DETERGENT COMPOSITION

Abstract

A surfactant containing detergent composition, preferably a manual dishwashing detergent composition, comprising either a combination of one or more hydroperoxy fatty acid producing enzymes and one or more hydroperoxy fatty acid converting enzymes, or at least one fatty acid processing fusion enzyme comprising at least two catalytic domains: a hydroperoxy fatty acid producing domain and a hydroperoxy fatty acid converting, and methods of using such compositions.

Description

REFERENCE TO A SEQUENCE LISTING

[0001] This application contains a Sequence Listing in computer readable form. The computer readable form is incorporated herein by reference.

FIELD OF THE INVENTION

[0002] The present invention relates to enzyme-containing detergent compositions which provide one or more benefits, including good cleaning particularly good grease emulsification, and long lasting suds especially in the presence of greasy soils.

BACKGROUND OF THE INVENTION

[0003] Detergent compositions should have a good suds profile in particular a long lasting suds profile especially in the presence of greasy soils while providing good soil and/or grease cleaning. Users usually see suds as an indicator of the performance of the detergent composition. Moreover, the user of a detergent composition may also use the suds profile and the appearance of the suds (e.g., density, whiteness) as an indicator that the wash solution still contains active detergent ingredients. This is particularly the case for manual washing, also referred to herein as hand-washing, where the user usually doses the detergent composition depending on the suds remaining and renews the wash solution when the suds subsides or when the suds does not look thick enough. Thus, a detergent composition, particularly a manual wash detergent composition that generates little or low density suds would tend to be replaced by the user more frequently than is necessary. Accordingly, it is desirable for a detergent composition to provide "good sudsing profile", which includes good suds height and/or density as well as good suds duration during the initial mixing of the detergent with water and/or during the entire washing operation.

[0004] The need also exists for an improved detergent composition, when used in a manual-washing process, the composition preferably also provides a pleasant washing experience, i.e, good feel on the user's hands during the wash. Preferably detergent compositions are also easy to rinse. Further it is desirous that the improved detergent composition is stable and will not phase separate, resulting in greater shelf-life of the product. Preferably in addition, the composition provides a good finish to the washed items. There is also the desire to reduce the amount of surfactants without negatively impacting sudsing nor grease cleaning and emulsification profile. Thus, there is the need to find new compositions that improve cleaning and suds longevity in hand washing conditions.

[0005] It has been found that some types of soil, in particular greasy soils comprising fatty acids, act as a suds suppressor, triggering consumers to replace the product more frequently than is necessary. As such there is a need to provide detergent compositions with desirable suds properties, especially in the presence of greasy soils, even more in the presence of greasy soils comprising fatty acids, and that at the same time provide good soil and grease removal.

[0006] US 2017/321161 A1 relates to the use of a detergent composition comprising a fatty acid-transforming enzyme to impart suds longevity in a washing process, as well as a method for promoting suds longevity in a washing process for washing soiled articles, comprising the step of: delivering a composition comprising a fatty acid-transforming enzyme to a volume of water to form a wash liquor and immersing the soiled article in the liquor. US 2003/166485 A1 relates to catalytically bleaching substrates, especially laundry fabrics, with a bleaching catalyst in the presence of an enzymatic bleach enhancing system. "Water Soluble Film Flakes Incorporating Functional Ingredients", IP.COM JOURNAL, IP.COM INC., WEST HENRIETTA, N.Y., US, 2 Jan. 2014, relates generally to water-soluble compositions useful for delivering functional ingredients, including enzymes. More particularly, the disclosure relates to particularly defined water soluble film flakes containing one or more functional ingredients, and related compositions containing such flakes, wherein the related compositions can be powders, liquids, or gels, for example, and wherein the combinations may be used, for example, as detergents.

SUMMARY OF THE INVENTION

[0007] The present invention, as described in claim 1 or in claim 9, provides a detergent composition with desirable suds properties, even in the presence of greasy soils comprising fatty acids, while at the same time providing good soil and grease removal.

[0008] The detergent composition is particularly suited for manually washing soiled articles, preferably dishware, using the method described in claim 10 or in claim 20. When the composition of the invention is used according to this method a good sudsing profile, with a long lasting effect is achieved.

[0009] The elements of the composition of the invention described in relation to the first aspect of the invention apply mutatis mutandis to the other aspects of the invention.

DETAILED DESCRIPTION OF THE INVENTION

Definitions

[0010] As used herein, the articles "a" and "an" when used in a claim, are understood to mean one or more of what is claimed or described.

[0011] As used herein, the term "substantially free of" or "substantially free from" means that the indicated material is present in an amount of no more than about 5 wt %, preferably no more than about 2%, and more preferably no more than about 1 wt % by weight of the composition.

[0012] As used therein, the term "essentially free of" or "essentially free from" means that the indicated material is present in an amount of no more than about 0.1 wt % by weight of the composition, or preferably not present at an analytically detectible level in such composition. It may include compositions in which the indicated material is present only as an impurity of one or more of the materials deliberately added to such compositions.

[0013] As used herein, the term "detergent composition" refers to a composition or formulation designed for cleaning soiled surfaces. Such compositions include but are not limited to, dishwashing compositions, laundry detergent compositions, fabric softening compositions, fabric enhancing compositions, fabric freshening compositions, laundry pre-wash, laundry pretreat, laundry additives, spray products, dry cleaning agent or composition, laundry rinse additive, wash additive, post-rinse fabric treatment, ironing aid, hard surface cleaning compositions, unit dose formulation, delayed delivery formulation, detergent contained on or in a porous substrate or nonwoven sheet, and other suitable forms that may be apparent to one skilled in the art in view of the teachings herein. Such compositions may be used as a pre-cleaning treatment, a post-cleaning treatment, or may be added during the rinse or wash cycle of the cleaning process. The detergent compositions may have a form selected from liquid, powder, single-phase or multi-phase unit dose or pouch form, tablet, gel, paste, bar, or flake. Preferably the composition is for manual-washing. Preferably, the detergent composition of the present invention is a dishwashing detergent. Preferably the composition is in the form of a liquid.

[0014] As used herein the term "fragment" means an amino acid sequence of at least 30, 60, 100, 150 contiguous amino acids of the reference sequences or any integer there between.

[0015] As used herein the term "identity" means the identity between two or more sequences and is expressed in terms of the identity or similarity between the sequences as calculated over the entire length of a sequence aligned against the entire length of the reference sequence. Sequence identity can be measured in terms of percentage identity; the higher the percentage, the more identical the sequences are. The percentage identity is calculated over the length of comparison. For example, the identity is typically calculated over the entire length of a sequence aligned against the entire length of the reference sequence. Methods of alignment of sequences for comparison are well known in the art and identity can be calculated by many known methods. Various programs and alignment algorithms are described in the art. It should be noted that the terms `sequence identity` and `sequence similarity` can be used interchangeably.

[0016] Identity, or homology, percentages as mentioned herein in respect of the present invention are those that can be calculated with the GAP program, obtainable from GCG (Genetics Computer Group Inc., Madison, Wis., USA). Alternatively, a manual alignment can be performed.

[0017] For enzyme sequence comparison the following settings can be used: Alignment algorithm: Needleman and Wunsch, J. Mol. Biol. 1970, 48: 443-453. As a comparison matrix for amino acid similarity the Blosum62 matrix is used (Henikoff S. and Henikoff J. G., P.N.A.S. USA 1992, 89: 10915-10919). The following gap scoring parameters are used: Gap penalty: 12, gap length penalty: 2, no penalty for end gaps.

[0018] As used herein the term "increased suds longevity" means an increase in the duration of visible suds in a washing process cleaning soiled articles using the composition comprising either one or more hydroperoxy fatty acid producing enzymes, and one or more hydroperoxy fatty acid converting enzymes, and/or comprising a fatty acid processing fusion enzyme, compared with the suds longevity provided by the same composition and process in the absence of the hydroperoxy fatty acid producing enzymes, the hydroperoxy fatty acid converting, or the fatty acid processing fusion enzymes.

[0019] As used herein, the term "soiled surfaces" refers non-specifically to any type of flexible material consisting of a network of natural or artificial fibers, including natural, artificial, and synthetic fibers, such as, but not limited to, cotton, linen, wool, polyester, nylon, silk, acrylic, and the like, as well as various blends and combinations. Soiled surfaces may further refer to any type of hard surface, including natural, artificial, or synthetic surfaces, such as, but not limited to, tile, granite, grout, glass, composite, vinyl, hardwood, metal, cooking surfaces, plastic, and the like, as well as blends and combinations, as well as dishware. Key targeted soiled surfaces by this application are soiled dishware.

[0020] As used herein, the term "variant" of hydroperoxy fatty acid producing enzyme or hydroperoxy fatty acid converting enzyme or variant of a fatty acid processing fusion enzyme means an amino acid sequence when the hydroperoxy fatty acid producing enzyme or hydroperoxy fatty acid converting enzyme or fatty acid processing fusion enzyme is modified by, or at, one or more amino acids (for example 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 or more amino acid modifications) selected from substitutions, insertions, deletions and combinations thereof. The variant may have "conservative" substitutions, wherein a substituted amino acid has similar structural or chemical properties to the amino acid that replaces it, for example, replacement of leucine with isoleucine. A variant may have "non-conservative" changes, for example, replacement of a glycine with a tryptophan. Variants may also include sequences with amino acid deletions or insertions, or both. Guidance in determining which amino acid residues may be substituted, inserted, or deleted without abolishing the activity of the protein may be found using computer programs well known in the art. Variants may also include truncated forms derived from a wild-type hydroperoxy fatty acid producing enzyme or hydroperoxy fatty acid converting or fatty acid processing fusion enzymes, such as for example, a protein with a truncated N-terminus. Variants may also include forms derived by adding an extra amino acid sequence to a wild-type protein, such as for example, an N-terminal tag, a C-terminal tag or an insertion in the middle of the protein sequence.

[0021] As used herein, the term "water hardness" or "hardness" means uncomplexed cation ions (i.e., Ca.sup.2+ or Mg.sup.2+) present in water that have the potential to precipitate with anionic surfactants or any other anionically charged detergent actives under alkaline conditions, and thereby diminishing the surfactancy and cleaning capacity of surfactants. Further, the terms "high water hardness" and "elevated water hardness" can be used interchangeably and are relative terms for the purposes of the present invention, and are intended to include, but not limited to, a hardness level containing at least 12 grams of calcium ion per gallon water (gpg, "American grain hardness" units).

Detergent Composition

[0022] A preferred detergent composition is a manual dishwashing composition, preferably in liquid form. It typically contains from 30% to 95%, preferably from 40% to 90%, more preferably from 50% to 85% by weight of the composition of a liquid carrier in which the other essential and optional components are dissolved, dispersed or suspended. One preferred component of the liquid carrier is water.

[0023] Preferably the pH of the detergent composition of the invention, measured as a 10% product concentration in demineralized water at 20.degree. C., is adjusted to between 3 and 14, more preferably between 4 and 13, more preferably between 6 and 12 and most preferably between 8 and 10. The pH of the detergent composition can be adjusted using pH modifying ingredients known in the art.

Enzymes

[0024] Fatty acids can be oxidized in the presence of molecular oxygen (O.sub.2) by oleate lipoxygenases, linoleate lipoxygenases, and arachidonate lipoxygenases, to produce hydroperoxy fatty acids. These hydroperoxylated compounds can be further processed by other enzymes or spontaneously transform to a diverse group of oxygenated fatty acids and other derivatives. In the context of the current application, a "hydroperoxy fatty acid producing enzyme" is an enzyme that is capable of converting at least one fatty acid into a mixture of oxygenated compounds, comprising at least a hydroperoxy fatty acid as an intermediate or as a final product.

[0025] Unexpectedly, the Applicants found that a group of hydroperoxy fatty acid producing enzymes in combination with hydroperoxy fatty acid converting enzymes are capable of producing a more stable hence longer lasting sudsing profile in detergent wash solutions comprising oily and/or greasy soils. Not wishing to be bound by theory, the Applicants believe that the increased sudsing benefits are due to the conversion of fatty acids, present in the oily and/or greasy soils, into oxygenated fatty acids with enhanced surfactant properties and/or decreased tendency to precipitation in the presence of hard water.

[0026] Accordingly, the detergent composition of the invention comprises one or more hydroperoxy fatty acid producing enzymes. The hydroperoxy fatty acid producing enzymes are capable of converting one or more fatty acids into one or more hydroperoxy fatty acids. The hydroperoxy fatty acid producing enzymes are selected from the group consisting of: oleate lipoxygenases, linoleate lipoxygenases, arachidonate lipoxygenases, and mixtures thereof, preferably the hydroperoxy fatty acid producing enzymes are selected from the group consisting of: oleate 10S-lipoxygenases (EC 1.13.11.77), linoleate 8R-lipoxygenases (EC 1.13.11.60), linolenate 9R-lipoxygenases (EC 1.13.11.61), linoleate 9S-lipoxygenases (EC 1.13.11.58), linoleate 10R-lipoxygenases (EC 1.13.11.62), linoleate 10S-lipoxygenases, linoleate 11-lipoxygenases (EC 1.13.11.45), linoleate 13S-lipoxygenases (EC 1.13.11.12), linoleate 9/13-lipoxygenases (EC 1.13.11.B6), arachidonate 5-lipoxygenases (EC 1.13.11.34), arachidonate 8-lipoxygenases (EC 1.13.11.40), arachidonate 12-lipoxygenases (E.C. 1.13.11.31), arachidonate 15-lipoxygenase (EC 1.13.11.33), and mixtures thereof, more preferably the hydroperoxy fatty acid producing enzymes are selected from the group consisting of: oleate 10S-lipoxygenases (EC 1.13.11.77), linoleate 8R-lipoxygenases (EC 1.13.11.60), linoleate 9R-lipoxygenases (EC 1.13.11.61), linoleate 9S-lipoxygenases (EC 1.13.11.58), linoleate 10R-lipoxygenases (EC 1.13.11.62), linoleate 10S-lipoxygenases, linoleate 13S-lipoxygenases (EC 1.13.11.12), and mixtures thereof.

[0027] Alpha dioxygenases are also hydroperoxy fatty acid producing enzymes which are capable of converting one or more fatty acids into one or more hydroperoxy fatty acids. While not of use as part of the invention, they can optionally be added as co-enzymes.

[0028] Preferably the one or more fatty acids being converted by the hydroperoxy fatty acid producing enzymes are unsaturated fatty acids, wherein the unsaturated fatty acids are selected from the group consisting of: mono unsaturated fatty acids, di unsaturated fatty acids, tri unsaturated fatty acids, tetra unsaturated fatty acids, penta unsaturated fatty acids, hexa unsaturated fatty acids, and mixtures thereof; preferably myristoleic acid, palmitoleic acid, sapienic acid, oleic acid, elaidic acid, vaccenic acid, linoleic acid, linoelaidic acid, .alpha.-linolenic acid, .gamma.-linolenic acid, gadoleic acid, .alpha.-eleostearic acid, .beta.-eleostearic acid, ricinoleic acid, eicosenic acid, arachidonic acid, eicosapentaenoic acid, erucic acid, docosadienoic acid, docosahexaenoic acid, tetracosenoic acid, and mixtures thereof, preferably palmitoleic acid, oleic acid, linoleic acid, .alpha.-linolenic acid, .gamma.-linolenic acid, and mixtures thereof, more preferably oleic acid.

[0029] Lipoxygenases (EC 1.13.11.-) are a family of (non-heme), iron-containing dioxygenases that catalyze the insertion of molecular oxygen into fatty acids to produce the corresponding hydroperoxy fatty acids. The present invention comprises different groups of lipoxygenases, including linoleate lipoxygenases, arachidonate lipoxygenases, and oleate lipoxygenases. Even though linoleate, arachidonate, and oleate lipoxygenases typically recognize linoleic acid/linoleate, arachidonic acid/arachidonate, and oleic acid/oleate as the preferred substrates, respectively, the terms "linoleate lipoxygenases," "arachidonate lipoxygenases," and "oleate lypoxygenases" are used interchangeably herein and do not suggest any substrate specificity, i.e., the respective enzymes may act on any of these substrates.

[0030] Regiospecific dioxygenases catalyze the positional-specific hydroperoxylation of unsaturated fatty acids. For example, animal 5-8-, 12-, and 15-lipoxygenases and microbial 15-lipoxygenases convert arachidonic acid into 5-, 8-, 12-, 15-hydroperoxy fatty acids; whereas 11-lipoxygenases from coral and sea urchin produce 11-hydroperoxy fatty acids as intermediate or final products. Similarly, plant and bacterial 9-, and 13-lipoxygenases and fungal 11- and 13-lipoxygenases transform linoleic acid into its 9-, 11-, and 13-hydroperoxy fatty acid derivatives. Furthermore, some dioxygenases are able to catalyze the incorporation of molecular oxygen at several positions of the unsaturated fatty acid.

[0031] Non-limiting examples of hydroperoxy fatty acid producing enzymes that are part of the current invention include the wild-types listed in Table 1 and variants thereof. Preferred hydroperoxy fatty acid producing enzymes exhibit at least 20%, preferably at least 30%, preferably at least 40%, preferably at least 50%, preferably at least 60%, preferably at least 70%, preferably at least 80%, preferably at least 90%, preferably at least 95%, preferably at least 98% or preferably even 100% identity as calculated over the entire length of a sequence aligned against the entire length of at least one reference sequence selected from the group consisting of the wild-types listed in Table 1.

TABLE-US-00001 TABLE 1 Hydroperoxy Fatty Acid Producing Enzymes Origin SEQ ID Linoleate 8R-lipoxygenases (EC 1.13.11.60) Gaeumannomyces graminis 1 Linolenate 9R-lipoxygenases (EC 1.13.11.61) Nostoc sp. PCC 7120 2 Acaryochloris marina 3 Linoleate 9S-lipoxygenases (EC 1.13.11.58) Avena sativa 4 Oryza sativa subsp. Japonica 5 Magnaporthe oryzae 6 Glycine max 58 Glycine max 59 Glycine max 60 Glycine max 61 Linoleate 10R-lipoxygenases (EC 1.13.11.62) Aspergillus fumigatus 7 Aspergillus nidulans 8 Aspergillus terreus 9 Aspergillus clavatus 10 Penicillium marneffei 11 Penicillium decumbens 12 Penicillium chrysogenum 13 Aspergillus niger 14 Linoleate 10S-lipoxygenases Nostoc punctiforme 15 Oleate 10S-lipoxygenases (EC 1.13.11.77) Pseudomonas aeruginosa 16 Pseudomonas aeruginosa 17 Pseudomonas aeruginosa 18 Linoleate 11-lipoxygenases (EC 1.13.11.45) Fusarium oxysporum 19 Gaeumannomyces graminis var. avenue 20 Colletotrichum gloeosporioides 21 Linoleate 13S-lipoxygenases (EC 1.13.11.12) Arabidopsis thaliana 22 Oryza sativa subsp. Japonica 23 Glycine max 57 Linoleate 9/13-lipoxygenases (EC 1.13.11.B6) Pseudomonas aeruginosa 24 Momordica charantia 25 Arachidonate 5-lipoxygenases (EC 1.13.11.34) Homo sapiens 26 Arachidonate 8-lipoxygenases (EC 1.13.11.40) Homo sapiens 27 Arachidonate 12-lipoxygenases (E.C. 1.13.11.31) Homo sapiens 28 Arachidonate 15-lipoxygenase (EC 1.13.11.33) Homo sapiens 29 Alpha-dioxygenases Arabidopsis thaliana 30 Arabidopsis thaliana 31 Fusarium graminearum 32 Fusarium verticillioides 33 Fusarium oxysporum 34

[0032] Hydroperoxy fatty acids can be converted catalytically or spontaneously to oxygenated derivatives including hydroxy-, dihydroxy-, oxo-, epoxy-, and keto fatty acids, divinyl ethers, and aldehydes (Andreou, A., et al. (2009), Prog. Lipid Res. 48(3-4): 148-170). The detergent compositions of the present invention further comprises one or more hydroperoxy fatty acid converting enzyme capable of converting said hydroperoxy fatty acids into one or more derivatives of hydroperoxy fatty acids, wherein the hydroperoxy fatty acid converting enzymes are selected from the group consisting of: cyclooxygenases (EC 1.14.99.1), allene oxide synthases (EC 4.2.1.92), hydroperoxide isomerases (EC 4.2.1.92, EC 5.3.99.1, EC 5.4.4.5, EC 5.4.4.6), hydroperoxide lyases (EC 4.2.1.92), hydroperoxide dehydratases (EC 4.2.1.92), divinyl ether synthases (EC 4.2.1.121, EC 4.2.1.B8, EC 4.2.1.B9), 9,12-octadecadienoate 8-hydroperoxide 8R-isomerases (EC 5.4.4.5), 9,12-octadecadienoate 8-hydroperoxide 8S-isomerases (EC 5.4.4.6), 7,10-hydroperoxide diol synthases, epoxy alcohol synthases, and mixtures therefore, preferably allene oxide synthases (EC 4.2.1.92), hydroperoxide isomerases (EC 4.2.1.92, EC 5.3.99.1, EC 5.4.4.5, EC 5.4.4.6), hydroperoxide lyases (EC 4.2.1.92), hydroperoxide dehydratases (EC 4.2.1.92), 7,10-hydroperoxide diol synthases, epoxy alcohol synthases, and mixtures thereof, preferably 7,10-hydroperoxide diol synthases

[0033] Suitable examples of hydroperoxy fatty acid converting enzymes include the wild-types listed in Table 2 and variants thereof which exhibit hydroperoxy fatty acid converting enzyme activity. Preferred hydroperoxy fatty acid converting enzymes exhibit at least 20%, preferably at least 30%, preferably at least 40%, preferably at least 50%, preferably at least 60%, preferably at least 70%, preferably at least 80%, preferably at least 90%, preferably at least 95%, preferably at least 98% or preferably even 100% identity as calculated over the entire length of a sequence aligned against the entire length of at least one reference sequence selected from the group consisting of wild-types listed in Table 2. Preferred hydroperoxy fatty acid converting enzymes can also be fragments (e.g., N-terminal domain or C-terminal domain) of the wild-types listed in Table 2.

TABLE-US-00002 TABLE 2 Hydroperoxy Fatty Acid Converting Enzymes Origin SEQ ID Cyclooxygenases (EC 1.14.99.1) Homo sapiens 35 Hydroperoxide isomerases (EC 4.2.1.92, EC 5.3.99.1, EC 5.4.4.5, EC 5.4.4.6) Pseudomonas aeruginosa 36 Pseudomonas aeruginosa 37 Homo sapiens 39 7,10-oleate diol synthase Pseudomonas aeruginosa 38 Hydroperoxide lyases (EC 4.2.1.92) Nostoc punctiforme 40 Hydroperoxide dehydratases, allene oxide synthases (EC 4.2.1.92) Aspergillus terreus 41 Arabidopsis thaliana 42 Plexaura homomalla 47 Fusarium oxysporum 48 Colletotrichum graminicola 49 Glomerella cingulate 50 Aspergillus niger 51 Divinyl ether synthases (EC 4.2.1.121, EC 4.2.1.B8, EC 4.2.1.B9) Solanum tuberosum 43 Allium sativum 44 9,12-Octadecadienoate 8-hydroperoxide 8R-isomerases (EC 5.4.4.5) Asperigullus nidalus 45 Aspergillus fumigatus 46 9,12-Octadecadienoate 8-hydroperoxide 8S-isomerases (EC 5.4.4.6) Gaeumannomyces graminis 1 7,10-Hydroperoxide diol synthases Pseudomonas aeruginosa 36 Pseudomonas aeruginosa 37 Epoxy alcohol synthases Magnaporthe oryzae 52 Glomerella cingulate 53 Fusarium oxysporum 54

[0034] Preferably the detergent composition of the invention comprises:

[0035] a) hydroperoxy fatty acid producing enzymes which are selected from the group consisting of oleate 10S-lipoxygenases (EC 1.13.11.77), linoleate 10S-lipoxygenases, and mixtures thereof, having at least 60%, preferably at least 70%, preferably at least 80%, preferably at least 85%, preferably at least 90%, preferably at least 95%, preferably at least 98% or preferably even 100% identity as calculated over the entire length of a sequence aligned against the entire length of at least one reference sequence selected from a wild-type Pseudomonas aeruginosa 105-dioxygenase selected from the group consisting of: SEQ ID NO: 16, SEQ ID NO: 17, or SEQ ID NO: 18, and the wild-type Nostoc punctiforme linoleate 10S-lipoxygenases SEQ ID NO: 15, preferably a wild-type Pseudomonas aeruginosa 10S-dioxygenase selected from the group consisting of: SEQ ID NO: 16, SEQ ID NO: 17, or SEQ ID NO: 18;

[0036] b) hydroperoxy fatty acid converting enzymes which are 7,10-hydroperoxide diol synthases having at least 60%, preferably at least 70%, preferably at least 80%, preferably at least 85%, preferably at least 90%, preferably at least 95%, preferably at least 98% or preferably even 100% identity as calculated over the entire length of a sequence aligned against the entire length of at least one reference sequence selected from the group consisting of a wild-type Pseudomonas aeruginosa 7,10-oleate diol synthase selected from the group consisting of: SEQ ID NO: 36, SEQ ID NO: 37, or SEQ ID NO: 38; and

[0037] c) a surfactant system.

[0038] Preferably the detergent composition of the invention comprises:

[0039] a) hydroperoxy fatty acid producing enzymes which are selected from the group consisting of linoleate 10S-lipoxygenases and oleate 10S-lipoxygenases (EC 1.13.11.77), having at least 60%, preferably at least 70%, preferably at least 80%, preferably at least 85%, preferably at least 90%, preferably at least 95%, preferably at least 98% or preferably even 100% identity as calculated over the entire length of a sequence aligned against the entire length of at least one reference sequence selected from the wild-type Nostoc punctiforme linoleate 10S-lipoxygenases SEQ ID NO: 15 and the wild-type Pseudomonas aeruginosa 10S-dioxygenase selected from the group consisting of: SEQ ID NO: 16, SEQ ID NO: 17, or SEQ ID NO: 18, preferably the wild-type Nostoc punctiforme linoleate 10S-lipoxygenases SEQ ID NO: 15;

[0040] b) hydroperoxy fatty acid converting enzymes which are hydroperoxide lyases (EC 4.2.1.92) having at least 60%, preferably at least 70%, preferably at least 80%, preferably at least 85%, preferably at least 90%, preferably at least 95%, preferably at least 98% or preferably even 100% identity as calculated over the entire length of a sequence aligned against the entire length of at least one reference sequence selected from a wild-type Nostoc punctiforme HPL (SEQ ID NO: 40); and

[0041] c) a surfactant system.

[0042] A given sequence is typically compared against the full-length sequence of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41, SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46, SEQ ID NO: 56, SEQ ID NO: 57, SEQ ID NO: 58, SEQ ID NO: 59, SEQ ID NO: 60, SEQ ID NO: 61, SEQ ID NO: 63.

[0043] SEQ ID NO: 2 to 34, and 56 to 61 relate to hydroperoxy fatty acid producing enzymes and SEQ ID NO: 1, 35 to 46, and 63 relate to hydroperoxy fatty acid converting enzymes.

[0044] The composition of the present invention may alternatively or in addition comprise at least one fatty acid processing fusion enzyme, wherein the at least one fatty acid processing fusion enzyme comprises at least two catalytic domains: a hydroperoxy fatty acid producing domain, capable of converting one or more fatty acids into one or more hydroperoxy fatty acids; and a hydroperoxy fatty acid converting domain, capable of converting the hydroperoxy fatty acids into one or more derivatives of hydroperoxy fatty acids, in combination with a surfactant system.

[0045] The hydroperoxy fatty acid producing catalytic domain of the fusion enzyme can exhibit at least one activity selected from the group consisting of: oleate lipoxygenases, linoleate lipoxygenases, arachidonate lipoxygenases, and mixtures thereof; preferably the activity is selected from the group consisting of: oleate 10S-lipoxygenases (EC 1.13.11.77), linoleate 8R-lipoxygenases (EC 1.13.11.60), linolenate 9R-lipoxygenases (EC 1.13.11.61), linoleate 9S-lipoxygenases (EC 1.13.11.58), linoleate 10R-lipoxygenases (EC 1.13.11.62), linoleate 10S-lipoxygenases, linoleate 11-lipoxygenases (EC 1.13.11.45), linoleate 13S-lipoxygenases (EC 1.13.11.12), linoleate 9/13-lipoxygenases (EC 1.13.11.B6), arachidonate 5-lipoxygenases (EC 1.13.11.34), arachidonate 8-lipoxygenases (EC 1.13.11.40), arachidonate 12-lipoxygenases (E.C. 1.13.11.31), arachidonate 15-lipoxygenase (EC 1.13.11.33), and mixtures thereof; more preferably the activity is selected from the group consisting of: oleate 10S-lipoxygenases (EC 1.13.11.77), linoleate 8R-lipoxygenases (EC 1.13.11.60), linoleate 9R-lipoxygenases (EC 1.13.11.61), linoleate 9S-lipoxygenases (EC 1.13.11.58), linoleate 10R-lipoxygenases (EC 1.13.11.62), linoleate 10S-lipoxygenases, linoleate 13S-lipoxygenases (EC 1.13.11.12), and mixtures thereof; most preferably the activity is selected from the group consisting of: linoleate 9S-lipoxygenases (EC 1.13.11.58), linoleate 10R-lipoxygenases (EC 1.13.11.62), and mixtures thereof.

[0046] The hydroperoxy fatty acid converting catalytic domain of the fusion enzyme can exhibit at least one activity selected from the group consisting of: cyclooxygenases (EC 1.14.99.1), allene oxide synthases (AOS--EC 4.2.1.92), hydroperoxide isomerases (EC 4.2.1.92, EC 5.3.99.1, EC 5.4.4.5, EC 5.4.4.6), hydroperoxide lyases (HPL--EC 4.2.1.92), hydroperoxide dehydratases (EC 4.2.1.92), divinyl ether synthases (DES--EC 4.2.1.121, EC 4.2.1.B8, EC 4.2.1.B9), 9,12-octadecadienoate 8-hydroperoxide 8R-isomerases (EC 5.4.4.5), 9,12-octadecadienoate 8-hydroperoxide 8S-isomerases (EC 5.4.4.6), 7,10-hydroperoxide diol synthases, epoxy alcohol synthases (EAS), and mixtures thereof; preferably the activity is selected from the group consisting of: allene oxide synthase (AOS--EC 4.2.1.92), epoxy alcohol synthases (EAS), hydroperoxide lyase (HPL--EC 4.2.1.92), 9,12-octadecadienoate 8-hydroperoxide 8R-isomerases (EC 5.4.4.5), 9,12-octadecadienoate 8-hydroperoxide 8S-isomerases (EC 5.4.4.6); most preferably allene oxide synthases (AOS--EC 4.2.1.92), epoxy alcohol synthases (EAS), and mixtures thereof.

[0047] When both the hydroperoxy fatty acid producing catalytic activity and the hydroperoxy fatty acid converting activity are derived together from a single fusion enzyme, the rate of conversion and the selectivity towards desirable derivatives of hydroperoxy fatty acids can be enhanced. Hence, such fusion enzymes are capable of producing a more stable, hence longer lasting, sudsing profile in detergent wash solutions when oily and/or greasy soils comprising fatty acids. Not wishing to be bound by theory, the Applicants believe that the increased sudsing benefits are due to the conversion of the fatty acids, present in the oily and/or greasy soils, into oxygenated fatty acids with enhanced surfactant properties and/or decreased tendency to precipitation in the presence of hard water.

[0048] Several examples of multi-domain fusion enzymes comprising: a) a hydroperoxy fatty acid producing domain and b) hydroperoxy fatty acid converting domain are found in nature. For example, enzymes containing a dioxygenase (DOX) domain and an allene oxide synthase (AOS) domain produce a diverse series of oxygenated derivatives of unsaturated fatty acids and are included in the current invention. Non-limiting examples of these DOX-AOS enzymes are Plexaura homomalla 8R-DOX-AOS (SEQ ID NO: 47), Fusarium oxysporum 9S-DOX-AOS (SEQ ID NO: 48), Colletotrichum graminicola 9S-DOX-AOS (SEQ ID NO: 49), Glomerella cingulate 9S-DOX-AOS (SEQ ID NO: 50), and Aspergillus niger 9R-DOX-AOS (SEQ ID NO: 51). In another example, enzymes can contain a dioxygenase (DOX) domain and an epoxy alcohol synthase (EAS) domain and also are included in the current invention. Non-limiting examples of DOX-EAS enzymes include Magnaporthe oryzae 10R-DOX-EAS (SEQ ID NO: 52), Glomerella cingulate 10R-DOX-EAS (SEQ ID NO: 53), and Fusarium oxysporum 10R-DOX-EAS (SEQ ID NO: 54). Finally, diol synthases are fusion proteins that contain an N-terminal dioxygenase (DOX) domain and a C-terminal hydroperoxide isomerase (HPI) domain or an N-terminal allene oxide synthase (AOS) domain and a C-terminal dioxygenase (DOX) domain. Based on the reaction products, several diol synthases have been characterized in the art: 5,8-linoleate diol synthases (5,8-LDS), 7,8-linoleate diol synthases (7,8-LDS), 8,11-linoleate diol synthases (8,11-LDS), and 9,14-linoleate diol synthases (9,14-LDS). Although they are frequently referred as linoleate diol synthases, they can convert substrates different than linoleate (e.g., oleate). Non-limiting examples of 5,8-LDS include Aspergillus nidulans PpoA, Aspergillus fumigatus PpoA, Aspergillus terreus PpoA, Aspergillus kawachii PpoA, Aspergillus clavatus PpoA, and Aspergillus niger PpoA. Non-limiting examples of 7,8-LDS include Glomerella cingulate 7,8-LDS, Gaeumannomyces graminis 7,8-LDS, and Magnaporthe oryzae 7,8-LDS. Non-limiting examples of 8,11-LDS include Penicillium oxalicum 8,11-LDS, Penicillium chrysogenum 8,11-LDS, and Penicillium digitatum 8,11-LDS. Non-limiting examples of 9,14-LDS include Nostoc sp. PCC 7120 9,14-LDS, Acaryochloris marina putative 9,14-LDS, and Nostoc sp. NIES-4103 putative 9,14-LDS. In the first step of the reaction, the DOX domains of these enzymes convert the unsaturated fatty acid into a hydroperoxy fatty acid, frequently followed by an additional transformation catalyzed by the HPI, AOS, or EAS domain.

[0049] The fusion enzyme can have at least 60%, preferably at least 70%, preferably at least 80%, preferably at least 85%, preferably at least 90%, preferably at least 95%, preferably at least 98% or preferably even 100% identity as calculated over the entire length of a sequence aligned against the entire length of at least one reference sequence selected from the wild-type multi-domain enzymes selected from the group consisting of: Plexaura homomalla 8R-DOX-AOS (SEQ ID NO: 47), Fusarium oxysporum 9S-DOX-AOS (SEQ ID NO: 48), Colletotrichum graminicola 9S-DOX-AOS (SEQ ID NO: 49), Glomerella cingulate 9S-DOX-AOS (SEQ ID NO: 50), Aspergillus niger 9R-DOX-AOS (SEQ ID NO: 51), Magnaporthe oryzae 10R-DOX-EAS (SEQ ID NO: 52), Glomerella cingulate 10R-DOX-EAS (SEQ ID NO: 53), or Fusarium oxysporum 10R-DOX-EAS (SEQ ID NO: 54); preferably Fusarium oxysporum 9S-DOX-AOS (SEQ ID NO: 48), or Magnaporthe oryzae 10R-DOX-EAS (SEQ ID NO: 52).

[0050] A given sequence is typically compared against the entire length of a sequence of SEQ ID NO: 47, SEQ ID NO: 48, SEQ ID NO: 49, SEQ ID NO: 50, SEQ ID NO: 51, SEQ ID NO: 52, SEQ ID NO: 53, SEQ ID NO: 54, SEQ ID NO: 65, or SEQ ID NO: 67 to obtain a score.

[0051] The present invention also includes variants of enzymes. Variants of enzymes, as used herein, include a sequence resulting when a wild-type protein of the respective protein is modified by, or at, one or more amino acids (for example 1, 2, 5 or 10 amino acids). The invention also includes variants in the form of truncated forms derived from a wild-type enzyme, such as a protein with a truncated N-terminus or a truncated C-terminus. Some enzymes may include an N-terminal signal peptide that is likely removed upon secretion by the cell. The present invention includes variants without the N-terminal signal peptide. Bioinformatic tools, such as SignalP ver 4.1 (Petersen T N., Brunak S., von Heijne G. and Nielsen H. (2011), Nature Methods, 8:785-786), can be used to predict the existence and length of such signal peptides. The invention also includes variants derived by adding an extra amino acid sequence to a wild-type protein, such as for example, an N-terminal tag, a C-terminal tag or an insertion in the middle of the protein sequence. Non-limiting examples of tags are maltose binding protein (MBP) tag, glutathione S-transferase (GST) tag, thioredoxin (Trx) tag, His-tag, and any other tags known by those skilled in art. Tags can be used to improve solubility and expression levels during fermentation or as a handle for enzyme purification.

[0052] It is important that variants of enzymes retain and preferably improve the ability of the wild-type protein to catalyze the conversion of the fatty acids. Some performance drop in a given property of variants may of course be tolerated, but the variants should retain and preferably improve suitable properties for the relevant application for which they are intended. Screening of variants of one of the wild-types can be used to identify whether they retain and preferably improve appropriate properties.

[0053] The variants may have "conservative" substitutions.

