Leu Asn Val Glu Lys Cys Leu Lys Tyr Lys Gln Lys Val Asn 325 330 335 Ser Leu Gly Leu Ile Ala Ser Phe Gly Ile Gly Thr Phe Phe Thr Asn 340 345 350 Asp Phe Ala Ser Val Ser Asp Pro Ser Thr Lys Ser Val Pro Leu Asn 355 360 365 Ile Val Ile Lys Leu Lys Glu Ala Asn Gly Asn Pro Ser Ile Lys Ile 370 375 380 Ser Asp Asn Leu Gly Lys Asn Met Gly Asp Pro Ala Val Val Ser Arg 385 390 395 400 Val Lys Lys Glu Leu Asn Tyr Glu Glu His Ser Trp Ala Glu Gly Asp 405 410 415 Glu Glu Lys Arg Trp Asp 420 53421PRTCandida albicans 53Met Asn Gly Thr Glu Asp Lys Pro Val Ile Lys Ser Phe Leu Asp Thr 1 5 10 15 Asp Leu Tyr Lys Leu Phe Met His Ala Ala Val Asn Lys Gln Phe Pro 20 25 30 Asp Val Pro Val Lys Tyr Arg Tyr Thr Asn Arg Thr Pro Gln Leu Lys 35 40 45 Leu Asn Ser Gln Ala Ile Ser Trp Leu Lys Lys Gln Ile Glu Tyr Leu 50 55 60 Gly Asp Leu Arg Phe Ser Ala Glu Glu Ile Leu Tyr Leu His Arg Val 65 70 75 80 Leu Pro Gln Leu Pro Ser Asp Tyr Leu Glu Tyr Leu Ala Asp Phe Lys 85 90 95 Leu Val Pro Ser Ser Gln Ile Lys Tyr Leu Asp Asn Asp Glu Gly Asp 100 105 110 Phe Glu Leu Glu Ile Val Gly Lys Trp Asn Asp Thr Ile Leu Tyr Glu 115 120 125 Ile Pro Leu Leu Ala Leu Val Ser Glu Ala Tyr Phe Lys Phe Val Asp 130 135 140 Thr Asp Trp Asn Tyr Glu Gly Gln Tyr Ala Leu Ala Gln Lys Lys Ala 145 150 155 160 Lys Gln Leu Ile Ser Asn Glu Cys Asn Phe Ser Glu Phe Gly Thr Arg 165 170 175 Arg Arg Arg Ser Tyr Glu Ser Gln Glu Ile Val Ile Lys Ala Ile Lys 180 185 190 Asp Val Gln Ile Asp Thr Gln Ser Lys Tyr Ile Ala Gly Thr Ser Asn 195 200 205 Val Tyr Phe Ala Met Lys Tyr Asp Leu Pro Pro Ile Gly Thr Val Ala 210 215 220 His Glu Trp Tyr Met Gly Ile Ala Ser Ile Thr Gln Asp Tyr Val His 225 230 235 240 Ala Asn Lys Leu Ala Met Asp Tyr Trp Ile Asp Thr Phe Gly Ala Lys 245 250 255 Tyr Ala Gly Leu Ala Leu Thr Asp Thr Phe Gly Thr Asp Asn Tyr Leu 260 265 270 Thr Met Phe Val Ala Pro Tyr Val Asn Glu Tyr Ser Gly Val Arg Gln 275 280 285 Asp Ser Gly Asp Pro Glu Leu Tyr Ala Glu Lys Ile Ala Arg His Tyr 290 295 300 Glu Lys Met Gly Ile Ala Lys Asn Thr Lys Ile Ile Cys Phe Ser Asp 305 310 315 320 Ser Leu Asn Val Glu Lys Cys Leu Lys Tyr Lys Asn Thr Ala Asp Lys 325 330 335 Leu Gly Leu Ile Ser Thr Phe Gly Ile Gly Thr Phe Phe Thr Asn Asp 340 345 350 Phe Asn Lys Leu Ser Asn Gly Glu Lys Ser Gln Pro Met Asn Ile Val 355 360 365 Ile Lys Ile Lys Glu Ala Asn Gly Lys Pro Ala Ile Lys Ile Ser Asp 370 375 380 Asn Ile Gly Lys Asn Met Gly Asp Gln Ala Thr Val Asp Arg Val Lys 385 390 395 400 Gln Glu Leu Gly Tyr Thr Glu Arg Thr Trp Ser Glu Gly Asp Glu Thr 405 410 415 His Arg Trp Ser Lys 420 54414PRTYarrowia lipolytica 54Met Ser Thr Ile Thr Ser Leu Leu Asp Thr Asp Leu Tyr Lys Leu Thr 1 5 10 15 Met Gln Ala Ala Val Leu Gln His Phe Pro Ala Ala Gln Ala Thr Phe 20 25 30 Leu Phe Lys Asn Arg Thr Pro Ser Lys Gln Leu Asn Asp Asp Ala Ile 35 40 45 Glu Trp Leu Lys Ser Glu Ile Ala Ala Leu Gly Glu Leu Arg Phe Thr 50 55 60 Glu Asp Glu Ile Val Phe Leu Gln Lys His Val Gly Phe Leu Pro Ala 65 70 75 80 Glu Tyr Phe Glu Tyr Leu Lys Thr Cys Gln Leu Asp Pro Ala Ala Gln 85 90 95 Val Lys Val Thr Val Asn Thr Glu Gly His Leu Glu Ile Glu Val Asn 100 105 110 Gly Pro Trp Lys Asp Thr Ile Leu Tyr Glu Ile Pro Leu Leu Ala Leu 115 120 125 Val Ser Glu Ala Tyr Phe Lys Phe Val Asp Lys Asp Trp Ser Tyr Asp 130 135 140 Gly Gln Ser Glu Leu Ala Ala Thr Lys Ala Gln Glu Leu Ile Ala Gln 145 150 155 160 Gly Cys Ala Phe Ser Glu Phe Gly Thr Arg Arg Arg Arg Ser Leu Lys 165 170 175 Thr His Asp Ile Val Ile Ala Gly Ile Leu Glu Gly Leu Lys Ser Ala 180 185 190 Gln Gly Asn Gly Ile Phe Thr Gly Thr Ser Asn Val Tyr Leu Ala Lys 195 200 205 Lys Tyr Asn Leu Lys Pro Ile Gly Thr Val Ala His Glu Trp Met Met 210 215 220 Gly Val Ala Ala Ala Thr Gly Asp Tyr Ser Thr Ala Asn Leu Arg Ala 225 230 235 240 Met Glu Leu Trp Ile Gln Thr Val Gly Asp Ala Asn Ala Gly Val Ala 245 250 255 Leu Thr Asp Thr Phe Gly Thr Glu Ser Phe Leu Leu Asp Phe Asn Lys 260 265 270 Pro Leu Thr Asp Ile Tyr Asn Gly Val Arg Gln Asp Ser Gly Asp Pro 275 280 285 Leu Glu Tyr Thr Lys Leu Leu Gly Asp His Tyr Lys Gln Leu Gly Tyr 290 295 300 Glu Pro Met Ser Lys Val Ile Val Tyr Ser Asp Ser Leu Asp Val Glu 305 310 315 320 Lys Cys Gly Lys Tyr Lys Ala Ala Ala Ala Glu Asn Gly Leu Lys Ala 325 330 335 Ala Phe Gly Val Gly Thr Phe Phe Thr Asn Asp Phe Lys Arg Leu Ser 340 345 350 Asp Gly Gln Lys Ser Thr Pro Leu Asn Ile Val Ile Lys Ile Gln Gln 355 360 365 Leu Asn Gly Gln Ser Cys Ile Lys Leu Ser Asp Asn Leu Ser Lys Asn 370 375 380 Met Gly Asp Pro Glu Thr Val Glu Arg Val Lys Arg Glu Leu Gly Tyr 385 390 395 400 Val Glu Lys Gly Asp Val Ile Asp Glu Ser Lys Arg Trp Asn 405 410 55490PRTAspergillus fumigatus 55Met Ser Gln Glu Thr Thr Pro Pro Tyr Pro Glu Gly Ile Phe Ser Leu 1 5 10 15 Leu Asp Thr Asp Leu Tyr Lys Leu Thr Met Gln Cys Ala Ile Leu Lys 20 25 30 Tyr Phe Pro Asp Val His Val Thr Tyr Gly Phe Thr Asn Arg Thr Pro 35 40 45 Asp Met Lys Leu Thr Arg Gly Ala Tyr Lys Trp Leu Leu Glu Gln Met 50 55 60 Asp Arg Leu Ala Asn Val Arg Val Thr Asp Glu Glu Ile Ala Phe Leu 65 70 75 80 Lys Lys Gln Cys Pro Tyr Phe Asn His Ala Tyr Leu Arg Tyr Leu Ser 85 90 95 Thr Phe Gln Leu Lys Pro Ser Glu Gln Ile Asp Ile Lys Phe Arg Pro 100 105 110 Val Gln Asp Ser Gly Ser Asp Asp Asp Leu Gly Asp Ile Glu Tyr Met 115 120 125 Val Lys Gly Leu Trp Val Glu Thr Ile Leu Tyr Glu Ile Pro Leu Leu 130 135 140 Ala Leu Thr Ser Gln Ala Tyr Phe Met Phe Thr Asp Lys Asp Trp Asp 145 150 155 160 His Ser Asn Gln Glu Glu Lys Ala Phe Arg Lys Gly Cys Thr Leu Leu 165 170 175 Glu Asn Gly Cys Ile Phe Ser Glu Phe Gly Ser Arg Arg Arg Arg Asp 180 185 190 Tyr His Thr Gln Asp Leu Val Met Gln Gly Leu Cys Arg Ala Ala Glu 195 200 205 Glu Gly Lys Arg Gln Gly Trp Lys Gly Val Phe Ser Gly Thr Ser Asn 210 215 220 Val His Phe Ala Met Arg Tyr Gly Val Thr Pro Ile Gly Thr Val Ala 225 230 235 240 His Glu Trp Phe Met Ala Ile Ala Ala Ile Thr Asp Asp Tyr Glu Asn 245 250 255 Ala Asn Glu Leu Ala Leu Arg Tyr Trp Leu Gly Cys Phe Gly Glu Gly 260 265 270 Val Leu Gly Ile Ala Leu Thr Asp Thr Phe Gly Thr Pro Ala Phe Leu 275 280 285 Asp Ala Phe Arg Lys Pro Ile Pro His His Thr Ser Ala Gly Val Gly 290 295 300 Ala Val Ala Thr Ile Ala Ser Gly Ala Ser Thr Thr Ser Glu Ser Gln 305 310 315 320 Pro Gln Thr Glu Ala Glu Thr Lys Pro Pro Val Thr Ala Pro Leu His 325 330 335 Glu Asn Asp Ser Gln His Ser Pro Lys Thr Tyr Ala Gln Val Tyr Thr 340 345 350 Gly Val Arg Gln Asp Ser Gly Asp Pro Thr Tyr Phe Val Lys Met Val 355 360 365 Arg Asp Phe Tyr Asp Asn Glu Gly Ile Lys Glu Lys Lys Thr Val Val 370 375 380 Phe Ser Asp Ser Leu Asn Ile Glu His Cys Leu Glu Tyr Lys Thr Ile 385 390 395 400 Ala Glu Glu Ala Gly Phe Ala Pro Ile Phe Gly Val Gly Thr Phe Phe 405 410 415 Thr Asn Asp Phe Thr Asn Lys Ser Asp Gly Lys Lys Ser Lys Pro Leu 420 425 430 Asn Ile Val Ile Lys Ile Ala Thr Ala Asn Gly Arg Pro Ala Val Lys 435 440 445 Leu Ser Asp Asn Met Gly Lys Asn Thr Gly Asp Lys Asn Met Val Gln 450 455 460