[0054] Suitable examples of conservative substitution includes one conservative substitution in the enzyme, such as a conservative substitution in SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41, SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46, SEQ ID NO: 56, SEQ ID NO: 57, SEQ ID NO: 58, SEQ ID NO: 59, SEQ ID NO: 60, SEQ ID NO: 61, SEQ ID NO: 63.

[0055] SEQ ID NO: 2 to 34, and 56 to 61 relate to hydroperoxy fatty acid producing enzymes and SEQ ID NO: 1, 35 to 46, and 63 relate to hydroperoxy fatty acid converting enzymes. SEQ ID NO: 47 to 54, 65, and 67 relate to fusion enzymes.

[0056] Other suitable examples include 10 or fewer conservative substitutions in the protein, such as five or fewer. An enzyme of the invention may therefore include 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or more conservative substitutions. An enzyme can be produced to contain one or more conservative substitutions by manipulating the nucleotide sequence that encodes that enzyme using, for example, standard procedures such as site-directed mutagenesis or PCR.

[0057] For the fatty acid processing fusion enzyme, suitable examples of conservative substitution includes one conservative substitution in the enzyme, such as a conservative substitution in SEQ ID NO: 47, SEQ ID NO: 48, SEQ ID NO: 49, SEQ ID NO: 50, SEQ ID NO: 51, SEQ ID NO: 52, SEQ ID NO: 53, SEQ ID NO: 54, SEQ ID NO: 65, or SEQ ID NO: 67.

[0058] Examples of amino acids which may be substituted for an original amino acid in an enzyme and which are regarded as conservative substitutions include: Ser for Ala; Lys for Arg; Gln or His for Asn; Glu for Asp; Asn for Gln; Asp for Glu; Pro for Gly; Asn or Gln for His; Leu or Val for Ile; Ile or Val for Leu; Arg or Gln for Lys; Leu or Ile for Met; Met, Leu or Tyr for Phe; Thr for Ser; Ser for Thr; Tyr for Trp; Trp or Phe for Tyr; and Ile or Leu for Val.

[0059] A variant includes a "modified enzyme" or a "mutant enzyme" which encompasses proteins having at least one substitution, insertion, and/or deletion of an amino acid. A modified enzyme may have 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 or more amino acid modifications (selected from substitutions, insertions, deletions and combinations thereof).

[0060] Enzymes can be modified by a variety of chemical techniques to produce derivatives having essentially the same or preferably improved activity as the unmodified enzymes, and optionally having other desirable properties. For example, carboxylic acid groups of the protein, whether carboxyl-terminal or side chain, may be provided in the form of a salt of a pharmaceutically-acceptable cation or esterified, for example to form a C1-C6 alkyl ester, or converted to an amide, for example of formula CONR1R2 wherein R1 and R2 are each independently H or C1-C6 alkyl, or combined to form a heterocyclic ring, such as a 5- or 6-membered ring Amino groups of the enzyme, whether amino-terminal or side chain, may be in the form of a pharmaceutically-acceptable acid addition salt, such as the HCl, HBr, acetic, benzoic, toluene sulfonic, maleic, tartaric and other organic salts, or may be modified to C1-C20 alkyl or dialkyl amino or further converted to an amide. Hydroxyl groups of the protein side chains may be converted to alkoxy or ester groups, for example C1-C20 alkoxy or C1-C20 alkyl ester, using well-recognized techniques. Phenyl and phenolic rings of the protein side chains may be substituted with one or more halogen atoms, such as F, Cl, Br or I, or with C1-C20 alkyl, C1-C20 alkoxy, carboxylic acids and esters thereof, or amides of such carboxylic acids. Methylene groups of the protein side chains can be extended to homologous C2-C4 alkylenes. Thiols can be protected with any one of a number of well-recognized protecting groups, such as acetamide groups. Those skilled in the art will also recognize methods for introducing cyclic structures into the proteins of this disclosure to select and provide conformational constraints to the structure that result in enhanced stability.

[0061] Preferably the hydroperoxy fatty acid producing enzyme and hydroperoxy fatty acid converting enzymes, and/or the fatty acid processing fusion enzyme are each present in an amount from 0.0001 wt % to 1 wt %, by weight of the detergent composition, based on active protein in the composition. More preferably the enzymes are each is present in an amount of from 0.001 wt % to 0.2 wt %, by weight of the detergent composition, based on active protein in the composition.

[0062] Especially, but not exclusively, when the composition comprises a liquid, it may be preferred to incorporate the enzymes via an encapsulate. The hydroperoxy fatty acid producing enzymes and hydroperoxy fatty acid converting enzymes, and/or the fatty acid processing fusion enzyme may be incorporated into the detergent composition via an additive particle, such as an enzyme granule or in the form of an encapsulate, or may be added in the form of a liquid formulation. Encapsulating the enzymes promote the stability of the enzymes in the composition and helps to counteract the effect of any hostile compounds present in the composition, such as bleach, protease, surfactant, chelant, etc.

[0063] The aforementioned enzyme or enzymes can be present in an additive particle as the only enzyme in the additive particle or may be present in the additive particle in combination with one or more additional co-enzymes.

[0064] Preferably the composition of the invention may further comprise one or more co-enzymes selected from the group consisting of: fatty-acid peroxidases (EC 1.11.1.3), unspecific peroxygenases (EC 1.11.2.1), plant seed peroxygenases (EC 1.11.2.3), fatty acid peroxygenases (EC 1.11.2.4), linoleate diol synthases (EC 1.13.11.44), 5,8-linoleate diol synthases (EC 1.13.11.60 and EC 5.4.4.5), 7,8-linoleate diol synthases (EC 1.13.11.60 and EC 5.4.4.6), 9,14-linoleate diol synthases (EC 1.13.11.B1), 8,11-linoleate diol synthases, oleate diol synthases, other linoleate diol synthases, unspecific monooxygenase (EC 1.14.14.1), alkane 1-monooxygenase (EC 1.14.15.3), oleate 12-hydroxylases (EC 1.14.18.4), alpha-dioxygenases, fatty acid amide hydrolase (EC 3.5.1.99), oleate hydratases (EC 4.2.1.53), linoleate isomerases (EC 5.2.1.5), linoleate (10E,12Z)-isomerases (EC 5.3.3.B2), fatty acid decarboxylases (OleT-like), iron-dependent decarboxylases (UndA-like), other CYP450 monooxygenases, amylases, lipases, proteases, cellulases, and mixtures thereof. Preferably the co-enzymes are fatty-acid peroxidases (EC 1.11.1.3), unspecific peroxygenases (EC 1.11.2.1), plant seed peroxygenases (EC 1.11.2.3), fatty acid peroxygenases (EC 1.11.2.4), and mixtures thereof.

[0065] Other suitable additional co-enzymes include protease such as metalloprotease or alkaline serine protease, such as subtilisin, mannanase, pectinase, DNAse, oxidoreductase, peroxidases, lipases, phospholipases, cellobiohydrolases, cellobiose dehydrogenases, esterases, cutinases, pectinases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, ligninases, pullulanases, tannases, pentosanases, glucanases, arabinosidases, hyaluronidase, chondroitinase, laccases, amylases, and mixtures thereof.

[0066] Alpha-dioxygenases convert saturated and unsaturated fatty acids to their corresponding 2-hydroperoxy fatty acids via stereoselective dioxygenation. The resulting hydroperoxy fatty acids can undergo spontaneous decarboxylation to shorter aldehydes. Alpha-dioxygenases differs from lipoxygenases in that an unsaturated carbon bond is not required during the oxidation. They are generally encoded by different species of plants and fungi, where they are up-regulated during the host defense response against pathogen attack, but homologs are also found in bacteria.

[0067] Where necessary, the composition comprises, provides access to or forms in situ any additional substrate necessary for the effective functioning of the enzyme. For example, molecular oxygen is provided as an additional substrate for lipoxygenases and diol synthases; water for oleate hydratases; and hydrogen peroxide for peroxidases, peroxygenase, lipoxygenases, and/or fatty acid decarboxylases (OleT-like). When oxygen is required, it can be obtained from the atmosphere or from a precursor that can be transformed to produce it in situ. In many applications, oxygen from the atmosphere can be present in sufficient amounts. Similarly, when hydrogen peroxide is required, it can be produced from a precursor in situ.

Surfactant System

[0068] Preferably the detergent composition comprises from 1% to 60%, preferably from 5% to 50%, more preferably from 8% to 40%, by weight of the total composition of a surfactant system.

[0069] The surfactant system of the composition of the present invention preferably comprises one or more anionic surfactants. Preferably, the surfactant system for the detergent composition of the present invention comprises from 1% to 40%, preferably 6% to 35%, more preferably 8% to 30% by weight of the total composition of the anionic surfactants. The anionic surfactants can be any anionic cleaning surfactants, preferably selected from sulfate and/or sulfonate anionic surfactants. HLAS (linear alkylbenzene sulfonates) would be the most preferred sulfonate anionic surfactants. Especially preferred anionic surfactants are selected from the group consisting of alkyl sulfates, alkyl alkoxy sulfates and mixtures thereof, and preferably wherein the alkyl alkoxy sulfates is an alkyl ethoxy sulfates. Preferred anionic surfactants are a combination of alkyl sulfates and alkyl ethoxy sulfates with a combined average ethoxylation degree of less than 5, preferably less than 3, more preferably less than 2 and more than 0.5 and an average level of branching of from about 5% to about 40%, more preferably from about 10% to 35%, and even more preferably from about 20% to 30%.

[0070] The average alkoxylation degree is the mol average alkoxylation degree of all the components of the mixture (i.e., mol average alkoxylation degree) of the anionic surfactants. In the mol average alkoxylation degree calculation the weight of sulfate anionic surfactant components not having alkoxylate groups should also be included.

Mol average alkoxylation degree=(x1*alkoxylation degree of surfactant 1+x2*alkoxylation degree of surfactant 2+ . . . )/(x1+x2+ . . . )

[0071] wherein x1, x2, . . . are the number of moles of each sulfate anionic surfactant of the mixture and alkoxylation degree is the number of alkoxy groups in each sulfate anionic surfactant.

[0072] The average level of branching is the weight average % of branching and it is defined according to the following formula:

Weight average of branching (%)=[(x1*wt % branched alcohol 1 in alcohol 1+x2*wt % branched alcohol 2 in alcohol 2+ . . . )/(x1+x2+ . . . )]*100

[0073] wherein x1, x2, . . . are the weight in grams of each alcohol in the total alcohol mixture of the alcohols which were used as starting material for the anionic surfactant for the composition of the invention. In the weight average branching degree calculation the weight of anionic surfactant components not having branched groups should also be included.

[0074] Suitable examples of commercially available sulfates include, those based on Neodol alcohols ex the Shell company, Lial--Isalchem and Safol ex the Sasol company, natural alcohols ex The Procter & Gamble Chemicals company. Suitable sulfonate surfactants for use herein include water-soluble salts of C8-C18 alkyl or hydroxyalkyl sulfonates; C11-C18 alkyl benzene sulfonates (LAS), modified alkylbenzene sulfonate (MLAS); methyl ester sulfonate (MES); and alpha-olefin sulfonate (AOS). Those also include the paraffin sulfonates may be monosulfonates and/or disulfonates, obtained by sulfonating paraffins of 10 to 20 carbon atoms. The sulfonate surfactants also include the alkyl glyceryl sulfonate surfactants.

[0075] The surfactant system of the composition of the present invention preferably comprises a primary co-surfactant system, wherein the primary co-surfactant system is preferably selected from the group consisting of amphoteric surfactant, zwitterionic surfactant and mixtures thereof. Preferably the amphoteric surfactant is an amine oxide surfactant and the zwitterionic surfactant is a betaine surfactant. Preferably, the surfactant system for the detergent composition of the present invention comprises from 0.5% to 15%, preferably from 1% to 12%, more preferably from 2% to 10%, by weight of the total composition of a primary co-surfactant system.

[0076] Preferably the weight ratio of the anionic surfactants to the primary co-surfactants is less than 9:1, more preferably from 5:1 to 1:1, more preferably from 4:1 to 2:1. Preferably the primary co-surfactant system is an amphoteric surfactant. Preferably, the primary co-surfactant system is an amine oxide surfactant, and wherein the composition comprises anionic surfactant and amine oxide surfactant in a weight ratio of less than 9:1, more preferably from 5:1 to 1:1, more preferably from 4:1 to 2:1, preferably from 3:1 to 2.5:1. Preferably the composition of the present invention, wherein the surfactant system comprises one or more anionic surfactants and one or more co-surfactants, wherein the anionic surfactants are a mixture of alkyl sulfates and alkyl alkoxy sulfates, the co-surfactants are alkyl dimethyl amine oxides, and wherein the weight ratio of the anionic surfactants to the co-surfactants is from 4:1 to 2:1.

[0077] Preferred amine oxides are alkyl dimethyl amine oxide or alkyl amido propyl dimethyl amine oxide, more preferably alkyl dimethyl amine oxide and especially coco dimethyl amino oxide. Amine oxide may have a linear or branched alkyl moiety.

[0078] The composition may further comprise a C10AO, especially n-decyl dimethyl amine, and preferably comprises less than 5% preferably less than 3% by weight of total amine oxide of a C8 amine oxide such as a C8 dimethyl amine oxide.

[0079] Preferably the primary co-surfactant system is a zwitterionic surfactant. Suitable examples of zwitterionic surfactants include betaines, preferably alkyl betaines, alkylamidobetaine, and mixtures thereof. Cocoamidopropylbetaine is most preferred.

[0080] Preferably, the surfactant system of the composition of the present invention further comprises from 0.1% to 10% by weight of the total composition of a secondary co-surfactant system preferably comprising a non-ionic surfactant. Suitable non-ionic surfactants include the condensation products of aliphatic alcohols with from 1 to 25 moles of ethylene oxide. The alkyl chain of the aliphatic alcohol can either be straight or branched, primary or secondary, and generally contains from 8 to 22 carbon atoms. Particularly preferred are the condensation products of alcohols having an alkyl group containing from 10 to 18 carbon atoms, preferably from 10 to 15 carbon atoms with from 2 to 18 moles, preferably 2 to 15, more preferably 5-12 of ethylene oxide per mole of alcohol. Highly preferred non-ionic surfactants are the condensation products of guerbet alcohols with from 2 to 18 moles, preferably 2 to 15, more preferably 5-12 of ethylene oxide per mole of alcohol. Preferably, the non-ionic surfactants are an alkyl ethoxylated surfactants, preferably comprising from 9 to 15 carbon atoms in its alkyl chain and from 5 to 12 units of ethylene oxide per mole of alcohol. Other suitable non-ionic surfactants for use herein include fatty alcohol polyglycol ethers, alkylpolyglucosides and fatty acid glucamides, preferably alkylpolyglucosides. Preferably the alkyl polyglucoside surfactant is a C8-C16 alkyl polyglucoside surfactant, preferably a C8-C14 alkyl polyglucoside surfactant, preferably with an average degree of polymerization of between 0.1 and 3, more preferably between 0.5 and 2.5, even more preferably between 1 and 2. Most preferably the alkyl polyglucoside surfactant has an average alkyl carbon chain length between 10 and 16, preferably between 10 and 14, most preferably between 12 and 14, with an average degree of polymerization of between 0.5 and 2.5 preferably between 1 and 2, most preferably between 1.2 and 1.6. C8-C16 alkyl polyglucosides are commercially available from several suppliers (e.g., Simusol.RTM. surfactants from Seppic Corporation; and Glucopon.RTM. 600 CSUP, Glucopon.RTM. 650 EC, Glucopon.RTM. 600 CSUP/MB, and Glucopon.RTM. 650 EC/MB, from BASF Corporation). Preferably, the composition comprises the anionic surfactant and the non-ionic surfactant in a ratio of from 2:1 to 50:1, preferably 2:1 to 10:1.

Enzyme Stabilizer

[0081] Preferably the composition of the invention further comprises an enzyme stabilizer, selected from the group consisting of chemical and physical stabilizers, preferably the physical stabilizer comprises encapsulating the enzyme. Suitable enzyme stabilizers may be selected from the group consisting of (a) univalent, bivalent and/or trivalent cations preferably selected from the group of inorganic or organic salts of alkaline earth metals, alkali metals, aluminum, iron, copper and zinc, preferably alkali metals and alkaline earth metals, preferably alkali metal and alkaline earth metal salts with halides, sulfates, sulfites, carbonates, hydrogencarbonates, nitrates, nitrites, phosphates, formates, acetates, propionates, citrates, maleates, tartrates, succinates, oxalates, lactates, and mixtures thereof. In a preferred embodiment the salt is selected from the group consisting of sodium chloride, calcium chloride, potassium chloride, sodium sulfate, potassium sulfate, sodium acetate, potassium acetate, sodium formate, potassium formate, calcium lactate, calcium nitrate and mixtures thereof. Most preferred are salts selected from the group consisting of calcium chloride, potassium chloride, potassium sulfate, sodium acetate, potassium acetate, sodium formate, potassium formate, calcium lactate, calcium nitrate, and mixtures thereof, and in particular potassium salts selected from the group of potassium chloride, potassium sulfate, potassium acetate, potassium formate, potassium propionate, potassium lactate and mixtures thereof. Most preferred are potassium acetate and potassium chloride. Preferred calcium salts are calcium formate, calcium lactate and calcium nitrate including calcium nitrate tetrahydrate. Calcium and sodium formate salts may be preferred. These cations are present at least 0.01 wt %, preferably at least 0.03 wt %, more preferably at least 0.05 wt %, most preferably at least 0.25 wt % up to 2 wt % or even up to 1 wt % by weight of the total composition. These salts are formulated from 0.1 wt % to 5 wt %, preferably from 0.2 wt % to 4 wt %, more preferably from 0.3 wt % to 3 wt %, most preferably from 0.5 wt % to 2 wt % relative to the total weight of the composition. Further enzyme stabilizers can be selected from the group (b) carbohydrates selected from the group consisting of oligosaccharides, polysaccharides and mixtures thereof, such as a monosaccharide glycerate as described in WO201219844; (c) mass efficient reversible protease inhibitors selected from the group consisting of phenyl boronic acid and derivatives thereof, preferably 4-formyl phenylboronic acid; (d) alcohols such as 1,2-propane diol, propylene glycol; (e) peptide aldehyde stabilizers such as tripeptide aldehydes such as Cbz-Gly-Ala-Tyr-H, or disubstituted alaninamide; (f) carboxylic acids such as phenyl alkyl dicarboxylic acid as described in WO2012/19849 or multiply substituted benzyl carboxylic acid comprising a carboxyl group on at least two carbon atoms of the benzyl radical such as described in WO2012/19848, phthaloyl glutamine acid, phthaloyl asparagine acid, aminophthalic acid and/or an oligoamino-biphenyl-oligocarboxylic acid; and (g) mixtures thereof.

Additional Enzymes

[0082] Preferred compositions of the invention comprise one or more additional enzymes selected from the group consisting of amylases, lipases, proteases, cellulases, lipoxygenases, diol synthases, and mixtures thereof. Even more preferred compositions of the invention comprise one or more enzymes selected from lipases, proteases, cellulases, amylases and any combination thereof. Most preferably compositions of the invention comprise one or more enzymes selected from lipases, proteases, amylases and any combination thereof.

[0083] It may be particularly preferred for the compositions of the present invention to additionally comprise a protease enzyme. Since oleic acid and other foam suppressing unsaturated fatty acids are present in body soils or even human skin, as protease enzyme acts as a skin care agent, or breaks down proteinaceous soils, fatty acids released are broken down, preventing suds suppression.

[0084] It may be particularly preferred for the compositions of the present invention to additionally comprise an amylase enzyme. Since oily soils are commonly entrapped in starchy soils, the amylase and unsaturated fatty acid transforming enzymes work synergistically together: fatty acid soils are released by breakdown of starchy soils with amylase, thus, the unsaturated fatty acid transforming enzyme is particularly effective in ensuring there is no negative impact on suds in the wash liquor.

[0085] Each additional enzyme is typically present in an amount of from 0.0001 wt % to 1 wt %, preferably from 0.0005 wt % to 0.5 wt %, more preferably from 0.005 wt % to 0.1 wt %, by weight of the composition, based on active protein.

Salt

[0086] The composition of the present invention may optionally comprise from 0.01% to 3%, preferably from 0.05% to 2%, more preferably from 0.2% to 1.5%, or most preferably 0.5% to 1%, by weight of the total composition of a salt, preferably a monovalent, divalent inorganic salt or a mixture thereof, preferably sodium chloride. Most preferably the composition alternatively or further comprises a multivalent metal cation in the amount of from 0.01 wt % to 2 wt %, preferably from 0.1% to 1%, more preferably from 0.2% to 0.8% by weight of the composition, preferably the multivalent metal cation is magnesium, aluminum, copper, calcium or iron, more preferably magnesium, most preferably said multivalent salt is magnesium chloride. Without wishing to be bound by theory, it is believed that use of a multivalent cation helps with the formation of protein/protein, surfactant/surfactant or hybrid protein/surfactant network at the oil water and air water interface that is strengthening the suds.

Carbohydrates

[0087] Preferably the composition of the present invention comprises one or more carbohydrates selected from the group comprising 0-glycan, N-glycan, and mixtures thereof. Suitable carbohydrates include alpha or beta glucan with 1,3 and/or 1.4 and/or 1,6 linkage. Glucans can be modified especially with carboxyl sulfate, glycol ether of amino groups. Glucan can be extracted from dextran, starch or cellulose. Glucan with structure close to natural glucan such as schizophyllan, scleroglucan or paramylon are particularly preferred.

Hydrotrope

[0088] The composition of the present invention may optionally comprise from 1% to 10%, or preferably from 0.5% to 10%, more preferably from 1% to 6%, or most preferably from 0.1% to 3%, or combinations thereof, by weight of the total composition of a hydrotrope, preferably sodium cumene sulfonate. Other suitable hydrotropes for use herein include anionic-type hydrotropes, particularly sodium, potassium, and ammonium xylene sulfonate, sodium, potassium and ammonium toluene sulfonate, sodium potassium and ammonium cumene sulfonate, and mixtures thereof, as disclosed in U.S. Pat. No. 3,915,903.

Organic Solvent

[0089] The composition of the present invention may optionally comprise an organic solvent. Preferably the organic solvents include alcohols, glycols, and glycol ethers, alternatively alcohols and glycols. The composition comprises from 0% to less than 50%, preferably from 0.01% to 25%, more preferably from 0.1% to 10%, or most preferably from 0.5% to 5%, by weight of the total composition of an organic solvent, preferably an alcohol, more preferably an ethanol, a polyalkyleneglycol, more preferably polypropyleneglycol, and mixtures thereof.

Amphiphilic Polymer

[0090] The composition of the present invention may further comprise from about 0.01% to about 5%, preferably from about 0.05% to about 2%, more preferably from about 0.07% to about 1% by weight of the total composition of an amphiphilic polymer selected from the groups consisting of amphiphilic alkoxylated polyalkyleneimine and mixtures thereof, preferably an amphiphilic alkoxylated polyalkyleneimine.

[0091] A preferred polyethyleneimine has the general structure of Formula (II):

##STR00001##

[0092] wherein the polyethyleneimine backbone has a weight average molecular weight of about 600 Da, n of Formula (II) has an average of about 24, m of Formula (II) has an average of about 16 and R of Formula (II) is selected from hydrogen, a C.sub.1-C.sub.4 alkyl and mixtures thereof, preferably hydrogen. The degree of permanent quaternization of Formula (II) may be from 0% to about 22% of the polyethyleneimine backbone nitrogen atoms. The molecular weight of this polyethyleneimine preferably is between 25,000 Da and 30,000 Da, preferably about 28,000 Da.

Chelant

[0093] The detergent composition herein can comprise a chelant at a level of from 0.1% to 20%, preferably from 0.2% to 5%, more preferably from 0.2% to 3% by weight of total composition.

[0094] Preferably, the composition of the present invention comprises one or more chelants, preferably selected from the group comprising carboxylate chelants, amino carboxylate chelants, amino phosphonate chelants, and mixtures thereof. Preferably the chelants are selected from the group consisting of MGDA (methylglycine-N,N-diacetic acid), GLDA (glutamic-N,N-diacetic acid), and mixtures thereof.

Adjunct Ingredients

[0095] The detergent composition herein may optionally comprise a number of other adjunct ingredients such as builders (e.g., preferably citrate), cleaning solvents, cleaning amines, conditioning polymers, cleaning polymers, surface modifying polymers, soil flocculating polymers, structurants, emollients, humectants, skin rejuvenating actives, enzymes, carboxylic acids, scrubbing particles, bleach and bleach activators, perfumes, malodor control agents, pigments, dyes, opacifiers, beads, pearlescent particles, microcapsules, inorganic cations such as alkaline earth metals such as Ca/Mg-ions, antibacterial agents, preservatives, viscosity adjusters (e.g., salt such as NaCl, and other mono-, di- and trivalent salts) and pH adjusters and buffering means (e.g., carboxylic acids such as citric acid, HCl, NaOH, KOH, alkanolamines, phosphoric and sulfonic acids, carbonates such as sodium carbonates, bicarbonates, sesquicarbonates, borates, silicates, phosphates, imidazole and alike).

Method of Washing

[0096] The present invention includes a method of manually washing soiled articles, preferably dishware, comprising the step of: delivering a composition of the invention into a volume of water to form a wash solution and immersing the soiled articles in the wash solution, wherein the soil on the soiled articles comprise at least one fatty acid, preferably at least one unsaturated fatty acid selected from the group consisting of: mono unsaturated fatty acids, di unsaturated fatty acids, tri unsaturated fatty acids, tetra unsaturated fatty acids, penta unsaturated fatty acids, hexa unsaturated fatty acids, and mixtures thereof. Preferred unsaturated fatty acids include: myristoleic acid, palmitoleic acid, sapienic acid, oleic acid, elaidic acid, vaccenic acid, linoleic acid, linoelaidic acid, .alpha.-linolenic acid, .gamma.-linolenic acid, gadoleic acid, .alpha.-eleostearic acid, .beta.-eleostearic acid, ricinoleic acid, eicosenic acid, arachidonic acid, eicosapentaenoic acid, erucic acid, docosadienoic acid, docosahexaenoic acid, tetracosenoic acid, and mixtures thereof, more preferably palmitoleic acid, oleic acid, linoleic acid, .alpha.-linolenic acid, .gamma.-linolenic acid, and mixtures thereof, more preferably oleic acid.

[0097] Preferably the resultant hydroperoxy fatty acids formed from the conversion reaction of the fatty acids with the hydroperoxy fatty acid producing enzymes, or of the hydroperoxy fatty acid producing domain of the fatty acid processing fusion enzyme, are selected from the group consisting of 8R-hydroxyperoxy fatty acids, 8S-hydroxyperoxy fatty acids, 9R-hydroperoxy fatty acids, 9S-hydroperoxy fatty acids, 10R-hydroperoxy fatty acids, 11R-hydroperoxy fatty acids, 11S-hydroperoxy fatty acids, 12R-hydroperoxy fatty acids, 12S-hydroperoxy fatty acids, 13R-hydroperoxy fatty acids, 13S-hydroperoxy fatty acids, 14R-hydroperoxy fatty acids, 14S-hydroperoxy fatty acids, 15S-hydroperoxy fatty acids, their derivatives, and mixtures thereof; preferably unsaturated 8R-hydroperoxy fatty acids, unsaturated 8S-hydroperoxy fatty acids, unsaturated 9R-hydroperoxy fatty acids, unsaturated 10R-hydroperoxy fatty acids, their derivatives, and mixtures thereof.

[0098] The derivatives of hydroperoxy fatty acids formed from the conversion of hydroperoxy fatty acids by the hydroperoxy fatty acid converting enzymes, or of the hydroperoxy fatty acid converting domain of the fusion enzyme, preferably can be selected from the group consisting of monohydroxy fatty acids, dihydroxy fatty acids, epoxy fatty acids, oxo fatty acids, divinyl ether fatty acids, alkenals, aldehydes, epoxy alcohols, and mixtures thereof, preferably dihydroxy fatty acids.

[0099] Preferably each of the hydroperoxy fatty acid producing enzymes, and hydroperoxy fatty acid converting enzymes, are present at a concentration of from 0.005 ppm to 15 ppm, preferably from 0.01 ppm to 5 ppm, more preferably from 0.02 ppm to 0.5 ppm, in an aqueous wash liquor during the washing process.

[0100] Alternatively or in addition, the wash liquor can comprise a fatty acid processing fusion enzyme at a concentration of from 0.005 ppm to 15 ppm, preferably from 0.01 ppm to 5 ppm, more preferably from 0.02 ppm to 0.5 ppm, in an aqueous wash liquor during the washing process.

[0101] As such, the composition herein will be applied in its diluted form to the dishware. Soiled surfaces e.g. dishes are contacted with an effective amount, typically from 0.5 mL to 20 mL (per 25 dishes being treated), preferably from 3 mL to 10 mL, of the detergent composition of the present invention, preferably in liquid form, diluted in water. The actual amount of detergent composition used will be based on the judgment of user, and will typically depend upon factors such as the particular product formulation of the composition, including the concentration of active ingredients in the composition, the number of soiled dishes to be cleaned, the degree of soiling on the dishes, and the like. Generally, from 0.01 mL to 150 mL, preferably from 3 mL to 40 mL of a liquid detergent composition of the invention is combined with from 2,000 mL to 20,000 mL, more typically from 5,000 mL to 15,000 mL of water in a sink having a volumetric capacity in the range of from 1,000 mL to 20,000 mL, more typically from 5,000 mL to 15,000 mL. The soiled dishes are immersed in the sink containing the diluted compositions then obtained, where contacting the soiled surface of the dish with a cloth, sponge, or similar article cleans them. The cloth, sponge, or similar article may be immersed in the detergent composition and water mixture prior to being contacted with the dish surface, and is typically contacted with the dish surface for a period of time ranged from 1 to 10 seconds, although the actual time will vary with each application and user. The contacting of cloth, sponge, or similar article to the surface is preferably accompanied by a concurrent scrubbing of the surface.

[0102] Alternatively, the composition of the present invention can be delivered directly onto the dishware or by contacting a cleaning implement (such as a sponge) comprising the composition with the dishware, before cleaning the dishware with the composition in the presence in water, and optionally, rinsing. Such direct application dishwashing methods are particularly beneficial for cleaning greasy dishware, and especially where the grease has been baked on.

[0103] The enzymes described herein can be used to provide increased suds longevity in an aqueous wash liquor comprising soil, wherein the soil comprises fatty acid. The enzymes are preferably comprised in a detergent composition, especially a detergent composition of the present invention, which is used for manually washing dishes.

Test Methods

[0104] The following assays set forth must be used in order that the invention described and claimed herein may be more fully understood.

Test Method 1--Glass Vial Suds Mileage Method

[0105] The objective of the glass vial suds mileage test method is to measure the evolution of suds volume over time generated by a certain solution of detergent composition in the presence of a greasy soil, e.g., olive oil. The steps of the method are as follows:

[0106] 1. Test solutions are prepared by subsequently adding aliquots at room temperature of: a) 10 g of an aqueous detergent solution at specified detergent concentration and water hardness, b) 1.0 g of an aqueous protein (or mixture of proteins) solution at specified concentration and water hardness), and c) 0.11 g of olive oil (Bertolli.RTM., Extra Virgin Olive Oil), into a 40 mL glass vial (dimensions: 95 mm H.times.27.5 mm D). For the reference samples, the protein solutions are substituted with 1.0 mL of demineralized water.

[0107] 2. The test solutions are mixed in the closed test vials by stirring at room temperature for 2 minutes on a magnetic stirring plate (IKA, model # RTC B 5001; VWR magnetic stirrer, catalog #58949-012; 500 RPM), followed by manually shaking for 20 seconds with an upwards downwards movement (about 2 up and down cycles per second, +/-30 cm up and 30 cm down).

[0108] 3. Following the shaking, the test solutions in the closed vials are further stirred on a magnetic stirring plate (IKA, model # RTC B 5001; VWR magnetic stirrer, catalog #58949-012; 500 RPM) for 60 minutes inside a water bath at 46.degree. C. to maintain a constant temperature. The samples are then shaken manually for another 20 seconds as described above and the initial suds heights (H1) are recorded with a ruler.

[0109] 4. The samples are incubated for an additional 30 minutes inside the water bath at 46.degree. C. while stirring (IKA, model # RTC B 5001; VWR magnetic stirrer, catalog #58949-012; 500 RPM), followed by manual shaking for another 20 seconds as described above. The final suds heights (H2) are recorded.

[0110] 5. Protein solutions that produce larger suds heights (H1 and H2), preferably combined with lower drops in suds height between H1 and H2, are more desirable.

Test Method 2--Small Sink Suds Mileage Method

[0111] The evolution of the suds volume generated by a solution of a liquid detergent composition can be determined while adding soil loads periodically as follows. An aliquot of 500 mL of solution of the liquid detergent composition in 15 dH hard water (final concentration of 0.12 w %, initial temperature 46.degree. C.) is added into a cylindrical container (dimensions: 150 mm D.times.150 mm H). The container is incubated in a water bath during the test to maintain the temperature of the solution between 46.degree. C. and 40.degree. C. An initial suds volume is generated in the container by mechanical agitation at 135 rpm for 120 seconds with a paddle (dimensions: 50 mm.times.25 mm) positioned in the middle of the container.

[0112] Then, an aliquot of 0.5 mL of greasy soil (composition: see Table 3, 0.5 mL) is dosed into the solution using a 20-mL syringe and an automated pump (KDS Legato 110 Single Syringe 1/W Pump), while the paddle rotates into the solution at 135 rpm for 14 seconds. After mixing, the solution is incubated for 166 additional seconds before the next cycle. The soil injecting, paddling, and incubation steps are repeated every 180 seconds until the end-point is reached and the amount of soil additions needed is recorded. The end-point occurs when a clear suds-free ring that circles the impeller at least half way around is observed two or more consecutive times. The complete process is repeated a number of times and the average of the number of additions for all the replicates is calculated for each liquid detergent composition.

[0113] Finally, the suds mileage index is then calculated as: (average number of soil additions for test liquid detergent composition)/(average number of soil additions for reference liquid detergent composition).times.100. Pending on the test purpose the skilled person could choose to select an alternative water hardness, solution temperature, product concentration or soil type.

TABLE-US-00003 TABLE 3 Greasy Soil Composition Ingredient Weight % Crisco oil 12.730 Crisco shortening 27.752 Lard 7.638 Refined Rendered Edible Beef Tallow 51.684 Oleic Acid, 90% (Techn) 0.139 Palmitic Acid, 99+% 0.036 Stearic Acid, 99+% 0.021

Test Method 3--Large Sink Suds Mileage Method

[0114] The evolution of the suds volume generated by a solution of a detergent composition can be determined while adding soil loads periodically as follows. A stream of hard water (15 dH) fills a sink (cylinder dimensions: 300 mm D.times.288 mm H) to 4 L with a constant pressure of 4 bar. Simultaneously, an aliquot of the detergent composition (final concentration 0.12 w %) is dispensed through a pipette with a flow rate of 0.67 mL/sec at a height of 37 cm above the bottom of the sink surface. An initial suds volume is generated in the sink due to the pressure of the water. The temperature of the solution is maintained at 46.degree. C. during the test.

[0115] After recording the initial suds volume (average suds height.times.sink surface area), a fixed amount of greasy soil (composition: see Table 3, 4 mL) is injected in the middle of the sink, while a paddle (dimensions: 10 cm.times.5 cm, positioned in the middle of the sink at the air liquid interface at an angle of 45 degrees) rotates 20 times into the solution at 85 rpm. This step is followed immediately by another measurement of the total suds volume. The soil injecting, paddling, and measuring steps are repeated until the measured suds volume reaches a minimum level, which is set at 400 cm.sup.3. The amount of soil additions needed to get to that level is recorded. The complete process is repeated a number of times and the average of the number of additions for all the replicates is calculated for each detergent composition.

[0116] Finally, the suds mileage index is then calculated as: (average number of soil additions for test detergent composition)/(average number of soil additions for reference detergent composition).times.100.

[0117] Pending on the test purpose the skilled person could choose to select an alternative water hardness, solution temperature, product concentration or soil type.

EXAMPLES

[0118] The following examples are provided to further illustrate the present invention and are not to be construed as limitations of the present invention, as many variations of the present invention are possible without departing from its spirit or scope.

Example 1a--Pseudomonas aeruginosa Strain 42A2 10S-DOX

[0119] Pseudomonas aeruginosa 10S-DOX (SEQ ID NO: 18) is a hydroperoxy fatty acid producing enzyme (oleate 10S-lipoxygenase, EC 1.13.11.77) that converts unsaturated fatty acids (e.g. oleic acid and linoleic acid) into the corresponding hydroperoxylated materials and that is included as part of the current invention. A codon optimized gene (SEQ ID NO: 55) encoding for a P. aeruginosa strain 42A2 10S-DOX variant, including an N-terminal amino acid sequence containing a His-tag, a MBP tag and a TEV protease cleavage site (SEQ ID NO: 56), is designed and synthesized. After gene synthesis, the protein is expressed and purified by Genscript (Piscataway, N.J.). In brief, the complete synthetic gene sequence is subcloned into a pET28a vector for heterologous expression. Escherichia coli BL21 (DE3) cells are transformed with the recombinant plasmid and a single colony is inoculated into LB medium containing kanamycin. Cultures are incubated at 15.degree. C. for 16 h at 200 rpm and isopropyl .beta.-D-1-thiogalactopyranoside (IPTG) is added (final concentration 1 mM) to induce protein expression. Cells are harvested by centrifugation and the pellets are lysed by sonication. After centrifugation, the supernatant is collected and the protein is purified by one-step purification using a nickel affinity column and standard protocols known in the art. The protein is stored in a buffer containing 50 mM Tris-HCl, 150 mM NaCl, and 10% Glycerol at pH 8.0. The final protein concentration is 0.12 mg/mL as determined by Bradford protein assay with BSA as a standard (ThermoFisher, catalog #23236).

Example 1b--Nostoc punctiforme HPL

[0120] Nostoc punctiforme HPL (SEQ ID NO: 40) is an enzyme (hydroperoxide lyase, EC 4.2.1.92) that converts hydroperoxide fatty acids (e.g. 10S-hydroperoxy linoleate) into smaller fatty acids and alcohols and that is included as part of the current invention. A codon optimized gene (SEQ ID NO: 62) encoding for a N. punctiforme HPL variant, including an N-terminal amino acid sequence containing a His-tag, a MBP tag and a TEV protease cleavage site (SEQ ID NO: 63), is designed and synthesized. After gene synthesis, the protein is expressed and purified by Genscript (Piscataway, N.J.). In brief, the complete synthetic gene sequence is subcloned into a pET28a vector for heterologous expression. Escherichia coli BL21 (DE3) cells are transformed with the recombinant plasmid and a single colony is inoculated into TB medium containing kanamycin at 37.degree. C. When the OD600 reaches about 0.8-1.0, protein expression is induced by adding isopropyl .beta.-D-1-thiogalactopyranoside (IPTG) (final concentration 0.1 mM) and 6-aminolevulinic acid (final concentration 0.25 mM). Cultures are incubated at 16.degree. C. for 16 h at 200 rpm. Cells are harvested by centrifugation and the pellets are lysed by sonication. After centrifugation, the supernatant is collected and the protein is purified by two-step purification using nickel affinity columns and standard protocols known in the art. The protein is stored in 1.times.PBS buffer (pH 7.4) containing 10% Glycerol. The final protein concentration is 1.58 mg/mL as determined by Bradford protein assay with BSA as a standard (ThermoFisher, catalog #23236) and purity of about 75% as estimated by densitometric analysis of the Coomassie Blue-stained SDS-PAGE gel under reducing condition.

Example 1c--Hydroperoxy Fatty Acid Producing & Converting Enzymes Detergent Compositions

[0121] The evolution of suds volume generated by a certain solution of detergent composition in presence of a soil, i.e., olive oil or greasy soil, is followed under specific conditions (e.g., water hardness, solution temperature, detergent concentrations, etc.). The following solutions are prepared:

[0122] A. Hard water (15 dH): 0.75 g MgCl.sub.2.6H.sub.2O (Sigma-Aldrich, catalog # M9272), 2.10 g CaCl.sub.2.6H.sub.2O (Sigma-Aldrich, catalog #21108), and 0.689 g NaHCO.sub.3 (Sigma-Aldrich, catalog #31437) are dissolved in 5 L of demineralized water.

[0123] B. Detergent solution of a control reference detergent composition ("solution DG-R") is prepared using Fairy Dark Green, as commercially available in the UK in February 2017, diluted in hard water (15 dH) prepared as above, at targeted detergent concentration of 0.12%.

[0124] C. Protein solutions: Proteins are diluted in demineralized water to the required concentration before proceeding with the suds mileage method.

[0125] D. Greasy soil: A grease soil is prepared according to the composition described in Table 3.

Example 2: Exemplary Manual Dish-Washing Detergent Compositions

[0126] Manual dish-washing detergent compositions comprising: a) the hydroperoxy fatty acid producing enzyme Pseudomonas aeruginosa strain 42A2 10S-DOX (SEQ ID NO: 18) and b) the hydroperoxy fatty acid converting enzyme(s) Pseudomonas aeruginosa strain 42A2 7,10-DS/HP-isomerase (SEQ ID NO: 38) or Nostoc punctiforme HPL_(SEQ ID NO: 40) according to the invention are shown in Table 5. The enzymes can be produced following the protocols described on Examples 1a and 1b or similar procedures described in the art (Estupinan, M., et al. (2015)). PLoS One 10(7): e0131462/0131461-e0131462/0131420).

TABLE-US-00004 TABLE 5 Detergent Compositions Ingredient Wt % Wt % Sodium alkyl ethoxy sulfate (C1213EO0.6S) 22.91% 22.91% n-C12-14 Di Methyl Amine Oxide 7.64% 7.64% Lutensol .RTM. XP80 (non-ionic 0.45% 0.45% surfactant supplied by BASF) Sodium Chloride 1.2% 1.2% Poly Propylene Glycol (MW 2000) .sup. 1% .sup. 1% Ethanol .sup. 2% .sup. 2% Sodium Hydroxide 0.24% 0.24% Pseudomonas aeruginosa strain 42A2 0.1% 0.1% 10S-DOX (SEQ ID NO: 18) Pseudomonas aeruginosa strain 42A2 0.1% 0.0% 7,10-DS/HP-isomerase (SEQ ID NO: 38) Nostoc punctiforme HPL 0.0% 0.1% (SEQ ID NO: 40) Minors (perfume, preservative, dye) + To 100% To 100% water pH (@ 10% solution) 9 9

Example 3a--Fusarium oxysporum 9S-DOX-AOS

[0127] Fusarium oxysporum 9S-DOX-AOS (SEQ ID NO: 48) is fusion enzyme that contains an N-terminal DOX domain (linoleate or oleate lipoxygenase) and a C-terminal AOS domain (allene oxide synthase EC 4.2.1.92) and that converts unsaturated fatty acids (e.g. linoleate) to hydroperoxy fatty acids (e.g. 9S-hydroperoxy linoleate) and subsequently to allene oxides. This enzyme is included as part of the current invention. A codon optimized gene (SEQ ID NO: 64) encoding for a Fusarium oxysporum 9S-DOX-AOS, including an N-terminal amino acid sequence containing a His-tag (SEQ ID NO: 65), is designed and synthesized. After gene synthesis, the protein is expressed and purified by Genscript (Piscataway, N.J.). In brief, the complete synthetic gene sequence is subcloned into a pET30a vector for heterologous expression. Escherichia coli BL21 (DE3) cells are transformed with the recombinant plasmid and a single colony is inoculated into LB medium containing kanamycin at 37.degree. C. When the OD600 reaches about 0.8-1.0, protein expression is induced by adding isopropyl .beta.-D-1-thiogalactopyranoside (IPTG) (final concentration 0.1 mM) and 6-aminolevulinic acid (final concentration 0.25 mM). Cultures are incubated at 16.degree. C. for 16 h at 200 rpm. Cells are harvested by centrifugation and the pellets are lysed by sonication. After centrifugation, the supernatant is collected and the protein is purified by one-step purification using a nickel affinity column and standard protocols known in the art. The protein is stored in 1.times.PBS buffer (pH 8.0) containing 10% Glycerol. The final protein concentration is 0.50 mg/mL as determined by Bradford protein assay with BSA as a standard (ThermoFisher, catalog #23236) and purity of about 80% as estimated by densitometric analysis of the Coomassie Blue-stained SDS-PAGE gel under reducing condition.

Example 3b--Magnaporthe oryzae 10R-DOX-EAS

[0128] Magnaporthe oryzae 10R-DOX-EAS (SEQ ID NO: 52) is fusion enzyme that contains an N-terminal DOX domain (linoleate or oleate lipoxygenase) and a C-terminal EAS domain (epoxy alcohol synthase) and that converts unsaturated fatty acids (e.g. linoleate) to hydroperoxy fatty acids (e.g. 10R-hydroperoxy linoleate) and subsequently to epoxy alcohols. This enzyme is included as part of the current invention. A codon optimized gene (SEQ ID NO: 66) encoding for a Magnaporthe oryzae 10R-DOX-EAS, including an N-terminal amino acid sequence containing a His-tag, a MBP tag and a TEV protease cleavage site (SEQ ID NO: 67), is designed and synthesized. After gene synthesis, the protein is expressed and purified by Genscript (Piscataway, N.J.). In brief, the complete synthetic gene sequence is subcloned into a pET28a vector for heterologous expression. Escherichia coli BL21 (DE3) cells are transformed with the recombinant plasmid and a single colony is inoculated into 2.times.YT medium containing kanamycin at 37.degree. C. When the OD600 reaches about 0.8-1.0, protein expression is induced by adding isopropyl .beta.-D-1-thiogalactopyranoside (IPTG) (final concentration 0.1 mM) and 6-aminolevulinic acid (final concentration 0.25 mM). Cultures are incubated at 16.degree. C. for 16 h at 200 rpm. Cells are harvested by centrifugation and the pellets are lysed by sonication. After centrifugation, the supernatant is collected and the protein is purified by two-step purification using a nickel affinity column, a Superdex 200 column, and standard protocols known in the art. The protein is stored in 1.times.PBS buffer (pH 7.4) containing 10% Glycerol. The final protein concentration is 0.63 mg/mL as determined by Bradford protein assay with BSA as a standard (ThermoFisher, catalog #23236) and purity of about 45% as estimated by densitometric analysis of the Coomassie Blue-stained SDS-PAGE gel under reducing condition.

Example 3c--Fatty Acid Processing Fusion Enzyme Comprising Detergent Compositions

[0129] The evolution of suds volume generated by a certain solution of detergent composition in presence of a soil, i.e., olive oil or greasy soil, is followed under specific conditions (e.g., water hardness, solution temperature, detergent concentrations, etc.). The following solutions are prepared:

[0130] E. Hard water (15 dH): 0.75 g MgCl.sub.2.6H.sub.2O (Sigma-Aldrich, catalog # M9272), 2.10 g CaCl.sub.2.6H.sub.2O (Sigma-Aldrich, catalog #21108), and 0.689 g NaHCO.sub.3 (Sigma-Aldrich, catalog #31437) are dissolved in 5 L of demineralized water.

[0131] F. Detergent solution of a control reference detergent composition ("solution DG-R") is prepared using Fairy Dark Green, as commercially available in the UK in February 2017, diluted in hard water (15 dH) prepared as above, at targeted detergent concentration of 0.12%.

[0132] G. Protein solutions: Proteins are diluted in demineralized water to the required concentration before proceeding with the suds mileage method.

[0133] H. Greasy soil: A grease soil is prepared according to the composition described in Table 3.

Example 4--Suds Mileage of Fatty Acid Processing Fusion Enzymes

[0134] Inventive Composition A is an example of a liquid detergent composition according to the present invention, made with a) detergent solution DG-R (prepared as described in Example 3c) and b) diluted samples of purified Fusarium oxysporum 9S-DOX-AOS (prepared as described in Example 3a).

[0135] Inventive Composition B is an example of a liquid detergent composition according to the present invention, made with a) detergent solution DG-R (prepared as described in Example 3c) and b) diluted samples of purified Magnaporthe oryzae 10R-DOX-EAS (prepared as described in Example 3b).

[0136] Comparative Composition C contains the same detergent solution DG-R in the absence of the respective fusion enzymes.

[0137] The compositions were tested using the small sink suds mileage method (Test Method 2), as described in the test methods section. The results are shown in Table 4.

TABLE-US-00005 TABLE 4 Suds Mileage Fatty Acid Processing Suds Fusion Enzyme Concentration Mileage in the Composition [ppm] Index Inventive Composition A 1.2 125 Inventive Composition B 1.2 132 Comparative Composition C 0.0 100

[0138] The results in Table 4 confirm that Inventive Compositions A and B comprising both, a fatty acid processing fusion enzyme domain according to the invention, have a superior suds profile over the entire washing process as single variably compared to Comparative Composition C lacking the fatty acid processing fusion enzymes according to the invention.

Example 5: Exemplary Manual Dish-Washing Detergent Composition

[0139] A manual dish-washing detergent composition comprising Fusarium oxysporum 9S-DOX-AOS (SEQ ID NO: 48) according to the invention is shown in Table 7. The enzyme can be produced as described on Example 3a.

TABLE-US-00006 TABLE 7 Detergent Compositions Ingredient Wt % Sodium alkyl ethoxy sulfate (C1213EO0.6S) 22.91% n-C12-14 Di Methyl Amine Oxide 7.64% Lutensol .RTM. XP80 (non-ionic surfactant supplied by BASF) 0.45% Sodium Chloride 1.2% Poly Propylene Glycol (MW 2000) 1% Ethanol 2% Sodium Hydroxide 0.24% Fusarium oxysporum 9S-DOX-AOS (SEQ ID NO: 48) 0.1% Minors (perfume, preservative, dye) + water To 100% pH (@ 10% solution) 9

Example 6: Exemplary Manual Dish-Washing Detergent Composition

[0140] A manual dish-washing detergent composition comprising Magnaporthe oryzae 10R-DOX-EAS (SEQ ID NO: 52) according to the invention is shown in Table 8. The enzyme can be produced as described on Example 3b.

TABLE-US-00007 TABLE 8 Detergent Compositions Ingredient Wt % Sodium alkyl ethoxy sulfate (C1213EO0.6S) 22.91% n-C12-14 Di Methyl Amine Oxide 7.64% Lutensol .RTM. XP80 (non-ionic surfactant supplied by BASF) 0.45% Sodium Chloride 1.2% Poly Propylene Glycol (MW 2000) 1% Ethanol 2% Sodium Hydroxide 0.24% Magnaporthe oryzae 10R-DOX-EAS (SEQ ID NO: 52) 0.1% Minors (perfume, preservative, dye) + water To 100% pH (@ 10% solution) 9

[0141] All percentages and ratios given for enzymes are based on active protein. All percentages and ratios herein are calculated by weight unless otherwise indicated. All percentages and ratios are calculated based on the total composition unless otherwise indicated.

[0142] It should be understood that every maximum numerical limitation given throughout this specification includes every lower numerical limitation, as if such lower numerical limitations were expressly written herein. Every minimum numerical limitation given throughout this specification will include every higher numerical limitation, as if such higher numerical limitations were expressly written herein. Every numerical range given throughout this specification will include every narrower numerical range that falls within such broader numerical range, as if such narrower numerical ranges were all expressly written herein.

[0143] The dimensions and values disclosed herein are not to be understood as being strictly limited to the exact numerical values recited. Instead, unless otherwise specified, each such dimension is intended to mean both the recited value and a functionally equivalent range surrounding that value. For example, a dimension disclosed as "40 mm" is intended to mean "about 40 mm."

Sequence CWU 1

1

6711165PRTGaeumannomyces graminis 1Met Thr Val Ser Thr His His Asp Asp Ser Pro Gly Leu Ser Gly Arg1 5 10 15Leu Arg Asp Leu Leu His His Val Phe Gly Asn Gln Lys Ser Pro Thr 20 25 30Val Tyr Pro Asn Ala Pro Gly Asn Ser Ala Lys Pro Val Pro Thr Gly 35 40 45Leu Ala Asp Asp Ile Asp Lys Leu Gly Phe Lys Asp Ile Asp Thr Leu 50 55 60Leu Ile Phe Leu Asn Ser Ala Val Lys Gly Val Asn Asp Asp Gln Gln65 70 75 80Phe Leu Leu Glu Lys Met Ile Gln Leu Leu Ala Lys Leu Pro Pro Ala 85 90 95Ser Arg Glu Gly Lys Lys Leu Thr Asp Gly Leu Ile Asn Asp Leu Trp 100 105 110Asp Ser Leu Asp His Pro Pro Val Ala Ser Leu Gly Lys Gly Phe Ser 115 120 125Phe Arg Glu Pro Asp Gly Ser Asn Asn Asn Ile His Leu Pro Ser Leu 130 135 140Gly Ala Ala Asn Thr Pro Tyr Ala Arg Ser Thr Lys Pro Leu Val Phe145 150 155 160Gln Asn Pro Asn Pro Pro Asp Pro Ala Thr Ile Phe Asp Thr Leu Met 165 170 175Val Arg Asp Pro Ala Lys Phe Arg Pro His Pro Asn Lys Ile Ser Ser 180 185 190Met Leu Phe Tyr Leu Ala Thr Ile Ile Thr His Asp Ile Phe Gln Thr 195 200 205Ser Pro Arg Asp Phe Asn Ile Asn Leu Thr Ser Ser Tyr Leu Asp Leu 210 215 220Ser Pro Leu Tyr Gly Arg Asn His Asp Glu Gln Met Ala Val Arg Thr225 230 235 240Gly Lys Asp Gly Leu Leu Lys Pro Asp Thr Phe Ser Ser Lys Arg Val 245 250 255Ile Gly Phe Pro Pro Gly Val Gly Ala Phe Leu Ile Met Phe Asn Arg 260 265 270Phe His Asn Tyr Val Val Thr Gln Leu Ala Lys Ile Asn Glu Gly Gly 275 280 285Arg Phe Lys Arg Pro Thr Thr Pro Asp Asp Thr Ala Gly Trp Glu Thr 290 295 300Tyr Asp Asn Ser Leu Phe Gln Thr Gly Arg Leu Ile Thr Cys Gly Leu305 310 315 320Tyr Ile Asn Ile Val Leu Gly Asp Tyr Val Arg Thr Ile Leu Asn Leu 325 330 335Asn Arg Ala Asn Thr Thr Trp Asn Leu Asp Pro Arg Thr Lys Glu Gly 340 345 350Lys Ser Leu Leu Ser Lys Pro Thr Pro Glu Ala Val Gly Asn Gln Val 355 360 365Ser Val Glu Phe Asn Leu Ile Tyr Arg Trp His Cys Thr Ile Ser Glu 370 375 380Arg Asp Asp Lys Trp Thr Thr Asn Ala Met Arg Glu Ala Leu Gly Gly385 390 395 400Gln Asp Pro Ala Thr Ala Lys Met Glu Asp Val Met Arg Ala Leu Gly 405 410 415Met Phe Glu Lys Asn Ile Pro Asp Glu Pro Glu Lys Arg Thr Leu Ala 420 425 430Gly Leu Thr Arg Gln Ser Asp Gly Ala Phe Asp Asp Thr Glu Leu Val 435 440 445Lys Ile Leu Gln Glu Ser Ile Glu Asp Val Ala Gly Ala Phe Gly Pro 450 455 460Asn His Val Pro Ala Cys Met Arg Ala Ile Glu Ile Leu Gly Ile Lys465 470 475 480Gln Ser Arg Thr Trp Asn Val Ala Thr Leu Asn Glu Phe Arg Gln Phe 485 490 495Ile Gly Leu Thr Pro His Asp Ser Phe Tyr His Met Asn Pro Asp Pro 500 505 510Lys Ile Cys Lys Ile Leu Ala Gln Met Tyr Asp Ser Pro Asp Ala Val 515 520 525Glu Leu Tyr Pro Gly Ile Met Ala Glu Ala Ala Lys Pro Pro Phe Ser 530 535 540Pro Gly Ser Gly Leu Cys Pro Pro Tyr Thr Thr Ser Arg Ala Ile Leu545 550 555 560Ser Asp Ala Val Ser Leu Val Arg Gly Asp Arg Phe Tyr Thr Val Asp 565 570 575Tyr Thr Pro Arg Asn Ile Thr Asn Trp Gly Phe Asn Glu Ala Ser Thr 580 585 590Asp Lys Ala Val Asp Trp Gly His Val Ile Tyr Lys Leu Phe Phe Arg 595 600 605Ala Phe Pro Asn His Phe Leu Pro Asn Ser Val Tyr Ala His Phe Pro 610 615 620Phe Val Val Pro Ser Glu Asn Lys Leu Ile Phe Glu Gly Leu Gly Ala625 630 635 640Ala Asn Lys Tyr Ser Trp Asp Pro Pro Lys Ala Arg Ala Pro Ile Gln 645 650 655Phe Ile Arg Ser His Lys Ala Val Leu Glu Val Leu Ser Asn Gln Lys 660 665 670Asp Tyr Lys Val Thr Trp Gly Pro Ala Ile Lys Met Leu Ser Gly Asp 675 680 685Pro Ala Thr Ser Phe Ala Leu Ala Gly Asp Glu Pro Ala Asn Ala Ala 690 695 700Ser Arg His His Val Ile Ala Ala Leu Thr Ala Pro Lys Gln Trp Arg705 710 715 720Asp Glu Val Arg Arg Phe Tyr Glu Val Thr Thr Arg Asp Leu Leu Arg 725 730 735Arg His Gly Ala Pro Val His Gly Val Gly Ala Gly Pro Arg Thr His 740 745 750Glu Val Asp Val Ile Arg Asp Val Ile Gly Leu Ala His Ala Arg Phe 755 760 765Met Ala Ser Leu Phe Ser Leu Pro Leu Lys Glu Glu Gly Lys Glu Glu 770 775 780Gly Ala Tyr Gly Glu His Glu Leu Tyr Arg Ser Leu Val Thr Ile Phe785 790 795 800Ala Ala Ile Phe Trp Asp Ser Asp Val Cys Asn Ser Leu Lys Leu His 805 810 815Gln Ala Ser Lys Ala Ala Ala Asp Lys Met Ser Ala Leu Ile Ala Glu 820 825 830His Val Arg Glu Met Glu Ala Gly Thr Gly Phe Leu Gly Ala Leu Gly 835 840 845Lys Leu Lys Asp Leu Ile Thr Gly Asn Asp Val His Ala Asn Gly Asn 850 855 860Gly Val Tyr Thr Asn Gly Asn Gly Val Tyr Thr Asn Gly Asn Gly Val865 870 875 880His Thr Asn Gly Asn Gly Val His Thr Asn Gly Asn Gly Val Pro His 885 890 895Ala Ala Pro Ser Leu Arg Ser Phe Gly Asp Gln Leu Leu Gln Arg Met 900 905 910Leu Ser Gln Asp Gly Arg Ser Ile Glu Glu Thr Val Ser Gly Thr Ile 915 920 925Leu Pro Val Val Met Ala Gly Thr Ala Asn Gln Thr Gln Leu Leu Ala 930 935 940Gln Cys Leu Asp Tyr Tyr Leu Gly Val Gly Glu Lys His Leu Pro Glu945 950 955 960Met Lys Arg Leu Ala Met Leu Asn Thr Ser Glu Ala Asp Glu Lys Leu 965 970 975Leu Lys Tyr Thr Met Glu Gly Cys Arg Ile Arg Gly Cys Val Ala Leu 980 985 990Tyr Arg Ala Val Val Thr Asp Gln Ala Val Asp Asp Thr Ile Pro Cys 995 1000 1005Ile Pro Asn Lys Asp Asp Pro Thr Phe Ala Arg Pro Leu Ser Asn 1010 1015 1020Pro Gln Val Ala Glu Ser Ala Arg Thr Leu Lys Leu Ser Thr Gly 1025 1030 1035Thr Arg Met Leu Val Asp Leu Thr Thr Ala Ser His Asp Pro Ala 1040 1045 1050Ala Phe Pro Asp Pro Asp Glu Val Arg Leu Asp Arg Pro Leu Glu 1055 1060 1065Ser Tyr Val His Phe Gly Leu Gly Pro His Arg Cys Ala Gly Glu 1070 1075 1080Pro Ile Ser Gln Ile Ala Leu Ser Ser Val Met Lys Val Leu Leu 1085 1090 1095Gln Leu Asp Gly Leu Arg Arg Ala Ala Gly Pro Arg Gly Glu Ile 1100 1105 1110Arg Ser Tyr Pro Ala Ser Gln Trp Pro Gly Gln Ala Gly Arg Pro 1115 1120 1125Pro Arg Asp Pro Ala Trp Ser Gly Leu Arg Thr Phe Thr Ser Ala 1130 1135 1140Asp Gln Ser Ala Phe Ser Pro Leu Ala Thr Thr Met Lys Ile Asn 1145 1150 1155Trp Glu Gly Arg Gly Asp Leu 1160 11652773PRTNostoc sp. PCC7120 2Met Asp Leu Asn Thr Tyr Leu Lys Leu Leu Asn Leu Leu Asp Ser Glu1 5 10 15Ser Gln Lys Ile Met Leu Glu Leu Gln Ala Met Phe Ser Ala Ala Gly 20 25 30Leu Ala Leu Arg Gly Arg Gly Thr His Thr Asp Gly Ile Ile Val Lys 35 40 45Gly Asn Leu Thr Val Leu His Ser Ser Asp Val Pro Ser His Ser Leu 50 55 60Phe Thr Pro Gly Lys Lys Tyr Asp Val Ile Phe Arg His Ala Asn Ile65 70 75 80Val Gly Gly Ala Lys Asp Asp Ala Leu Ile Asn Gly Arg Gly Ser Ala 85 90 95Ile Arg Ile Gly Asn Ile Gly Asp Asp Leu Ser Lys Pro Arg Leu Leu 100 105 110Asp Leu Val Leu Asn Thr Gly Glu Val Phe Gly Leu Pro Thr Ala Arg 115 120 125Leu Tyr His Gln Phe Phe Gly Ser Asp Phe His Gln Lys Ser Asp Met 130 135 140Leu Ala Ser Gly Ser Leu Arg Arg Tyr Ala Val Glu Ala Ala Leu Arg145 150 155 160Asn Pro Asp Ser Phe Thr Glu Leu Tyr Tyr His Thr Gln Leu Cys Tyr 165 170 175Glu Trp Val Asp Ser Lys Lys Lys Ser Arg Tyr Ala Arg Phe Arg Leu 180 185 190Leu Asn Pro Asn Gln Ser Thr Glu Gly Gly Leu Leu Asp Asp Ser Val 195 200 205Glu Ile Gly Pro Arg Leu Val Leu Pro Arg Lys Arg Gly Asp Thr Arg 210 215 220Glu Lys Asn Tyr Leu Arg Asn Glu Phe Arg Gln Arg Leu Thr Asp Gly225 230 235 240Asn Ile Val Glu Tyr Val Leu Gln Ala Gln Phe Arg Ser Ile Glu Asp 245 250 255Val Ala Val Asp Cys Ser Asn Ile Trp Asp Pro Asn Thr Tyr Pro Trp 260 265 270Leu Asp Ile Ala Ala Ile Val Leu Asn Gln Asp Glu Ser Glu Asn Asp 275 280 285Tyr Tyr Gln Glu Ile Ala Tyr Asn Pro Gly Asn Thr His Tyr Asp Leu 290 295 300Lys Leu Pro Asn Ser Tyr Ser Val Asp Asp Phe Ala Ser Leu Gly Val305 310 315 320Ser Gly Ala Leu Val His Tyr Phe Gly Ser Ile Val Arg Ala Glu Arg 325 330 335Thr Gln Tyr Leu Tyr Gly Ser Lys Asp Asp Leu Pro Gly Lys Pro Val 340 345 350Tyr Phe Pro Leu Pro Val Thr Glu Ile Pro Ser Lys Arg Phe Leu Phe 355 360 365Leu Leu Glu Lys Tyr Asn Phe Leu Thr Asp Asn Ser Tyr Pro Ser Asp 370 375 380Gly Glu His Asp Lys Ile Glu Ala Leu Val Ser Ala Met Pro Thr Thr385 390 395 400Ala Leu Asp Leu Ala Val Gly Thr Thr Asp Pro Thr Asp Ile Pro Asp 405 410 415Ser Tyr Phe Leu Glu Arg Arg Leu Asn Gly Tyr Asn Pro Gly Ala Ile 420 425 430Arg Glu Ser Ser Gly Gln Glu Gly Trp Thr His Glu Leu Thr His Asn 435 440 445Leu Ala Lys Tyr Asp Ile Lys Pro Gly Leu His Phe Pro Asp Phe Val 450 455 460Gln Cys Arg Leu Phe Val Asp Lys Gln Asn Gly Val Lys Leu His Ser465 470 475 480Ile Lys Ile Asp Asp His Glu Ile Thr Pro Cys Gln Glu Gln Trp Gln 485 490 495Tyr Ala Lys Arg Thr Tyr Leu Gln Ala Glu Phe Leu Ser Gln Glu Leu 500 505 510Lys Leu His Leu Ala Arg Cys His Phe Asn Ile Glu Gln Tyr Val Met 515 520 525Ala Ile Lys Arg Arg Leu Ala Pro Thr His Pro Val Arg Ala Phe Ile 530 535 540Asn Pro His Leu Glu Gly Leu Ile Phe Ile Asn Ser Ser Ala Val Pro545 550 555 560Lys Ile Ile Gly Ser Thr Gly Phe Ile Pro Ile Ala Ser Met Leu Thr 565 570 575Gln Gly Ser Ile Val Asp Val Met Lys Asn Glu Leu Ser Lys Leu Ser 580 585 590Tyr Met Trp Asn Pro Ile Ala Asp Leu Pro Arg Asp Ile Pro Gly Asp 595 600 605Leu Phe Thr Pro Ala Ala Thr Ala Tyr Trp Glu Leu Leu Asn Asn Tyr 610 615 620Val Glu Gln Gly Leu Leu Gln Pro Phe Glu Asp Glu Leu Arg Thr Glu625 630 635 640Val Asn Ala Ile Gln Val Asp Glu Leu Phe Ala Glu Leu Lys Glu Arg 645 650 655Ser Leu Tyr Ser Gly Asp Gln Pro Pro Lys Tyr Asp Ser Ser Glu Leu 660 665 670Lys Ser Leu Leu Met Tyr Ile Ile Tyr His Ser Ser Phe Leu His Ser 675 680 685Trp Ala Asn Phe Lys Gln Tyr Asp Asp Ala Gly Asn Pro Asn His Val 690 695 700Ser Met Gly Asp Tyr Ser Gln Tyr Asp Gln Gln Thr Gln Asp Lys Ile705 710 715 720Arg Phe Ser Gln Arg Ser Leu Thr Trp Val Leu Ser Ser Ile Arg Tyr 725 730 735Asn Ser Val Ala Val Tyr Gly Ser Asp Leu Leu Lys Gln Leu Ile Arg 740 745 750Glu Lys Ser Ser Ile Leu Glu Pro Gly Leu Pro Leu Glu Asp Leu Met 755 760 765Met Ser Ile Asn Ile 7703805PRTAcaryochloris marina 3Met Asp Ser Arg Asp Pro Arg Thr Glu His Val Asp Asp Glu Phe Lys1 5 10 15Lys Leu Ile Ser Asn Ile Ala Arg Ala Phe Gly Arg Thr Ala Gln Ile 20 25 30Lys Gly Arg Arg Ala Thr His Ser Tyr Gly Thr Val Ala Lys Gly Val 35 40 45Leu Lys Val Leu Asp Thr Leu Asp Ile Pro Gln His Gln Ile Phe Ser 50 55 60Ala Gly Lys Gln Tyr Pro Val Leu Leu Arg His Ala Asn Ile Lys Gly65 70 75 80Phe Arg Asp Asp Ala Ile Leu Asp Gly Arg Gly Ala Thr Val Arg Val 85 90 95Leu Ala Gly Asp Ala Gln Ala Pro Leu Ser Asp Leu Asn Leu Asp Glu 100 105 110Gly Ile Val Asp Ile Leu Met Ser Thr Gly Arg Ser Phe Ile Leu Ala 115 120 125Glu Ala Leu Ser Phe Ala Arg Trp Ala Ala Gly Pro Met Lys Ser Arg 130 135 140Ala Ala Met Leu Gln Glu Phe Pro Lys Ile Ala Pro Ile Phe His Glu145 150 155 160Ile Ile Arg Asp Pro Asp Ser Tyr Thr Gln Leu His Tyr Tyr Ser Glu 165 170 175Thr Thr Tyr Ser Phe Thr Ser Leu Asn Gln Gln Ser Phe Phe Leu Arg 180 185 190Tyr Arg Leu Val Asn Arg Gln Asn Pro Ser Ala Asp Thr Gly Trp Leu 195 200 205Lys Pro Glu Glu Val Lys Leu Pro Leu Asp Tyr Leu Pro Arg Val Ala 210 215 220Ser Asp Thr Arg Pro Glu Thr Tyr Leu Gln Asp Asp Phe Arg Gln Gln225 230 235 240Val Arg Ser Thr Gly Val Ser Tyr Leu Leu Gln Ile Gln Leu Gln Pro 245 250 255Val Ser Asp Asp Ala Ala Met Asn Glu Thr Ala Lys Asp Cys Thr Ile 260 265 270Pro Trp Glu Glu Glu Asp His Pro Phe His Asp Val Ala Val Leu Asp 275 280 285Leu Gly Ser Ile Leu Pro Asp Glu Leu Ala Glu Ala Leu Glu Phe Asn 290 295 300Pro Tyr Asn Ala Pro Pro Glu Leu Ser Leu Ile Leu Ala Lys Thr Ala305 310 315 320Arg Glu Thr Ala Ser Val Asn His Leu Arg Ser Val Val Tyr Gln Ile 325 330 335Ser Ala Asn Met Arg Lys Tyr Gln Thr Pro Ser Ser Ser Leu Val Asp 340 345 350Trp Gly Ser Gly His Gln Pro Ser Leu Pro Glu Gln Tyr Pro Tyr Gly 355 360 365Thr Gly Lys Thr Pro Ser Phe Asp Asn Thr Lys Pro Leu Pro Ala Arg 370 375 380Val Lys Pro Lys Pro Arg Tyr Trp Ala Asn Phe Gly Leu Lys Leu Ile385 390 395 400Pro Asn Gln Gln Leu Asp Pro Asp Leu Pro Glu Leu Gly Ile Thr Gly 405 410 415Ala Leu Asp Leu Met Gly Thr Ser Val Val Ser Tyr Met Pro Pro Asn 420 425 430Leu Thr Arg Thr Arg Leu Asp Lys Phe Ser Asp Asp Phe Phe Val Glu 435 440 445Arg Arg Leu Asn Gly Phe Asn Pro Gly Lys Leu Asn Arg Val Thr Gly 450 455 460His Ala Trp Gln Tyr Gln Val Cys Tyr Asp Cys Ser Lys His Gln Val465 470 475 480Glu Pro Ala Gly Ile Leu Pro Thr Lys Ile Thr Ala Arg Phe Asn Phe 485 490 495Cys Gly Gln Tyr Leu His Pro His Ser Ile Gln Phe Thr Leu Asn Gly 500 505 510Gln Thr Glu Thr Gln Gln Pro Gly Asp Glu Asn Trp Glu Trp