Glu Val Lys Lys Arg Leu Gly Tyr Ile Glu His Tyr Trp Glu Glu Gly 465 470 475 480 Asp Glu Ser Asn Arg Trp Ala Lys Gln Gly 485 490 56489PRTAspergillus oryzae 56Met Asp Gln Glu Gly Ser Pro Pro Ile Pro Glu Gly Ile Cys Ser Leu 1 5 10 15 Leu Asp Thr Asp Leu Tyr Lys Leu Thr Met Gln Cys Ala Val Leu Lys 20 25 30 Tyr Phe Pro Asp Thr His Val Thr Tyr Gly Phe Thr Asn Arg Thr Pro 35 40 45 His Met Lys Leu Thr Arg Gly Ala His Lys Trp Leu Leu Lys Gln Met 50 55 60 Asp Arg Leu Ala Asn Ile Arg Ile Thr Glu Glu Glu Ile Lys Phe Leu 65 70 75 80 Lys Thr Arg Cys Pro Tyr Phe Asn Asp Ala Tyr Leu Asp Phe Leu Thr 85 90 95 Thr Phe Lys Leu Lys Pro Ser Glu Gln Ile Glu Ile Lys Phe Thr Pro 100 105 110 Val Asn Asp Thr Gly Ser Asp Ser Asp Thr Gly Asp Val Glu Tyr Leu 115 120 125 Val Lys Gly Leu Trp Val Asp Thr Ile Leu Tyr Glu Ile Pro Leu Leu 130 135 140 Ala Leu Thr Ser Glu Ala Tyr Phe Met Phe Ser Asp Lys Asp Trp Asp 145 150 155 160 Tyr Ser Cys Gln Glu Glu Lys Ala Tyr Arg Lys Gly Cys Thr Leu Leu 165 170 175 Glu Asn Gly Cys Ile Phe Ser Glu Phe Gly Ser Arg Arg Arg Arg Asp 180 185 190 Tyr His Thr His Asp Leu Val Met Val Gly Leu Met Lys Ala Ala Glu 195 200 205 Glu Gly Lys Arg Gln Gly Trp Lys Gly Arg Phe Thr Gly Ser Ser Asn 210 215 220 Val His Phe Ala Met Lys Tyr Gly Val Asp Pro Val Gly Thr Val Ala 225 230 235 240 His Glu Trp Tyr Met Thr Ile Ala Ala Ile Thr Asp Asp Tyr Glu Asn 245 250 255 Ala Asn Glu Leu Ala Leu Arg Tyr Trp Leu Gly Cys Phe Gly Lys Gly 260 265 270 Val Leu Gly Ile Ala Leu Thr Asp Thr Phe Gly Thr Pro Ala Phe Leu 275 280 285 Asp Ala Phe Arg Lys Pro Ile Pro Ala Phe Thr Ser Ala Gly Ala Gly 290 295 300 Ala Val Ser Thr Ser Ala Ser Gly Pro Ala Thr Thr Asn Glu Ser Thr 305 310 315 320 Val Gln Ser Glu Ala Glu Thr Lys Ala Pro Ile Thr Ala Pro Leu Arg 325 330 335 Asp Gly Gly Ala Arg Thr Ser His Glu Thr Tyr Ala Gln Ala Tyr Thr 340 345 350 Gly Val Arg Gln Asp Ser Gly Asp Pro Val Tyr Phe Val Lys Met Val 355 360 365 Arg Asp Phe Tyr Asp Arg Glu Gly Ile Thr Asp Lys Lys Thr Met Val 370 375 380 Phe Ser Asp Ser Leu Asn Ile Glu His Cys Leu Glu Tyr Lys Val Ile 385 390 395 400 Ala Glu Glu Ala Gly Phe Gln Pro Val Phe Gly Val Gly Thr Phe Phe 405 410 415 Thr Asn Asp Phe Thr Asn Lys Ser Asn Asp Glu Lys Ser Lys Pro Leu 420 425 430 Asn Ile Val Ile Lys Ile Ser Thr Ala Asn Gly His Pro Ala Val Lys 435 440 445 Leu Ser Asp Asn Met Gly Lys Asn Thr Gly Asp Lys Gln Lys Val Gln 450 455 460 Glu Val Lys Lys Lys Leu Gly Tyr Val Glu His Glu Trp Glu Glu Gly 465 470 475 480 Asp Glu Ser Asn Arg Trp Ser Lys Arg 485 57477PRTNeurospora crassa 57Met Asp Phe Asn Ser Ser Leu Pro His Pro Ala Gly Val Ile Ser Phe 1 5 10 15 Leu Asp Thr Asp Leu Tyr Lys Leu Thr Met Gln Cys Ala Val Leu Lys 20 25 30 Tyr Phe Lys Asp Val Pro Val Thr Tyr Ser Phe Thr Asn Arg Thr Pro 35 40 45 Glu Lys Lys Leu Ser Arg Glu Ala Phe Val Trp Leu Glu Glu Gln Val 50 55 60 Met Lys Leu Gly Asn Ile Ser Leu Ser Pro Glu Glu Leu Gln Phe Leu 65 70 75 80 Lys Thr His Cys Pro Tyr Leu Thr Glu Glu Tyr Leu Asp Tyr Leu Ser 85 90 95 Glu Phe Arg Leu Arg Pro Arg Glu Gln Val Ala Val Ser Phe Arg Pro 100 105 110 Asp Gly Asp Ser Asp Leu Gly Asp Ile His Tyr Asp Ile Lys Gly Asn 115 120 125 Trp Ala Glu Thr Ile Leu Tyr Glu Ile Pro Leu Leu Ala Leu Thr Ser 130 135 140 Glu Ala Tyr Phe Lys Phe Met Asp Thr Asp Trp Asp Tyr Asp Gly Gln 145 150 155 160 Glu Glu Lys Ala Tyr Glu Lys Gly Met Arg Leu Leu Glu Ala Gly Cys 165 170 175 Val Phe Ser Glu Phe Gly Thr Arg Arg Arg Arg Asp Tyr His Thr Gln 180 185 190 Ala Leu Val Phe Arg Gly Leu Thr Lys Ala Ala Lys Glu Ala Glu Lys 195 200 205 Arg Gly Leu Thr Gly Lys Leu Ser Gly Thr Ser Asn Val His Leu Ala 210 215 220 Met Arg Phe Asn Ile Pro Pro Val Gly Thr Val Ala His Glu Trp Phe 225 230 235 240 Met Gly Asn Ala Ala Ile Leu Gly Asp Tyr Lys Ser Ala Thr Glu Glu 245 250 255 Ala Leu Ser Arg Trp Val Gly Cys Tyr Gly Pro Gly Val Leu Gly Ile 260 265 270 Ala Leu Thr Asp Thr Phe Gly Thr Pro Glu Phe Leu Arg Ala Phe Ser 275 280 285 Lys Pro Met Ser Ala Ser Gly Glu Pro Val Pro Gln Pro Arg Asp Arg 290 295 300 Lys Ile Ser Thr Ala Asp Ala Phe Ile Ser Ala Ala Lys Asp Phe Ile 305 310 315 320 Lys Asp Leu His Pro Asp Lys Thr Tyr Ala Gln Val Phe Thr Gly Val 325 330 335 Arg Gln Asp Ser Gly Asp Pro Lys Glu Phe Val Lys Leu Met Arg Lys 340 345 350 Phe Tyr Asp Glu Gln Gly Ile Lys Asp Lys Lys Val Ile Val Phe Ser 355 360 365 Asp Ser Leu Asp Ile Asp Arg Cys Leu Glu Tyr Lys Glu Val Ala Glu 370 375 380 Ala Ala Gly Phe Gln Pro Thr Phe Gly Val Gly Thr Tyr Phe Thr Asn 385 390 395 400 Asp Phe Val His Lys Ala Thr Gly Lys Lys Ser Thr Pro Leu Asn Ile 405 410 415 Val Ile Lys Leu Ser Ser Ala Ala Gly Asn Pro Ala Val Lys Ile Ser 420 425 430 Asp Asn Val Gly Lys Asn Thr Gly Asp Lys Ala Thr Val Glu Lys Val 435 440 445 Lys Arg Glu Leu Gly Tyr Val Glu Lys Asp Trp Ser Glu Gly Asp Glu 450 455 460 Ser Ala Arg Trp Gly His Asp Gly Asp Ala Ala Thr Ala 465 470 475 58481PRTChaetomium globosum 58Met Asp Phe Asn Ser Ser Ser Pro Tyr Pro Glu Gly Val Ile Ser Phe 1 5 10 15 Leu Asp Thr Asp Leu Tyr Lys Leu Thr Met Gln Cys Ala Val Leu Lys 20 25 30 Tyr Tyr Lys Asn Val Pro Val Thr Tyr Ala Phe Thr Asn Arg Thr Pro 35 40 45 Glu Lys Lys Leu Ser Arg Lys Ala Phe Arg Trp Leu Glu Asp Gln Val 50 55 60 Arg Lys Leu Gly Asn Ile Ser Leu Ser Ala Glu Glu Leu Tyr Tyr Leu 65 70 75 80 Lys Glu His Cys Pro Tyr Leu Ser Pro Ala Tyr Leu Glu Phe Leu Ser 85 90 95 Glu Phe Arg Leu Arg Pro Arg Glu Gln Val Val Leu Ser Phe Leu Pro 100 105 110 Thr Gly Glu Asp Thr Gly Ala Glu Ser Asp Ile Gly Asp Leu Asp Ile 115 120 125 Lys Ile Ser Gly Ile Trp Ser Glu Ala Ile Leu Tyr Glu Ile Pro Leu 130 135 140 Leu Ser Leu Thr Ser Glu Ala Tyr Phe Lys Phe