Ser Lys 515 520 525Arg Leu Phe Arg Cys Ala Glu Phe Val Phe Gln Glu Ala Gln Ser His 530 535 540Leu Gly Arg Thr His Met Asn Leu Asp Gln Tyr Ala Met Ala Tyr Tyr545 550 555 560Arg Asn Val Val Asn Asn Pro Ile Arg Leu Leu Leu Glu Pro His Leu 565 570 575Glu Gly Leu Leu Ser Ile Asn Lys Leu Gly Ala Asn Leu Ile Ser Gly 580 585 590Pro Thr Gly Phe Ile Pro Glu Ala Ser Ser Leu Thr Pro Glu Ser Val 595 600 605Asp Asp Val Leu Lys Asp Glu Ile Ser His Leu Ser Tyr His Trp Thr 610 615 620Pro His Arg Gln Thr Leu Pro Asp Arg Val Leu Asn Asn His Tyr Asp625 630 635 640Pro Ala Ala Ile Ala Met Trp Asn Leu Leu Thr Gln Tyr Val Arg Glu 645 650 655Phe Phe Glu Asp His Gln Ala Gly Met Glu Glu Tyr Trp Ser Glu Ile 660 665 670Gln Ala Met Ser His Asp Leu Val Thr His Ser Ile Leu Lys Pro Glu 675 680 685Leu Gly Thr Leu Ala Val Gln Asn Asn Ala Asp Leu Gln Gln Leu Cys 690 695 700Val Tyr Val Ile Phe Leu Ser Ser Phe Phe His Ser Trp Val Asn Asn705 710 715 720Lys Gln Tyr Glu Asp Gly Gly Asp Val Ser Tyr Ser Thr Ile Gly Leu 725 730 735Trp Asp Thr Arg His Pro Lys Tyr Asp Pro Leu Arg Val Ala Glu Arg 740 745 750Glu Ala Lys Gln Val Thr Leu Leu Trp Thr Leu Ser His Val Arg Tyr 755 760 765Asn Pro Ile Met Asp Val Gly Pro Thr Ala Leu Lys Asn Leu Leu Trp 770 775 780Gln Gln Arg Gln His Ile Glu Pro Gly Ile Pro Leu Ala Asn Leu Met785 790 795 800Met Ser Thr Asn Ile 8054862PRTAvena sativa 4Met Leu Leu Gly Gly Leu Ile Asp Asn Leu Thr Gly Ala Asn Lys His1 5 10 15Ala Arg Leu Lys Gly Thr Val Val Leu Met Arg Lys Asn Val Leu Asp 20 25 30Leu Asn Asp Phe Gly Ala Thr Ile Ile Asp Gly Val Ser Glu Phe Leu 35 40 45Gly Lys Gly Val Thr Cys Gln Leu Ile Ser Ser Thr Val Val Asp Asn 50 55 60Asn Asn Gly Asn Arg Gly Lys Val Gly Ala Glu Ala Gly Leu Glu Gln65 70 75 80Trp Leu Thr Ser Leu Pro Ser Leu Thr Thr Gly Glu Ser Lys Phe Gly 85 90 95Leu Thr Phe Asp Trp Glu Val Asp Lys Leu Gly Val Pro Gly Ala Ile 100 105 110Val Val Asn Asn Tyr His Ser Ala Gln Phe Phe Leu Lys Thr Ile Thr 115 120 125Leu Asp Asp Val Pro Gly Arg Ala Gly Lys Leu Thr Phe Val Ala Asn 130 135 140Ser Trp Ile Tyr Pro Ala Glu Lys Tyr Arg Tyr Asn Arg Val Phe Phe145 150 155 160Ala Asn Asp Thr Tyr Leu Pro Ser Gln Met Pro Ala Ala Leu Lys Pro 165 170 175Tyr Arg Asp Asp Glu Leu Arg Asn Leu Arg Gly Asp Asp Gln Gln Gly 180 185 190Pro Tyr Glu Glu His Asp Arg Val Tyr Arg Tyr Asp Val Tyr Asn Asp 195 200 205Leu Gly Glu Asp Arg Pro Val Leu Gly Gly Thr Ala Asp His Pro Tyr 210 215 220Pro Arg Arg Gly Arg Thr Gly Arg Lys Pro Asn Pro Asn Asp Pro Ser225 230 235 240Leu Glu Ser Arg Leu Ser Leu Leu Glu Gln Ile Tyr Val Pro Arg Asp 245 250 255Glu Lys Phe Gly His Leu Lys Met Ser Asp Phe Leu Gly Tyr Ser Ile 260 265 270Lys Ala Ile Thr Gln Gly Ile Leu Pro Ala Val Arg Thr Tyr Val Asp 275 280 285Cys Thr Pro Gly Glu Phe Asp Ser Phe Gln Asp Ile Ile Asn Leu Tyr 290 295 300Glu Gly Gly Ile Lys Leu Pro Lys Ile Ala Ala Leu Glu Glu Leu Arg305 310 315 320Lys Arg Phe Pro Phe Gln Leu Leu Lys Asp Leu Leu Pro Val Gly Gly 325 330 335Asp Phe Leu Leu Lys Leu Pro Leu Pro His Ile Ile Lys Glu Asp Lys 340 345 350Gln Ala Trp Arg Thr Asp Glu Glu Phe Ala Arg Glu Val Leu Ala Gly 355 360 365Val Asn Pro Val Met Ile Thr Arg Leu Thr Glu Phe Pro Pro Lys Ser 370 375 380Thr Leu Asp Pro Ser Lys Tyr Gly Asp His Thr Ser Thr Ile Thr Ala385 390 395 400Ala His Ile Glu Lys Asn Leu Glu Gly Leu Thr Val Gln Gln Ala Leu 405 410 415Glu Gly Asn Lys Leu Tyr Ile Leu Asp His His Asp Arg Phe Met Pro 420 425 430Phe Leu Ile Asp Val Asn Asn Leu Asp Gly Asn Phe Ile Tyr Ala Thr 435 440 445Arg Thr Leu Phe Phe Leu Arg Gly Asp Gly Arg Leu Thr Pro Leu Ala 450 455 460Ile Glu Leu Ser Glu Pro Phe Ile Gln Asp Gly Leu Thr Thr Ala Lys465 470 475 480Ser Lys Val Tyr Thr Pro Val Pro Ser Gly Ser Val Glu Gly Trp Val 485 490 495Trp Glu Leu Ala Lys Ala Tyr Val Ala Val Gly Asp Ser Gly Trp His 500 505 510Gln Leu Val Ser His Trp Leu Asn Thr His Ala Val Met Glu Pro Phe 515 520 525Val Ile Ala Thr Asn Arg Gln Leu Ser Val Thr His Pro Val His Lys 530 535 540Leu Leu Ser Pro His Tyr Arg Asp Thr Met Thr Ile Asn Ala Leu Ala545 550 555 560Arg Gln Thr Leu Ile Asn Ala Gly Gly Ile Phe Glu Met Thr Val Phe 565 570 575Pro Gly Lys Phe Ala Leu Gly Met Ser Ser Val Val Tyr Lys Asp Trp 580 585 590Asn Phe Ala Glu Gln Gly Leu Pro Asp Asp Leu Leu Arg Arg Gly Val 595 600 605Ala Val Pro Asp Pro Ser Ser Pro Tyr Lys Val Arg Leu Leu Ile Glu 610 615 620Asp Tyr Pro Tyr Ala Ala Asp Gly Leu Ala Ile Trp His Ala Ile Glu625 630 635 640Gln Tyr Val Thr Glu Tyr Leu Ala Ile Tyr Tyr Pro Asp Asp Ala Val 645 650 655Leu Gln Asp Asp Val Glu Leu Gln Ala Trp Trp Lys Glu Ala Arg Glu 660 665 670Val Gly His Gly Asp Leu Lys Asp Ala Pro Trp Trp Pro Ser Met Gln 675 680 685Thr Val Ala Glu Leu Ala Lys Ser Cys Ala Thr Ile Ile Trp Ile Ala 690 695 700Ser Ala Leu His Ala Ala Val Asn Phe Gly Gln Tyr Pro Tyr Ala Gly705 710 715 720Tyr Leu Pro Asn Arg Pro Thr Val Ser Arg Arg Arg Met Pro Glu Pro 725 730 735Gly Thr Gln Glu Tyr Ala Glu Leu Glu Arg Asp Pro Glu Arg Ala Phe 740 745 750Ile His Thr Ile Thr Ser Gln Ile Gln Thr Ile Ile Gly Ile Ser Leu 755 760 765Leu Glu Val Leu Ser Lys His Ser Ser Asp Glu Leu Tyr Leu Gly Gln 770 775 780Arg Asp Thr Pro Glu Trp Thr Ser Asp Pro Lys Ala Leu Ala Val Phe785 790 795 800Gln Arg Phe Ser Asp Arg Leu Val Asp Ile Glu Ser Lys Val Val Gly 805 810 815Met Asn His Asp Pro Gln Leu Lys Asn Arg Asn Gly Pro Ala Lys Leu 820 825 830Pro Tyr Met Leu Leu Tyr Pro Asn Thr Ser Asp Arg Lys Gly Asp Ala 835 840 845Ala Gly Leu Thr Ala Lys Gly Ile Pro Asn Ser Ile Ser Ile 850 855 8605863PRTOryza sativa 5Met Leu Gly Gly Leu Lys Asp Lys Leu Thr Gly Lys Asn Gly Asn Lys1 5 10 15Ile Lys Gly Leu Ala Val Leu Met Ser Arg Lys Leu Leu Asp Pro Arg 20 25 30Asp Phe Thr Ala Ser Leu Leu Asp Asn Val His Glu Val Phe Gly Asn 35 40 45Ser Ile Thr Cys Gln Leu Val Ser Ala Thr Val Ala Asp Gln Asn Asn 50 55 60Glu Gly Arg Gly Ile Val Gly Ser Glu Ala Asn Leu Glu Gln Gly Leu65 70 75 80Thr Asp Leu Pro Ser Val Ser Gln Gly Glu Ser Lys Leu Thr Val Arg 85 90 95Phe Asn Trp Glu Met Asp Lys His Gly Val Pro Gly Ala Ile Ile Ile 100 105 110Lys Asn His His Ser Thr Lys Phe Phe Leu Lys Thr Ile Thr Leu His 115 120 125Asp Val Pro Gly Cys Asp Thr Ile Val Phe Val Ala Asn Ser Trp Ile 130 135 140Tyr Pro Val Gly Lys Tyr His Tyr Asn Arg Ile Phe Phe Ala Asn Asn145 150 155 160Ser Tyr Leu Pro Ser Gln Met Pro Glu Ala Leu Arg Pro Tyr Arg Glu 165 170 175Asp Glu Leu Arg Tyr Leu Arg Gly Glu Asp Arg Gln Gly Pro Tyr Gln 180 185 190Glu His Asp Arg Ile Tyr Arg Tyr Asp Val Tyr Asn Asp Leu Gly Glu 195 200 205Pro Asp Arg Asp Asn Pro Arg Pro Val Leu Gly Gly Ser Gln Lys His 210 215 220Pro Tyr Pro Arg Arg Gly Arg Thr Gly Arg Ile Pro Thr Lys Lys Asp225 230 235 240Pro Asn Ser Glu Ser Arg Leu Ser Leu Leu Glu Gln Ile Tyr Val Pro 245 250 255Ser Asp Glu Arg Phe Ala His Leu Lys Met Ser Asp Phe Ala Gly Tyr 260 265 270Ser Ile Lys Ala Ile Val Gln Gly Ile Leu Pro Ala Ile Arg Thr Tyr 275 280 285Val Asp Leu Thr Pro Gly Glu Phe Asp Ser Phe Glu Asp Ile Leu Lys 290 295 300Leu Tyr Arg Gly Gly Leu Lys Leu Pro Ser Ile Pro Ala Leu Glu Glu305 310 315 320Leu Arg Lys Ser Phe Pro Val Gln Leu Ile Lys Asp Leu Leu Pro Val 325 330 335Gly Gly Ser Tyr Leu Leu Lys Phe Pro Lys Pro Asp Ile Ile Lys Glu 340 345 350Asn Glu Val Ala Trp Arg Thr Asp Glu Glu Phe Ala Arg Glu Ile Leu 355 360 365Ala Gly Leu Asn Pro Met Val Ile Arg Arg Leu Thr Glu Phe Pro Pro 370 375 380Lys Ser Thr Leu Asp Pro Ser Lys Tyr Gly Asp Gln Thr Ser Thr Ile385 390 395 400Thr Pro Ala His Ile Glu Lys Asn Leu Glu Gly Leu Ser Val Gln Gln 405 410 415Ala Leu Asp Ser Asn Arg Leu Tyr Ile Leu Asp His His Asp His Phe 420 425 430Met Pro Phe Leu Ile Asp Ile Asn Ser Leu Asp Gly Ile Phe Thr Tyr 435 440 445Ala Thr Arg Thr Leu Leu Phe Leu Arg Asp Asp Asp Thr Leu Lys Pro 450 455 460Leu Ala Ile Glu Leu Ser Leu Pro His Ile Glu Gly Asn Leu Thr Ser465 470 475 480Ala Lys Ser Lys Val His Thr Pro Ala Ser Ser Gly Ile Glu Ser Trp 485 490 495Val Trp Gln Leu Ala Lys Ala Tyr Val Ala Val Asn Asp Ser Gly Trp 500 505 510His Gln Leu Ile Ser His Trp Leu Asn Thr His Ala Val Met Glu Pro 515 520 525Phe Val Ile Ala Thr Asn Arg Gln Leu Ser Val Thr His Pro Val Tyr 530 535 540Lys Leu Leu Gln Pro His Tyr Arg Asp Thr Met Thr Ile Asn Ala Leu545 550 555 560Ala Arg Gln Thr Leu Ile Asn Gly Gly Gly Ile Phe Glu Gln Thr Val 565 570 575Phe Pro Gly Lys His Ala Leu Ala Met Ser Ser Ala Val Tyr Lys Asn 580 585 590Trp Asn Phe Thr Glu Gln Gly Leu Pro Asp Asp Leu Ile Lys Arg Gly 595 600 605Ile Ala Ile Lys Asp Pro Ser Ser Pro Ser Lys Val Lys Leu Leu Ile 610 615 620Lys Asp Tyr Pro Tyr Ala Thr Asp Gly Leu Ala Ile Trp Gln Ala Ile625 630 635 640Glu Gln Trp Val Thr Glu Tyr Cys Ala Ile Tyr Tyr Pro Asn Asp Gly 645 650 655Val Leu Gln Gly Asp Val Glu Leu Gln Ala Trp Trp Lys Glu Val Arg 660 665 670Glu Val Gly His Gly Asp Leu Lys Asp Ala Asp Trp Trp Pro Lys Met 675 680 685Gln Ser Leu Pro Glu Leu Thr Lys Ala Cys Thr Thr Ile Ile Trp Ile 690 695 700Ala Ser Ala Leu His Ala Ala Val Asn Phe Gly Gln Tyr Pro Tyr Ala705 710 715 720Gly Tyr Leu Pro Asn Arg Pro Thr Ile Ser Arg Arg Pro Met Pro Glu 725 730 735Pro Gly Ser Lys Glu Tyr Thr Glu Leu Asp Glu Asn Pro Glu Lys Phe 740 745 750Phe Ile Arg Thr Ile Thr Ser Gln Phe Gln Thr Ile Leu Gly Val Ser 755 760 765Leu Ile Glu Ile Leu Ser Lys His Ser Ala Asp Glu Ile Tyr Leu Gly 770 775 780Gln Arg Asp Thr Pro Glu Trp Thr Ser Asp Pro Lys Ala Leu Glu Ala785 790 795 800Phe Lys Arg Phe Ser Arg Gln Leu Val Glu Ile Glu Ser Lys Val Leu 805 810 815Asn Met Asn Lys Asp Pro Leu Leu Lys Asn Arg Val Gly Pro Ala Asn 820 825 830Phe Pro Tyr Thr Leu Met Phe Pro Asn Thr Ser Asp Asn Lys Gly Ala 835 840 845Ala Glu Gly Ile Thr Ala Arg Gly Ile Pro Asn Ser Ile Ser Ile 850 855 8606619PRTMagnaporthe oryzae 6Met Arg Val Leu Val Trp Ile Ala Gly Leu Ala Pro Leu Ala Val Ala1 5 10 15Val Pro Ser Ser Ser Tyr Arg Val Ala Val Ala Ala Arg Ala Asp Asn 20 25 30Thr Ser Ala Ser Val Ala Pro Ser Gln Asn Val Ser Gly Ala Ala Pro 35 40 45Pro Glu Leu Val Val Tyr Thr Leu Pro Cys Glu Asp Gly Asn Ser Thr 50 55 60Ala Arg Thr Ala Glu Ile Arg Leu Lys Gln Ala Thr Leu Leu Tyr Gly65 70 75 80Pro Ser Leu Leu Gly Asn Ala Ser Tyr Phe Pro Gly Gly Pro Leu Gly 85 90 95Asp Ala Ile Ser Leu Arg Asp Gln Thr Val Trp Glu Gly Ala Ala Val 100 105 110Val Gln Ser Leu Arg Ala Phe Thr Asp Ala Ala Lys Val Ala Ala Asn 115 120 125Ile Lys Gln Asn Gly Gly Leu Asn Ser Leu Asp Asp Phe Lys Val Leu 130 135 140Tyr Gln Asp Gly Trp Lys Gly Ser Val Pro Gln Gly Ile Ala Arg Gly145 150 155 160Gln Ser Glu Asn Tyr Thr Ser Asp Leu Leu Phe Ser Met Glu Arg Leu 165 170 175Ser Val Asn Pro Tyr Ile Leu Lys Arg Leu His Pro Thr Glu Asp Ala 180 185 190Leu Pro Phe Gln Val Asp Arg Ala Thr Val Lys Gln Leu Thr Lys Thr 195 200 205Ser Leu Lys Ala Leu His Ala Ala Gly Arg Leu Phe Val Ala Asp His 210 215 220Ser Tyr Gln Arg Asn Tyr Thr Arg Leu Ala Asn Arg Tyr Ser Ala Ala225 230 235 240Cys Thr Ala Leu Phe Tyr Leu Asp Pro Arg Ser Asn Gln Phe Leu Pro 245 250 255Leu Ala Ile Lys Thr Asn Val Gly Ala Asp Leu Thr Tyr Thr Pro Leu 260 265 270Asp Thr Asp Asn Asn Asn Trp Leu Leu Ala Lys Ile Met Phe Asn Asn 275 280 285Asn Asp Leu Phe His Gly Gln Ile Phe His Val Ala Tyr Pro His Ala 290 295 300Ile Ala Glu Ile Val His Leu Ala Ala Leu Arg Thr Met Ser Ala Arg305 310 315 320His Pro Val Leu Ala Leu Met Glu Arg Leu Met Tyr Gln Ala Tyr Ala 325 330 335Val Arg Pro Leu Gly Glu Arg Val Leu Phe Asn Lys Gly Gly Leu Phe 340 345 350Glu Gln Asn Phe Ala Tyr Pro Gln Asp Met Val Tyr Lys Phe Val Gly 355 360 365Asp Ser Tyr Pro Thr Thr Gly Arg Trp Arg Ala Gly Tyr Leu Asp Thr 370 375 380Asp Val Arg Ala Arg Gly Leu Val Asp Ala Asp Tyr Gly Pro Glu Leu385 390 395 400Pro His Phe Pro Phe Tyr Glu Asp Gly Ser Arg Leu Val Glu Val Ile 405 410 415Arg Arg Phe Val Arg Ser Phe Val Asp Ala Thr Tyr His Glu Ser Asp 420 425 430Glu Met Val Ala Lys Asp Ala Glu Leu Gln Ala Trp Val Ala Glu Ala 435 440 445Asn Gly Pro Ala Gly Val Glu Asp Phe Glu Pro Gly Pro Leu Asp Thr 450

455 460Arg Glu Arg Leu Val Glu Val Leu Thr His Met Ala Trp Leu Thr Gly465 470 475 480Cys Ala His His Val Leu Asn Gln Gly Glu Pro Val Thr Ala Ser Gly 485 490 495Val Leu Pro Met His Pro Thr Ala Leu Tyr Ala Pro Val Pro Thr Ser 500 505 510Lys Ala Asn Thr Thr Ala Asp Leu Leu Gly Tyr Leu Pro Ser Ala Gln 515 520 525Lys Ser Val Asp Gln Val Thr Leu Leu Ala Arg Phe Asn Arg Pro Asp 530 535 540Val Val Pro Thr Asn Gln Thr Leu Arg Tyr Met Phe Ala Ala Pro Gln545 550 555 560Leu Leu Leu Gly Asn Gly Glu Ala Tyr Arg Arg Ala Asn Gln Arg Phe 565 570 575Val Arg Ala Met Gly Arg Ile Ser Asp Glu Val Lys Ala Arg Arg Phe 580 585 590Asp Asp Arg Gly Leu Ser Gln Gly Met Pro Phe Ile Trp Gln Ala Leu 595 600 605Asp Pro Gly Asn Ile Pro Phe Tyr Leu Ser Val 610 61571121PRTAspergillus fumigatus 7Met Leu Arg Arg Phe Ser Ser Thr Phe Lys Lys Lys Gly Asp Arg Glu1 5 10 15Ser Lys Gln Asn Gly Thr Ala Ser Ser Ser Ser Ala Ala Val Ala Asn 20 25 30Thr Asn Asn Asn Asp Asn Lys Arg His Ser Lys Ile Ser Ala Ala Arg 35 40 45Lys Ser Ser Ser Asp Asp Asp Arg Asn Glu Lys Lys Gly Asn Ser Val 50 55 60Ser Pro Phe Glu Lys Tyr Ala Ser Val Leu His Ala Ser Arg Ser Pro65 70 75 80Ile Pro Asn Gln Thr Gly Asp Gly Ala Tyr Leu Glu His Glu His Thr 85 90 95Thr Ser Leu Leu Gln Asp Ala Arg His Leu Gly Phe Lys Asp Phe Lys 100 105 110Thr Leu Lys Glu Val Ile Glu Ser Lys Leu Pro Gly Gly Gln Leu Ile 115 120 125Asp Asp Lys Thr Met Leu Met Glu Arg Ile Ile Gln Leu Val Ser Arg 130 135 140Leu Pro His Asn Ser Lys His Arg Glu Glu Leu Thr Asn Ala Phe Leu145 150 155 160Thr Glu Leu Trp Asp Ser Leu Pro His Pro Pro Leu Ser Tyr Met Gly 165 170 175Asn Asp Tyr Ala Tyr Arg Ser Ala Asp Gly Ser Asn Asn Asn Pro Thr 180 185 190Leu Pro Arg Leu Gly Ala Ala Asn Thr Leu Tyr Ala Arg Thr Ile Pro 195 200 205Pro Leu Ile Ile Gln Pro Gly Gly Leu Pro Asp Pro Gly Leu Val Phe 210 215 220Asp Thr Leu Phe Ala Arg Gln Thr Phe Lys Pro His Pro Asn Lys Val225 230 235 240Ser Ser Val Phe Phe Tyr Trp Ala Ser Leu Ile Ile His Asp Ile Phe 245 250 255Gln Thr Asp Tyr Lys Asn Pro Asn Met Asn Lys Thr Ser Gly Tyr Leu 260 265 270Asp Leu Ser Ile Leu Tyr Gly Asp Val Gln Glu Glu Gln Asn Leu Ile 275 280 285Arg Thr Phe Lys Asp Gly Lys Leu Lys Pro Asp Ser Phe Ser Glu Pro 290 295 300Arg Leu Gln Ala Phe Pro Ala Thr Cys Cys Val Leu Met Val Met Leu305 310 315 320Asn Arg Phe His Asn Tyr Ala Val Glu Gln Leu Ala Ala Ile Asn Glu 325 330 335Asn Gly Arg Phe Thr Lys Pro Ala Asp Asn Leu Ser Glu Glu Glu Ala 340 345 350Lys Lys Ala Trp Ala Lys Tyr Asp Glu Asp Leu Phe Gln Thr Gly Arg 355 360 365Leu Ile Thr Cys Gly Leu Tyr Ile Asn Ile Thr Leu Tyr Asp Tyr Leu 370 375 380Arg Thr Ile Val Asn Leu Asn Arg Thr Asn Ser Thr Trp Cys Leu Asp385 390 395 400Pro Arg Ala Gln Met Glu Gly Ser His Thr Ala Pro Ser Gly Leu Gly 405 410 415Asn Gln Cys Ser Val Glu Phe Asn Leu Ala Tyr Arg Trp His Ser Ala 420 425 430Thr Ser Ala Thr Asp Glu Lys Trp Thr Glu Asp Val Tyr Glu Arg Leu 435 440 445Met Gly Lys Pro Ala Ser Glu Val Ser Met Thr Glu Leu Leu Met Gly 450 455 460Leu Gly Lys Tyr Gln Ala Glu Leu Pro Lys Asp Pro Ser Lys Arg Thr465 470 475 480Phe Ala Asp Leu Glu Arg Gln Ala Asp Gly Arg Phe Lys Asp Glu Asp 485 490 495Leu Val Asn Leu Leu Val Asn Ala Val Glu Asp Val Ala Gly Ser Phe 500 505 510Gly Ala Arg Asn Val Pro Lys Val Leu Lys Asn Val Glu Ile Leu Gly 515 520 525Ile Ile Gln Ser Arg Lys Trp Asn Val Gly Ser Leu Asn Glu Phe Arg 530 535 540Lys Phe Phe Gly Leu Lys Pro Tyr Glu Thr Phe Glu Glu Ile Asn Ser545 550 555 560Asp Pro Asp Val Ala Glu Ser Leu Arg Ser Leu Tyr Asp His Pro Asp 565 570 575Phe Val Glu Leu Tyr Pro Gly Ile Val Ala Glu Glu Ala Lys Gln Pro 580 585 590Met Val Pro Gly Val Gly Ile Ala Pro Thr Tyr Thr Ile Ser Arg Ala 595 600 605Val Leu Ser Asp Ala Val Ala Leu Val Arg Gly Asp Arg Phe Tyr Thr 610 615 620Ile Asp Tyr Asn Pro Arg Asn Leu Thr Asn Trp Gly Tyr Ser Glu Val625 630 635 640Arg Tyr Asp Leu Ser Ile Asn Gln Gly Cys Ile Phe Tyr Lys Leu Ala 645 650 655Thr Arg Ala Phe Pro Asn Trp Phe Lys Pro Asp Ser Ile Tyr Ala His 660 665 670Tyr Pro Met Thr Ile Pro Ser Glu Asn Arg Lys Ile Met Lys Asp Leu 675 680 685Gly Arg Glu Ile His Tyr Ser Trp Asp Arg Pro Gln Tyr Thr Pro Pro 690 695 700Arg Val Asp Leu Val Ser Tyr Ser Asn Ala Lys Leu Val Ala Glu Gln705 710 715 720Gln Asn Gln Phe Arg Ala Ala Trp Gly Asp Thr Val Glu Phe Val Phe 725 730 735Gly Lys Ala Ser Lys Glu Phe Lys Leu Tyr Gln Asp Ser Ala Phe Ile 740 745 750Gln Lys His Ala Asp Val Met Ser Lys Leu Leu Asn Lys Glu Glu Trp 755 760 765His Arg Ser Val Lys Glu Phe Tyr Glu Asp Ile Thr Ala Lys Leu Leu 770 775 780Glu Asp Lys Thr Arg Arg Phe Gly Gly Ile Asn Gln Val Asp Ile Thr785 790 795 800Asn Asp Val Gly Asn Leu Thr Pro Val Ile Phe Ala Ala Asn Val Phe 805 810 815Ser Leu Pro Leu Lys Ser Lys Glu Asn Pro Arg Gly Ile Tyr Thr Glu 820 825 830His Glu Met Phe Lys Val Leu Ala Ala Leu Tyr Asn Cys Leu Tyr Phe 835 840 845Asp Ile Asp Lys Thr Lys Ser Tyr Pro Leu His His Ala Ser Gln Ala 850 855 860Val Gly Glu Pro Leu Gly Lys Ala Leu Glu Ala Asn Val Lys Ala Leu865 870 875 880Gly Gly Ser Ser Leu Leu Ser Gly Ile Phe Arg Ser Phe Arg Glu Asn 885 890 895Lys Asn Ala Leu Lys Glu Tyr Gly Val His Leu Thr Lys Gln Leu Leu 900 905 910Glu Asn Gly Leu Gly Ala His Glu Ile Ala Trp Ala Gln Phe Leu Pro 915 920 925Thr Val Ile Ala Met Val Pro Ala Gln Ala Gln Ala Phe Thr Gln Ile 930 935 940Val Asp Phe Tyr Leu Ser Lys Glu Gly Ser Lys His Leu Pro Ala Ile945 950 955 960Gln Arg Leu Ala Lys Gln Asp Thr Lys Lys Ser Asp Glu Gln Leu Leu 965 970 975His Tyr Cys Leu Glu Ala Val Arg Leu Asn Asp Met Ser Gly Leu Tyr 980 985 990Arg Gln Ser Glu Thr Thr Leu Ala Val Thr Asp Glu Ala Val Glu Val 995 1000 1005Thr Ile Gln Pro Gly Asp Lys Val Phe Val Ser Phe Ala Lys Ala 1010 1015 1020Asn Arg Asp Ala Ser Val Phe Pro Asp Pro Ala Glu Val Arg Leu 1025 1030 1035Asp Arg Pro Met Asn Ser Tyr Ile Asn Pro Thr Leu Gly Pro His 1040 1045 1050Gly Phe Leu Ser Lys Glu Thr Ser His Ile Ala Leu Thr Ala Met 1055 1060 1065Leu Arg Ala Val Gly Arg Leu Asn Asn Leu Arg Val Ala Pro Gly 1070 1075 1080Val Gln Gly Gln Leu Lys Lys Ile Pro Gln Pro Gly Gly Tyr Ser 1085 1090 1095Ala Tyr Leu Arg Glu Asp His Gly Ser Tyr Ser Ile Phe Pro Thr 1100 1105 1110Thr Phe Arg Val Gln Tyr Asp Ala 1115 112081117PRTAspergillus nidulans 8Met Leu Arg Arg Phe Ser Thr Phe Arg Lys Ser Lys Gly Asp Lys Thr1 5 10 15Glu Lys Ala Asp Arg Asp Ser Lys Ala Asn Gly Ser Asn Ala Asn Ser 20 25 30Ala Ala Ala Ala Ser Asn Ser Ser Lys Arg Gln Ser Lys Val Pro Pro 35 40 45Pro Arg Arg Pro Ser Ser Asp Ser Gly Ser Ser Ala Glu Ser Glu Asp 50 55 60Val Pro Ala Val Phe Glu Lys Tyr Ala Gln Val Leu His Ala Ser Ser65 70 75 80Arg Pro Ile Pro His Gln Gly Gly Glu Ala Ala Tyr Leu Glu Lys Glu 85 90 95His Pro Ser Gly Leu Phe Asn Asp Leu Lys Ser Leu Gly Phe Lys Asp 100 105 110Phe Ala Ser Leu Lys Asp Val Ile Lys Thr Lys Ile Asn Gly Glu Leu 115 120 125Thr Asp Asp Lys Thr Met Ile Met Glu Arg Ile Ile Gln Ile Val Ser 130 135 140Ser Leu Pro Ser Asn Ser Lys Met Arg Val Asp Leu Thr Asn Met Phe145 150 155 160Leu Asp Glu Leu Trp Gly Ser Leu Pro His Pro Pro Leu Ser Tyr Met 165 170 175Gly Asn Asp Tyr Gln Tyr Arg Ser Ala Asp Gly Ser Asn Asn Asn Pro 180 185 190Thr Leu Pro Trp Leu Gly Ala Ala Asn Thr Ala Tyr Ala Arg Ser Ile 195 200 205Glu Pro Leu Thr Val Gln Pro Gly Gly Leu Pro Asp Ala Gly Leu Val 210 215 220Phe Asp Thr Leu Phe Ala Arg Gln Lys Phe Thr Pro His Pro Asn Lys225 230 235 240Val Ser Ser Leu Phe Phe Asp Trp Ala Ser Leu Ile Ile His Asp Ile 245 250 255Phe Gln Thr Asp Tyr Arg Asp Tyr Asn Lys Asn Lys Thr Ser Ala Tyr 260 265 270Leu Asp Leu Ala Ile Leu Tyr Gly Asp Val Gln Glu Glu Gln Asp Leu 275 280 285Val Arg Thr His Lys Asp Gly Lys Leu Lys Pro Asp Ser Phe Ser Glu 290 295 300Pro Arg Leu Gln Ala Phe Pro Ala Ala Cys Cys Val Leu Leu Val Met305 310 315 320Leu Asn Arg Phe His Asn Tyr Val Val Glu Glu Leu Ala Ala Ile Asn 325 330 335Glu Asn Gly Arg Phe Thr Lys Pro Ser Pro Asp Leu Pro Glu Glu Gln 340 345 350Ala Lys Lys Ala Trp Ala Lys Tyr Asp Glu Asp Leu Phe Gln Thr Gly 355 360 365Arg Leu Ile Thr Cys Gly Leu Phe Ile Asn Ile Thr Leu Tyr Asp Tyr 370 375 380Leu Arg Thr Ile Val Asn Leu Asn Arg Val Asn Ser Thr Trp Cys Leu385 390 395 400Asp Pro Arg Ala Gln Met Glu Gly Ser Ala Thr Pro Ala Gly Leu Gly 405 410 415Asn Gln Cys Ser Val Glu Phe Asn Leu Ala Tyr Arg Trp His Ser Ala 420 425 430Ile Ser Ala Asn Asp Glu Lys Trp Thr Glu Lys Val Tyr Glu Glu Leu 435 440 445Ile Gly Lys Pro Gly Ser Glu Ile Ser Thr Gln Glu Leu Leu Met Gly 450 455 460Leu Gly Lys Tyr Gly Ala Ser Leu Pro Lys Asp Pro Ser Gln Arg Thr465 470 475 480Phe Ala Gly Leu Lys Arg Gln Glu Asp Gly Thr Phe Lys Asp Glu Glu 485 490 495Leu Val Asn Ile Leu Thr Ser Ala Ile Glu Asp Val Ala Gly Ser Phe 500 505 510Gly Ala Arg Asn Val Pro Lys Val Leu Lys Ala Val Glu Val Leu Gly 515 520 525Ile Glu Gln Gly Arg Lys Trp Asn Val Gly Ser Leu Asn Glu Phe Arg 530 535 540Lys Phe Phe Gly Leu Lys Asn Tyr Glu Thr Phe Glu Glu Ile Asn Ser545 550 555 560Asp Pro Glu Val Ala Glu Ser Leu Arg Ala Leu Tyr Gly His Pro Asp 565 570 575Tyr Val Glu Leu Tyr Pro Gly Ile Val Ser Glu Glu Ala Lys Glu Pro 580 585 590Met Ile Pro Gly Val Gly Ile Ala Pro Thr Tyr Thr Ile Ser Arg Ala 595 600 605Val Leu Ser Asp Ala Val Ala Leu Val Arg Gly Asp Arg His Tyr Thr 610 615 620Val Asp Tyr Asn Pro Arg Asn Leu Thr Asn Trp Gly Tyr Asn Glu Val625 630 635 640Arg Tyr Asp Leu Asn Ile Asn Gln Gly Cys Val Phe Tyr Lys Leu Ala 645 650 655Thr Arg Ala Phe Pro Asn Trp Phe Lys Pro Asp Ser Ile Tyr Ala His 660 665 670Tyr Pro Met Thr Ile Pro Ser Glu Asn Lys Val Ile Met Lys Asn Leu 675 680 685Gly Arg Glu Ala Asp Tyr Ser Trp Asp Arg Pro Gln Tyr Gln Ala Pro 690 695 700Arg Ala Ser Leu Thr Ser Tyr Ser Asn Val Lys Leu Ile Leu Asp Gln705 710 715 720Gln Lys Asp Phe Arg Val Val Trp Gly Asp Cys Thr Pro Leu His Ser 725 730 735Gly Lys Gly Gly Glu Asp Phe Trp Ser Lys Thr Leu Ser Asp Pro Gln 740 745 750Phe Lys Lys Ser Ile Lys Glu Phe Tyr Glu Lys Thr Thr Leu Glu Leu 755 760 765Phe Ala Asp Lys Ser Val Asn Leu Ala Gly Arg Lys Gln Ile Asp Ile 770 775 780Val Lys Asp Val Gly Asn Ile Val Pro Ala Arg Phe Ala Ser Lys Leu785 790 795 800Leu Ser Leu Pro Leu Arg Ser Lys Glu Asn Ser Lys Gly Val Phe Thr 805 810 815Asp His Glu Ile Phe Met Ala Leu Ala Val Ile Tyr Asn Ala Ile Phe 820 825 830Phe Asp Val Asp Thr Thr Lys Ser Phe Pro Leu Arg Lys Ala Ala Asp 835 840 845Ala Val Ser Lys Glu Leu Gly Lys His Val Glu Ser His Val Lys Ser 850 855 860Val Ser Ser Pro Gly Phe Leu Ser Arg Val Ile Asp Asn Phe Arg Asp865 870 875 880Asp His Asn Ala Leu Lys Asp Leu Gly Asp Gln Leu Ile Lys Arg Leu 885 890 895Ala Glu Gly Gly Leu Ser Val Ser Asp Ile Thr Tyr Gly Gln Ile Leu 900 905 910Pro Thr Ala Val Glu Leu Val His Gly Gln Ala Gln Met Phe Thr Arg 915 920 925Val Val Glu Tyr Tyr Leu Asn Glu Gly Lys Gln His Leu Pro Glu Leu 930 935 940Ser Leu Leu Ala Lys Gln Asp Ser Ala Glu Thr Asp Ala Lys Leu Thr945 950 955 960Arg Tyr Ala Leu Glu Ala Ile Arg Leu Asn Ala Gly Ser Gly Ala Tyr 965 970 975Arg Lys Ala Glu Thr Asn Phe Tyr Phe Lys Glu Gly Asp Ala Asp Ile 980 985 990Asn Leu Lys Pro Gly Asp Glu Ile Phe Ile Ser Ser Thr Gln Ala Asn 995 1000 1005Arg Asp Pro Thr Ala Phe Pro Asp Pro Asp Glu Val Arg Leu Asp 1010 1015 1020Arg Pro Asp Glu Ser Tyr Leu Asn Tyr Gly Ile Gly Ser Gln Ile 1025 1030 1035Gly Leu Gly Lys Asp Ala Thr Leu Thr Ala Val Thr Ala Met Val 1040 1045 1050Arg Ala Ala Phe Ser Leu Glu Gly Leu Arg Pro Ala Pro Gly Val 1055 1060 1065Gln Gly Val Leu Lys Lys Val Val Arg Pro Glu Gly Tyr Thr Leu 1070 1075 1080Tyr Met Arg Glu Asp His Gly Ala Phe Ser Pro Phe Pro Thr Thr 1085 1090 1095Phe Arg Val His Phe Asp Gly Glu Val Val Thr Pro Lys Lys Gln 1100 1105 1110Ile Asp Ser Ala 111591113PRTAspergillus terreus 9Met Leu Arg Arg Phe Ser Thr Gln Phe Lys Lys Ser Lys Gly Asp Arg1 5 10 15Glu Ser Lys Gln Asn Gly Thr Pro Gly Pro Ala Asn Asn Ser Ser Lys 20 25 30Arg Gln Ser Lys Leu Ala Gln Pro Arg Lys Ser Ser Ser Ser Ser Ser 35 40 45Asp Gly Glu Arg Ser Ser Lys Asn Glu Asp Gly Val Pro Ala Phe Glu 50

55 60Lys Tyr Ala Gln Val Leu His Ala Ser Arg Ser Pro Leu Pro Asn Gln65 70 75 80Thr Gly Asp Gly Ala Thr Ser Ala His Asp His Gln Thr Thr Leu Phe 85 90 95Gln Asp Leu Arg Ser Phe Gly Phe Lys Asp Phe Gly Thr Leu Lys Glu 100 105 110Val Ile Ala Thr Lys Ala Lys Gly Glu His Val Asp Asp Lys Thr Met 115 120 125Val Met Glu Arg Ile Ile Gln Leu Val Ser Gly Leu Pro Ala Asn Ser 130 135 140Lys Ser Arg Thr Glu Leu Thr His Leu Phe Leu Asp Gln Leu Trp Asp145 150 155 160Ser Leu Pro His Pro Pro Leu Ser Tyr Met Gly Ser Asp Tyr Ala Tyr 165 170 175Arg Ser Ala Asp Gly Ser Asn Asn Asn Pro Thr Leu Pro Trp Leu Gly 180 185 190Ala Ala Asn Thr Pro Tyr Ala Arg Ser Ile Ala Pro Leu Thr Ile Gln 195 200 205Pro Gly Gly Leu Pro Asp Ala Gly Leu Val Phe Asp Ser Leu Phe Ala 210 215 220Arg Asp Lys Phe Arg Pro His Pro Asn Lys Val Ser Ser Val Phe Phe225 230 235 240Asp Trp Ala Ser Leu Ile Ile His Asp Ile Phe Gln Thr Asp His Gln 245 250 255Asn Pro Asn Ile Asn Lys Thr Ser Gly Tyr Leu Asp Leu Ser Ile Leu 260 265 270Tyr Gly Asp Val Lys Glu Glu Gln Asp Leu Val Arg Thr His Lys Asp 275 280 285Gly Lys Leu Lys Pro Asp Ala Phe Ser Glu Pro Arg Leu Gln Ala Phe 290 295 300Pro Ala Thr Cys Cys Val Leu Leu Val Met Leu Asn Arg Phe His Asn305 310 315 320His Val Val Glu Gln Leu Ala Glu Ile Asn Glu Asn Gly Arg Phe Thr 325 330 335Lys Pro Ser Pro Asp Leu Pro Glu Asp Lys Ala Lys Ala Ala Trp Glu 340 345 350Lys Tyr Asp Glu Asp Leu Phe Gln Thr Gly Arg Leu Ile Thr Cys Gly 355 360 365Leu Tyr Ile Asn Ile Thr Leu Tyr Asp Tyr Leu Arg Thr Ile Val Asn 370 375 380Leu Asn Arg Val Asn Ser Thr Trp Cys Leu Asp Pro Arg Ala Gln Met385 390 395 400Glu Gly Ser Ser Ser Thr Pro Ser Gly Leu Gly Asn Gln Cys Ser Val 405 410 415Glu Phe Asn Leu Ala Tyr Arg Trp His Ser Ala Ile Ser Ala Asn Asp 420 425 430Glu Lys Trp Thr Glu Gln Val Tyr Gln Asp Leu Met Gly Lys Pro Ala 435 440 445Glu Glu Val Ser Val Glu Glu Leu Leu Gly Gly Leu Met Lys Tyr Gly 450 455 460Arg Ser Leu Glu Lys Asp Pro Ser Lys Arg Thr Phe Ala Gly Leu Gln465 470 475 480Arg Gln Ala Asp Gly Thr Phe Lys Asp Glu Glu Leu Val Glu Ile Leu 485 490 495Thr Asn Ala Val Glu Asp Val Ala Gly Ser Phe Gly Ala Arg His Val 500 505 510Pro Lys Ala Leu Lys Ala Val Glu Val Leu Gly Ile Asn Gln Ala Arg 515 520 525Gln Trp Asn Val Gly Ser Leu Asn Glu Phe Arg Lys Phe Phe Asp Leu 530 535 540Lys Pro Tyr Glu Ser Phe Glu Glu Ile Asn Ser Asp Pro Asp Val Ala545 550 555 560Asp Ala Leu Arg Asn Leu Tyr Glu His Pro Asp Tyr Val Glu Leu Tyr 565 570 575Pro Gly Ile Val Ala Glu Glu Ala Lys Glu Pro Met Ile Pro Gly Val 580 585 590Gly Ile Ala Pro Thr Tyr Thr Ile Ser Arg Ala Val Leu Ser Asp Ala 595 600 605Val Ala Leu Val Arg Gly Asp Arg His Tyr Thr Ile Asp Tyr Asn Pro 610 615 620Arg Asn Leu Thr Asn Trp Gly Tyr Asn Glu Cys Arg Tyr Asp Leu Ser625 630 635 640Ile Asn Gln Gly Cys Val Phe Tyr Lys Leu Ala Thr Arg Ala Phe Pro 645 650 655Asn Trp Phe Lys Pro Asp Ser Ile Tyr Ala His Tyr Pro Met Thr Ile 660 665 670Pro Ser Glu Asn Arg Asn Ile Met Lys Asn Leu Gly Arg Glu Ser His 675 680 685Tyr Ser Trp Glu Arg Pro Lys Phe Thr Pro Pro Gln Val Asn Leu Val 690 695 700Ser Tyr Pro Asn Val Lys Leu Ala Leu Glu Gln Glu Lys Gln Leu Arg705 710 715 720Val Ile Trp Ser Gly Asn Thr Pro Leu Arg Pro Ala Lys Gly Gly Asp 725 730 735Asp Phe Trp Ser Lys Ala Leu Asn Asn Asp Glu Trp Arg Lys Asn Ile 740 745 750Lys Glu Phe Tyr Glu Asp Met Thr Ile Lys Leu Leu Asn Glu Lys Ser 755 760 765Cys Lys Leu Gly Gly Ile Arg Gln Ile Asp Ile Thr Arg Asp Leu Gly 770 775 780Asn Leu Ala Pro Val His Phe Ala Ser Lys Val Phe Ser Leu Pro Leu785 790 795 800Lys Thr Lys Gln Asn Ser Lys Gly Val Phe Thr Glu His Glu Met Phe 805 810 815Met Ile Met Ala Val Val Phe Thr Ser Val Phe Phe Asp Val Asp Pro 820 825 830Thr Lys Ser Phe Pro Leu His Phe Ala Ser Arg Ala Val Ser Gln Gln 835 840 845Leu Gly Ser Ala Ile Glu Ser His Val Lys Ser Ile Gly His Pro Gly 850 855 860Phe Leu Ser Ala Ile Ile Asp Ser Phe Arg Asp Asp Asp Asn Val Leu865 870 875 880Lys Glu Tyr Gly Asp Gln Leu Ile Lys Lys Leu Leu Asp Ser Gly Leu 885 890 895Gly Val Ser Asp Val Thr Tyr Ser Gln Ile Leu Pro Thr Ala Val Ser 900 905 910Met Val His Asn Gln Ala Arg Met Phe Thr His Ile Val Asp Tyr Tyr 915 920 925Val Thr Glu Gly Lys Lys His Leu Pro Glu Ile Asn Arg Leu Ala Lys 930 935 940Glu Ser Thr Pro Glu Ala Asp Glu Lys Leu Thr Arg Tyr Cys Leu Glu945 950 955 960Ala Phe Arg Leu Phe Gly Thr Phe Gly Ser Tyr Arg Glu Ala Gln Thr 965 970 975Asp Phe Thr Val Asn Asp Glu Ser Gly Pro Val Asp Ile Lys Gln Gly 980 985 990Asp Lys Val Phe Val Gly Ala Val Lys Ala Asn Arg Asp Pro Ser Val 995 1000 1005Phe Pro Asp Pro Asp Glu Val Arg Leu Asp Arg Pro Leu Asp Ser 1010 1015 1020Tyr Ile Gln Phe Gly Leu Gly Pro His Ala Gly Leu Gly Lys Glu 1025 1030 1035Ala Thr Leu Leu Ala Leu Thr Ala Met Leu Arg Val Val Gly Arg 1040 1045 1050Leu Asp Asn Leu Arg Pro Ala Pro Gly Pro Gln Gly Gln Leu Lys 1055 1060 1065Lys Ile Pro Arg Glu Gly Gly Tyr Tyr Val Tyr Leu Arg Glu Asp 1070 1075 1080Trp Gly Ser Tyr Ser Pro Phe Pro Thr Thr Phe Lys Val His Phe 1085 1090 1095Asp Gly Glu Leu Pro Ala Pro Lys Lys Arg Gly Ile Ala Ser Ala 1100 1105 1110101117PRTAspergillus clavatus 10Met Leu Arg Arg Phe Ser Ser Thr Phe Asn Lys Lys Lys Gly Asp Arg1 5 10 15Glu Pro Lys Gln Asn Gly Val Ala Thr Thr Thr Thr Thr Thr Thr Pro 20 25 30Thr Thr Asn Lys Arg Tyr Ser Lys Val Pro Glu Gly His Lys Ser Ser 35 40 45Ser Glu Glu Glu Arg Asn Glu Lys Lys Gly Gly Ala Val Ser Pro Phe 50 55 60Glu Lys Tyr Ala Ser Val Leu His Ala Ser Arg Thr Pro Ile Pro Asn65 70 75 80Gln Thr Gly Asp Gly Ala Tyr Leu Glu His Glu His Thr Thr Ser Leu 85 90 95Leu Gln Asp Ala Arg His Leu Gly Phe Lys Asp Leu Ala Thr Leu Lys 100 105 110Glu Val Ile Lys Asn Lys Ala Thr Gly Gln Leu Val Asp Asp Lys Thr 115 120 125Met Leu Met Glu Arg Val Ile Gln Leu Val Ser Ser Leu Pro His Asn 130 135 140Ser Lys His Arg Glu Glu Leu Thr His Ser Phe Leu Asp Glu Leu Trp145 150 155 160Gly Ser Leu Pro His Pro Pro Leu Ser Tyr Met Gly Ser Glu Tyr Ala 165 170 175Tyr Arg Ser Ala Asp Gly Ser Asn Asn Asn Pro Thr Leu Pro Trp Leu 180 185 190Gly Ala Ala Asn Thr Ala Tyr Ala Arg Thr Ile Ala Pro Leu Ile Ile 195 200 205Gln Pro Gly Gly Leu Pro Asp Pro Gly Leu Val Phe Asp Thr Leu Phe 210 215 220Ala Arg Gln Ser Phe Lys Pro His Pro Asn Asn Val Ser Ser Leu Phe225 230 235 240Phe Asp Trp Ala Ser Leu Ile Ile His Asp Ile Phe Gln Thr Asp Tyr 245 250 255Arg Asn Pro His Val Asn Lys Thr Ser Gly Tyr Leu Asp Leu Ser Ile 260 265 270Leu Tyr Gly Asp Val Gln Glu Glu Gln Asn Leu Ile Arg Thr Phe Glu 275 280 285Gly Gly Arg Leu Lys Thr Asp Ser Phe Ser Glu Pro Arg Leu Gln Ala 290 295 300Phe Pro Ala Ala Cys Cys Val Leu Leu Val Met Leu Asn Arg Phe His305 310 315 320Asn His Val Val Glu Gln Leu Ala Ala Ile Asn Glu Asn Gly Arg Phe 325 330 335Thr Gln Pro Arg Asp Gly Leu Pro Glu Asp Gln Ala Lys Lys Ala Trp 340 345 350Glu Lys Tyr Asp Glu Asp Leu Phe Gln Thr Gly Arg Leu Ile Thr Cys 355 360 365Gly Leu Tyr Ile Asn Ile Thr Leu Tyr Asp Tyr Leu Arg Thr Ile Val 370 375 380Asn Leu Asn Arg Thr Asn Ser Thr Trp Cys Leu Asp Pro Arg Ala Gln385 390 395 400Met Glu Gly Asn Asn Thr Thr Pro Ser Gly Leu Gly Asn Gln Cys Ser 405 410 415Val Glu Phe Asn Leu Ala Tyr Arg Trp His Ser Ala Ile Ser Ala Asn 420 425 430Asp Glu Lys Trp Thr Glu Lys Ile Tyr Glu Asp Leu Met Gly Lys Pro 435 440 445Ala Ser Glu Val Ser Met Thr Glu Leu Leu Met Gly Leu Gly Lys Tyr 450 455 460Glu Ala Gly Leu Ser Lys Asp Pro Ser Gln Arg Thr Phe Ala Gly Leu465 470 475 480Glu Arg Gln Ala Asp Gly Arg Phe Arg Asp Glu Asp Leu Val Asn Ile 485 490 495Leu Thr Gly Ala Ile Glu Asp Val Ala Gly Ser Phe Gly Ala Arg Asn 500 505 510Val Pro Lys Val Leu Lys Asn Val Glu Val Leu Gly Ile Leu Gln Ser 515 520 525Arg Lys Trp Asn Val Gly Ser Leu Asn Glu Phe Arg Lys Phe Phe Gly 530 535 540Leu Lys Pro Tyr Glu Thr Phe Glu Glu Ile Asn Ser Asp Pro Asp Val545 550 555 560Ala Glu Ser Leu Arg Ser Leu Tyr Asp His Pro Asp Phe Val Glu Leu 565 570 575Tyr Pro Gly Ile Val Ser Glu Glu Ala Lys Glu Pro Met Ile Pro Gly 580 585 590Val Gly Ile Ala Pro Thr Tyr Thr Ile Ser Arg Ala Val Leu Ser Asp 595 600 605Ala Val Ala Leu Val Arg Gly Asp Arg Tyr Tyr Thr Ile Asp Tyr Asn 610 615 620Ala Arg Asn Leu Thr Asn Trp Gly Tyr Ser Glu Val Arg Tyr Asp Leu625 630 635 640Ser Ile Asn Gln Gly Cys Val Phe Tyr Lys Leu Ala Thr Arg Ala Phe 645 650 655Pro Asp Trp Phe Lys Ser Asp Ser Ile Tyr Ala His Tyr Pro Met Thr 660 665 670Ile Pro Ser Glu Asn Arg Lys Ile Met Lys Asn Leu Gly Arg Glu Ala 675 680 685His Tyr Ser Tyr Asp Arg Pro Gln Tyr Ile Pro Pro Pro Val Asp Leu 690 695 700Leu Ser Tyr Pro Ser Ala Lys Leu Val Ala Glu Gln Arg Lys Asp Phe705 710 715 720His Thr Val Trp Ala Asp Thr Val Glu Phe Val Phe Gly Lys Ala Ser 725 730 735Lys Asn Phe Lys Leu Ser Glu Asp Thr Ala Phe Ile Glu Arg Gln Arg 740 745 750Glu Thr Ile Ser Lys Leu Leu Ser Gln Asp Glu Trp Gln Arg Asn Val 755 760 765Lys Glu Phe Tyr Glu Glu Ile Thr Thr Gly Leu Leu Glu Glu Lys Thr 770 775 780Arg Arg Phe Ala Gly Ile Asn Gln Val Asp Ile Thr Arg Asp Ile Gly785 790 795 800Asn Leu Val Pro Val Ile Phe Ala Ser Asn Leu Phe Ser Leu Pro Leu 805 810 815Arg Ser Lys Glu Asn Ser Arg Gly Ile Phe Thr Glu His Glu Met Phe 820 825 830Asn Val Leu Ala Val Leu Tyr Asn Cys Ile Tyr Phe Asp Ile Asp Lys 835 840 845Thr Lys Ser Phe Pro Leu His His Ala Ser Gln Ala Val Gly Glu Gln 850 855 860Leu Gly Lys Ala Val Glu Ala Asn Val Lys Ser Leu Gly Gly Ser Ser865 870 875 880Leu Leu Ser Gly Ile Leu Gly Gly Ser Arg Asp Asn Lys Asn Ala Leu 885 890 895Lys Glu Tyr Gly Ala His Met Thr Lys Gln Leu Leu Glu Asn Gly Leu 900 905 910Gly Ala Ser Glu Ile Thr Trp Ser Gln Ile Leu Pro Thr Val Ile Ala 915 920 925Met Val Pro Ser Gln Ala Gln Ala Phe Thr Gln Ile Ile Asp Phe Tyr 930 935 940Leu Ser Lys Glu Gly Ser Lys Tyr Leu Pro Glu Ile Gln Arg Leu Ala945 950 955 960Arg Glu Glu Ser Lys Glu Ser Asp Glu Gln Leu Leu Arg Tyr Cys Met 965 970 975Glu Ala Ile Arg Leu Asn Lys Thr Ser Gly Ala Tyr Arg Glu Ala Arg 980 985 990Thr Ser Leu Thr Val Thr Glu Glu Thr Gly Gln Val Thr Leu Gln Pro 995 1000 1005Gly Asp Lys Val Phe Val Gly Phe Ala Lys Ala Asn Arg Asp Pro 1010 1015 1020Ser Val Phe Pro Asp Pro Ser Glu Val Arg Leu Asp Arg Pro Leu 1025 1030 1035Asp Ala Tyr Ile Asn His Ser Leu Gly Pro His Gly Phe Leu Ser 1040 1045 1050Lys Glu Thr Ser Gln Ile Ala Leu Thr Ala Met Leu Arg Ala Val 1055 1060 1065Gly Arg Leu Asn Asn Leu Arg Arg Ala Pro Gly Ala Gln Gly Glu 1070 1075 1080Val Lys Lys Val Pro Ile Ala Asp Gly Tyr Ser Ala Tyr Leu Arg 1085 1090 1095Glu Asp His Gly Ser Tyr Ser Val Phe Pro Thr Thr Phe Arg Val 1100 1105 1110His Tyr Asp Val 1115111125PRTPenicillium marneffei 11Met Arg Arg Phe Ser Ser Val Phe Lys Lys Lys Glu Glu Ser Lys Ala1 5 10 15Lys Glu Asn Gly His Ile Ser Glu Lys Val Asn Gly Lys Arg Gln Ser 20 25 30Lys Ala Val Ser Thr Ser Gln Pro Pro Ala Glu Pro Glu Asp His Ser 35 40 45Lys Ala Arg His Glu Val Ser Ala Ile Phe Glu Arg Tyr Ala Gln Val 50 55 60Ile His Ala Ser Arg Gln Pro Leu Pro Thr Gln Ser Gly Asp Gly Thr65 70 75 80Tyr Leu Glu His Gly His Asp His Ser Ser Ser Leu Phe Ser Asp Leu 85 90 95Arg Ser Leu Gly Phe Lys Asp Tyr Gly Thr Leu Val Glu Val Met Lys 100 105 110Asn Lys Ala Ser Gly Ser Tyr Val Asp Asp Lys Thr Met Leu Met Glu 115 120 125Arg Ile Ile Gln Leu Val Ser Gly Leu Pro Ser Asn Ser Glu Arg Arg 130 135 140Thr Glu Leu Thr Asn Ala Phe Leu Asp Glu Leu Trp Asp Ser Leu Pro145 150 155 160His Pro Pro Leu Ser Phe Val Gly Pro Lys Phe Glu Tyr Arg Ser Ala 165 170 175Asp Gly Ser Trp Asn Asn Pro Thr Ile Pro Trp Leu Gly Ala Ala Asn 180 185 190Thr Glu Tyr Ser Arg Ser Ile Pro Pro Leu Thr Ile Gln Pro Ser Gly 195 200 205Leu Pro Asp Ala Gly Leu Val Phe Asp Ser Ile Met Ala Arg Glu Lys 210 215 220Phe Thr Pro His Pro Asn Lys Val Ser Ser Val Phe Phe Ala Trp Ala225 230 235 240Ser Leu Ile Ile His Asp Ile Phe Gln Thr Asp Tyr Arg Asn Pro His 245 250 255Ile Ser Gln Thr Ser Ser Tyr Leu Asp Leu Ser Ile Leu Tyr Gly Asp 260 265 270Asn Gln Asp Asp Gln Asn Gln Met Arg Thr Phe Lys Asp Gly Lys Ile 275 280 285Lys Pro

Asp Ser Phe Ser Glu Pro Arg Leu Gln Ala Phe Pro Ala Met 290 295 300Cys Asn Val Leu Met Val Met Leu Asn Arg Phe His Asn Asn Val Val305 310 315 320Glu Gln Ile Ala Gln Ile Asn Glu Asn Gly Arg Phe Asn Lys Pro Arg 325 330 335Pro Gly Leu Ser Pro Glu Gln Thr Glu Ala Ala Trp Lys Lys Tyr Asp 340 345 350Glu Asp Leu Phe Gln Thr Gly Arg Leu Ile Thr Cys Gly Leu Tyr Ile 355 360 365Asn Ile Thr Leu Tyr Asp Tyr Leu Arg Thr Ile Val Asn Leu Asn Arg 370 375 380Thr Asn Ser Thr Trp Cys Leu Asp Pro Arg Ala Arg Met Gln Gly Thr385 390 395 400His Thr Thr Pro Ser Gly Leu Gly Asn Gln Cys Ser Val Glu Phe Asn 405 410 415Leu Ala Tyr Arg Trp His Ser Ala Thr Ser Tyr Asn Asp Glu Lys Trp 420 425 430Thr Glu Glu Val Tyr Arg Asp Leu Phe Gly Lys Pro Ala Glu Glu Ile 435 440 445Ser Met Pro Glu Leu Leu Met Gly Leu His Lys Tyr Glu Gln Ser Ile 450 455 460Asp Lys Asp Pro Ser Lys Arg Thr Phe Ala Asn Leu Gln Arg Gln Ala465 470 475 480Asp Gly Thr Phe Lys Asp Asp Asp Leu Val Lys Ile Met Thr Ser Ala 485 490 495Val Glu Asp Val Ala Gly Ser Phe Gly Ala Arg Asn Val Pro Lys Val 500 505 510Met Arg Ser Ile Glu Ile Leu Gly Ile Glu Gln Ala Arg Lys Trp Asn 515 520 525Val Gly Ser Leu Asn Glu Phe Arg Lys Phe Phe Asn Leu Lys Pro Tyr 530 535 540Glu Thr Phe Glu Glu Ile Asn Ser Asp Pro Tyr Val Ala Asp Gln Leu545 550 555 560Arg His Leu Tyr Glu His Pro Asp Tyr Val Glu Leu Tyr Pro Gly Ile 565 570 575Val Ala Glu Glu Ala Lys Ala Pro Met Val Pro Gly Val Gly Ile Ala 580 585 590Pro Thr Tyr Thr Ile Ser Arg Ala Val Leu Ser Asp Ala Val Ala Leu 595 600 605Val Arg Gly Asp Arg Phe Tyr Thr Thr Asp Gln Thr Pro Arg Asn Leu 610 615 620Thr Asn Trp Gly Trp Gln Glu Ser Gly His Asp Leu Asn Ile Asn Gln625 630 635 640Gly Cys Val Phe Tyr Lys Leu Ala Phe Arg Ala Phe Pro Asn His Phe 645 650 655Lys Pro Asp Ser Ile Tyr Ala His Tyr Pro Met Thr Ile Pro Glu Glu 660 665 670Asn Lys Val Ile Met Lys Asp Leu Gly Arg Glu Asp Asp Tyr Ser Trp 675 680 685Asp Gln Pro Thr Phe Asn Ala Pro Arg Val Glu Leu Lys Thr Tyr Gln 690 695 700Ala Ala Gln Thr Val Leu Asn Asp Thr Arg Asn Phe Arg Val Thr Trp705 710 715 720Gly Asp Ala Ser Ala Trp Val Phe Gly Glu Lys Thr Gly Phe Asp Tyr 725 730 735Met Leu Ser Gly Asp Thr Pro Phe His Gly Gln Gln Arg Glu Leu Leu 740 745 750Glu Arg Ser Leu Tyr Gln Glu Gly Trp Asp Ser Arg Leu Lys Glu Phe 755 760 765Tyr Glu Gln Ile Thr Leu Gln Leu Leu His Asp Lys Ser Tyr Thr Leu 770 775 780Ala Gly Thr Lys Gln Val Asp Leu Thr Arg Asp Val Gly Asn Leu Ala785 790 795 800Thr Val His Phe Ala Ala His Leu Phe Gly Leu Pro Leu Lys Thr Lys 805 810 815Gly Asn Pro Arg Gly Ile Phe Thr Glu His Glu Leu Tyr Met Ala Asn 820 825 830Ala Val Ile Phe Gln Ala Val Phe Phe Asp Tyr Asp Leu Met Arg Ser 835 840 845Tyr Pro Leu Arg Gln Ala Ala Arg Ala Val Ala Lys Lys Ile Gly Glu 850 855 860Met Val Glu Leu Asn Val Lys Ser Ile Gly Ser Asn Gly Ile Ile Ser865 870 875 880His Phe Ile Asp Gly Leu Arg Lys Gln Asp Asn Pro Leu Ser Asp Tyr 885 890 895Gly Glu Asn Leu Val Lys Lys Leu Leu Asp Ser Gly Leu Asn Ala His 900 905 910Glu Val Thr Trp Thr Gln Ile Leu Pro Ala Val Val Ser Met Val Pro 915 920 925Lys Leu Gly Gln Val Phe Thr Gln Ile Ile Asp Phe Tyr Leu Ser Asp 930 935 940Ala Gly Lys Ala Tyr Leu Pro Glu Ile Asn Arg Leu Thr Lys Leu Asn945 950 955 960Thr Pro Glu Ser Asp Gln Ala Leu Thr His Tyr Val Leu Glu Ala Ile 965 970 975Arg Leu Asn Gly Thr Tyr Gly Ala Tyr Arg Glu Ala Gln Arg Asp Val 980 985 990Thr Val Asn Asp Gly Gly Asn Glu Ile Gln Val Asn Lys Gly Ala Lys 995 1000 1005Val Phe Val Ser Phe Ile Ser Ala Ser Arg Asp Pro Ala Ala Phe 1010 1015 1020Pro Glu Pro Glu Lys Val Val Leu Asp Arg Pro Val Glu Ser Tyr 1025 1030 1035Val His Tyr Gly Ile Gly Pro His Ser Cys Leu Gly Gln Asp Ala 1040 1045 1050Ser Leu Ile Ala Leu Thr Ser Met Leu Arg Val Val Gly Arg Leu 1055 1060 1065Glu Asn Leu Arg Arg Ala Arg Gly Thr Gln Gly Leu Leu Lys Lys 1070 1075 1080Ile Pro Arg Glu Gly Gly Ser Tyr His Tyr Leu Arg Glu Asp Gly 1085 1090 1095Gly Ser Phe Thr Pro Phe Pro Ala Thr Phe Lys Val Glu Trp Asp 1100 1105 1110Ser Glu Leu Pro Pro Leu Lys Asn Arg Gly Thr Trp 1115 1120 1125121117PRTPenicillium decumbens 12Met Leu Arg Arg Phe Ser Thr Gln Phe Arg Lys Asn Lys Glu Ser Asn1 5 10 15Ser Asp Ala Asp Ser Ser Lys Asn Ser Lys Glu Asn Gly Lys Arg His 20 25 30Ser Lys Pro Ile Gln Pro Ser Arg Lys Ala Ser Ser His Asp Glu Lys 35 40 45Gln His Ser Val Asn Arg Ala Glu Val Val Ala Val Phe Glu Lys His 50 55 60Ala Gln Ala Ile His Ala Ser Arg Glu Pro Leu Pro Ser Gln Gly Gly65 70 75 80Asp Gly Ala Tyr Leu Lys His Asp Gln Ser Ser Gly Leu Phe Glu Asp 85 90 95Ile Lys Ser Leu Gly Phe Arg Asp Leu Ser Thr Val Lys Ser Leu Ile 100 105 110Lys Ser Lys Ala Ser Gly Glu Leu Ile Asp Asp Lys Thr Tyr Leu Met 115 120 125Glu Arg Ile Ile Gln Leu Val Ala Asp Met Pro Gly His Ser Lys Asn 130 135 140Arg Val Glu Leu Thr Asn Gln Phe Leu Asp Glu Leu Trp Asp Ser Leu145 150 155 160Pro His Pro Pro Leu Ser Tyr Met Gly Asp Glu Tyr Lys Tyr Arg Ser 165 170 175Ala Asp Gly Ser Arg Asn Asn Pro Thr Leu Pro Gln Leu Gly Ala Ala 180 185 190Asn Thr Pro Tyr Cys Arg Thr Ile Pro Pro Leu Thr Ile Gln Pro Ser 195 200 205Gly Leu Pro Asp Ala Gly Leu Leu Phe Asp Ser Leu Phe Ala Arg Gln 210 215 220Lys Phe Thr Pro His Pro Asn Lys Val Ser Ser Ile Phe Phe Asp Trp225 230 235 240Ala Ser Leu Ile Ile His Asp Ile Phe Gln Thr Asp Tyr Arg Gln Gln 245 250 255His Val Asn Lys Thr Ser Ser Tyr Leu Asp Leu Ser Ile Leu Tyr Gly 260 265 270Asp Val Lys Glu Gln Gln Asp Leu Ile Arg Ser His Gln Asp Gly Lys 275 280 285Leu Lys Pro Asp Cys Phe Ser Glu Gly Arg Leu Gln Ala Leu Pro Ala 290 295 300Ala Cys Gly Val Leu Leu Val Met Leu Asn Arg Phe His Asn His Val305 310 315 320Val Glu Gln Leu Ala Ala Ile Asn Glu Asn Gly Arg Phe Thr Lys Pro 325 330 335Leu Asp Gly Leu Pro Glu Asp Ala Ala Lys Lys Ala Trp Ala Lys Tyr 340 345 350Asp Glu Asp Leu Phe Gln Thr Gly Arg Leu Ile Thr Cys Gly Leu Tyr 355 360 365Ile Asn Ile Thr Leu Tyr Asp Tyr Leu Arg Thr Ile Val Asn Leu Asn 370 375 380Arg Thr Asn Ser Thr Trp Cys Leu Asp Pro Arg Ala Gln Met Glu Lys385 390 395 400Thr Gly Ala Thr Pro Ser Gly Leu Gly Asn Gln Cys Ser Val Glu Phe 405 410 415Asn Leu Ala Tyr Arg Trp His Ser Thr Ile Ala Gln Gly Asp Glu Lys 420 425 430Trp Ile Glu Gln Ile Tyr Tyr Asp Leu Met Gly Lys Pro Ala Glu Glu 435 440 445Val Ser Met His Glu Leu Leu Met Gly Met Lys Lys Val Glu Gly Ser 450 455 460Leu Asp Pro Asp Pro Ser Lys Arg Thr Phe Ala Arg Leu Glu Arg Gln465 470 475 480Ala Asp Gly Thr Phe Lys Asp Glu Glu Leu Val Ala Ile Leu Thr Ser 485 490 495Ala Cys Glu Asp Val Ala Ser Ser Phe Gly Pro Arg Asn Val Pro Lys 500 505 510Ala Leu Arg Ser Ile Glu Ile Leu Gly Ile Glu Ala Ala Arg Arg Trp 515 520 525His Val Gly Ser Leu Asn Glu Phe Arg Lys His Phe Gly Leu Lys Pro 530 535 540Tyr Asp Thr Phe Glu Glu Ile Asn Ser Asn Pro Glu Ile Ala Asn Cys545 550 555 560Leu Arg His Leu Tyr Glu His Pro Asp Tyr Val Glu Leu Tyr Pro Gly 565 570 575Ile Val Ser Glu Glu Pro Lys Glu Pro Met Val Pro Gly Val Gly Ile 580 585 590Ala Pro Thr Tyr Thr Ile Ser Arg Ala Ile Leu Ser Asp Ala Val Ala 595 600 605Leu Val Arg Gly Asp Arg His Tyr Thr Ile Asp Tyr Asn Ala Arg Asn 610 615 620Leu Thr Asn Trp Gly Tyr Asn Glu Cys Arg Tyr Asp Leu Asn Ile Asn625 630 635 640Gln Gly Cys Val Phe Tyr Lys Leu Ala Leu Arg Ala Phe Pro Asn Trp 645 650 655Tyr Lys Pro Asp Ser Ile Tyr Ala His Tyr Pro Met Thr Ile Pro Ser 660 665 670Glu Asn Arg Asn Ile Met Lys Ser Leu Gly Arg Glu Gln Asp Tyr Ser 675 680 685Trp Glu Arg Pro Ser Phe Thr Pro Ser Arg Ile Asn Leu Ser Ser His 690 695 700Asn Asn Ala Arg Leu Val Leu Glu Asn Ser Thr Asp Phe Thr Pro Val705 710 715 720Trp Ser Glu Ala Met Thr Glu Leu Phe Gly Lys Gly Glu Phe Gly Ala 725 730 735Gln Gln Arg Glu Ala Met Ser Ala Ala Phe Ala Thr Glu Asp Phe Leu 740 745 750Thr Leu Val Lys Asn Phe Tyr Glu Glu Val Thr Leu Arg Leu Ile Lys 755 760 765Glu Lys Gly Ala Asn Leu Val Gly Thr Asn Gln Val Asp Ile Thr Arg 770 775 780Asp Val Gly Asn Leu Ala His Val His Phe Ala Ser Ala Leu Phe Gly785 790 795 800Leu Pro Leu Lys Thr Asp Glu Asn Pro Arg Gly Leu Phe Thr Glu His 805 810 815Glu Met Tyr Met Ile Leu Ala Thr Ile Tyr Ser Ala Leu Phe Tyr Asp 820 825 830Val Asp Pro Ala Lys Ser Leu Pro Leu Asn Ser Ala Ala Ser Ala Val 835 840 845Ala Arg Gln Leu Gly Ser Val Val Glu Ala Thr Val Lys Thr Asp Thr 850 855 860His Ser Gly Leu Phe Ser Gly Leu Ile Asn Ser Phe Arg Pro His Asp865 870 875 880Asn Ala Ile Arg Glu His Gly Thr Ala Ala Leu Arg Arg Val Glu Glu 885 890 895Ser Gly Gln Ser Ala Ser Gln Ile Thr Trp Ser His Ile Ile Pro Thr 900 905 910Val Val Gly Met Val Pro Ser Gln Gly Gln Val Phe Thr Gln Val Ile 915 920 925Glu Tyr Tyr Thr Ser Pro Glu Gly Lys His His Trp Ser Glu Ile Ser 930 935 940Arg Leu Ala Arg Gln Asp Ser Lys Glu Ser Asp Glu Met Leu His Arg945 950 955 960Tyr Cys Leu Glu Ala Ile Arg Ile Asn Gly Thr Phe Gly Glu Tyr Arg 965 970 975Glu Ala Lys Asn Pro Val Ile Leu Glu Glu Asn Glu Glu Val Ile Asn 980 985 990Val Gln Pro Gly Asn Lys Ile Phe Ala Ser Phe Ile Gln Ala Asn Leu 995 1000 1005Asp Pro Ser Val Phe Pro Glu Pro Asn Ser Val Asn Leu Ser Arg 1010 1015 1020Pro Leu Ser Ser Tyr Ile His Gln Gly Gln Gly Pro Ala Asn Gly 1025 1030 1035Leu Gly Gln Glu Thr Thr Lys Ile Ala Leu Val Ser Met Leu Arg 1040 1045 1050Val Val Ala Arg Leu Pro Asn Leu Arg Arg Ala Pro Gly Ala Gln 1055 1060 1065Gly Gln Leu Lys Arg Ile Pro Gln Lys Gly Gly His Tyr Val Tyr 1070 1075 1080Leu Arg Gln Asp Gly Thr Ser Tyr Phe Pro Phe Pro Thr Thr Leu 1085 1090 1095Lys Leu His Trp Asp Gly Asp Phe Glu Phe Gln Thr Ser Gln Thr 1100 1105 1110Ser Lys Lys His 1115131118PRTPenicillium chrysogenum 13Met Leu Lys Arg Phe Ser Thr Gln Phe Lys Arg Ser Lys Asp Ser Lys1 5 10 15Asp Pro Lys Glu Ser Asn Gly Asp Ala Glu Pro Lys Ser Thr Asp Lys 20 25 30Ser Ser Lys Arg Ala Ser Lys Val Ser Pro Ser Pro Lys Ser Thr His 35 40 45Lys Glu Glu Asn His Val Val Lys Arg Ser Glu Val Val Ala Val Phe 50 55 60Asp Lys Tyr Ala Gln Ala Ile His Ala Ser Gln Glu Pro Leu Pro Asn65 70 75 80Gln Thr Ser Asp Gly Ala Tyr Leu Lys His Asp Lys Ser Ser Gly Leu 85 90 95Ile Asn Asp Ile Lys Ala Leu Gly Phe Arg Asp Val Gly Thr Val Lys 100 105 110Asp Leu Ile Ala Ser Lys Ala Ser Gly Gly Ile Ile Asp Asp Lys Thr 115 120 125Tyr Leu Met Glu Arg Ile Ile Gln Met Val Ala Asp Leu Pro Gly Asn 130 135 140Ser Lys Asn Arg Thr Asp Leu Thr Gly Leu Phe Leu Asp Asp Leu Trp145 150 155 160Asn Ser Ile Pro His Pro Pro Leu Ser Tyr Met Gly Asp Asp Tyr Lys 165 170 175Tyr Arg Ser Ala Asp Gly Ser Asn Asn Asn Pro Thr Leu Pro Trp Leu 180 185 190Gly Ala Ala Asn Thr Pro Tyr Cys Arg Thr Ile Ala Pro Leu Thr Ile 195 200 205Gln Pro Ser Gly Leu Pro Asp Ala Gly Leu Ile Phe Asp Thr Leu Tyr 210 215 220Ala Arg Gln Glu Phe Thr Pro His Pro Asn Lys Val Ser Ser Val Phe225 230 235 240Phe Asp Trp Ala Ser Leu Ile Ile His Asp Ile Phe Gln Thr Asp Tyr 245 250 255Ser Gln Gln His Leu Asn Gln Thr Ser Ala Tyr Leu Asp Leu Ser Ile 260 265 270Leu Tyr Gly Asp Val Lys Glu Gln Gln Asp Lys Ile Arg Ser His Glu 275 280 285Asn Gly Lys Leu Lys Pro Asp Cys Phe Ser Glu Gly Arg Leu Gln Ala 290 295 300Leu Pro Pro Ala Cys Gly Val Leu Leu Val Met Leu Asn Arg Phe His305 310 315 320Asn His Ile Val Thr Gln Leu Ala Ala Ile Asn Glu Asn Gly Arg Phe 325 330 335Ser Ala Pro Arg Pro Gly Leu Ser Glu Glu Glu Thr Lys Ala Ala Trp 340 345 350Ala Lys Arg Asp Glu Asp Leu Phe Gln Thr Gly Arg Leu Ile Thr Cys 355 360 365Gly Leu Tyr Ile Asn Ile Thr Leu Tyr Asp Tyr Leu Arg Thr Ile Val 370 375 380Asn Leu Asn Arg Thr Asn Ser Thr Trp Cys Leu Asp Pro Arg Ala Gln385 390 395 400Ala Glu Lys Ala Asp Ala Thr Pro Ser Gly Leu Gly Asn Gln Cys Ser 405 410 415Val Glu Phe Asn Leu Ala Tyr Arg Trp His Ser Thr Ile Ser Gln Gly 420 425 430Asp Glu Lys Trp Ile Glu Gln Ile Tyr Tyr Asp Leu Met Gly Lys Pro 435 440 445Ala Glu Gln Val Ser Met Pro Glu Leu Leu Met Gly Met Lys Lys Val 450 455 460Lys Gly Met Leu Glu Ala Asp Pro Ala Lys Arg Thr Phe Gly His Leu465 470 475 480Gln Arg Asn Ala Asp Gly Tyr Phe Asp Asp Gly Glu Leu Val Asn Ile 485 490 495Leu Thr Arg Ala Thr Glu Asp Val Ala Ser Ser Phe Gly Pro Arg Asn