Met Glu Pro Asp Trp 145 150 155 160 Thr Tyr Glu Gly Gln Glu Asp Gln Ala Phe Glu Lys Gly Met Arg Leu 165 170 175 Leu Glu Ala Gly Cys Val Phe Ser Glu Phe Gly Thr Arg Arg Arg Arg 180 185 190 Asp Tyr His Thr Gln Ala Leu Val Phe Arg Gly Leu Thr Lys Ala Ser 195 200 205 Lys Glu Ala Glu Lys Arg Gly Leu Ser Gly Lys Leu Ser Gly Thr Ser 210 215 220 Asn Val His Leu Ala Met Arg Phe Asn Ile Pro Pro Val Gly Thr Val 225 230 235 240 Ala His Glu Trp Phe Met Gly Ser Ala Ala Ile Val Gly Asp Tyr Arg 245 250 255 Lys Ala Thr Glu Glu Ala Leu Arg His Trp Val Gly Cys Phe Gly Glu 260 265 270 Gly Val Leu Gly Ile Ala Leu Thr Asp Thr Phe Gly Thr Pro Asp Phe 275 280 285 Leu Thr Ala Phe Ser Lys Pro Ile Glu Tyr Leu Glu Pro Pro Ser Pro 290 295 300 Thr Thr Ala Arg Lys Pro Ser Val Ala Asp Ser Phe Ile Ser Thr Ser 305 310 315 320 Pro Ser Val Ala Ser His Gln Lys Pro Asn Lys Thr Tyr Ala Glu Val 325 330 335 Phe Thr Gly Val Arg Gln Asp Ser Gly Asp Pro Lys Thr Phe Val Lys 340 345 350 Ile Ile Gly Lys Phe Tyr Arg Glu Gln Gly Ile Lys Asp Lys Lys Val 355 360 365 Ile Val Phe Ser Asp Ser Leu Asn Ile Asp Arg Cys Leu Glu Tyr Lys 370 375 380 Gln Val Ser Glu Glu Ala Gly Phe Gln Pro Thr Phe Gly Val Gly Thr 385 390 395 400 Phe Leu Thr Asn Asp Phe Val Asn Thr Lys Thr Gly Lys Lys Ser Thr 405 410 415 Pro Leu Asn Ile Val Ile Lys Leu Ser Ser Ala Asp Gly Asn Pro Ala 420 425 430 Ile Lys Ile Ser Asp Asn Ile Gly Lys Asn Thr Gly Asp Lys Ala Thr 435 440 445 Val Glu Lys Val Lys Arg Glu Leu Gly Tyr Val Glu Lys Met Trp Glu 450 455 460 Gly Gly Asp Glu Thr Ala Arg Trp Gly Arg Glu Asp Asp Ala Pro Lys 465 470 475 480 Gln 59487PRTAspergillus nidulans 59Met Gly Glu His Ser Leu Leu Pro Asp Gly Val Phe Ser Leu Leu Asp 1 5 10 15 Thr Asp Leu Tyr Lys Leu Thr Met Gln Cys Ala Ile Leu Lys Tyr Phe 20 25 30 Pro Asp Val Gln Val Thr Tyr Gly Phe Thr Asn Arg Thr Pro His Met 35 40 45 Lys Leu Thr Arg Gly Ala Tyr Lys Trp Met Leu Ala Gln Met Asp Lys 50 55 60 Leu Ala Asn Ile Arg Val Thr Glu Asp Glu Ile Ala Phe Leu Lys Arg 65 70 75 80 Arg Cys Pro Tyr Phe Asn Thr Ala Tyr Leu Asp Phe Leu Thr Asn Phe 85 90 95 Arg Leu Lys Pro Ser Glu Gln Ile Asp Ile Asn Phe Thr Pro Val Asn 100 105 110 Asp Thr Gly Ser Asp Ser Asp Phe Gly Asp Ile Asp Tyr Ile Val Lys 115 120 125 Gly Ala Trp Val Asp Thr Ile Leu Tyr Glu Ile Pro Leu Leu Ala Leu 130 135 140 Thr Ser Gln Ala Tyr Phe Met Phe Ser Asp Lys Asp Trp Asn Tyr Glu 145 150 155 160 Cys Gln Glu Gly Lys Ala Tyr Arg Lys Gly Tyr Val Leu Leu Glu Asn 165 170 175 Gly Cys Thr Phe Ser Glu Phe Gly Thr Arg Arg Arg Arg Ser Tyr His 180 185 190 Thr Gln Asp Leu Val Met Gln Gly Leu Cys Arg Ala Ala Arg Glu Gly 195 200 205 Lys Ala Lys Gly Leu Pro Gly Val Phe Thr Gly Ser Ser Asn Val His 210 215 220 Phe Ala Met Lys Tyr Asp Val Asp Pro Val Gly Thr Val Ala His Glu 225 230 235 240 Trp Tyr Met Thr Ile Ala Ala Ile Thr Asp Asp Tyr Glu Asn Ala Asn 245 250 255 Glu Met Ala Leu Lys Tyr Trp Leu Gly Cys Phe Gly Glu Gly Val Leu 260 265 270 Gly Ile Ala Leu Thr Asp Thr Phe Gly Thr Pro Ala Phe Leu Asp Ala 275 280 285 Phe Arg Lys Pro Ile Pro Asp Tyr Thr Ser Ala Gly Thr Gly Ala Val 290 295 300 Ser Thr Thr Ala Ser Gly Pro Ser Thr Thr Ala Glu Ser Asn Ile Gln 305 310 315 320 Ser Glu Ala Glu Thr Lys Ala Pro Ile Thr Ala Pro Leu Ser Pro Asp 325 330 335 His Pro Pro Pro Ala Val Lys Thr Tyr Ala Gln Val Tyr Ala Gly Val 340 345 350 Arg Gln Asp Ser Gly Asp Pro Ser Tyr Phe Val Lys Met Ala Arg Asp 355 360 365 Phe Tyr Asp Arg Glu Gly Ile Thr Gly Thr Lys Thr Val Val Phe Ser 370 375 380 Asp Ser Leu Asp Ile Glu His Cys Leu Glu Tyr Lys Val Leu Ala Glu 385 390 395 400 Glu Ala Gly Phe Lys Pro Val Phe Gly Val Gly Thr Phe Phe Thr Asn 405 410 415 Asp Phe Ile Asn Thr Thr Thr Asn Glu Lys Ser Gln Pro Leu Asn Ile 420 425 430 Val Ile Lys Ile Ser Ser Ala Asn Gly Arg Ala Ala Val Lys Leu Ser 435 440 445 Asp Asn Met Gly Lys Asn Thr Gly Asp Lys Asp Thr Val Gln Ala Val 450 455 460 Lys Lys Arg Leu Gly Tyr Val Glu His Glu Trp Glu Glu Gly Asp Glu 465 470 475 480 Arg Asn Arg Trp Ala Arg Lys 485 60459PRTGibberella moniliformis 60Met Asp Phe Asn Ser Ser Ser Pro Phe Pro Glu Gly Val Ile Ser Phe 1 5 10 15 Leu Asp Thr Asp Leu Tyr Lys Leu Thr Met Gln Cys Ala Val Phe Lys 20 25 30 Phe Phe Lys Asp Val Pro Val Thr Tyr Ala Tyr Thr Asn Arg Thr Pro 35 40 45 Asp Lys Lys Leu Ser Arg Thr Ala Phe Lys Trp Leu Glu Glu Gln Ile 50 55 60 Arg Lys Leu Gly Asn Ile Ser Leu Ser Thr Asp Glu Tyr Leu Phe Leu 65 70 75 80 Lys Lys His Cys Asp Tyr Leu Ser Asp Asp Tyr Leu Asn Phe Leu Lys 85 90 95 Glu Phe Arg Leu Ser Pro Arg Glu Gln Val Val Ala Thr Phe Thr Pro 100 105 110 Val Gly Glu Asp Asn Gly Asp Asp Ser Ile Glu Gly Asp Val Asp Ile 115 120 125 Gln Ile Lys Gly Thr Trp Val Asp Thr Ile Leu Tyr Glu Ile Pro Met 130 135 140 Leu Ala Leu Thr Ser Glu Ala Tyr Phe Lys Phe Met Asp Thr Asp Trp 145 150 155 160 Asn Tyr Glu Gly Gln Glu Lys Gln Ala Phe Glu Lys Gly Leu Lys Leu 165 170 175 Leu Glu Ala Gly Cys Ile Thr Ser Glu Phe Gly Thr Arg Arg Arg Arg 180 185 190 Asp Tyr His Thr Gln Ala Leu Val Phe Arg Gly Leu Val Gln Ala Ser 195 200 205 Lys Glu Ala Glu Lys Lys Gly Phe Pro Gly Lys Leu Ser Gly Thr Ser 210 215 220 Asn Val His Leu Ala Met Arg Phe Asn Ile Pro Pro Val Gly Thr Val 225 230 235 240 Ala His Glu Trp Phe Met Gly Val Ala Ala Ile Ile Gly Asp Tyr Arg 245 250 255 Ser Ala Thr Glu Val Ala Leu Arg His Trp Val Ala Cys Phe Gly Asn 260 265 270 Lys Leu Gly Ile Ala Leu Thr Asp Thr Phe Gly Thr Gln Glu Phe Leu 275 280 285 Arg Ala Phe Thr Gln Pro Val Gln Thr Ile Glu Gly Gly Phe Pro Ala 290 295 300 Glu Thr Phe Lys Lys Ala Asp Gly Thr Met Lys Thr Tyr Ala Glu Thr 305 310 315 320 Phe Ala Gly Ile Arg Gln Asp Ser Gly Asp Pro Ala