500 505 510Val Pro Lys Ala Met Arg Ser Ile Glu Ile Leu Gly Ile Glu Ala Ser 515 520 525Arg Arg Trp Asn Val Gly Ser Leu Asn Glu Phe Arg Lys His Phe Gly 530 535 540Leu Lys Pro Tyr Glu Thr Phe Glu Asp Val Asn Ser Asn Pro Glu Ile545 550 555 560Ala Asn Thr Leu Arg His Leu Tyr Glu His Pro Asp Tyr Ile Glu Leu 565 570 575Tyr Pro Gly Ile Val Ser Glu Glu Ala Lys Glu Pro Met Ile Pro Gly 580 585 590Val Gly Ile Ala Pro Thr Tyr Thr Ile Ser Arg Ala Val Leu Ser Asp 595 600 605Ala Val Ala Leu Val Arg Gly Asp Arg His Tyr Thr Ile Asp Tyr Asn 610 615 620Pro Arg Asn Leu Thr Asn Trp Gly Tyr Asn Glu Cys Arg Tyr Asp Leu625 630 635 640Asn Ile Asn Gln Gly Cys Ile Phe Tyr Lys Leu Ala Thr Arg Ala Phe 645 650 655Pro Asn His Tyr Lys Pro Asp Ser Ile Tyr Ala His Tyr Pro Met Thr 660 665 670Ile Pro Ser Glu Asn Arg Asn Ile Met Lys Asp Leu Gly Arg Glu Gln 675 680 685Asp Tyr Ser Trp Asp Lys Pro Ala Phe Met Glu Pro Arg Val Asn Leu 690 695 700Thr Ser His Gln Asn Ala Lys Leu Leu Leu Glu Asn Gln Lys Asp Phe705 710 715 720Arg Pro Ser Trp Ala Arg Ser Met Ser Glu Leu Phe Gly Lys Gly Glu 725 730 735Phe Asp Thr Lys Gln Arg Glu Ala Ile Gly Lys Ala Leu Asn Thr Glu 740 745 750Glu Phe Pro Lys Leu Val Lys Thr Phe Tyr Glu Asp Ile Thr Glu Arg 755 760 765Leu Ile Ala Glu Lys Gly Gly Gln Leu Gly Lys Ile Asn Gln Ile Asp 770 775 780Ile Thr Arg Asp Val Gly Asn Leu Ala His Val His Phe Ala Ser Thr785 790 795 800Ile Phe Gly Val Pro Leu Lys Thr Glu Asp Asn Pro Arg Gly Leu Phe 805 810 815Thr Glu His Glu Met Tyr Met Ile Leu Ser Thr Ile Phe Ser Ala Leu 820 825 830Phe Phe Asp Val Asp Ala Pro Arg Ser Tyr Ala Leu Asn Arg Ala Ala 835 840 845Ser Ala Val Ser Asn Gln Leu Gly Gln Val Val Glu Ala Thr Val Lys 850 855 860Ala Asp Thr Asn Ser Gly Leu Phe Ala Gly Ile Met Asp Asn Phe Arg865 870 875 880Pro His Asp Asn Ala Leu Arg Glu Phe Gly Thr Glu Ala Ile Arg Arg 885 890 895Met Lys Glu Ala Gly Ser Ser Ala Ser Asp Ile Thr Trp Ser Ala Ile 900 905 910Val Pro Thr Ile Val Gly Leu Val Pro Asn Gln Ala Gln Val Phe Thr 915 920 925Gln Ile Ile Glu Phe Tyr Thr Ala Pro Glu Asn Lys Ala His Leu Ala 930 935 940Glu Ile Asn Arg Phe Ala Lys Thr Asp Ser Ala Glu Ser Asp Glu Lys945 950 955 960Leu Tyr Arg Tyr Cys Leu Glu Ala Val Arg Leu Asn Gly Thr Phe Gly 965 970 975Ala Phe Arg Glu Ala Lys Glu Thr Val Thr Val Glu Glu Asp Gly Lys 980 985 990Thr Tyr Thr Val Gln Pro Gly Gln Gln Val Phe Ala Ser Phe Asp Gln 995 1000 1005Ala Asn His Asp Pro Ser Val Phe Pro Glu Pro Asn Glu Val Asn 1010 1015 1020Leu Asp Arg Pro Leu Asp Ser Tyr Ile Asn His Gly Gln Gly Pro 1025 1030 1035Thr Thr Gly Phe Gly Glu Gln Val Thr Lys Ile Ala Leu Ile Ala 1040 1045 1050Met Leu Arg Val Val Gly Arg Leu Gln Gly Leu Arg Arg Ala Pro 1055 1060 1065Gly Ala Gln Gly Gln Leu Lys Lys Ile Pro Gln Glu Gly Gly Tyr 1070 1075 1080Gln Val Tyr Leu Arg Gly Asp Gly Thr Ala Tyr Cys Pro Phe Pro 1085 1090 1095Met Ser Leu Lys Leu His Trp Asp Gly Pro Phe Glu Gln Lys Lys 1100 1105 1110Lys Val Thr Ser Ser 1115141110PRTAspergillus niger 14Met Leu Arg Arg Phe Ser Ser Thr Phe Lys Arg Ser Ser Lys Gly Asp1 5 10 15Arg Asp Ser Lys Pro Asn Gly Thr Gln Val Asn Gly Gln Lys Arg Gln 20 25 30Ser Lys Val Pro Ala Pro Arg Lys Ser Ser Ser Asp Glu Ser His Ser 35 40 45Asp His Gly Val Glu Ser Asp Asp Gly Val Ser Val Phe Glu Lys Tyr 50 55 60Ala Gln Val Leu His Ala Ser Arg Arg Pro Leu Pro Asn Gln Asn Gly65 70 75 80Asp Gly Thr Tyr Leu Glu Gln Glu His Ser Gly Ser Leu Phe Lys Asp 85 90 95Leu Arg Ala Leu Gly Phe Lys Asp Ile Gly Thr Leu Lys Asp Leu Ile 100 105 110Lys Thr Lys Ala Lys Gly Glu Tyr Ile Asp Asp Lys Thr Met Leu Met 115 120 125Glu Arg Ile Ile Gln Leu Val Ser Ser Leu Pro Gly Asn Ser Lys Thr 130 135 140Arg Val Asp Leu Thr Asn Ala Phe Leu Asp Glu Leu Trp Gly Ser Leu145 150 155 160Pro His Pro Pro Leu Ser Tyr Met Gly Glu Glu Tyr Ala Tyr Arg Ser 165 170 175Ala Asp Gly Ser Asn Asn Asn Pro Thr Leu Pro Trp Leu Gly Ala Ala 180 185 190Gly Thr Pro Tyr Ala Arg Ser Ile Ala Pro Leu Thr Ile Gln Pro Gly 195 200 205Gly Leu Pro Asp Ala Gly Leu Val Phe Asp Cys Leu Phe Ala Arg Glu 210 215 220Lys Phe Thr Pro His Pro Asn Lys Val Ser Ser Leu Phe Phe Asp Trp225 230 235 240Ala Ser Leu Val Ile His Asp Ile Phe Gln Thr Asp Tyr Thr Asn Ser 245 250 255His Val Asn Lys Thr Ser Ala Tyr Leu Asp Leu Ser Ile Leu Tyr Gly 260 265 270Asp Asp Gln Glu Asp Gln Asn Leu Val Arg Thr Phe Lys Asp Gly Lys 275 280 285Leu Lys Pro Asp Thr Phe Ser Glu Gln Arg Leu Gln Ala Phe Pro Pro 290 295 300Ala Cys Ser Val Leu Met Val Met Leu Ser Arg Phe His Asn Trp Val305 310 315 320Val Glu Glu Leu Ala Ala Ile Asn Glu Asn Gly Arg Phe Asn Lys Pro 325 330 335Asp Pro Arg Leu Asp Glu Glu Lys Ala Arg Lys Ala Trp Glu Lys Tyr 340 345 350Asp Asn Asp Leu Phe Gln Thr Gly Arg Leu Val Thr Cys Gly Leu Phe 355 360 365Ile Asn Ile Thr Leu Tyr Asp Tyr Leu Arg Thr Ile Val Asn Leu Asn 370 375 380Arg Ser Asn Ser Thr Trp Cys Leu Asp Pro Arg Val Gln Met Glu Gly385 390 395 400Thr Lys Ser Thr Pro Ser Gly Leu Gly Asn Gln Cys Ser Val Glu Phe 405 410 415Asn Leu Ala Tyr Arg Trp His Ser Ala Ile Ser Ala Asn Asp Glu Lys 420 425 430Trp Thr Glu Glu Ile Tyr Glu Glu Leu Met Gly Lys Pro Ala Ser Glu 435 440 445Val Ser Met Arg Glu Leu Leu Val Gly Leu Gly Lys Tyr Glu Arg Glu 450 455 460Ile Pro Lys Asp Pro Ser Lys Arg Thr Phe Ala Gly Leu Lys Arg Gln465 470 475 480Glu Asp Gly Thr Phe Lys Asp Glu Asp Leu Val Arg Ile Leu Ala Asn 485 490 495Ala Ile Glu Asp Val Ala Ser Ser Phe Gly Ala Arg Asn Val Pro Lys 500 505 510Val Leu Arg Ser Val Glu Ile Leu Gly Ile Glu Gln Gly Arg Lys Trp 515 520 525Asn Val Gly Ser Leu Asn Glu Phe Arg Lys Phe Phe Asp Leu Lys Pro 530 535 540Tyr Glu Thr Phe Glu Glu Ile Asn Ser Asp Pro Asp Val Ala Asp Ser545 550 555 560Leu Arg His Leu Tyr Glu His Pro Asp Tyr Val Glu Leu Tyr Pro Gly 565 570 575Ile Val Ala Glu Glu Ala Lys Glu Pro Met Ile Pro Gly Val Gly Ile 580 585 590Ala Pro Thr Tyr Thr Ile Ser Arg Ala Val Leu Ser Asp Ala Val Ala 595 600 605Leu Val Arg Gly Asp Arg Tyr Tyr Thr Ile Asp Tyr Asn Pro Arg Asn 610 615 620Leu Thr Asn Trp Gly Tyr Asn Glu Val Arg Tyr Asp Leu Asn Ile Asn625 630 635 640Gln Gly Cys Val Phe Tyr Lys Leu Ala Met Arg Ala Phe Pro Asn Tyr 645 650 655Phe Lys Pro Asp Ser Ile Tyr Ala His Tyr Pro Met Thr Ile Pro Ser 660 665 670Glu Asn Arg Asn Ile Met Lys Asn Leu Gly Arg Glu Ser His Tyr Ser 675 680 685Tyr Asp Arg Pro Arg Tyr Thr Glu Pro Val Pro Asn Leu Leu Ser Tyr 690 695 700Ala Asn Ala Lys Leu Val Leu Asn Asn Gln Lys Asp Phe Thr Val Pro705 710 715 720Trp Gly Gly Leu Ser Ser Ile His Ala Gly Lys Gly Gly Ala Asp Phe 725 730 735Trp Ser Lys Ser Phe Asp Asn Glu Gln Trp Arg Asn Ser Val Lys Glu 740 745 750Phe Tyr Glu Asp Ala Thr Leu Lys Leu Leu Asn Glu Lys Ser Cys Lys 755 760 765Leu Ala Gly Asn Lys Gln Val Asp Ile Ala Arg Asp Val Gly Asn Leu 770 775 780Val Pro Val His Phe Val Ser Lys Val Phe Ser Leu Pro Leu Lys Thr785 790 795 800Lys Ser Asn Pro Arg Gly Ile Phe Thr Glu His Glu Met Phe Met Ile 805 810 815Met Ala Val Val Phe Asn Ser Thr Phe Phe Asp Val Asp Pro Thr Lys 820 825 830Ser Phe Pro Leu Gln His Ala Ala Arg Ala Val Ser Gln Glu Leu Gly 835 840 845Lys Val Val Glu Ala His Val Lys Ser Ile Asn His Pro Gly Phe Leu 850 855 860His Gly Ile Ile Asp Ser Phe Arg Asp Asp His Asn Ala Leu Lys Asp865 870 875 880Tyr Gly Asp Gln Leu Ile Lys Arg Leu Leu Glu Ser Gly Leu Gly Val 885 890 895Ser Asp Val Thr Trp Gly Gln Ile Leu Pro Ala Ala Val Glu Met Val 900 905 910His Thr Gln Ser Gln Met Phe Thr Gln Ile Ile His Phe Tyr Leu Thr 915 920 925Glu Gly Gln Lys Tyr Leu Pro Glu Ile Asn Arg Leu Ala Asn Glu Asn 930 935 940Thr Ala Glu Ala Asn Asp Arg Leu Thr Arg Phe Cys Leu Glu Ala Val945 950 955 960Arg Leu Asn Gly Asn Leu Gly Ile Tyr Arg Glu Ala Gln Ala Asp Ile 965 970 975Asn Val Ser Asp Glu Thr Gly Gln Tyr Ser Val Lys Ser Gly Glu Lys 980 985 990Val Phe Val Gly Ser Ser Lys Ala Asn Arg Asp Pro Gln Ala Phe Pro 995 1000 1005Ser Pro Asp Glu Val Arg Leu Asp Arg Pro Leu Asp Ser Tyr Leu 1010 1015 1020His Tyr Gly Leu Gly Pro Gln Ser Gly Leu Gly Lys Asp Ala Thr 1025 1030 1035Leu Ala Ala Val Thr Ala Met Val Arg Val Val Ala Arg Leu Asp 1040 1045 1050Thr Leu Arg Pro Ala Pro Gly Ala Gln Gly Gln Leu Lys Lys Ile 1055 1060 1065Pro Gln Glu Ala Gly Phe Ser Val Tyr Met Arg Glu Asp Tyr Gly 1070 1075 1080Ser Tyr Ser Pro Phe Pro Thr Thr Tyr Lys Val His Tyr Asn Gly 1085 1090 1095Asp Val Pro Ala Pro Lys Arg Gln Val Thr Thr Ala 1100 1105 111015542PRTNostoc punctiforme 15Met Ala Gly Lys Arg Asp Thr Ser Lys Asp Gly Leu Gly Asn Lys Ile1 5 10 15Gln Thr Leu Val Leu Thr Asn Phe Lys Gly Leu Trp Gln Leu Leu Gln 20 25 30Ser Asn Glu Phe Ile Lys Arg Lys Val Asn Lys Thr Leu Leu Asn Ser 35 40 45Leu Ile Tyr Lys Ile Pro Thr Arg Pro Asn Ala Tyr Ser Met Met Thr 50 55 60Leu Asp Glu His Ile Pro Asp Thr Asn Ile Pro Lys Lys Thr Asp Thr65 70 75 80Tyr Thr Ser Trp Glu Ser Leu Asn Asp Arg Thr Tyr Thr Gly Arg His 85 90 95Leu Pro Pro Asp Pro Lys Leu Asn Ala Glu Gly Asn Leu Pro Lys Val 100 105 110Glu Asp Leu Ala Ile Leu Phe Arg Lys Arg Asp Gly Lys Thr Ile Tyr 115 120 125Ser Gly Lys Ser Thr Met Leu Phe Pro Tyr Trp Val Gln Trp Phe Thr 130 135 140Asp Ser Phe Leu Arg Leu Asn His Tyr Asn Lys Leu Lys Asn Thr Ser145 150 155 160Asn His Glu Ile Asp Leu Cys Asn Val Tyr Gly Leu Thr Arg Lys Gln 165 170 175Thr His Leu Leu Arg Ser Phe Gln Gly Gly Lys Leu Lys Thr Gln Lys 180 185 190Leu Lys Arg Gln Asp Gly Val Glu Glu Glu Tyr Pro Leu Phe Tyr Tyr 195 200 205Ala Asp Pro Ala Gln Asp Lys Val Lys Pro Glu Phe Glu Gly Leu Tyr 210 215 220Glu Pro Ile Asn Asp Glu Lys Arg Gln Pro Ile Asp Lys Lys Gln Tyr225 230 235 240Met Phe Ala Met Gly Val Glu Arg Ala Asn Val Gln Ile Gly Tyr Val 245 250 255Met Leu Asn Thr Leu Cys Phe Arg Glu His Asn Arg Leu Cys Asp Glu 260 265 270Leu Ala Arg Asn Tyr Pro Asp Trp Asp Asp Glu Arg Leu Phe Gln Thr 275 280 285Ser Arg Asn Ile Leu Met Ala Ile Ile Leu Lys Ile Ile Met Glu Glu 290 295 300Tyr Ile Asn His Ile Thr Pro Tyr His Phe Lys Leu Phe Ala Asp Pro305 310 315 320Glu Ala Phe Thr Lys Glu Ser Trp His Arg Pro Asn Tyr Met Ala Ile 325 330 335Glu Phe Asp Phe Val Tyr Arg Trp His Ser Ala Ile Pro Glu Thr Phe 340 345 350Asn Tyr Asn Gly Lys Pro Thr His Ile Val Thr Ser Leu Trp Asn Asn 355 360 365Lys Met Phe Ile Asp Gln Gly Leu Gly Ala Leu Met Glu Glu Thr Cys 370 375 380Ser Gln Pro Gly Thr Lys Ile Gly Leu Phe Asn Thr Pro Asp Ile Leu385 390 395 400Val Glu Leu Thr Glu Leu Pro Ser Ile Arg Leu Gly Arg Gln Leu Gln 405 410 415Leu Ala Ser Tyr Asn Asp Tyr Arg Glu Leu Cys Gly Phe Pro Arg Val 420 425 430Thr Arg Phe Glu Gln Val Thr Gly Asn Glu Phe Ala Gln Glu Lys Leu 435 440 445Lys Glu Leu Tyr Gly His Val Asp Lys Ile Glu Phe Phe Val Gly Leu 450 455 460Tyr Ala Glu Asp Gly Arg Glu Asn Ser Thr Ile Pro Ala Leu Val Ala465 470 475 480Arg Leu Ile Gly Ile Asp Ala Phe Ser Gln Ala Leu Thr Asn Pro Leu 485 490 495Leu Ser Pro Asn Ile Phe Asn Lys Glu Thr Phe Ser Pro Val Gly Trp 500 505 510Glu Ile Leu Gln Asn Thr Lys Thr Val Ser Asp Leu Val Asn Arg Asn 515 520 525Val Pro Pro Ser Gly Lys Lys Tyr Lys Val Thr Phe Asp Leu 530 535 54016634PRTPseudomonas aeruginosa 16Met Thr Leu Ser Arg Leu Ser Leu Ala Ile Leu Ser Val Leu Ala Gly1 5 10 15Ala Pro Ala Phe Ala Asp Asp Ser Gly Val Asp Leu Asp Gln Gly Trp 20 25 30Asn Gln Thr Gln Lys Thr Ala Trp Leu Glu Ala Gly Gln Gly Ser Arg 35 40 45Met Leu Pro Leu Ala Trp Leu Val Ala Leu Glu Gln Arg Ala Ser Glu 50 55 60Glu Pro Leu Met Ser Asp Ala Leu Ile Arg Gln Tyr Gly Tyr Val Pro65 70 75 80His Thr Leu Gly Gly Ser Ser Val Lys Val Val Gln Gly Tyr Ala Val 85 90 95Asp Arg Ser Asp Asp Ser Asp Leu Thr Phe Thr Lys Leu Arg Trp Lys 100 105 110Ala Leu Gln Gly Ser Arg Glu Pro Trp Val Gly Pro Thr Cys Ser Met 115 120 125Cys His Thr Ser His Ile Ser Tyr Gln Gly Thr Gln Leu Thr Val Tyr 130 135 140Gly Gly Gln Thr Met Gly Asp Leu Ala Gly Phe Gln Leu Glu Ile Leu145 150 155 160Gly Ala Leu Gln Ser Thr Arg Ala Asp Thr Ala Lys Phe Glu Arg Phe 165 170 175Ala Arg Lys Val Leu Gly Ala Asp Gly Leu Val Ser Gly Tyr Asn Asp 180 185

190Ala Asn Lys Ala Arg Leu Gln Ala Ala Leu Asp Ala Thr Ile Val Arg 195 200 205Leu Arg Asp Gly Ser His Phe Asn Leu Pro His Asp Pro Glu Phe Gly 210 215 220Pro Gly Arg Leu Asp Ala Ile Gly Ser Ile Phe Asn Ser Val Gly Tyr225 230 235 240Glu Leu His Ala Asp Glu Gln Ile Tyr Gly Ala Glu Asp Ala Pro Val 245 250 255Ser Tyr Pro Phe Leu Trp Asn Val Pro Gln Leu Asp Arg Val Gln Trp 260 265 270Thr Gly Phe Asn Pro Asn His Ile Asn Val Val Asp Ile Asp Asn Arg 275 280 285Lys Phe Asp Val Gly Ala Leu Ala Arg Asn Ala Gly Glu Ala Val Gly 290 295 300Val Phe Ala Asp Val Lys Val Leu Ser Pro Ile Gln Ser Ala Leu His305 310 315 320Ile Gly Tyr Pro Ser Ser Ile Asn Val Asp Asn Leu Ile Arg Ile Glu 325 330 335Asp Gln Leu Gly Gln Leu Lys Pro Pro Ala Trp Pro Asn Gln Leu Phe 340 345 350Gly Ala Pro Glu Pro Thr Arg Val Ala Glu Gly Arg Glu Leu Tyr Arg 355 360 365Gln His Cys Ser Ser Cys His Thr Pro Leu Asp Arg Asn Asp Leu Arg 370 375 380Thr Pro Val Lys Thr Val Leu Thr His Leu Gln Ala Arg Gly Glu Val385 390 395 400Ala Pro Ile Gly Thr Asp Pro Trp Thr Ala Cys Asn Ser Ile Ala Gln 405 410 415Leu Lys Thr Gly Tyr Val Arg Gly Lys Pro Tyr Leu Ser Phe Val Gly 420 425 430Thr Gly Gln Arg Gly Phe Tyr Gly Lys Gln Ala Tyr Ala Val Asp Val 435 440 445Leu Gln Glu Val Val Val Gln Ala Leu Ala Ala Arg Gly Leu Ser Val 450 455 460Ala Leu Gly Ala Phe Gln Thr Ala Ala Leu Gly Ile Phe Asp Gly Gln465 470 475 480Leu Pro Pro Leu Ile Ser Pro Val Pro Asp Ser Pro Asp Ala Asp Ser 485 490 495Ala Glu Ala Thr Ala Ala Asp Ala Pro Gly Ala Leu Leu Leu Ala Glu 500 505 510Asn Val Ala Ala Asp Ser Asp Lys Ala Arg Arg Leu Glu Gln Cys Leu 515 520 525Ala Met Thr Ser Asp Leu Met Ala Tyr Lys Ala Arg Pro Leu Asn Gly 530 535 540Ile Trp Ala Ser Pro Pro Tyr Leu His Asn Gly Ser Val Ala Thr Leu545 550 555 560Tyr Asp Leu Leu Leu Pro Pro Asp Leu Arg Pro Arg Thr Phe Tyr Thr 565 570 575Gly Ser Val Glu Phe Asp Pro Val Asn Val Gly Tyr Ile Thr Asp Ala 580 585 590Gly Gly Ala Asn Arg Phe Leu Phe Asp Ser Gly Lys Pro Gly Asn Ala 595 600 605Asn Gly Gly His Asp Tyr Gly Asn Ala Gln Phe Asn Glu Gln Gln Arg 610 615 620Arg Ala Leu Val Glu Tyr Met Lys Thr Leu625 63017634PRTPseudomonas aeruginosa 17Met Thr Leu Ser Arg Leu Ser Leu Ala Ile Leu Ser Val Leu Ala Gly1 5 10 15Ala Pro Ala Phe Ala Asp Asp Ser Gly Val Asp Leu Asp Gln Gly Trp 20 25 30Asn Gln Thr Gln Lys Thr Ala Trp Leu Glu Ala Gly Gln Gly Ser Arg 35 40 45Met Leu Pro Leu Ala Trp Leu Val Ala Leu Glu Gln Arg Ala Ser Glu 50 55 60Glu Pro Leu Met Ser Asp Ala Leu Ile Arg Gln Tyr Gly Tyr Val Pro65 70 75 80His Thr Leu Gly Gly Ser Ser Val Lys Val Val Gln Gly Tyr Ala Val 85 90 95Asp Arg Ser Asp Asp Ser Asp Leu Thr Phe Thr Lys Leu Arg Trp Lys 100 105 110Ala Leu Gln Gly Ser Arg Glu Pro Trp Val Gly Pro Thr Cys Ser Met 115 120 125Cys His Thr Ser His Ile Ser Tyr Gln Gly Thr Gln Leu Thr Val Tyr 130 135 140Gly Gly Gln Thr Met Gly Asp Leu Ala Gly Phe Gln Leu Glu Ile Leu145 150 155 160Gly Ala Leu Gln Ser Thr Arg Ala Asp Thr Ala Lys Phe Glu Arg Phe 165 170 175Ala Arg Lys Val Leu Gly Ala Asp Gly Leu Val Ser Gly Tyr Asn Asp 180 185 190Ala Asn Lys Ala Arg Leu Gln Ala Ala Leu Asp Ala Thr Ile Val Arg 195 200 205Leu Arg Asp Gly Ser His Phe Asn Leu Pro His Asp Pro Glu Phe Gly 210 215 220Pro Gly Arg Leu Asp Ala Ile Gly Ser Ile Phe Asn Ser Val Gly Tyr225 230 235 240Glu Leu His Ala Asp Glu Gln Ile Tyr Gly Ala Glu Asp Ala Pro Val 245 250 255Ser Tyr Pro Phe Leu Trp Asn Val Pro Gln Leu Asp Arg Val Gln Trp 260 265 270Thr Gly Phe Asn Pro Asn His Ile Asn Val Val Asp Ile Asp Asn Arg 275 280 285Lys Phe Asp Val Gly Ala Leu Ala Arg Asn Ala Gly Glu Ala Val Gly 290 295 300Val Phe Ala Asp Val Lys Val Leu Ser Pro Ile Gln Ser Ala Leu His305 310 315 320Ile Gly Tyr Pro Ser Ser Ile Lys Val Asp Asn Leu Ile Arg Ile Glu 325 330 335Asp Gln Phe Gly Gln Leu Lys Pro Pro Ala Trp Pro Asn Gln Leu Phe 340 345 350Gly Ala Pro Glu Pro Thr Arg Val Ala Glu Gly Arg Glu Leu Tyr Arg 355 360 365Gln His Cys Ser Ser Cys His Thr Pro Leu Asp Arg Asn Asp Leu Arg 370 375 380Thr Pro Val Lys Thr Val Leu Thr His Leu Gln Ala Arg Gly Glu Val385 390 395 400Ala Pro Ile Gly Thr Asp Pro Trp Thr Ala Cys Asn Ser Ile Ala Gln 405 410 415Leu Lys Thr Gly Tyr Val Arg Gly Lys Pro Tyr Leu Ser Phe Val Gly 420 425 430Thr Gly Gln Arg Gly Phe Tyr Gly Lys Gln Ala Tyr Ala Val Asp Val 435 440 445Leu Gln Glu Val Val Val Gln Ala Leu Ala Ala Arg Gly Leu Ser Val 450 455 460Ala Leu Gly Ala Phe Gln Thr Ala Ala Leu Gly Ile Phe Asp Gly Gln465 470 475 480Leu Pro Pro Leu Ile Ser Pro Val Pro Asp Ser Pro Asp Ala Asp Ser 485 490 495Val Glu Ala Thr Ala Ala Asp Ala Pro Gly Ala Leu Leu Leu Ala Glu 500 505 510Asn Val Ala Ala Asp Ser Asp Lys Ala Arg Arg Leu Glu Gln Cys Leu 515 520 525Ala Met Thr Ser Asp Leu Met Ala Tyr Lys Ala Arg Pro Leu Asn Gly 530 535 540Ile Trp Ala Ser Pro Pro Tyr Leu His Asn Gly Ser Val Ala Thr Leu545 550 555 560Tyr Asp Leu Leu Leu Pro Pro Asp Leu Arg Pro Arg Thr Phe Tyr Thr 565 570 575Gly Ser Val Glu Phe Asp Pro Val Asn Val Gly Tyr Ile Thr Asp Ala 580 585 590Gly Gly Ala Asn Arg Phe Leu Phe Asp Ser Gly Lys Pro Gly Asn Ala 595 600 605Asn Gly Gly His Asp Tyr Gly Asn Ala Gln Phe Asn Glu Gln Gln Arg 610 615 620Arg Ala Leu Val Glu Tyr Met Lys Thr Leu625 63018613PRTPseudomonas aeruginosa 18Asp Asp Ser Gly Val Asp Leu Asp Gln Gly Trp Asn Gln Thr Gln Lys1 5 10 15Thr Ala Trp Leu Glu Ala Gly Gln Gly Ser Arg Met Leu Pro Leu Ala 20 25 30Trp Leu Val Ala Leu Glu Gln Arg Ala Ser Glu Glu Pro Leu Met Ser 35 40 45Asp Ala Leu Ile Arg Gln Tyr Gly Tyr Val Pro His Thr Leu Gly Gly 50 55 60Ser Ser Val Lys Val Val Gln Gly Tyr Ala Val Asp Arg Ser Asp Asp65 70 75 80Ser Asp Leu Thr Phe Thr Lys Leu Arg Trp Lys Ala Leu Gln Gly Ser 85 90 95Arg Glu Pro Trp Val Gly Pro Thr Cys Ser Met Cys His Thr Ser His 100 105 110Ile Ser Tyr Gln Gly Thr Gln Leu Thr Val Tyr Gly Gly Gln Thr Met 115 120 125Gly Asp Leu Ala Gly Phe Gln Leu Glu Ile Leu Gly Ala Leu Gln Ser 130 135 140Thr Arg Ala Asp Thr Ala Lys Phe Glu Arg Phe Ala Arg Lys Val Leu145 150 155 160Gly Ala Asp Gly Leu Val Ser Gly Tyr Asn Asp Ala Asn Lys Ala Arg 165 170 175Leu Gln Ala Ala Leu Asp Ala Thr Ile Val Arg Leu Arg Asp Gly Ser 180 185 190His Phe Asn Leu Pro His Asp Pro Glu Phe Gly Pro Gly Arg Leu Asp 195 200 205Ala Ile Gly Ser Ile Phe Asn Ser Val Gly Tyr Glu Leu His Ala Asp 210 215 220Glu Gln Ile Tyr Gly Ala Glu Asp Ala Pro Val Ser Tyr Pro Phe Leu225 230 235 240Trp Asn Val Pro Gln Leu Asp Arg Val Gln Trp Thr Gly Phe Asn Pro 245 250 255Asn His Ile Asn Val Val Asp Ile Asp Asn Arg Lys Phe Asp Val Gly 260 265 270Ala Leu Ala Arg Asn Ala Gly Glu Ala Val Gly Val Phe Ala Asp Val 275 280 285Lys Val Leu Ser Pro Ile Gln Ser Ala Leu His Ile Gly Tyr Pro Ser 290 295 300Ser Ile Lys Val Asp Asn Leu Ile Arg Ile Glu Asp Gln Phe Gly Gln305 310 315 320Leu Lys Pro Pro Ala Trp Pro Asn Gln Leu Phe Gly Ala Pro Glu Pro 325 330 335Thr Arg Val Ala Glu Gly Arg Glu Leu Tyr Arg Gln His Cys Ser Ser 340 345 350Cys His Thr Pro Leu Asp Arg Asn Asp Leu Arg Thr Pro Val Lys Thr 355 360 365Val Leu Thr His Leu Gln Ala Arg Gly Glu Val Ala Pro Ile Gly Thr 370 375 380Asp Pro Trp Thr Ala Cys Asn Ser Ile Ala Gln Leu Lys Thr Gly Tyr385 390 395 400Val Arg Gly Lys Pro Tyr Leu Ser Phe Val Gly Thr Gly Gln Arg Gly 405 410 415Phe Tyr Gly Lys Gln Ala Tyr Ala Val Asp Val Leu Gln Glu Val Val 420 425 430Val Gln Ala Leu Ala Ala Arg Gly Leu Ser Val Ala Leu Gly Ala Phe 435 440 445Gln Thr Ala Ala Leu Gly Ile Phe Asp Gly Gln Leu Pro Pro Leu Ile 450 455 460Ser Pro Val Pro Asp Ser Pro Asp Ala Asp Ser Val Glu Ala Thr Ala465 470 475 480Ala Asp Ala Pro Gly Ala Leu Leu Leu Ala Glu Asn Val Ala Ala Asp 485 490 495Ser Asp Lys Ala Arg Arg Leu Glu Gln Cys Leu Ala Met Thr Ser Asp 500 505 510Leu Met Ala Tyr Lys Ala Arg Pro Leu Asn Gly Ile Trp Ala Ser Pro 515 520 525Pro Tyr Leu His Asn Gly Ser Val Ala Thr Leu Tyr Asp Leu Leu Leu 530 535 540Pro Pro Asp Leu Arg Pro Arg Thr Phe Tyr Thr Gly Ser Val Glu Phe545 550 555 560Asp Pro Val Asn Val Gly Tyr Ile Thr Asp Ala Gly Gly Ala Asn Arg 565 570 575Phe Leu Phe Asp Ser Gly Lys Pro Gly Asn Ala Asn Gly Gly His Asp 580 585 590Tyr Gly Asn Ala Gln Phe Asn Glu Gln Gln Arg Arg Ala Leu Val Glu 595 600 605Tyr Met Lys Thr Leu 61019610PRTFusarium oxysporum 19Met Val Ala Leu Leu Ile Phe Leu Gly Ile Phe Thr Cys Val Glu Thr1 5 10 15Leu Pro Leu Ser Asp Ser Pro Ser Ser Tyr Ile Pro Glu Glu Val Pro 20 25 30Ser Ser Gln Thr Ala Asp Ile Gly Leu Pro Pro Pro Thr Glu Phe Thr 35 40 45Leu Pro Asn Glu Asp Asp Glu Ile Leu Ile Arg Lys Leu Asn Ile Gln 50 55 60Lys Thr Arg Lys Glu Ile Leu Tyr Gly Pro Ser Leu Ile Gly Lys Thr65 70 75 80Ser Phe Phe Ile Ser Gly Pro Leu Gly Asp Gln Ile Ser Gln Arg Asp 85 90 95Gln Thr Leu Trp Ser Arg Asp Ala Ala Pro Val Val Gln Ala Val Ser 100 105 110His Asp Ala Ala Ala Ala Leu His Asp Ile Gln Ile His Gly Gly Leu 115 120 125Gln Asn Leu Asp Asp Tyr Lys Ile Leu Tyr Gln Gly His Trp Ser Ser 130 135 140Ser Val Pro Gly Gly Ile Ala Lys Gly Gln Phe Ser Asn Phe Thr Ser145 150 155 160Asp Leu Leu Phe Ser Met Glu Arg Leu Ser Thr Asn Pro Tyr Ile Leu 165 170 175Arg Arg Leu His Pro His Ala Asp Glu Leu Pro Phe Ala Val Asp Ser 180 185 190Lys Ile Val Gln Lys Leu Thr Gly Ser Thr Leu Pro Ser Leu His Lys 195 200 205Ala Gly Arg Leu Phe Leu Ala Asp His Ser Tyr Gln Lys Asp Tyr Val 210 215 220Ala Gln Glu Gly Arg Tyr Ala Ala Ala Cys Gln Ala Leu Phe Tyr Leu225 230 235 240Asp Asp Arg Cys His Gln Phe Leu Pro Leu Ala Ile Lys Thr Asn Val 245 250 255Gly Ser Asn Leu Thr Tyr Thr Pro Leu Asp Glu Pro Asn Asp Trp Leu 260 265 270Leu Ala Lys Val Met Phe Asn Val Asn Asp Leu Phe His Gly Gln Met 275 280 285Tyr His Leu Ala Ser Thr His Ala Val Ala Glu Ile Val His Leu Ala 290 295 300Ala Leu Arg Thr Met Ser Ser Arg His Pro Val Leu Ala Leu Leu Gln305 310 315 320Arg Leu Met Tyr Gln Ala Tyr Ala Ile Arg Pro Ile Gly Asn Asn Ile 325 330 335Leu Phe Asn Pro Gly Gly Leu Ile Asp Gln Asn Ser Val Phe Ser Asn 340 345 350Val Ala Val Arg Lys Phe Ala Thr Asp Phe Tyr Pro Thr Val Ala Gly 355 360 365Pro Val Arg Ser Asn Tyr Phe Glu Ala Asn Leu Arg Ser Arg Gly Leu 370 375 380Leu Asn Ala Thr His Gly Pro Asp Leu Pro His Phe Pro Phe Tyr Glu385 390 395 400Asp Gly Ala Arg Ile Ile Lys Val Ile Arg Thr Phe Ile Gln Ser Phe 405 410 415Val Lys Ser Ile Tyr Lys Ser Asp Lys Val Leu Ala Lys Asp Trp Glu 420 425 430Leu Gln Ala Trp Ile Ala Glu Ala Asn Gly Ala Ala Glu Val Ile Asp 435 440 445Phe Pro Pro Thr Pro Leu Lys Lys Arg Lys His Leu Val Asp Ile Leu 450 455 460Thr His Met Ala Trp Leu Thr Gly Val Ser His His Val Leu Asn Gln465 470 475 480Gly Glu Pro Val Thr Thr Ser Gly Val Leu Pro Leu His Pro Gly Ser 485 490 495Leu Tyr Ala Pro Val Pro Gly Glu Lys Gly Val Val Asp Ser Leu Leu 500 505 510Pro Trp Leu Pro Asn Glu Gln Lys Ser Val Asp Gln Ile Ser Phe Leu 515 520 525Ala Leu Phe Asn Arg Pro Gln Ile Val Glu Asn Asn Arg Thr Leu Arg 530 535 540Tyr Met Phe Asn Ser Glu Ser Leu Leu Ala Gly Thr Val Arg Ala Val545 550 555 560Ala Ala Ala Asn Glu Arg Phe Met Glu Glu Met Gly His Ile Ser Gln 565 570 575Glu Ile Ser Asn Arg Lys Phe Asp Asp Asp Gly Leu Ser Gln Gly Met 580 585 590Pro Phe Ile Trp Thr Gly Met Asp Pro Gly Val Ile Pro Phe Tyr Leu 595 600 605Ser Val 61020618PRTGaeumannomyces graminis 20Met Arg Ser Arg Ile Leu Ala Ile Val Phe Ala Ala Arg His Val Ala1 5 10 15Ala Leu Pro Leu Ala Ala Glu Asp Ala Ala Ala Thr Leu Ser Leu Thr 20 25 30Ser Ser Ala Ser Ser Thr Thr Val Leu Pro Ser Pro Thr Gln Tyr Thr 35 40 45Leu Pro Asn Asn Asp Pro Asn Gln Gly Ala Arg Asn Ala Ser Ile Ala 50 55 60Arg Lys Arg Glu Leu Phe Leu Tyr Gly Pro Ser Thr Leu Gly Gln Thr65 70 75 80Thr Phe Tyr Pro Thr Gly Glu Leu Gly Asn Asn Ile Ser Ala Arg Asp 85 90 95Val Leu Leu Trp Arg Gln Asp Ala Ala Asn Gln Thr Ala Thr Ala Tyr 100 105 110Arg Glu Ala Asn Glu Thr Phe Ala Asp Ile Thr Ser Arg Gly Gly Phe 115 120 125Lys Thr Leu Asp Asp Phe Ala Leu Leu Tyr Asn Gly His Trp Lys Glu 130 135 140Ser Val Pro Glu Gly Ile Ser Lys Gly Met Leu Ser Asn Cys Thr Ser145 150 155 160Asp Leu Leu Phe Ser Met Glu Arg Leu Ser Ser Asn Pro Tyr Val Leu

165 170 175Lys Arg Leu His Pro Thr Lys Asp Lys Leu Pro Phe Ser Val Glu Ser 180 185 190Lys Val Val Lys Lys Leu Thr Ala Thr Thr Leu Glu Ala Leu His Lys 195 200 205Gly Gly Arg Leu Phe Leu Val Asp His Ser Tyr Gln Lys Lys Tyr Thr 210 215 220Pro Gln Pro Gly Arg Tyr Ala Ala Ala Cys Gln Gly Leu Phe Tyr Leu225 230 235 240Asp Ala Arg Ser Asn Gln Phe Leu Pro Leu Ala Ile Lys Thr Asn Val 245 250 255Gly Val Asp Leu Thr Tyr Thr Pro Leu Asp Asp Lys Asp Asp Trp Leu 260 265 270Leu Ala Lys Ile Met Phe Asn Asn Asn Asp Leu Phe Tyr Ser Gln Met 275 280 285Tyr His Val Leu Phe His Thr Ile Pro Glu Ile Val His Glu Ala Ala 290 295 300Phe Arg Thr Leu Ser Asp Arg His Pro Val Met Gly Val Leu Asn Arg305 310 315 320Leu Met Tyr Gln Ala Tyr Ala Ile Arg Pro Val Gly Gly Ala Val Leu 325 330 335Phe Asn Pro Gly Gly Phe Trp Asp Gln Asn Phe Gly Leu Pro Ala Ser 340 345 350Ala Ala Ile Asp Phe Pro Gly Ser Val Tyr Ala Gln Gly Gly Gly Gly 355 360 365Phe Gln Ala Gly Tyr Leu Glu Lys Asp Leu Arg Ser Arg Gly Leu Ile 370 375 380Gly Glu Asp Ser Gly Pro Arg Leu Pro His Phe Pro Phe Tyr Glu Asp385 390 395 400Ala His Arg Leu Ile Gly Ala Ile Arg Arg Phe Met Gln Ala Phe Val 405 410 415Asp Ser Thr Tyr Gly Ala Asp Asp Gly Asp Asp Gly Ala Leu Leu Arg 420 425 430Asp Tyr Glu Leu Gln Asn Trp Ile Ala Glu Ala Asn Gly Pro Ala Gln 435 440 445Val Arg Asp Phe Pro Ala Ala Pro Leu Arg Arg Arg Ala Gln Leu Val 450 455 460Asp Val Leu Thr His Val Ala Trp Ile Thr Gly Gly Ala His His Val465 470 475 480Met Asn Gln Gly Ser Pro Val Lys Phe Ser Gly Val Leu Pro Leu His 485 490 495Pro Ala Ala Leu Tyr Ala Pro Ile Pro Thr Ala Lys Gly Ala Thr Gly 500 505 510Asn Gly Thr Arg Ala Gly Leu Leu Ala Trp Leu Pro Asn Glu Arg Gln 515 520 525Ala Val Glu Gln Val Ser Leu Leu Ala Arg Phe Asn Arg Ala Gln Val 530 535 540Gly Asp Arg Lys Gln Thr Val Arg Asp Ala Phe Ala Ala Pro Asp Leu545 550 555 560Leu Ala Gly Asn Gly Pro Gly Tyr Ala Ala Ala Asn Ala Arg Phe Val 565 570 575Glu Asp Thr Gly Arg Ile Ser Arg Glu Ile Ala Gly Arg Gly Phe Asp 580 585 590Gly Lys Gly Leu Ser Gln Gly Met Pro Phe Val Trp Thr Ala Leu Asn 595 600 605Pro Ala Val Asn Pro Phe Phe Leu Ser Val 610 61521609PRTColletotrichum gloeosporioides 21Met Arg Leu Leu Leu Ser Ile Ala Gly Leu Thr Thr Val Val Asn Ala1 5 10 15Leu Ala Val Arg Ala Asp Gly Asn Val Thr Ser Ser Thr Ala Val Ala 20 25 30Thr Pro Thr Ala Trp Thr Gly Phe Pro Val Pro Thr Glu Tyr Thr Leu 35 40 45Pro Gln Asp Asp His Asp Phe Gln Glu Arg Lys Glu Glu Ile Lys Leu 50 55 60Lys Arg Asp Thr Ile Thr Tyr Val Pro Ser Ile Ile Gly Glu Thr Ser65 70 75 80Leu Phe Ile Gly Gly Ser Val Gly Thr Gln Ile Val Arg Gln Glu Gln 85 90 95Ala Lys Trp Ile Gln Asp Leu Thr Pro Val Gln Gln Asp Ala Phe Arg 100 105 110Glu Gly Asn Ala Ser Leu Lys Ala Ile Gln Asp His Gly Gly Leu Lys 115 120 125Thr Leu Glu Asp Tyr Lys Ile Leu Tyr Asp Gly His Trp Ser Gly Ser 130 135 140Val Pro Gly Gly Ile Ala Gln Gly Gln Phe Asn Asn Phe Thr Ser Asp145 150 155 160Leu Leu Phe Ala Met Glu Arg Leu Ser Thr Asn Pro Tyr Val Val Arg 165 170 175Arg Leu Asn Pro Glu Ser Asp Lys Ile Pro Phe Ser Val Asp Ala Asn 180 185 190Asn Val Thr His Leu Thr Gly Thr Thr Leu Asp Thr Leu Phe Lys Ser 195 200 205Gly Ser Leu Phe Leu Ala Asp His Ser Tyr Gln Ala Glu Tyr Thr Ala 210 215 220Gln Asp Gly Arg Tyr Ser Ala Ala Cys Gln Ala Leu Phe Phe Leu Asp225 230 235 240Gln Arg Ser Gly Gln Phe Leu Pro Leu Ala Ile Lys Thr Asn Val Gly 245 250 255Ser Asp Leu Val Tyr Thr Pro Leu Asp Asp Pro Asn Asp Trp Leu Leu 260 265 270Ala Lys Ile Met Tyr Asn Val Asn Asp Phe Phe His Gly Gln Ile Tyr 275 280 285His Leu Ala Asn Ser His Ala Val Ala Glu Ile Val Asn Leu Ala Ala 290 295 300Ile Arg Thr Leu Ser Ser Arg His Pro Val Phe Gly Leu Leu Gln Arg305 310 315 320Leu Met Phe Gln Ala Tyr Ala Ile Arg Ala Thr Gly Glu Ile Ala Leu 325 330 335Phe Asn Pro Gly Gly Leu Phe Asp Gln Ser Phe Ala Phe Ser Asn Val 340 345 350Tyr Ala Arg Lys Phe Ala Thr Asp Phe Tyr Pro Thr Val Ala Gly Pro 355 360 365Phe Gln Ala Asn Tyr Phe Glu Glu Asp Leu Arg Ala Arg Gly Leu Leu 370 375 380Asn Ala Ser Tyr Gly Pro Glu Leu Pro His Leu Pro Phe His Glu Asp385 390 395 400Gly His Lys Ile Ile Asn Ala Ile Arg Thr Phe Ile Gly Thr Phe Val 405 410 415Asp Thr Val Tyr Glu Ser Asp Lys Val Leu Ala Glu Asp Ser Glu Leu 420 425 430Gln Ala Trp Ile Ala Glu Ala Asn Gly Pro Ala Lys Val Ile Asn Phe 435 440 445Pro Ser Ala Pro Leu Asn Thr Arg Lys Gln Leu Ala Glu Ile Leu Thr 450 455 460His Met Ala Trp Leu Thr Gly Val Ser His His Val Leu Asn Gln Gly465 470 475 480Glu Pro Phe Thr Thr Ser Gly Val Leu Pro Leu His Pro Ala Ser Leu 485 490 495Tyr Ala Pro Val Pro Thr Ala Lys Gly Gly Ile Lys Asp Leu Leu Pro 500 505 510Trp Leu Pro Asn Glu Gln Lys Ser Val Glu Gln Ile Ser Leu Leu Ala 515 520 525Arg Phe Asn Arg Pro Lys Ile Val Glu Asn Asn Glu Thr Leu Leu His 530 535 540Met Phe Asp Val Lys Thr Leu Leu Ser Gly Thr Gly Glu Ala Val Lys545 550 555 560Ala Ala Asn Glu Gln Phe Met Ile Ala Met Gly Thr Ile Ser Lys Glu 565 570 575Ile Ser Thr Arg Lys Phe Asp Asp Gln Gly Leu Ser Gln Gly Met Pro 580 585 590Phe Ile Trp Thr Gly Met Asp Pro Gly Val Ile Pro Phe Tyr Leu Ser 595 600 605Val22896PRTArabidopsis thaliana 22Met Tyr Cys Arg Glu Ser Leu Ser Ser Leu Gln Thr Leu Asn Val Ala1 5 10 15Lys Ser Leu Ser Ser Leu Phe Pro Lys Gln Ser Ala Leu Ile Asn Pro 20 25 30Ile Ser Ala Gly Arg Arg Asn Asn Leu Pro Arg Pro Asn Leu Arg Arg 35 40 45Arg Cys Lys Val Thr Ala Ser Arg Ala Asn Ile Glu Gln Glu Gly Asn 50 55 60Thr Val Lys Glu Pro Ile Gln Asn Ile Lys Val Lys Gly Tyr Ile Thr65 70 75 80Ala Gln Glu Glu Phe Leu Glu Gly Ile Thr Trp Ser Arg Gly Leu Asp 85 90 95Asp Ile Ala Asp Ile Arg Gly Arg Ser Leu Leu Val Glu Leu Ile Ser 100 105 110Ala Lys Thr Asp Gln Arg Ile Thr Val Glu Asp Tyr Ala Gln Arg Val 115 120 125Trp Ala Glu Ala Pro Asp Glu Lys Tyr Glu Cys Glu Phe Glu Met Pro 130 135 140Glu Asp Phe Gly Pro Val Gly Ala Ile Lys Ile Gln Asn Gln Tyr His145 150 155 160Arg Gln Leu Phe Leu Lys Gly Val Glu Leu Lys Leu Pro Gly Gly Ser 165 170 175Ile Thr Phe Thr Cys Glu Ser Trp Val Ala Pro Lys Ser Val Asp Pro 180 185 190Thr Lys Arg Ile Phe Phe Ser Asp Lys Ser Tyr Leu Pro Ser Gln Thr 195 200 205Pro Glu Pro Leu Lys Lys Tyr Arg Lys Glu Glu Leu Glu Thr Leu Gln 210 215 220Gly Lys Asn Arg Glu Glu Val Gly Glu Phe Thr Lys Phe Glu Arg Ile225 230 235 240Tyr Asp Tyr Asp Val Tyr Asn Asp Val Gly Asp Pro Asp Asn Asp Pro 245 250 255Glu Leu Ala Arg Pro Val Ile Gly Gly Leu Thr His Pro Tyr Pro Arg 260 265 270Arg Cys Lys Thr Gly Arg Lys Pro Cys Glu Thr Asp Pro Ser Ser Glu 275 280 285Gln Arg Tyr Gly Gly Glu Phe Tyr Val Pro Arg Asp Glu Glu Phe Ser 290 295 300Thr Ala Lys Gly Thr Ser Phe Thr Gly Lys Ala Val Leu Ala Ala Leu305 310 315 320Pro Ser Ile Phe Pro Gln Ile Glu Ser Val Leu Leu Ser Pro Gln Glu 325 330 335Pro Phe Pro His Phe Lys Ala Ile Gln Asn Leu Phe Glu Glu Gly Ile 340 345 350Gln Leu Pro Lys Asp Ala Gly Leu Leu Pro Leu Leu Pro Arg Ile Ile 355 360 365Lys Ala Leu Gly Glu Ala Gln Asp Asp Ile Leu Gln Phe Asp Ala Pro 370 375 380Val Leu Ile Asn Arg Asp Arg Phe Ser Trp Leu Arg Asp Asp Glu Phe385 390 395 400Ala Arg Gln Thr Leu Ala Gly Leu Asn Pro Tyr Ser Ile Gln Leu Val 405 410 415Glu Glu Trp Pro Leu Ile Ser Lys Leu Asp Pro Ala Val Tyr Gly Asp 420 425 430Pro Thr Ser Leu Ile Thr Trp Glu Ile Val Glu Arg Glu Val Lys Gly 435 440 445Asn Met Thr Val Asp Glu Ala Leu Lys Asn Lys Arg Leu Phe Val Leu 450 455 460Asp Tyr His Asp Leu Leu Leu Pro Tyr Val Asn Lys Val Arg Glu Leu465 470 475 480Asn Asn Thr Thr Leu Tyr Ala Ser Arg Thr Leu Phe Phe Leu Ser Asp 485 490 495Asp Ser Thr Leu Arg Pro Val Ala Ile Glu Leu Thr Cys Pro Pro Asn 500 505 510Ile Asn Lys Pro Gln Trp Lys Gln Val Phe Thr Pro Gly Tyr Asp Ala 515 520 525Thr Ser Cys Trp Leu Trp Asn Leu Ala Lys Thr His Ala Ile Ser His 530 535 540Asp Ala Gly Tyr His Gln Leu Ile Ser His Trp Leu Arg Thr His Ala545 550 555 560Cys Thr Glu Pro Tyr Ile Ile Ala Ala Asn Arg Gln Leu Ser Ala Met 565 570 575His Pro Ile Tyr Arg Leu Leu His Pro His Phe Arg Tyr Thr Met Glu 580 585 590Ile Asn Ala Arg Ala Arg Gln Ser Leu Val Asn Gly Gly Gly Ile Ile 595 600 605Glu Thr Cys Phe Trp Pro Gly Lys Tyr Ala Leu Glu Leu Ser Ser Ala 610 615 620Val Tyr Gly Lys Leu Trp Arg Phe Asp Gln Glu Gly Leu Pro Ala Asp625 630 635 640Leu Ile Lys Arg Gly Leu Ala Glu Glu Asp Lys Thr Ala Glu His Gly 645 650 655Val Arg Leu Thr Ile Pro Asp Tyr Pro Phe Ala Asn Asp Gly Leu Ile 660 665 670Leu Trp Asp Ala Ile Lys Glu Trp Val Thr Asp Tyr Val Lys His Tyr 675 680 685Tyr Pro Asp Glu Glu Leu Ile Thr Ser Asp Glu Glu Leu Gln Gly Trp 690 695 700Trp Ser Glu Val Arg Asn Ile Gly His Gly Asp Lys Lys Asp Glu Pro705 710 715 720Trp Trp Pro Val Leu Lys Thr Gln Asp Asp Leu Ile Gly Val Val Thr 725 730 735Thr Ile Ala Trp Val Thr Ser Gly His His Ala Ala Val Asn Phe Gly 740 745 750Gln Tyr Gly Tyr Gly Gly Tyr Phe Pro Asn Arg Pro Thr Thr Thr Arg 755 760 765Ile Arg Met Pro Thr Glu Asp Pro Thr Asp Glu Ala Leu Lys Glu Phe 770 775 780Tyr Glu Ser Pro Glu Lys Val Leu Leu Lys Thr Tyr Pro Ser Gln Lys785 790 795 800Gln Ala Thr Leu Val Met Val Thr Leu Asp Leu Leu Ser Thr His Ser 805 810 815Pro Asp Glu Glu Tyr Ile Gly Glu Gln Gln Glu Ala Ser Trp Ala Asn 820 825 830Glu Pro Val Ile Asn Ala Ala Phe Glu Arg Phe Lys Gly Lys Leu Gln 835 840 845Tyr Leu Glu Gly Val Ile Asp Glu Arg Asn Val Asn Ile Thr Leu Lys 850 855 860Asn Arg Ala Gly Ala Gly Val Val Lys Tyr Glu Leu Leu Lys Pro Thr865 870 875 880Ser Glu His Gly Val Thr Gly Met Gly Val Pro Tyr Ser Ile Ser Ile 885 890 89523941PRTOryza sativa 23Met Leu Arg Pro Gln Leu Asn Pro Ser Ser Ser His His His Thr Thr1 5 10 15Thr Thr Ser Ser Ser Ser Ser Thr Gln Leu Tyr Phe Ala Ser Ser Ser 20 25 30Cys Ile Ala Ser Leu Arg Arg Pro Ser Pro Pro Ser Leu Ile Ala Gly 35 40 45Ala Gly Cys Arg Thr Thr Arg Arg Arg Gln Gln Gly Arg Gln Arg Val 50 55 60Val Val Arg Cys Ala Ser Ser Ser Ala Ala Ser Ser Ala Ser Glu Ala65 70 75 80Ala Arg Arg Gly Thr Gly Ser Ser Asp Met Ala Pro Ala Ala Val Val 85 90 95Lys Val Lys Ala Val Ala Thr Ile Lys Val Thr Val Glu Gly Leu Leu 100 105 110Asn Ser Leu Arg Pro Ser Lys Ala Ile Asp Asn Ile Arg Asp Leu Ile 115 120 125Gly Arg Ser Leu Phe Leu Glu Leu Val Ser Ser Glu Leu Glu Ala Lys 130 135 140Thr Gly Lys Lys Lys Ala Thr Val His Ser Tyr Ala His Lys Val Asp145 150 155 160Asp Asp Asp His Gly Val Val Thr Tyr Glu Ala Asp Phe Asp Val Pro 165 170 175Thr Gly Phe Gly Pro Ile Gly Ala Val Val Val Thr Asn Glu Leu Gly 180 185 190Gln Glu Met Phe Leu Glu Asp Leu Asn Leu Thr Ala Gly Asp Gly Ala 195 200 205Gly Asn Ser Thr Val Leu Pro Ile Arg Cys Asn Ser Trp Val Gln Pro 210 215 220Lys Ser Ser Ile Asp Glu Gly Thr Pro Gly Lys Arg Ile Phe Phe Ala225 230 235 240Lys Ala Tyr Leu Pro Gly Gln Thr Pro Ala Gly Leu Arg Ser Tyr Arg 245 250 255Glu Glu Asp Leu Lys Gln Lys Arg Gly Asn Gly Ala Gly Gln Arg Glu 260 265 270Ala Asp Asp Arg Val Tyr Asp Tyr Asp Val Tyr Asn Asp Leu Gly Asn 275 280 285Pro Asp Ser Asn Gly Asp Leu Ala Arg Pro Val Leu Gly Gly Ser Lys 290 295 300Gln Phe Pro Tyr Pro Arg Arg Cys Arg Thr Gly Arg Pro Pro Ser Lys305 310 315 320Lys Asp Pro Lys Ser Glu Thr Arg Lys Gly Asn Val Tyr Val Pro Arg 325 330 335Asp Glu Glu Phe Ser Glu Val Lys Asn Ala Gln Phe Leu Leu Lys Thr 340 345 350Leu Gln Ser Val Leu His Ala Ala Val Pro Ala Ala Gln Ser Ala Leu 355 360 365Ile Asp Asn Leu Ser Leu Asn Leu Pro Phe Pro Ser Phe Phe Val Ile 370 375 380Asp Lys Leu Phe Glu Asp Gly Val Glu Leu Pro Gly Val Glu Lys Leu385 390 395 400Gly Phe Leu His Ser Ile Val Pro Arg Leu Leu Glu Leu Leu Arg Asp 405 410 415Ser Pro Gly Asp Lys Ile Leu Leu Phe Asp Thr Pro Ala Asn Val Gln 420 425 430Lys Asp Lys Phe Ala Trp Leu Arg Asp Glu Glu Phe Ala Arg Glu Thr 435 440 445Leu Ala Gly Ile Asn Pro Tyr Ala Ile Glu Leu Val Arg Glu Phe Pro 450 455 460Leu Lys Ser Lys Leu Asp Pro Ala Val Tyr Gly Pro Ala Glu Ser Ala465 470 475 480Ile Thr Ala Asp Leu Leu Glu Glu Gln Met Arg Arg Val Met Thr Val 485 490 495Glu Glu Ala Ile Ser Gln Lys Arg Leu Phe Met Leu Asp Phe His Asp

500 505 510Leu Phe Leu Pro Tyr Val His Lys Ile Arg Ser Leu Lys His Thr Thr 515 520 525Met Tyr Gly Ser Arg Thr Ile Phe Phe Leu Thr Asp Asp Gly Thr Leu 530 535 540Arg Leu Leu Ala Ile Glu Leu Thr Arg Pro Ala Ser Pro Ser Gln Pro545 550 555 560Gln Trp Arg Gln Val Phe Thr Pro Ser Thr Asp Thr Thr Lys Ser Trp 565 570 575Leu Trp Arg Met Ala Lys Ala His Val Arg Ala His Asp Ala Gly His 580 585 590His Glu Leu Ile Thr His Trp Leu Arg Thr His Cys Ala Val Glu Pro 595 600 605Tyr Ile Ile Ala Ala Asn Arg Gln Leu Ser Glu Met His Pro Ile Tyr 610 615 620Gln Leu Leu His Pro His Phe Arg Tyr Thr Met Arg Ile Asn Ala Leu625 630 635 640Ala Arg Ser Arg Leu Ile Ser Ala Ala Gly Ile Ile Glu Leu Ser Phe 645 650 655Ser Pro Gln Lys Tyr Ser Met Glu Leu Ser Ser Val Ala Tyr Asp Lys 660 665 670Leu Trp Arg Phe Asp Met Glu Ala Leu Pro Ala Asp Leu Val Arg Arg 675 680 685Gly Met Ala Glu Glu Asp Pro Thr Ala Glu His Gly Leu Arg Leu Ala 690 695 700Ile Glu Asp Tyr Pro Phe Ala Asn Asp Gly Leu Leu Ile Trp Asp Ala705 710 715 720Ile Lys Thr Trp Val Gln Ala Tyr Val Ala Arg Phe Tyr Pro Asp Ala 725 730 735Asp Ser Val Ala Gly Asp Glu Glu Leu Gln Ala Phe Trp Thr Glu Val 740 745 750Arg Thr Lys Gly His Gly Asp Lys Lys Asp Ala Pro Trp Trp Pro Lys 755 760 765Leu Asp Ser Pro Glu Ser Leu Ala His Thr Leu Thr Thr Ile Val Trp 770 775 780Val Ala Ala Ala His His Ala Ala Val Asn Phe Gly Gln Tyr Asp Phe785 790 795 800Gly Gly Tyr Phe Pro Asn Arg Pro Ser Ile Ala Arg Thr Val Met Pro 805 810 815Val Glu Glu Pro Val Asp Gly Ala Ala Met Glu Arg Phe Leu Asp Asn 820 825 830Pro Asp Gln Ala Leu Arg Glu Cys Phe Pro Ser Gln Val Gln Ala Thr 835 840 845Val Val Met Ala Val Leu Asp Val Leu Ser Thr His Ser Thr Asp Glu 850 855 860Glu Tyr Leu Gly Gly Glu Gln Thr Arg Pro Trp Asn Ser Asp Ala Ala865 870 875 880Val Gln Ala Ala Tyr Ala Gly Phe Thr Ala Arg Leu Lys Glu Ile Glu 885 890 895Gly Val Ile Asp Gly Arg Asn Lys Asp Arg Lys Leu Lys Asn Arg Cys 900 905 910Gly Ala Gly Ile Leu Pro Tyr Gln Leu Met Lys Pro Phe Ser Asp Ala 915 920 925Gly Val Thr Gly Met Gly Ile Pro Asn Ser Thr Ser Ile 930 935 94024685PRTPseudomonas aeruginosa 24Met Lys Arg Arg Ser Val Leu Leu Ser Gly Val Ala Leu Ser Gly Thr1 5 10 15Ala Leu Ala Asn Asp Ser Ile Phe Phe Ser Pro Leu Lys Tyr Leu Gly 20 25 30Ala Glu Gln Gln Arg Ser Ile Asp Ala Ser Arg Ser Leu Leu Asp Asn 35 40 45Leu Ile Pro Pro Ser Leu Pro Gln Tyr Asp Asn Leu Ala Gly Lys Leu 50 55 60Ala Arg Arg Ala Val Leu Thr Ser Lys Lys Leu Val Tyr Val Trp Thr65 70 75 80Glu Asn Phe Ala Asn Val Lys Gly Val Pro Met Ala Arg Ser Val Pro 85 90 95Leu Gly Glu Leu Pro Asn Val Asp Trp Leu Leu Lys Thr Ala Gly Val 100 105 110Ile Val Glu Leu Ile Val Asn Phe Val Ala Ser Leu Pro Ala Ser Ala 115 120 125Ala Ala Gln Phe Glu Arg Ile Ala Ala Gly Leu Ser Gly Asp Leu Glu 130 135 140Ala Ala Arg Gln Val His Glu Ala Leu Leu Glu Glu Ala Lys Asn Asp145 150 155 160Pro Ala Ala Ala Gly Ser Leu Leu Leu Arg Phe Thr Glu Leu Gln Thr 165 170 175Arg Val Ile Ala Leu Leu Thr Arg Val Gly Leu Leu Val Asp Asp Ile 180 185 190Leu Lys Ser Ala Ser Asn Leu Val Thr Gln Gly Gly Gln Gly Asp Gly 195 200 205Leu Asn Arg Phe Arg Ala Val Phe Gly Thr Leu Arg Leu Pro Glu Val 210 215 220Ala Asp Ser Phe Arg Asp Asp Glu Ala Phe Ala Tyr Trp Arg Val Ala225 230 235 240Gly Pro Asn Pro Leu Leu Ile Arg Arg Val Asp Ala Leu Pro Ala Asn 245 250 255Phe Pro Leu Gly Glu Glu Gln Phe Arg Arg Val Met Gly Ala Asp Asp 260 265 270Ser Leu Leu Glu Ala Ala Ala Ser Arg Arg Leu Tyr Leu Leu Asp Tyr 275 280 285Ala Glu Leu Gly Lys Leu Ala Pro Ser Gly Ala Val Asp Lys Leu Leu 290 295 300Thr Gly Thr Gly Phe Ala Tyr Ala Pro Ile Ala Leu Phe Ala Leu Gly305 310 315 320Lys Asp Arg Ala Gly Leu Leu Pro Val Ala Ile Gln Cys Gly Gln Asp 325 330 335Pro Ala Thr His Pro Met Phe Val Arg Pro Ala Glu Ser Glu Ser Asp 340 345 350Leu Tyr Trp Gly Trp Gln Met Ala Lys Thr Val Val Gln Val Ala Glu 355 360 365Glu Asn Tyr His Glu Met Phe Val His Leu Ala Gln Thr His Leu Val 370 375 380Ser Glu Ala Phe Cys Leu Ala Thr Gln Arg Thr Leu Ala Pro Ser His385 390 395 400Pro Leu His Val Leu Leu Ala Pro His Phe Glu Gly Thr Leu Phe Ile 405 410 415Asn Glu Gly Ala Ala Arg Ile Leu Leu Pro Ser Ala Gly Phe Ile Asp 420 425 430Val Met Phe Ala Ala Pro Ile Gln Asp Thr Gln Ala Thr Ala Gly Gly 435 440 445Asn Arg Leu Gly Phe Asp Phe Tyr Arg Gly Met Leu Pro Glu Ser Leu 450 455 460Lys Ala Arg Asn Val Asp Asp Pro Ala Ala Leu Pro Asp Tyr Pro Tyr465 470 475 480Arg Asp Asp Gly Leu Leu Val Trp Asn Ala Ile Arg Gln Trp Ala Ala 485 490 495Asp Tyr Val Ala Val Tyr Tyr Ala Ser Asp Gly Asp Val Thr Ala Asp 500 505 510Val Glu Leu Ala Ala Trp Val Gly Glu Val Ile Gly Ser Gly Lys Val 515 520 525Ala Gly Phe Arg Pro Ile Thr Gly Arg Ser Gln Leu Val Glu Val Leu 530 535 540Thr Met Val Ile Phe Thr Ala Ser Ala Gln His Ala Ala Val Asn Phe545 550 555 560Pro Gln Pro Ser Met Met Thr Tyr Ala Pro Ala Ile Cys Ala Met Ser 565 570 575Ala Ala Pro Ala Pro Asp Ser Pro Ser Gly Lys Ser Glu Ala Asp Trp 580 585 590Leu Lys Met Met Pro Pro Thr Leu Val Ala Leu Glu Lys Val Asn Ile 595 600 605Tyr His Leu Leu Gly Ser Val Tyr His Gly Arg Leu Gly Asp Tyr Arg 610 615 620Gln Thr Gly Phe Pro Tyr Ala Pro Val Phe Ser Asp Arg Arg Val Thr625 630 635 640Ala Ser Gly Gly Pro Leu Glu Arg Phe Gln Ala Arg Leu Lys Glu Val 645 650 655Glu Ala Thr Ile Arg Thr Arg Asn Gln Ala Arg Arg Lys Pro Tyr Glu 660 665 670Tyr Leu Leu Pro Ser Arg Ile Pro Ala Ser Thr Asn Ile 675 680 68525880PRTMomordica charantia 25Met Phe Gly Ile Gly Lys Ser Ile Ile Glu Gly Ala Val Asn Thr Thr1 5 10 15Gly Asp Leu Ala Gly Ser Val Ile Asn Ala Gly Gly Asn Ile Val Gly 20 25 30Arg Val Thr Asn Ile Gly Gly Lys Lys Ile Lys Gly Thr Val Val Leu 35 40 45Met Arg Ser Asn Val Leu Asp Phe Thr Glu Phe His Ser Ser Leu Leu 50 55 60Asp Gly Val Thr Glu Leu Leu Gly Gly Gly Ile Ser Leu Gln Leu Ile65 70 75 80Ser Ala Thr His Ala Ser Asn Asp Ser Arg Gly Lys Val Gly Lys Gly 85 90 95Ala Phe Leu Glu Arg Trp Leu Thr Ser Val Pro Pro Leu Phe Ala Gly 100 105 110Glu Ser Val Phe Gln Val Asn Phe Asp Trp Glu Glu Asn Phe Gly Phe 115 120 125Pro Gly Ala Phe Phe Ile Lys Asn Gly His Thr Ser Glu Phe Phe Leu 130 135 140Lys Ser Val Thr Leu Glu Asp Val Pro Gly Phe Gly Arg Val His Phe145 150 155 160Asp Cys Asn Ser Trp Val Tyr Pro Ser Arg Arg Tyr Lys Lys Asp Arg 165 170 175Ile Phe Phe Ala Asn His Thr Cys Leu Pro Ile Asp Thr Pro Asp Ser 180 185 190Leu Arg Lys Tyr Arg Glu Glu Glu Leu Leu Asn Leu Arg Gly Asp Gly 195 200 205Thr Gly Glu Arg Lys Glu Trp Asp Arg Ile Tyr Asp Tyr Asp Val Tyr 210 215 220Asn Asp Leu Cys Asp Pro Asn Gly Gly Pro Asn Leu Val Arg Pro Ile225 230 235 240Leu Gly Gly Ser Asp Gln Tyr Pro Tyr Pro Arg Arg Gly Arg Thr Gly 245 250 255Arg Pro Pro Ala Arg Lys Asp His Lys Tyr Glu Ser Arg Leu Ser Asp 260 265 270Val Met Ser Leu Asn Ile Tyr Val Pro Arg Asp Glu Asn Phe Gly His 275 280 285Leu Lys Met Ala Asp Phe Leu Gly Asn Thr Leu Lys Val Leu Ser Thr 290 295 300Ser Ile Gln Pro Gly Leu Glu Ser Ile Phe Asp Ser Thr Pro Gly Glu305 310 315 320Phe Asp Lys Phe Lys Glu Val Asp Asp Leu Phe Glu Arg Gly Phe Pro 325 330 335Ile Pro Leu Asn Ile Phe Lys Asn Leu Thr Glu Asp Leu Ala Pro Pro 340 345 350Leu Phe Lys Ala Phe Leu Arg Ser Asp Gly Glu Arg Phe Leu Lys Tyr 355 360 365Pro Thr Pro Gln Val Ile Lys Asp Asn Lys Leu Gly Trp Arg Thr Asp 370 375 380Glu Glu Phe Ala Arg Glu Met Ile Ala Gly Val Asn Pro Leu Ile Ile385 390 395 400Arg Arg Leu Glu Val Phe Pro Pro Leu Ser Lys Leu Asp Pro His Val 405 410 415Tyr Gly Asn Gln Asn Ser Thr Met Thr Glu Glu Gln Ile Lys His Gly 420 425 430Leu Asp Gly Leu Thr Val Asp Glu Ala Ile Lys Glu Asn Lys Leu Tyr 435 440 445Ile Leu Asp His His Asp Ala Leu Met Pro Tyr Leu Arg Arg Ile Asn 450 455 460Ser Thr Ser Thr Lys Thr Tyr Ala Thr Arg Thr Leu Leu Phe Leu Lys465 470 475 480Asp Asp Ser Thr Leu Lys Pro Leu Ala Ile Glu Leu Ser Leu Pro His 485 490 495Pro Gln Gly Asp Glu His Gly Ala Ile Ser Lys Leu Tyr Phe Pro Ala 500 505 510Glu Gly Arg Val Glu Ser Ala Ile Trp Gln Leu Ala Lys Ala Tyr Val 515 520 525Ala Val Asn Asp Ser Gly Tyr His Gln Leu Asn Ser His Trp Leu His 530 535 540Thr His Ala Val Leu Glu Pro Phe Val Ile Thr Thr His Arg Arg Leu545 550 555 560Ser Val Leu His Pro Ile His Lys Leu Leu Ala Pro His Tyr Lys Asp 565 570 575Thr Met Phe Ile Asn Ala Ser Ala Arg Gln Val Leu Ile Asn Ala Gly 580 585 590Gly Leu Ile Glu Ser Thr Gln Phe Pro Ala Lys Tyr Ala Met Glu Leu 595 600 605Ser Ser Tyr Ile Tyr Lys Glu Trp Lys Phe Pro Asp Glu Ala Leu Pro 610 615 620Thr Asn Leu Ile Lys Arg Gly Val Ala Ile Glu Asp Ser Gly Ser Pro625 630 635 640His Gly Val Arg Leu Leu Ile Asn Asp Tyr Pro Phe Ala Val Asp Gly 645 650 655Leu Glu Ile Trp Ser Ala Ile Lys Thr Trp Val Thr Asp Tyr Cys Ser 660 665 670Leu Tyr Tyr Lys Asp Asp Asp Ala Ile Arg Asn Asp Val Glu Leu Gln 675 680 685Ser Trp Trp Lys Glu Leu Arg Glu Lys Gly His Thr Asp Lys Lys Asp 690 695 700Glu Pro Trp Trp Pro Lys Met Gln Thr Phe Ser Glu Leu Ile Glu Ser705 710 715 720Cys Thr Ile Ile Ile Trp Ile Ser Ser Ala Leu His Ala Ala Val Asn 725 730 735Phe Gly Gln Tyr Pro Tyr Gly Gly Tyr Val Pro Asn Arg Pro Thr Thr 740 745 750Ser Arg Arg Phe Met Pro Glu Val Gly Thr Ala Glu Tyr Lys Glu Val 755 760 765Glu Ser Asn Pro Glu Lys Ala Phe Leu Arg Thr Ile Ser Ser Gln Ile 770 775 780Val Ala Leu Leu Gly Leu Ser Ile Ile Glu Ile Leu Ser Lys His Ala785 790 795 800Ser Asp Glu Val Tyr Leu Gly Gln Arg Ala Ser Ile Glu Trp Thr Ser 805 810 815Asp Lys Ser Ala Ile Glu Ala Phe Glu Lys Phe Gly Lys Glu Leu Phe 820 825 830Glu Val Glu Asp Arg Ile Met Arg Arg Asn Gln Asp Val Asn Leu Lys 835 840 845Asn Arg Ala Gly Pro Val Asn Met Pro Tyr Thr Leu Leu Val Pro Ser 850 855 860Ser Thr Glu Gly Leu Thr Gly Arg Gly Ile Pro Asn Ser Ile Ser Ile865 870 875 88026674PRTHomo sapiens 26Met Pro Ser Tyr Thr Val Thr Val Ala Thr Gly Ser Gln Trp Phe Ala1 5 10 15Gly Thr Asp Asp Tyr Ile Tyr Leu Ser Leu Val Gly Ser Ala Gly Cys 20 25 30Ser Glu Lys His Leu Leu Asp Lys Pro Phe Tyr Asn Asp Phe Glu Arg 35 40 45Gly Ala Val Asp Ser Tyr Asp Val Thr Val Asp Glu Glu Leu Gly Glu 50 55 60Ile Gln Leu Val Arg Ile Glu Lys Arg Lys Tyr Trp Leu Asn Asp Asp65 70 75 80Trp Tyr Leu Lys Tyr Ile Thr Leu Lys Thr Pro His Gly Asp Tyr Ile 85 90 95Glu Phe Pro Cys Tyr Arg Trp Ile Thr Gly Asp Val Glu Val Val Leu 100 105 110Arg Asp Gly Arg Ala Lys Leu Ala Arg Asp Asp Gln Ile His Ile Leu 115 120 125Lys Gln His Arg Arg Lys Glu Leu Glu Thr Arg Gln Lys Gln Tyr Arg 130 135 140Trp Met Glu Trp Asn Pro Gly Phe Pro Leu Ser Ile Asp Ala Lys Cys145 150 155 160His Lys Asp Leu Pro Arg Asp Ile Gln Phe Asp Ser Glu Lys Gly Val 165 170 175Asp Phe Val Leu Asn Tyr Ser Lys Ala Met Glu Asn Leu Phe Ile Asn 180 185 190Arg Phe Met His Met Phe Gln Ser Ser Trp Asn Asp Phe Ala Asp Phe 195 200 205Glu Lys Ile Phe Val Lys Ile Ser Asn Thr Ile Ser Glu Arg Val Met 210 215 220Asn His Trp Gln Glu Asp Leu Met Phe Gly Tyr Gln Phe Leu Asn Gly225 230 235 240Cys Asn Pro Val Leu Ile Arg Arg Cys Thr Glu Leu Pro Glu Lys Leu 245 250 255Pro Val Thr Thr Glu Met Val Glu Cys Ser Leu Glu Arg Gln Leu Ser 260 265 270Leu Glu Gln Glu Val Gln Gln Gly Asn Ile Phe Ile Val Asp Phe Glu 275 280 285Leu Leu Asp Gly Ile Asp Ala Asn Lys Thr Asp Pro Cys Thr Leu Gln 290 295 300Phe Leu Ala Ala Pro Ile Cys Leu Leu Tyr Lys Asn Leu Ala Asn Lys305 310 315 320Ile Val Pro Ile Ala Ile Gln Leu Asn Gln Ile Pro Gly Asp Glu Asn 325 330 335Pro Ile Phe Leu Pro Ser Asp Ala Lys Tyr Asp Trp Leu Leu Ala Lys 340 345 350Ile Trp Val Arg Ser Ser Asp Phe His Val His Gln Thr Ile Thr His 355 360 365Leu Leu Arg Thr His Leu Val Ser Glu Val Phe Gly Ile Ala Met Tyr 370 375 380Arg Gln Leu Pro Ala Val His Pro Ile Phe Lys Leu Leu Val Ala His385 390 395 400Val Arg Phe Thr Ile Ala Ile Asn Thr Lys Ala Arg Glu Gln Leu Ile 405 410 415Cys Glu Cys Gly Leu Phe Asp Lys Ala Asn Ala Thr Gly Gly Gly Gly 420 425 430His Val Gln Met Val Gln Arg Ala Met Lys Asp Leu Thr Tyr Ala Ser 435 440 445Leu Cys Phe Pro Glu Ala Ile Lys Ala Arg Gly Met Glu Ser Lys Glu 450