Glu Tyr Thr Lys 325 330 335 Trp Met Lys Glu Phe Tyr Asp Lys Gln Gly Ile Thr Asp Lys Lys Leu 340 345 350 Ile Val Phe Ser Asp Ser Leu Asn Ile Glu Arg Cys Leu Glu Tyr Lys 355 360 365 Lys Ile Ala Glu Asp Leu Gly Phe Gln Pro Thr Phe Gly Val Gly Thr 370 375 380 Tyr Leu Thr Asn Asp Phe Val His Leu Thr Thr Gly Lys Lys Ser Val 385 390 395 400 Pro Leu Asn Ile Val Ile Lys Ile Ser Ser Ala Ala Gly Arg Pro Ala 405 410 415 Val Lys Ile Ser Asp Asn Ile Gly Lys Asn Thr Gly Asp Lys Glu Thr 420 425 430 Val Glu Lys Val Lys Gln Glu Leu Gly Tyr Val Glu Arg Glu Trp Lys 435 440 445 Glu Gly Asp Glu Thr Ser Arg Trp Gly Lys Glu 450 455 61410PRTSchizosaccharomyces pombe 61Met Ser Glu Pro Ala Val Val Ser Ile Leu Asp Thr Asp Leu Tyr Lys 1 5 10 15 Leu Thr Met Leu Gln Ala Val Leu Glu His Tyr Pro Asp Ala Gln Val 20 25 30 Ser Tyr Lys Tyr Thr Asn Arg Ser Pro Lys Met Ala Leu Asn Gln Glu 35 40 45 Ala Tyr Asn Trp Leu Arg Glu Gln Ile Arg Gly Leu Arg Asn Leu His 50 55 60 Leu Leu Pro Glu Glu Glu Gln Trp Leu Arg Lys Asn Cys Pro Tyr Leu 65 70 75 80 Lys Glu Ser Phe Tyr Glu Phe Met His Glu Phe Glu Phe Asp Pro Glu 85 90 95 Asn Ser Ile Ser Leu Asn Tyr Asp Ser Glu Thr Lys Asp Leu Ser Ile 100 105 110 Phe Ile His Gly Leu Trp Lys Asn Thr Ile Phe Tyr Glu Ile Pro Leu 115 120 125 Leu Ala Leu Val Ser Glu Ser Tyr Phe Lys Phe Val Asp Lys Asp Trp 130 135 140 Ser Pro Glu Gly Gln Phe Glu Lys Ala Tyr Glu Lys Gly Lys Arg Leu 145 150 155 160 Ile Arg Ala Gly Cys Ala Phe Thr Asp Phe Gly Thr Arg Arg Arg Arg 165 170 175 Asp Pro His Thr Gln Glu Ile Val Leu Gln Gly Leu Met Lys Ala Gln 180 185 190 Glu Asp Phe Lys Gly Pro Gly Ser Phe Leu Gly Thr Ser Asn Val Tyr 195 200 205 Phe Ala Ala Lys Tyr Asn Leu Asn Val Ser Gly Thr Val Ala His Glu 210 215 220 Trp Tyr Met Gly Ile Ala Ala Ile Thr Gln Asn Tyr Lys Gln Ala Asn 225 230 235 240 Arg Ile Ala Ser Leu Lys Trp Val Gln Thr Phe Gly Thr Ser Leu Leu 245 250 255 Ile Ala Leu Thr Asp Thr Phe Ser Thr Asp Val Phe Leu Lys Ser Phe 260 265 270 Thr Ala Asn Ser Ala Asp Asp Leu Ala Asn Val Phe His Gly Val Arg 275 280 285 Gln Asp Ser Gly Cys Ala Glu Glu Tyr Ile Glu Lys Val Val Lys His 290 295 300 Tyr Lys Ser Ile Gly Val Asp Pro Ser Thr Lys Val Ile Val His Ser 305 310 315 320 Asp Ala Leu Asn Val Asp Arg Cys Ile Glu Leu Tyr Lys Tyr Cys Glu 325 330 335 Lys Cys Gly Ile Lys Ser Ala Phe Gly Ile Gly Thr Asn Leu Thr Ser 340 345 350 Asp Phe Gln Lys Val Ser Asn Pro Ser Glu Val Ser Lys Pro Met Asn 355 360 365 Ile Val Ile Lys Leu Phe Ser Ala Glu Gly Thr Lys Ala Val Lys Ile 370 375 380 Ser Asp Asp Ile Met Lys Asn Thr Gly Asp Arg Asp Ala Val Ile Gln 385 390 395 400 Ala Lys His Gln Leu Cys Leu Pro Ile Ala 405 410 621971PRTMagnaporthe grisea 62Met Asp Phe Asn Ser Asp Ser Pro Phe Pro Glu Gly Val Ile Ser Phe 1 5 10 15 Leu Asp Thr Asp Leu Tyr Lys Leu Thr Met Gln Cys Ala Val Leu Lys 20 25 30 Tyr Tyr Ser Asn Thr Ser Val Thr Tyr Ser Phe Thr Asn Arg Thr Pro 35 40 45 Glu Lys Arg Leu Ser Arg Lys Ala Tyr Gln Trp Leu Gln Asp Gln Ile 50 55 60 Arg Asn Glu Glu Tyr Arg Phe Leu Lys Asp Asn Cys Pro Tyr Leu Gly 65 70 75 80 Thr Gln Tyr Leu Glu Phe Leu Gln Asn Phe Arg Leu Asn Pro Arg Asp 85 90 95 Gln Val Ile Val Ser Phe Ala Pro Val Gly Lys His Glu Gly Ala Asp 100 105 110 Ser Asp Val Gly Asp Ile Asp Ile Gln Ile Ser Gly Lys Trp Val Asp 115 120 125 Thr Ile Leu Tyr Glu Ile Pro Ile Leu Ala Leu Thr Ser Glu Ala Tyr 130 135 140 Phe Arg Phe Met Asp Thr Asp Trp Asp Tyr Gln Gly Gln Glu Glu Leu 145 150 155 160 Ala Tyr Glu Lys Gly Lys Arg Ile Leu Glu Ala Gly Cys Ile Leu Ser 165 170 175 Glu Phe Gly Thr Arg Arg Arg Arg Asp Tyr His Thr Gln Ala Leu Val 180 185 190 Phe Arg Gly Leu Val Lys Ala Ser Lys Glu Ala Gln Lys Arg Gly Leu 195 200 205 Ser Gly Lys Leu Ser Gly Thr Ser Asn Val His Leu Ala Met Arg Phe 210 215 220 Asn Met Ala Pro Val Gly Thr Val Ala His Glu Trp Phe Met Gly Ile 225 230 235 240 Ala Ala Ile Ile Gly Asp Tyr Arg Ser Ala Ser Glu Glu Ala Leu Ala 245 250 255 Arg Trp Val Gly Ala Phe Gly Pro Gly Val Leu Ala Ile Ala Leu Thr 260 265 270 Asp Thr Phe Gly Thr Pro Glu Phe Leu Lys Ser Phe Ser Arg Pro Val 275 280 285 Arg Trp Leu Glu Glu Ala His Ser Ala Ala Ala Gly Asn Glu Ser Lys 290 295 300 Thr Tyr Ala Gln Val Phe Ala Gly Val Arg Gln Asp Ser Gly Asp Pro 305 310 315 320 Thr Thr Phe Val Lys Arg Met Arg Glu Phe Tyr Asp Gln Gln Arg Ile 325 330 335 Lys Glu Lys Lys Thr Ile Val Phe Ser Asp Ser Leu Asp Ile Asp Arg 340 345 350 Cys Leu Val Tyr Lys Gln Val Ser Glu Ala Ala Gly Phe Gln Pro Thr 355 360 365 Phe Gly Val Gly Thr Phe Leu Thr Asn Asp Phe Val Gly Lys Ser Thr 370 375 380 Gly Lys Lys Ser Thr Pro Leu Asn Ile Val Ile Lys Leu Ser Ser Ala 385 390 395 400 Asp Gly Lys Pro Ala Val Lys Leu Ser Asp Asn Ile Gly Lys Asn Thr 405 410 415 Gly Asp Ala Asn Thr Val Glu Lys Val Lys Arg Glu Ile Gly Tyr Glu 420 425 430 Glu Lys Asp Trp Glu Gly Gly Asp Glu Thr Ser Arg Leu Asn Gly Asn 435 440 445 Arg Tyr Asp Arg Gly Ala His Ala Leu Met Asp Leu Ser Asp Pro Ala 450 455 460 Ala Thr Ser Arg Ser Arg Ser Val Val Tyr Phe Phe Lys Ser Gly Thr 465 470 475 480 Thr Leu Ser Glu Ile Pro Glu Ser Pro Pro Gly Arg Ser Gly Pro Met 485 490 495 Asn Ser Gln Arg Ser His Gly Gly Gly Ala Phe Asp Arg Glu Arg Asp 500 505 510 Pro Arg Glu Arg Asp Leu Asp Glu His Arg His Arg Pro Leu Thr Gln 515 520 525 Glu Glu Ala Ala Asn Arg Asp Arg Glu Arg Asp Ile Asp Arg Glu Arg 530 535 540 Glu Arg Glu His Ala Asp Arg Gln Gln Pro Arg Glu Ala Tyr Pro Pro 545 550 555 560 Gly Ala Pro Leu His Ser Thr Ala Gly Ser Ile Pro Ile His Gln Pro 565 570 575 Val Ala Ser Arg Ile Ala Gly Val Ile His Ser Pro Gly Gly Leu Leu 580 585 590 Gly Ala His Asn Gly Ala Pro Gly Gly Leu Pro Leu Gly Ala Pro Thr 595 600 605 Thr Gln Leu Ala Gly Phe Gly Gly Pro Ile His Ser Asp Pro Ala Arg 610 615 620 Gln Met Pro Pro Gln Pro Pro Asn Gln Asn Ser Thr Gly Gly Gln Gln 625 630 635 640 His Gln Met Phe Ala Pro Ile Pro Gln Gln Ala Gly Gly Pro Asn Gly 645 650 655 Ser Leu Gly Pro Gly Gly Ser Pro Gly Ser Val Phe Gly Gly Pro Leu 660 665 670 Gln Thr Glu Asn Gly Arg Ala Pro Val Gln Gln Ala Pro Pro Pro Ala 675 680 685 Val Val Pro Pro Ala Gln Thr Ser Ser Ala Ala Gly Leu Ser Gln Gln 690 695 700 Gly Ser Gln Pro Ile Leu Asn Asp Ala Leu Ser Tyr Leu Asp Gln Val 705 710 715 720 Lys Ala Gln Phe His Glu Gln Pro Asp Val Tyr Asn Arg Phe Leu Asp 725 730 735 Ile Met Lys Asp Phe Lys Ser Gln Thr Ile Asp Thr Pro Gly Val Ile 740 745 750 Asn Arg Val Ser Asp Leu Phe Ala Gly His Pro Asn Leu Ile Gln Gly 755 760 765 Phe Asn Thr Phe Leu Pro Pro Gly Tyr Arg Ile Glu Cys Gly Leu Asp 770 775 780 Asn Asn Pro Asn Ser Ile Arg Val Thr Thr Pro Ser Gly Ser Thr Val 785 790 795 800 His Ser Ile Gly Ala Gly Arg Gly Ala Leu Pro Pro Val Asp Gly Ser 805 810 815 Ala Gly Pro Pro Gly Gln Asn Ala Gln Tyr Leu Gly Pro Asn Ser Arg 820 825 830 Pro Gly Asn Trp Gln Gln Ser Val Gln His Ser Ile Glu Ser Pro Glu 835 840 845 Ala Gln Phe Ser Ala Pro Ala Gln Pro Gly Pro Gly Pro Phe Gly Pro 850 855 860 Val Gly Ala Pro Gly Ala Gln Phe Asp Gly His Ser Pro Ala His Gln 865 870 875 880 Gln Arg Val Val Ser Ser Gly Gln Gln Pro Ala Gly Pro Gly Ser Gly 885 890 895 Leu Val Ala Gly Pro Gly Ser Ala Met Pro Gly Pro Met Ala Arg Asn 900 905 910 Val Gln Thr Pro Thr Pro Gly Ala Gln Pro Ala Ser Leu Asn Gly Ser 915 920 925 Ser Ser Gln Gln Gly Gly Gln Arg Gly Pro Val Glu Phe Asn His Ala 930 935 940 Ile Ser Tyr Val Asn Lys Ile Lys Asn Arg Phe Gln Asp Lys Pro Glu 945 950 955 960 Ile Tyr Lys Gln Phe Leu Glu Ile Leu Gln Thr Tyr Gln Arg Glu Gln 965 970 975 Lys Pro Ile Gln Glu Val Tyr Ala Gln Val Thr Thr Leu Phe His Thr 980 985 990 Ala Pro Asp Leu Leu Glu Asp Phe Lys Gln Phe Leu Pro Glu Ser Ala 995 1000 1005 Ala Gln Thr Arg Thr Phe Gly Gln Arg Pro Ala Glu Asp Gly Gly 1010 1015 1020 Leu Leu Asn His Ile Asn Gln Met Pro Gln Ala Thr Asn Pro Ala 1025 1030 1035 Arg Glu Gly Pro Lys Met Pro Pro Val Gly Asn Phe Ala Val Pro 1040 1045 1050 Val Ser Ala Ser Lys Asp Asn Lys Lys Arg Pro Arg Ile Glu Lys 1055 1060 1065 Pro Pro Ala Ala Thr Pro Gln Ala Gln Gln Ser Pro Ala Val Gly 1070 1075 1080 Ser Ala Ser Ile Asn Ser Ala Asn Lys Arg Thr Lys Thr Thr His 1085 1090 1095 Lys Pro Ser Gly Asp Gly Pro Ser Ile Glu Pro Ser Leu Thr Pro 1100 1105 1110 Ile Val Pro Glu Pro Met Ser Pro Ser Ala Ser Thr Ser Val Ser 1115 1120 1125 Gln Glu Lys Ala Leu Asn Tyr Leu Glu Arg Ile Lys Lys His Ile 1130 1135 1140 Gly Asn Arg Thr Thr Leu His Glu Phe Phe Lys Leu Ile Asn Leu 1145 1150 1155 Tyr Thr Gln Gly Leu Ile Asp Lys Asn Val Leu Val Gln Lys Ala 1160 1165 1170 Gln Met Ile Ile Gly Ala Asn Val Glu Leu Met Thr Trp Phe Lys 1175 1180 1185 Asn Phe Val Arg Tyr Thr Gly Asp Asp Glu Leu Val Glu Asn Lys 1190 1195 1200 Pro Glu Pro Pro Thr Gly Arg Val Ser Leu Ser Asn Cys Arg Gly 1205 1210 1215 Tyr Gly Pro Ser Tyr Arg Leu Leu Arg Lys Arg Glu Arg Leu Lys 1220 1225 1230 Pro Cys Ser Gly Arg Asp Glu Leu Cys Asn Ser Val Leu Asn Asp 1235 1240 1245 Glu Trp Ala Ser His Pro Thr Trp Ala Ser Glu Asp Ser Gly Phe 1250 1255 1260 Val Ala His Arg Lys Asn Ala Phe Glu Glu Gly Leu His Arg Ile 1265 1270 1275 Glu Glu Glu Arg His Asp Tyr Asp Phe Phe Ile Glu Ala Asn Gln 1280 1285 1290 Lys Cys Ile Gln Leu Leu Glu Pro Ile Ala Gln Gln Met Leu Thr 1295 1300 1305 Leu Asn Pro Ala Asp Arg Gln Asn Phe Arg Met Pro Ser Gly Leu 1310 1315 1320 Gly Gly Gln Ser Thr Ser Ile Tyr Lys Arg Val Leu Lys Lys Val 1325 1330 1335 Tyr Gly Ala Asp Lys Gly Ala Glu Val Val Asn Asp Met Phe Gln 1340 1345 1350 His Pro Phe Thr Val Val Pro Ile Val Met Ala Arg Leu Lys Gln 1355 1360 1365 Lys Asp Glu Glu Trp Arg Phe Ser Gln Arg Glu Trp Glu Lys Val 1370 1375 1380 Trp Gln Ser Gln Thr Lys Ala Met His Leu Lys Ser Leu Asp His 1385 1390 1395 Gln Gly Ile Gln Val Lys Gly Asn Asp Lys Arg Thr Leu Ser Ala 1400 1405 1410 Lys His Leu Val Asp Leu Ile Lys Thr Lys His Glu Glu Gln Lys 1415 1420 1425 Arg Gln Arg Val Asn Lys Gly Lys Ala Pro Arg Val Gln His Leu 1430 1435 1440 Trp Ser Phe Thr Asp Gln Gly Val Leu Leu Asp Leu Leu Arg Phe 1445 1450 1455 Met Val Leu Tyr Ala Met Asn Ser Gly Gln His Gly Ser Ser Glu 1460 1465 1470 Lys Asp Arg Ile Leu Glu Phe Phe Glu Asn Ser Val Pro Gln Phe 1475 1480 1485 Phe Gly Ile Leu Pro Glu Gln Val Arg Gln His Leu Gly Asp Ile 1490 1495 1500 Asp Arg Asp Ala Gly Glu Glu Glu Ala Asp Asp Asn Thr Pro Ala 1505 1510 1515 Glu Leu Thr Asn Gly Arg Ser Arg Arg Asn Gly Lys Lys Ser Asp 1520 1525 1530 Leu Leu Arg Gly Leu Leu Asp Pro Gly Arg Asn Gly Ser Lys Thr 1535 1540 1545 Arg Ser Gln Pro Glu Glu Ser Asn Thr Ser Ala Ser Lys Glu Thr 1550 1555 1560 Thr Pro Asp Gln Gly Ser Thr Asn Glu Glu Glu Met Ala Asp Ala 1565 1570 1575 Pro Asp Asp Gly Ser Ala Thr Ala Glu Asn Ala Asn Asn Glu Arg 1580 1585 1590 Trp Leu Gln Asn Pro Pro Lys Ala Thr Val Leu Ser Gly Tyr Asn 1595 1600 1605 Pro Leu Ser Asp Gly Asp Ser Glu Leu Lys Ala Asp Gly Leu Phe 1610 1615 1620 Pro Arg Pro Trp Tyr Asn Phe Phe Cys Asn Gln Thr Ile Phe Val 1625 1630 1635 Phe Phe Ser Val Phe Gln Thr Leu Tyr Lys Arg Leu Lys Thr Val 1640 1645 1650 Lys Glu Ser Arg Glu Ser Val Leu Glu Glu Ile Arg Arg Glu Arg 1655 1660 1665 Ala Asp Lys Pro Ala Lys Gln Leu Gly Leu Val His Asp Glu Met 1670 1675 1680 Asn Tyr Phe Asp Gly Asp Pro Glu Thr Phe Trp Pro Arg Thr Val 1685 1690 1695 Glu Leu Ile Glu Asp Phe Ile Thr Gly Glu Ile Asp Glu Ser Arg 1700 1705 1710 Cys Gln Asp Val Leu Arg His Tyr Tyr Leu Gln Cys

Gly Trp Thr 1715 1720 1725 Leu Tyr Thr Ile Gln Asp Leu Leu Lys Thr Leu Cys Arg Gln Ala 1730 1735 1740 Leu Val Cys Asn Asn Ser Asp Asn Lys Glu Lys Thr Pro Asp Leu 1745 1750 1755 Val Gln Gln Phe Leu Thr Ala Lys Ser Gln Glu Glu Thr Ser Tyr 1760 1765 1770 Gln Val Glu Ile Ser Ala Arg Lys Phe Ala Glu Lys Cys Ile Lys 1775 1780 1785 Asp Gly Glu Met Phe Met Ile Thr Trp Ala Pro Ser Ser Asn Glu 1790 1795 1800 Ala Thr Val Arg Trp Leu Pro Lys Glu Asp Thr Thr Phe His Ala 1805 1810 1815 Glu Glu Met Glu Pro Thr Asp Arg Trp Lys Tyr Tyr Ile Ala Ser 1820 1825 1830 Tyr Met Arg Val Asp Pro Thr Glu Gly Val Pro Lys Leu Arg Leu 1835 1840 1845 Gln Lys Thr Val Leu Ala Arg Asn Leu Pro Ser Ser Asp Ser Asp 1850 1855 1860 Ser Asp Asp Gly Ala Val Pro Lys Pro Leu Ser Tyr Ser Glu Gly 1865 1870 1875 Leu Gly Leu Arg Ile Cys Val Asn Ser Ser Lys Ile Val Tyr Glu 1880 1885 1890 Lys Glu Thr Ser Glu Tyr Thr Ile Tyr Asn Met Thr Ser Leu Ser 1895 1900 1905 Glu Glu Arg Arg Ala Phe Asp Arg Asp Arg Arg Ala Gln Leu Phe 1910 1915 1920 Arg Glu Lys Leu Ile Met Asn Asn Ala Trp Met Lys Asp Leu Ser 1925 1930 1935 Gln Val Glu Val Gln Gly Met Asn Glu Asp Phe Gln Arg Trp Ala 1940 1945 1950 Lys Asp Gly Ile Val Pro Gly Thr Ser Ser Thr Gly Gly Ala Gly 1955 1960 1965 Ser Ser Ala 1970 63453PRTCryptococcus neoformans 63Met Pro Asp Lys Leu His Leu Pro Ile Asp Asp Val Gln Ile Pro Phe 1 5 10 15 Ser Ile Leu Asp Thr Asp Leu Tyr Lys Leu Thr Met Gln Asn Ala Val 20 25 30 Leu His His Phe Ser Asp Ala His Val Val Ile Lys Phe Thr Asn Arg 35 40 45 Ser Pro Gln Met Leu Phe Ser Lys Glu Cys Phe Asp Trp Val Gln Gln 50 55 60 Arg Val Asn Asp Leu Ser Lys Leu Lys Leu Thr Ser Glu Glu Arg Lys 65 70 75 80 Glu Leu Ser Lys Ala Cys Pro Tyr Phe Ser Glu Ser Tyr Leu Asp Tyr 85 90 95 Leu Ser Asn Met Gln Leu Asp Pro Val Lys Gln Val Lys Leu Thr Phe 100 105 110 Ile Pro Gln Gly Ser Asn Glu Lys Gly Glu Lys Met Gly Glu Ile Gly 115 120 125 Cys Val Ile Glu Gly Pro Trp Lys Asp Thr Met Leu Tyr Glu Val Pro 130 135 140 Val Met Ala Ile Leu Ser Glu Gly Tyr Phe Lys Phe Val Asp Thr Asp 145 150 155 160 Trp Asp Tyr Asp Gly Gln Phe Glu Leu Ala Lys Lys Lys Ala Leu Asp 165 170 175 Leu Leu Asn Pro Pro Ala Pro Thr Thr Ser Leu Ser Phe Ser Glu Phe 180 185 190 Gly Thr Arg Arg Arg Arg Ser Phe Lys Ala Gln Asp Ile Ile Met Arg 195 200 205 Gly Leu Ile Ala Gly His Glu Glu Tyr Lys Ser Lys Gly Gly Ser Gln 210 215 220 Gly Ile Leu Ser Gly Thr Ser Asn Val Tyr Leu Ala Leu Lys Tyr Gly 225 230 235 240 Leu Asn Pro Val Gly Thr Ile Ala His Glu Trp Ile Met Ala Val Gly 245 250 255 Ala Thr Tyr Gly Tyr Arg Gly Ala Asn Gly Arg Ala Met Asp Met Trp 260 265 270 Glu Glu Val Tyr Pro Pro Gly Thr Lys Phe Ser Ser Pro Leu Thr Met 275 280 285 Leu Thr Asp Thr Tyr Thr Ala Ala Ile Phe Phe Lys Asp Phe Ile Ser 290 295 300 Asp Pro Ala Arg Ala Leu Arg Trp Ala Val Leu Arg Gln Asp Ser Gly 305 310 315 320 Asp Ala Phe Lys Phe Val Glu Asp Ala Lys Glu Ala Trp Arg Thr Ile 325 330 335 Glu Asp Lys Ala Gly Ile Lys Arg Asp Val Gly Pro Asn Gly Glu Glu 340 345 350 Glu Val Ala Lys Gly Lys Lys Val Ile Phe Ser Asp Gly Leu Asp Val 355 360 365 Glu Lys Ala Ile Lys Leu Gln Gln Gly Cys Asp Lys Ala Gly Met Ala 370 375 380 Ala Ser Phe Gly Ile Gly Thr Asp Leu Thr Asn Asp Phe Arg Lys Ala 385 390 395 400 Ser Asp Pro Ser Gln Lys Ser Lys Ala Leu Asn Met Val Ile Lys Leu 405 410 415 Asn Lys Ile Asn Gly Lys Asp Cys Ile Lys Leu Ser Asp Asp Lys Gly 420 425 430 Lys His Thr Gly Ser Leu Glu Glu Val Arg Lys Ala Gln Gln Glu Leu 435 440 445 Gly Ile Asp Lys Asn 450 64718PRTCryptococcus neoformans 64Met Glu Glu Pro Ser Ser Pro Arg Lys Pro Ser Pro Ser Ser Pro Pro 1 5 10 15 Ser Ser Ser Ser Ser Pro Ala Gly Ser Leu Asp Leu Pro Ser Leu Gln 20 25 30 Pro Leu Ser His Asp His Pro Leu Leu Thr Ala Pro Thr Phe Asp Pro 35 40 45 Asp Ala Phe Leu Leu Ser Arg Ile His Ile Pro Leu Glu Glu Leu Arg 50 55 60 Gly Glu Leu Arg Glu Tyr Leu Gly Glu Leu Arg Glu Glu Leu Val Lys 65 70 75 80 Leu Ile Asn Glu Asp Tyr Glu Glu Phe Leu Ser Leu Gly Ile Gly Leu 85 90 95 Arg Gly Glu Glu Glu Arg Leu Lys Arg Leu Glu Gly Pro Leu Gln Gly 100 105 110 Val Arg Lys Glu Ile Val Ser Val Arg Asp Val Leu Ala Glu His Gln 115 120 125 Ala Lys Leu Gln Glu Lys Leu Asp Glu Arg Ala Ala Leu Arg Glu Glu 130 135 140 Lys Ala Leu Leu Asp Leu Leu Gln Arg Leu Phe Asp Thr Leu Ala Lys 145 150 155 160 Ala Glu Ala Leu Leu Asp Leu Pro His Thr Asp Glu Leu Glu Thr Ser 165 170 175 Lys Leu Val Thr Arg Val Ala Gly Glu Tyr Ser Gln Ile Val Tyr Leu 180 185 190 Met Asn Lys Ala Arg Thr Glu Glu Cys Ala Ile Val Asn Val Val Glu 195 200 205 Glu Arg Ile Lys Asn Ile Lys Ser Arg Leu Ser Lys Asp Leu Ser Thr 210 215 220 Val Leu Leu Ser Glu Leu Glu Asn Leu Asn Ala Thr Gly Leu Lys Gln 225 230 235 240 Cys Leu Lys Thr Tyr Glu Leu Ile Glu Gly Trp Glu Glu Ala Glu Glu 245 250 255 Val Val Arg Lys Val Phe Arg Glu Tyr Cys Arg Asn Thr Ile Ser Ser 260 265 270 Ser Ala Leu Ser Leu Pro Thr Ser Pro Thr Ala Pro Gln Thr Pro His 275 280 285 Gln Leu Arg Asn Pro Leu Asp Val Pro Arg Leu Pro Ala Ser Tyr Asn 290 295 300 Thr Pro Leu Ala Leu Leu Phe Asn Arg Val Leu Ala Gln Val Ala Ser 305 310 315 320 Tyr Gln Pro Leu Leu Asp Ala Ser Lys Glu Val Ser Glu Lys Phe Asp 325 330 335 Phe Phe Ala Arg Val Phe Trp Pro Glu Ile Gly Asp Thr Ile Ile Glu 340 345 350 Arg Leu Gly Ser Val Ile Phe Ala Ala Gly Arg Pro Asp Asp Leu His 355 360 365 Lys Tyr Tyr Thr Thr Ser His Lys Phe Leu Asp Leu Leu Glu Thr Ile 370 375 380 Ala Pro Ser Ala His Asn Val Leu Ala Met Arg Ser Ser Pro Ser Tyr 385 390 395 400 Thr Ala Phe Glu Arg Arg Trp Gln Leu Pro Val Tyr Phe Gln Leu Arg 405 410 415 Trp Lys Glu Ile Val Ser Ser Leu Glu Gln Ser Leu Ala Gly Gln Pro 420 425 430 Ser Tyr Thr Ser Thr Ser Asp His Lys Gly Ser Lys Trp Val Leu Val 435 440 445 Gln Ser Gly Ala Val Trp Lys Ala Leu Glu Ser Cys Trp Lys Glu Asp 450 455 460 Val Tyr Ile Ser Glu Leu Ala Pro Arg Phe Trp Arg Leu Ser Leu Gln 465 470 475 480 Ile Ser Ser Arg Tyr Gly Thr Tyr Leu Lys Ser Thr Val Asp Ser Tyr 485 490 495 Val Ile Thr Glu Glu Asp Asn Ser Gln Glu Asp Ala Ala Leu Arg Phe 500 505 510 Ala Ser Ala Ala Val Val Asp Leu Glu Asn Leu Ala Ala Lys Val Lys 515 520 525 Asp Leu Asp Val Val Lys Glu Leu Asn Leu Gly Glu His Leu Thr Leu 530 535 540 Pro Thr Thr Gln Tyr Thr Ser Lys Ile Leu Ser Ile Leu Thr Arg Arg 545 550 555 560 Cys Thr Asp Pro Leu Lys Leu Ile Arg Ser Ile Ala Ser Gln Phe Arg 565 570 575 Ser Ser Pro Thr Pro Ser Thr Pro Ser Ser Thr Arg Gln Pro Ser Tyr 580 585 590 Phe Val Pro Ser Val Phe Lys Pro Leu His Ser Leu Leu Ser Ser Gln 595 600 605 Pro Gln Leu Lys Glu Arg Tyr Gln Gln Asp Phe Ser Arg Gln Ile Ala 610 615 620 Asp Ala Val Phe Val Asn Tyr Ala Ser Thr Leu Ala Ser Val Lys Lys 625 630 635 640 Thr Glu Asp Leu Leu Arg Lys His Arg Lys Ser Lys Lys Ser Gly Ile 645 650 655 Thr Ser Phe Phe Gly Gly Gly Gly His Asp Gly Gly Ser Gly Glu Lys 660 665 670 Glu Glu Glu Arg Phe Thr Asn Gln Met Lys Val Asp Ile Asp Ala Leu 675 680 685 Lys Glu Asp Ala Lys Gly Leu Gly Val Asp Pro Glu Ser Met Asn Ser 690 695 700 Trp Asn Glu Leu Leu Ala Val Val Asn Lys Pro Asp Glu Ala 705 710 715 65612PRTUstilago maydis 65Met Cys Ala Ala Pro Ser Thr Ser Ala Pro Val Ala Lys His Ala Ser 1 5 10 15 Asp Ala Ser Pro Ile Arg Ser Ile Leu Asp Thr Asp Leu Tyr Lys Leu 20 25 30 Thr Met Gln Gln Ala Val Leu Arg His Tyr Pro His Thr Arg Val Ala 35 40 45 Tyr Lys Phe Thr Asn Arg Ser Ala Ala Thr Met Lys Phe Thr Arg Gln 50 55 60 Ala Met Asp Arg Ile Arg Asn His Ile Asp Asn Leu Val His Leu Ser 65 70 75 80 Leu Ser Ala Gln Glu Arg Ala Trp Leu Glu Arg Ser Cys Pro Tyr Leu 85 90 95 Gly Lys Asp Tyr Leu Asp Tyr Leu Glu Ala Phe Arg Phe Gln Pro Lys 100 105 110 Gln Gln Val Gln Leu Arg Phe Leu Pro Thr Gly Glu Asp Gly Trp Gly 115 120 125 His Leu Asp Leu Asn Val Ser Gly Val Trp Ser Asp Val Ile Phe Tyr 130 135 140 Glu Val Pro Leu Met Ala Ile Val Ser Glu Val Tyr Phe Ser Thr Ile 145 150 155 160 Asp Thr Asp Trp Ser Leu Gln Asp Gln Tyr Gln Gln Ala Phe Asp Lys 165 170 175 Ala Cys Arg Leu Thr Ser Asn Gly Ile Arg Tyr Ser Glu Phe Gly Thr 180 185 190 Arg Arg Arg Arg Ser Tyr Gln Thr His Arg Ile Val Leu Gln Gly Leu 195 200 205 Met Ala Gly Asp Leu Ser Ala Ser Ser Gly Cys Ser Ser Gly Lys Leu 210 215 220 Leu Gly Thr Ser Asn Val His Phe Ala Gln Gln Phe Asp Leu Val Pro 225 230 235 240 Ile Gly Thr Val Ala His Glu Trp Thr Met Ala Ile Ala Ala Leu Gln 245 250 255 Gly Tyr Ala His Ser Asn Leu Lys Ala Leu Gln Leu Trp Asp Ala Val 260 265 270 Tyr Ser Ala Pro Asp Phe Val Ala Asn Ser Ala Thr His Asp Leu Thr 275 280 285 Ile Ala Leu Thr Asp Thr Phe Ser Thr Asn Val Phe Trp Asn Asp Leu 290 295 300 Leu Asp Asn Pro Ser Gly Ile Glu Ile Ala Arg Arg Trp Arg Gly Leu 305 310 315 320 Arg Gln Asp Ser Gly Asp Ser Lys Ala Phe Ala Gln Lys Ala Leu Asp 325 330 335 Ala Tyr Arg Ser Ile Gly Val Asp Pro Lys Ser Lys Val Val Ile Tyr 340 345 350 Ser Asp Gly Leu Asp Val Asp Arg Cys Leu Glu Leu Ala Ala Tyr Ser 355 360 365 Asn His Ile Gly Ile Gly Ala Ala Phe Gly Ile Gly Thr Ser Phe Thr 370 375 380 Asn Asp Phe Ile Gln Leu Ser Thr Ala Gln Lys Ser Lys Pro Leu Asn 385 390 395 400 Ile Val Ile Lys Leu Asp Ser Val Glu His Arg Arg Val Val Lys Ile 405 410 415 Ser Asp Asp Leu Thr Lys Asn Thr Gly Asp Pro Thr Glu Val Leu Ala 420 425 430 Val Lys Arg Arg Phe Gly Ile Pro Thr Pro Ser Ser Ala Thr Pro Ala 435 440 445 Asp Ala Ser Val Ile Asn His Leu Asp Pro Gly Ala Pro Pro Asn Pro 450 455 460 Ser Ser His Ala His Leu Gly Thr Asp Asp Ala Thr Met Thr Gln Val 465 470 475 480 Ser Pro Leu Asp Gln Arg Asn Val Ala Ala Gly Val Glu Leu Thr Pro 485 490 495 Pro Asn Glu Pro Arg Arg Leu Leu Ser Ala Arg Ser Thr Ser Lys Leu 500 505 510 Ser Ser Pro Lys Asn Val Ala Ser Ser Cys Ala Trp Ser Asn Cys Ala 515 520 525 Leu Ala Ser Lys Leu Val Ser Ser Ile Pro Ala Ala Leu Ile Ala Gly 530 535 540 Val Ile Glu Arg Ala Arg Glu Gly Asp Cys Asp Cys Glu Pro Asp Ala 545 550 555 560 Pro Arg Glu Met Cys Leu Ala Leu Asn Ala Ala Asn Gly Asp Asp Ala 565 570 575 Gly Ala Thr Ala Pro Ile Ala Gly Leu Asn Ser Glu Ile Gly Val Pro 580 585 590 Gly Val Pro Gly Val Pro Gly Glu Pro Ile Arg Leu Leu Leu Cys Ala 595 600 605 Asn Pro Leu Leu 610 66395PRTSaccharomyces cereviseae 66Met Asp Pro Thr Lys Ala Pro Asp Phe Lys Pro Pro Gln Pro Asn Glu 1 5 10 15 Glu Leu Gln Pro Pro Pro Asp Pro Thr His Thr Ile Pro Lys Ser Gly 20 25 30 Pro Ile Val Pro Tyr Val Leu Ala Asp Tyr Asn Ser Ser Ile Asp Ala 35 40 45 Pro Phe Asn Leu Asp Ile Tyr Lys Thr Leu Ser Ser Arg Lys Lys Asn 50 55 60 Ala Asn Ser Ser Asn Arg Met Asp His Ile Pro Leu Asn Thr Ser Asp 65 70 75 80 Phe Gln Pro Leu Ser Arg Asp Val Ser Ser Glu Glu Glu Ser Glu Gly 85 90 95 Gln Ser Asn Gly Ile Asp Ala Thr Leu Gln Asp Val Thr Met Thr Gly 100 105 110 Asn Leu Gly Val Leu Lys Ser Gln Ile Ala Asp Leu Glu Glu Val Pro 115 120 125 His Thr Ile Val Arg Gln Ala Arg Thr Ile Glu Asp Tyr Glu Phe Pro 130 135 140 Val His Arg Leu Thr Lys Lys Leu Gln Asp Pro Glu Lys Leu Pro Leu 145 150 155 160 Ile Ile Val Ala Cys Gly Ser Phe Ser Pro Ile Thr Tyr Leu His Leu 165 170 175 Arg Met Phe Glu Met Ala Leu Asp Asp Ile Asn Glu Gln Thr Arg Phe 180 185 190 Glu Val Val Gly Gly Tyr Phe Ser Pro Val Ser Asp Asn Tyr Gln Lys 195 200 205 Arg Gly Leu Ala Pro Ala Tyr His Arg Val Arg Met Cys Glu Leu Ala 210 215 220 Cys Glu Arg Thr Ser Ser Trp Leu Met Val Asp Ala Trp Glu Ser Leu 225 230 235

240 Gln Ser Ser Tyr Thr Arg Thr Ala Lys Val Leu Asp His Phe Asn His 245 250 255 Glu Ile Asn Ile Lys Arg Gly Gly Ile Met Thr Val Asp Gly Glu Lys 260 265 270 Met Gly Val Lys Ile Met Leu Leu Ala Gly Gly Asp Leu Ile Glu Ser 275 280 285 Met Gly Glu Pro His Val Trp Ala Asp Ser Asp Leu His His Ile Leu 290 295 300 Gly Asn Tyr Gly Cys Leu Ile Val Glu Arg Thr Gly Ser Asp Val Arg 305 310 315 320 Ser Phe Leu Leu Ser His Asp Ile Met Tyr Glu His Arg Arg Asn Ile 325 330 335 Leu Ile Ile Lys Gln Leu Ile Tyr Asn Asp Ile Ser Ser Thr Lys Val 340 345 350 Arg Leu Phe Ile Arg Arg Gly Met Ser Val Gln Tyr Leu Leu Pro Asn 355 360 365 Ser Val Ile Arg Tyr Ile Gln Glu Tyr Asn Leu Tyr Ile Asn Gln Ser 370 375 380 Glu Pro Val Lys Gln Val Leu Asp Ser Lys Glu 385 390 395

Claims

1. A method for obtaining a plant with increased stress resistance comprising a. introducing a chimeric gene into a cells of a plant to obtain transgenic cells, said chimeric gene comprising the following operably linked DNA fragments: i. A plant-expressible promoter; ii. A DNA region coding for a plant-functional enzyme of the nicotinamide adenine dinucleotide salvage synthesis pathway selected from nicotinamidase, nicotinate phosphoribosyltransferase, nicotinic acid mononucleotide adenyl transferase or nicotinamide adenine dinucleotide synthetase; iii. A 3'end region involved in transcription termination and polyadenylation; b. regenerating said transgenic cells to obtain a population of transgenic plants; and selecting a plant from said population of transgenic plants which exhibits increased stress resistance or selecting a plant which exhibits a reduced level of reactive oxygen species or maintains a high level of NADH under stress conditions when compared to a similar non-transgenic plant characterized in that that the amino acid sequence encoded by the DNA region comprises the amino acid sequence of any one of SEQ ID Nos. 1 to 29, 31 to 47 or 49 to 66 or an amino acid sequence having at least 90% sequence identity to said amino acid sequences of any one of SEQ ID Nos. 1 to 29, 31 to 47 or 49 to 66.

2. A chimeric gene as described in claim 1.

3. A plant cell comprising a chimeric gene as described in claim 3.

4. A plant comprising a chimeric gene as described in claim 2.

5. The plant according to claim 4, further characterized in that it has a lower level of reactive oxygen species under stress conditions than a similar plant not comprising such a chimeric gene.

6. A seed of a plant according to claim 4 or 5 comprising a chimeric gene according to claim 2.

7. Use of a chimeric gene according to claim 2 to increase the stress resistance of a plant.

8. Use of a chimeric gene according to claim 2 to decrease the level of reactive oxygen species in a plant or a plant cell under stress conditions or to maintain the level of NAD in a plant or plant cell under stress conditions.

9. Use of a DNA sequence encoding a plant functional enzyme of the nicotinamide adenine dinucleotide salvage synthesis pathway selected from nicotinamidase, nicotinate phosphoribosyltransferase, nicotinic acid mononucleotide adenyl transferase or nicotinamide adenine dinucleotide synthetase to increase the stress resistance of a plant characterized in that said plant functional enzyme is derived from a fungal or yeast-like organism different than Saccharomyces cereviseae.

10. Use of a DNA sequence encoding a plant functional enzyme of the nicotinamide adenine dinucleotide salvage synthesis pathway selected from nicotinamidase, nicotinate phosphoribosyltransferase, nicotinic acid mononucleotide adenyl transferase or nicotinamide adenine dinucleotide synthetase to decrease the level of reactive oxygen species in a plant or a plant cell under stress conditions or to maintain the level of NAD in a plant or plant cell under stress conditions characterized in that said plant functional enzyme is derived from a fungal or yeast-like organism different than Saccharomyces cereviseae.