455 460Asp Ile Pro Tyr Tyr Phe Tyr Arg Asp Asp Gly Leu Leu Val Trp Glu465 470 475 480Ala Ile Arg Thr Phe Thr Ala Glu Val Val Asp Ile Tyr Tyr Glu Gly 485 490 495Asp Gln Val Val Glu Glu Asp Pro Glu Leu Gln Asp Phe Val Asn Asp 500 505 510Val Tyr Val Tyr Gly Met Arg Gly Arg Lys Ser Ser Gly Phe Pro Lys 515 520 525Ser Val Lys Ser Arg Glu Gln Leu Ser Glu Tyr Leu Thr Val Val Ile 530 535 540Phe Thr Ala Ser Ala Gln His Ala Ala Val Asn Phe Gly Gln Tyr Asp545 550 555 560Trp Cys Ser Trp Ile Pro Asn Ala Pro Pro Thr Met Arg Ala Pro Pro 565 570 575Pro Thr Ala Lys Gly Val Val Thr Ile Glu Gln Ile Val Asp Thr Leu 580 585 590Pro Asp Arg Gly Arg Ser Cys Trp His Leu Gly Ala Val Trp Ala Leu 595 600 605Ser Gln Phe Gln Glu Asn Glu Leu Phe Leu Gly Met Tyr Pro Glu Glu 610 615 620His Phe Ile Glu Lys Pro Val Lys Glu Ala Met Ala Arg Phe Arg Lys625 630 635 640Asn Leu Glu Ala Ile Val Ser Val Ile Ala Glu Arg Asn Lys Lys Lys 645 650 655Gln Leu Pro Tyr Tyr Tyr Leu Ser Pro Asp Arg Ile Pro Asn Ser Val 660 665 670Ala Ile27663PRTHomo sapiens 27Met Gly Arg Tyr Arg Ile Arg Val Ala Thr Gly Ala Trp Leu Phe Ser1 5 10 15Gly Ser Tyr Asn Arg Val Gln Leu Trp Leu Val Gly Thr Arg Gly Glu 20 25 30Ala Glu Leu Glu Leu Gln Leu Arg Pro Ala Arg Gly Glu Glu Glu Glu 35 40 45Phe Asp His Asp Val Ala Glu Asp Leu Gly Leu Leu Gln Phe Val Arg 50 55 60Leu Arg Lys His His Trp Leu Val Asp Asp Ala Trp Phe Cys Asp Arg65 70 75 80Ile Thr Val Gln Gly Pro Gly Ala Cys Ala Glu Val Ala Phe Pro Cys 85 90 95Tyr Arg Trp Val Gln Gly Glu Asp Ile Leu Ser Leu Pro Glu Gly Thr 100 105 110Ala Arg Leu Pro Gly Asp Asn Ala Leu Asp Met Phe Gln Lys His Arg 115 120 125Glu Lys Glu Leu Lys Asp Arg Gln Gln Ile Tyr Cys Trp Ala Thr Trp 130 135 140Lys Glu Gly Leu Pro Leu Thr Ile Ala Ala Asp Arg Lys Asp Asp Leu145 150 155 160Pro Pro Asn Met Arg Phe His Glu Glu Lys Arg Leu Asp Phe Glu Trp 165 170 175Thr Leu Lys Ala Gly Ala Leu Glu Met Ala Leu Lys Arg Val Tyr Thr 180 185 190Leu Leu Ser Ser Trp Asn Cys Leu Glu Asp Phe Asp Gln Ile Phe Trp 195 200 205Gly Gln Lys Ser Ala Leu Ala Glu Lys Val Arg Gln Cys Trp Gln Asp 210 215 220Asp Glu Leu Phe Ser Tyr Gln Phe Leu Asn Gly Ala Asn Pro Met Leu225 230 235 240Leu Arg Arg Ser Thr Ser Leu Pro Ser Arg Leu Val Leu Pro Ser Gly 245 250 255Met Glu Glu Leu Gln Ala Gln Leu Glu Lys Glu Leu Gln Asn Gly Ser 260 265 270Leu Phe Glu Ala Asp Phe Ile Leu Leu Asp Gly Ile Pro Ala Asn Val 275 280 285Ile Arg Gly Glu Lys Gln Tyr Leu Ala Ala Pro Leu Val Met Leu Lys 290 295 300Met Glu Pro Asn Gly Lys Leu Gln Pro Met Val Ile Gln Ile Gln Pro305 310 315 320Pro Asn Pro Ser Ser Pro Thr Pro Thr Leu Phe Leu Pro Ser Asp Pro 325 330 335Pro Leu Ala Trp Leu Leu Ala Lys Ser Trp Val Arg Asn Ser Asp Phe 340 345 350Gln Leu His Glu Ile Gln Tyr His Leu Leu Asn Thr His Leu Val Ala 355 360 365Glu Val Ile Ala Val Ala Thr Met Arg Cys Leu Pro Gly Leu His Pro 370 375 380Ile Phe Lys Phe Leu Ile Pro His Ile Arg Tyr Thr Met Glu Ile Asn385 390 395 400Thr Arg Ala Arg Thr Gln Leu Ile Ser Asp Gly Gly Ile Phe Asp Lys 405 410 415Ala Val Ser Thr Gly Gly Gly Gly His Val Gln Leu Leu Arg Arg Ala 420 425 430Ala Ala Gln Leu Thr Tyr Cys Ser Leu Cys Pro Pro Asp Asp Leu Ala 435 440 445Asp Arg Gly Leu Leu Gly Leu Pro Gly Ala Leu Tyr Ala His Asp Ala 450 455 460Leu Arg Leu Trp Glu Ile Ile Ala Arg Tyr Val Glu Gly Ile Val His465 470 475 480Leu Phe Tyr Gln Arg Asp Asp Ile Val Lys Gly Asp Pro Glu Leu Gln 485 490 495Ala Trp Cys Arg Glu Ile Thr Glu Val Gly Leu Cys Gln Ala Gln Asp 500 505 510Arg Gly Phe Pro Val Ser Phe Gln Ser Gln Ser Gln Leu Cys His Phe 515 520 525Leu Thr Met Cys Val Phe Thr Cys Thr Ala Gln His Ala Ala Ile Asn 530 535 540Gln Gly Gln Leu Asp Trp Tyr Ala Trp Val Pro Asn Ala Pro Cys Thr545 550 555 560Met Arg Met Pro Pro Pro Thr Thr Lys Glu Asp Val Thr Met Ala Thr 565 570 575Val Met Gly Ser Leu Pro Asp Val Arg Gln Ala Cys Leu Gln Met Ala 580 585 590Ile Ser Trp His Leu Ser Arg Arg Gln Pro Asp Met Val Pro Leu Gly 595 600 605His His Lys Glu Lys Tyr Phe Ser Gly Pro Lys Pro Lys Ala Val Leu 610 615 620Asn Gln Phe Arg Thr Asp Leu Glu Lys Leu Glu Lys Glu Ile Thr Ala625 630 635 640Arg Asn Glu Gln Leu Asp Trp Pro Tyr Glu Tyr Leu Lys Pro Ser Cys 645 650 655Ile Glu Asn Ser Val Thr Ile 66028676PRTHomo sapiens 28Met Ala Glu Phe Arg Val Arg Val Ser Thr Gly Glu Ala Phe Gly Ala1 5 10 15Gly Thr Trp Asp Lys Val Ser Val Ser Ile Val Gly Thr Arg Gly Glu 20 25 30Ser Pro Pro Leu Pro Leu Asp Asn Leu Gly Lys Glu Phe Thr Ala Gly 35 40 45Ala Glu Glu Asp Phe Gln Val Thr Leu Pro Glu Asp Val Gly Arg Val 50 55 60Leu Leu Leu Arg Val His Lys Ala Pro Pro Val Leu Pro Leu Leu Gly65 70 75 80Pro Leu Ala Pro Asp Ala Trp Phe Cys Arg Trp Phe Gln Leu Thr Pro 85 90 95Pro Arg Gly Gly His Leu Leu Phe Pro Cys Tyr Gln Trp Leu Glu Gly 100 105 110Ala Gly Thr Leu Val Leu Gln Glu Gly Thr Ala Lys Val Ser Trp Ala 115 120 125Asp His His Pro Val Leu Gln Gln Gln Arg Gln Glu Glu Leu Gln Ala 130 135 140Arg Gln Glu Met Tyr Gln Trp Lys Ala Tyr Asn Pro Gly Trp Pro His145 150 155 160Cys Leu Asp Glu Lys Thr Val Glu Asp Leu Glu Leu Asn Ile Lys Tyr 165 170 175Ser Thr Ala Lys Asn Ala Asn Phe Tyr Leu Gln Ala Gly Ser Ala Phe 180 185 190Ala Glu Met Lys Ile Lys Gly Leu Leu Asp Arg Lys Gly Leu Trp Arg 195 200 205Ser Leu Asn Glu Met Lys Arg Ile Phe Asn Phe Arg Arg Thr Pro Ala 210 215 220Ala Glu His Ala Phe Glu His Trp Gln Glu Asp Ala Phe Phe Ala Ser225 230 235 240Gln Phe Leu Asn Gly Leu Asn Pro Val Leu Ile Arg Arg Cys His Tyr 245 250 255Leu Pro Lys Asn Phe Pro Val Thr Asp Ala Met Val Ala Ser Val Leu 260 265 270Gly Pro Gly Thr Ser Leu Gln Ala Glu Leu Glu Lys Gly Ser Leu Phe 275 280 285Leu Val Asp His Gly Ile Leu Ser Gly Ile Gln Thr Asn Val Ile Asn 290 295 300Gly Lys Pro Gln Phe Ser Ala Ala Pro Met Thr Leu Leu Tyr Gln Ser305 310 315 320Pro Gly Cys Gly Pro Leu Leu Pro Leu Ala Ile Gln Leu Ser Gln Thr 325 330 335Pro Gly Pro Asn Ser Pro Ile Phe Leu Pro Thr Asp Asp Lys Trp Asp 340 345 350Trp Leu Leu Ala Lys Thr Trp Val Arg Asn Ala Glu Phe Ser Phe His 355 360 365Glu Ala Leu Thr His Leu Leu His Ser His Leu Leu Pro Glu Val Phe 370 375 380Thr Leu Ala Thr Leu Arg Gln Leu Pro His Cys His Pro Leu Phe Lys385 390 395 400Leu Leu Ile Pro His Thr Arg Tyr Thr Leu His Ile Asn Thr Leu Ala 405 410 415Arg Glu Leu Leu Ile Val Pro Gly Gln Val Val Asp Arg Ser Thr Gly 420 425 430Ile Gly Ile Glu Gly Phe Ser Glu Leu Ile Gln Arg Asn Met Lys Gln 435 440 445Leu Asn Tyr Ser Leu Leu Cys Leu Pro Glu Asp Ile Arg Thr Arg Gly 450 455 460Val Glu Asp Ile Pro Gly Tyr Tyr Tyr Arg Asp Asp Gly Met Gln Ile465 470 475 480Trp Gly Ala Val Glu Arg Phe Val Ser Glu Ile Ile Gly Ile Tyr Tyr 485 490 495Pro Ser Asp Glu Ser Val Gln Asp Asp Arg Glu Leu Gln Ala Trp Val 500 505 510Arg Glu Ile Phe Ser Lys Gly Phe Leu Asn Gln Glu Ser Ser Gly Ile 515 520 525Pro Ser Ser Leu Glu Thr Arg Glu Ala Leu Val Gln Tyr Val Thr Met 530 535 540Val Ile Phe Thr Cys Ser Ala Lys His Ala Ala Val Ser Ala Gly Gln545 550 555 560Phe Asp Ser Cys Ala Trp Met Pro Asn Leu Pro Pro Ser Met Gln Leu 565 570 575Pro Pro Pro Thr Ser Lys Gly Leu Ala Thr Cys Glu Gly Phe Ile Ala 580 585 590Thr Leu Pro Pro Val Asn Ala Thr Cys Asp Val Ile Leu Ala Leu Trp 595 600 605Leu Leu Ser Lys Glu Pro Gly Asp Gln Arg Pro Leu Gly Thr Tyr Pro 610 615 620Asp Glu His Phe Thr Glu Glu Ala Pro Arg Arg Ser Ile Ala Thr Phe625 630 635 640Gln Ser Arg Leu Ala Gln Ile Ser Arg Gly Ile Gln Glu Arg Asn Gln 645 650 655Gly Leu Val Leu Pro Tyr Thr Tyr Leu Asp Pro Pro Leu Ile Glu Asn 660 665 670Ser Val Ser Ile 67529685PRTPseudomonas aeruginosa 29Met Lys Arg Arg Ser Val Leu Leu Ser Gly Val Ala Leu Ser Gly Thr1 5 10 15Ala Leu Ala Asn Asp Ser Ile Phe Phe Ser Pro Leu Lys Tyr Leu Gly 20 25 30Ala Glu Gln Gln Arg Ser Ile Asp Ala Ser Arg Ser Leu Leu Asp Asn 35 40 45Leu Ile Pro Pro Ser Leu Pro Gln Tyr Asp Asn Leu Ala Gly Lys Leu 50 55 60Ala Arg Arg Ala Val Leu Thr Ser Lys Lys Leu Val Tyr Val Trp Thr65 70 75 80Glu Asn Phe Gly Asn Val Lys Gly Val Pro Met Ala Arg Ser Val Pro 85 90 95Leu Gly Glu Leu Pro Asn Val Asp Trp Leu Leu Lys Thr Ala Gly Val 100 105 110Ile Val Glu Leu Ile Val Asn Phe Val Ala Ser Leu Pro Ala Ser Ala 115 120 125Ala Ala Gln Phe Glu Arg Ile Ala Thr Gly Leu Ser Gly Asp Leu Glu 130 135 140Ala Ala Arg Gln Val His Glu Ala Leu Leu Glu Glu Ala Lys Asn Asp145 150 155 160Pro Ala Ala Ala Gly Ser Leu Leu Leu Arg Phe Thr Glu Leu Gln Thr 165 170 175Arg Val Ile Ala Ile Leu Thr Arg Val Gly Leu Leu Val Asp Asp Ile 180 185 190Leu Lys Ser Ala Ser Asn Leu Val Thr Gln Arg Gly Gln Gly Asp Gly 195 200 205Leu Asn Arg Phe Arg Ala Val Phe Gly Thr Leu Arg Leu Pro Glu Val 210 215 220Ala Asp Ser Phe Arg Asp Asp Glu Ala Phe Ala Tyr Trp Arg Val Ala225 230 235 240Gly Pro Asn Pro Leu Leu Ile Arg Arg Val Asp Ala Leu Pro Ala Asn 245 250 255Phe Pro Leu Gly Glu Glu Gln Phe Arg Arg Val Met Gly Ala Asp Asp 260 265 270Ser Leu Leu Glu Ala Ala Ala Ser Arg Arg Leu Tyr Leu Leu Asp Tyr 275 280 285Ala Glu Leu Gly Lys Leu Ala Pro Ser Gly Ala Val Asp Lys Leu Leu 290 295 300Thr Gly Thr Gly Phe Ala Tyr Ala Pro Ile Ala Leu Phe Ala Leu Gly305 310 315 320Lys Asp Arg Ala Arg Leu Leu Pro Val Ala Ile Gln Cys Gly Gln Asp 325 330 335Pro Ala Thr His Pro Met Phe Val Arg Pro Ala Glu Ser Glu Ser Asp 340 345 350Leu Tyr Trp Gly Trp Gln Met Ala Lys Thr Val Val Gln Val Ala Glu 355 360 365Glu Asn Tyr His Glu Met Phe Val His Leu Ala Gln Thr His Leu Val 370 375 380Ser Glu Ala Phe Cys Leu Ala Thr Gln Arg Thr Leu Ala Pro Ser His385 390 395 400Pro Leu His Val Leu Leu Ala Pro His Phe Glu Gly Thr Leu Phe Ile 405 410 415Asn Glu Gly Ala Ala Arg Ile Leu Leu Pro Ser Ala Gly Phe Ile Asp 420 425 430Val Met Phe Ala Ala Pro Ile Gln Asp Thr Gln Ala Thr Ala Gly Gly 435 440 445Asn Arg Leu Gly Phe Asp Phe Tyr Arg Gly Met Leu Pro Glu Ser Leu 450 455 460Lys Ala Arg Asn Val Asp Asp Pro Leu Ala Leu Pro Asp Tyr Pro Tyr465 470 475 480Arg Asp Asp Gly Leu Leu Val Trp Asn Ala Ile Arg Gln Trp Ala Ala 485 490 495Asp Tyr Val Ala Val Tyr Tyr Ala Ser Asp Gly Asp Val Thr Ala Asp 500 505 510Val Glu Leu Ala Ala Trp Val Gly Glu Val Ile Gly Ser Gly Lys Val 515 520 525Ala Gly Phe Arg Pro Ile Thr Gly Arg Ser Gln Leu Val Glu Val Leu 530 535 540Thr Met Val Ile Phe Thr Ala Ser Ala Gln His Ala Ala Val Asn Phe545 550 555 560Pro Gln Pro Ser Met Met Thr Tyr Ala Pro Ala Ile Cys Ala Met Ser 565 570 575Ala Ala Pro Ala Pro Asp Ser Pro Ser Gly Lys Ser Glu Ala Asp Trp 580 585 590Leu Lys Met Met Pro Pro Thr Leu Val Ala Leu Glu Lys Val Asn Ile 595 600 605Tyr His Leu Leu Gly Ser Val Tyr His Gly Arg Leu Gly Asp Tyr Arg 610 615 620Gln Thr Gly Phe Pro Tyr Ala Pro Val Phe Ser Asp Arg Arg Val Thr625 630 635 640Ala Ser Gly Gly Pro Leu Glu Arg Phe Gln Ala Arg Leu Lys Glu Val 645 650 655Glu Ala Thr Ile Arg Thr Arg Asn Gln Ala Arg Arg Arg Pro Tyr Glu 660 665 670Tyr Leu Leu Pro Ser Arg Ile Pro Ala Ser Thr Asn Ile 675 680 68530639PRTArabidopsis thaliana 30Met Lys Val Ile Thr Ser Leu Ile Ser Ser Ile Leu Leu Lys Phe Ile1 5 10 15His Lys Asp Phe His Glu Ile Tyr Ala Arg Met Ser Leu Leu Asp Arg 20 25 30Phe Leu Leu Leu Ile Val His Gly Val Asp Lys Met Val Pro Trp His 35 40 45Lys Leu Pro Val Phe Leu Gly Leu Thr Tyr Leu Glu Val Arg Arg His 50 55 60Leu His Gln Gln Tyr Asn Leu Leu Asn Val Gly Gln Thr Pro Thr Gly65 70 75 80Ile Arg Phe Asp Pro Ala Asn Tyr Pro Tyr Arg Thr Ala Asp Gly Lys 85 90 95Phe Asn Asp Pro Phe Asn Glu Gly Val Gly Ser Gln Asn Ser Phe Phe 100 105 110Gly Arg Asn Cys Pro Pro Val Asp Gln Lys Ser Lys Leu Arg Arg Pro 115 120 125Asp Pro Met Val Val Ala Thr Lys Leu Leu Gly Arg Lys Lys Phe Ile 130 135 140Asp Thr Gly Lys Gln Phe Asn Met Ile Ala Ala Ser Trp Ile Gln Phe145 150 155 160Met Ile His Asp Trp Ile Asp His Leu Glu Asp Thr His Gln Ile Glu 165 170 175Leu Val Ala Pro Lys Glu Val Ala Ser Lys Cys Pro Leu Ser Ser Phe 180 185 190Arg Phe Leu Lys Thr Lys Glu Val Pro Thr Gly Phe Phe Glu Ile Lys 195 200 205Thr Gly Ser Gln Asn Ile Arg Thr Pro Trp Trp Asp Ser Ser Val Ile 210 215

220Tyr Gly Ser Asn Ser Lys Thr Leu Asp Arg Val Arg Thr Tyr Lys Asp225 230 235 240Gly Lys Leu Lys Ile Ser Glu Glu Thr Gly Leu Leu Leu His Asp Glu 245 250 255Asp Gly Leu Ala Ile Ser Gly Asp Ile Arg Asn Ser Trp Ala Gly Val 260 265 270Ser Ala Leu Gln Ala Leu Phe Ile Lys Glu His Asn Ala Val Cys Asp 275 280 285Ala Leu Lys Asp Glu Asp Asp Asp Leu Glu Asp Glu Asp Leu Tyr Arg 290 295 300Tyr Ala Arg Leu Val Thr Ser Ala Val Val Ala Lys Ile His Thr Ile305 310 315 320Asp Trp Thr Val Gln Leu Leu Lys Thr Asp Thr Leu Leu Ala Gly Met 325 330 335Arg Ala Asn Trp Tyr Gly Leu Leu Gly Lys Lys Phe Lys Asp Ser Phe 340 345 350Gly His Ala Gly Ser Ser Ile Leu Gly Gly Val Val Gly Met Lys Lys 355 360 365Pro Gln Asn His Gly Val Pro Tyr Ser Leu Thr Glu Asp Phe Thr Ser 370 375 380Val Tyr Arg Met His Ser Leu Leu Pro Asp Gln Leu His Ile Leu Asp385 390 395 400Ile Asp Asp Val Pro Gly Thr Asn Lys Ser Leu Pro Leu Ile Gln Glu 405 410 415Ile Ser Met Arg Asp Leu Ile Gly Arg Lys Gly Glu Glu Thr Met Ser 420 425 430His Ile Gly Phe Thr Lys Leu Met Val Ser Met Gly His Gln Ala Ser 435 440 445Gly Ala Leu Glu Leu Met Asn Tyr Pro Met Trp Leu Arg Asp Ile Val 450 455 460Pro His Asp Pro Asn Gly Gln Ala Arg Pro Asp His Val Asp Leu Ala465 470 475 480Ala Leu Glu Ile Tyr Arg Asp Arg Glu Arg Ser Val Pro Arg Tyr Asn 485 490 495Glu Phe Arg Arg Ser Met Phe Met Ile Pro Ile Thr Lys Trp Glu Asp 500 505 510Leu Thr Glu Asp Glu Glu Ala Ile Glu Val Leu Asp Asp Val Tyr Asp 515 520 525Gly Asp Val Glu Glu Leu Asp Leu Leu Val Gly Leu Met Ala Glu Lys 530 535 540Lys Ile Lys Gly Phe Ala Ile Ser Glu Thr Ala Phe Tyr Ile Phe Leu545 550 555 560Ile Met Ala Thr Arg Arg Leu Glu Ala Asp Arg Phe Phe Thr Ser Asp 565 570 575Phe Asn Glu Thr Ile Tyr Thr Lys Lys Gly Leu Glu Trp Val Asn Thr 580 585 590Thr Glu Ser Leu Lys Asp Val Ile Asp Arg His Tyr Pro Asp Met Thr 595 600 605Asp Lys Trp Met Asn Ser Glu Ser Ala Phe Ser Val Trp Asp Ser Pro 610 615 620Pro Leu Thr Lys Asn Pro Ile Pro Leu Tyr Leu Arg Ile Pro Ser625 630 63531631PRTArabidopsis thaliana 31Met Gly Phe Ser Pro Ser Ser Ser Trp Phe Leu His Pro Gln Leu His1 5 10 15His Val Val Ser Lys Met Ser Tyr Phe Asp Ala Phe Leu Phe Tyr Ile 20 25 30Val His Leu Val Asp Lys Leu Gly Leu Trp His Arg Phe Pro Val Leu 35 40 45Leu Gly Val Ala Tyr Leu Gly Leu Arg Arg His Leu His Gln Arg Tyr 50 55 60Asn Leu Val His Val Gly Pro Ile Asn Gly Gln Gly Tyr Asp Thr Asp65 70 75 80Glu Phe Cys Tyr Arg Thr Ala Asp Gly Lys Cys Asn His Pro Ser Asp 85 90 95Asn Thr Ile Gly Ser Gln Gly Ser Phe Ile Gly Arg Asn Met Pro Pro 100 105 110Ser Thr Ser Gln Tyr Gly Ile Leu Asp Pro His Pro Ser Val Val Ala 115 120 125Thr Lys Leu Leu Ala Arg Lys Arg Phe Ile Asp Asn Gly Asp Gln Phe 130 135 140Asn Val Ile Ala Cys Ser Trp Ile Gln Phe Met Ile His Asp Trp Val145 150 155 160Asp His Leu Glu Asp Thr His Gln Ile Glu Leu Glu Ala Pro Glu Glu 165 170 175Val Ala Ser Gly Cys Pro Leu Lys Ser Phe Lys Phe Leu Arg Thr Lys 180 185 190Lys Val Pro Thr Asp Asp His His Lys Ser Gly Ala Val Asn Thr Arg 195 200 205Thr Pro Trp Trp Asp Gly Ser Val Ile Tyr Gly Asn Asp Glu Thr Gly 210 215 220Met Arg Arg Val Arg Val Phe Lys Asp Gly Lys Leu Lys Ile Ser Gly225 230 235 240Asp Gly Leu Leu Glu Arg Asp Glu Arg Gly Val Pro Ile Ser Gly Asp 245 250 255Ile Arg Asn Ser Trp Ser Gly Phe Ser Leu Leu Gln Ala Leu Phe Val 260 265 270Lys Glu His Asn Ser Val Cys Asp Met Leu Lys Glu Arg Tyr Pro Asp 275 280 285Phe Asp Asp Glu Lys Leu Tyr Arg Thr Ala Arg Leu Val Thr Ala Ala 290 295 300Val Ile Ala Lys Val His Thr Ile Asp Trp Thr Ile Glu Leu Leu Lys305 310 315 320Thr Asp Thr Leu Thr Ala Gly Met Arg Ile Asn Trp Tyr Gly Phe Phe 325 330 335Gly Lys Lys Val Lys Asp Met Val Gly Ala Arg Phe Gly Pro Leu Phe 340 345 350Ser Gly Leu Val Gly Leu Lys Lys Pro Asn Asp His Gly Val Pro Tyr 355 360 365Ser Leu Thr Glu Glu Phe Val Ser Val Tyr Arg Met His Cys Leu Leu 370 375 380Pro Glu Thr Leu Ile Leu Arg Asp Met Asn Ser Glu Asn Val Asp Lys385 390 395 400Glu Asn Pro Ala Ile Glu Arg Glu Ile Pro Met Thr Glu Leu Ile Gly 405 410 415Lys Lys Ala Gly Glu Lys Ala Ser Lys Leu Gly Phe Glu Gln Leu Leu 420 425 430Val Ser Met Gly His Gln Ser Cys Gly Ala Leu Thr Leu Trp Asn Tyr 435 440 445Pro Asn Trp Met Arg Asn Leu Val Ala Gln Asp Ile Asp Gly Glu Asp 450 455 460Arg Pro His Leu Ile Asp Met Ala Ala Leu Glu Ile Tyr Arg Asp Arg465 470 475 480Glu Arg Gly Val Pro Arg Tyr Asn Glu Phe Arg Lys Asn Leu Leu Met 485 490 495Ser Pro Ile Ser Lys Trp Glu Glu Leu Thr Asp Asp Glu Glu Ala Ile 500 505 510Lys Val Leu Arg Glu Val Tyr Glu Asp Asp Ile Glu Lys Leu Asp Leu 515 520 525Asn Val Gly Leu His Ala Glu Lys Lys Ile Lys Gly Phe Ala Ile Ser 530 535 540Glu Thr Ala Phe Phe Ile Phe Leu Leu Val Ala Ser Arg Arg Leu Glu545 550 555 560Ala Asp Arg Phe Phe Thr Thr Asn Phe Asn Glu Lys Thr Tyr Thr Lys 565 570 575Glu Gly Leu Glu Trp Val Asn Thr Thr Glu Thr Leu Lys Asp Val Ile 580 585 590Asp Arg His Phe Pro Arg Leu Thr Asp Gln Trp Met Arg Cys Ser Ser 595 600 605Ala Phe Ser Val Trp Gly Ser Asp Pro Asn Pro Lys Asn Trp Val Pro 610 615 620Leu Tyr Leu Arg Ser Ala Pro625 63032613PRTFusarium graminearum 32Met Ala Ser Val Thr Ser Ile Ile Phe Val Ala Leu Val Ala Gly Val1 5 10 15Leu Tyr Ala Ala Arg Met Ser Leu Val Pro Ile Leu Lys Ser Leu Tyr 20 25 30Ile Arg Leu Trp Lys Gly Val Asn His Phe Ile Glu Trp His Lys Leu 35 40 45Pro Thr Trp Phe Ala Val Phe Asn Leu Leu Ala Leu Arg Tyr Glu Leu 50 55 60Arg Glu Gly Asn Leu His Asp Thr Ser Pro Asn Ala Glu Phe Gln Gly65 70 75 80Thr Asp Lys Cys Pro Met Ser Asp Ser Lys Phe Val Ser Ser Arg Asp 85 90 95Ser Asp Gly Leu Tyr Asn Asp Leu Lys Gln Pro Lys Met Gly Cys Ala 100 105 110Gly Met Arg Phe Gly Arg Asn Val Pro Arg Lys Tyr Thr Lys Pro Pro 115 120 125Thr Glu Gln Glu Leu Leu Thr Pro Asn Pro Arg Val Ile Ser Glu Lys 130 135 140Ile Leu Ala Arg Pro Glu Gly Gln Phe Lys Pro Ala Glu Ile Val Asn145 150 155 160Leu Leu Ala Ala Ala Trp Ile Gln Phe Gln Val His Asp Trp Ala Gln 165 170 175His Phe Leu Val Thr Asn Gly Asp Lys Asp Ile Asp Ile Pro Leu His 180 185 190Asn Lys Asp Lys Trp Thr Glu Gln Ser Met Lys Ile Pro Arg Thr Lys 195 200 205Lys Ala Asp Ile Leu Ser Lys Gln Asp Ala Glu Thr Pro Ala Tyr Asp 210 215 220Asn Glu Asn Thr His Trp Trp Asp Ala Ser Gln Ile Tyr Gly Ser Ser225 230 235 240Glu Ala Glu Thr Gln Ala Leu Arg Ala Lys Cys His Lys Ser Lys Pro 245 250 255Gly Gln Leu Glu Leu His Leu Ser Asn Pro Ser Trp Ser Ser Asp His 260 265 270Ile Phe Asp Thr Ala Arg Leu Ile Asn Cys Ala Leu Met Ala Lys Ile 275 280 285His Thr Val Glu Trp Thr Pro Gly Ile Leu Gln His Pro Ala Leu Gln 290 295 300Ile Gly Met Asn Ala Asn Trp Trp Gly Leu Leu Gly Asp Lys Leu Trp305 310 315 320His Ala Phe Gly Arg Val Phe Asp Asn Lys Ser Glu Val Ile Ser Gly 325 330 335Ile Pro Gly Ser Gly Val Asp His Asp Lys Ala Pro Tyr Cys Leu Thr 340 345 350Glu Glu Phe Val Ser Val Tyr Arg Leu His Ser Leu Ile Pro Asp Asn 355 360 365Val Ala Phe Phe Asn Ile Lys Asp Gly Gln His Glu Gly Thr Leu Pro 370 375 380Ile Val Asp Val Ser Phe Glu Ser Ala Arg Lys Pro Phe Asp Glu Gly385 390 395 400Lys Ser Gly Leu Gly Leu Ser Phe Ala Asp Val Phe Tyr Ser Phe Gly 405 410 415Val Asn Tyr Pro Gly Ala Ile Arg Ala His Asn Met Pro Asn Phe Leu 420 425 430Arg Asp Leu Lys Ile Pro Ala Asp Lys Asp Phe Pro Glu Gly Arg His 435 440 445Leu Asp Leu Gly Thr Ile Asp Ile Leu Arg Asp Arg Glu Arg Gly Val 450 455 460Pro Arg Tyr Asn Ala Phe Arg Arg Leu Phe His Met Pro Ala Ala Lys465 470 475 480Ser Phe Ile Asp Leu Thr Gly Gly Asp Asp Lys Leu Ala Ser Glu Leu 485 490 495Glu Glu Val Tyr Glu Gly Asp Leu Glu Ala Val Asp Leu Leu Val Gly 500 505 510Thr Leu Cys Glu Pro Leu Pro Lys Gly Phe Gly Phe Ser Asp Thr Ala 515 520 525Phe Arg Val Phe Ile Leu Met Ala Thr Arg Arg Ile Lys Ser Asp Arg 530 535 540Phe Ile Ala Gly Asp Gly Trp Cys Pro Glu Val Tyr Thr Arg Glu Gly545 550 555 560Met Asp Trp Val Gln Lys Asn Thr Met Lys Asp Val Leu Cys Arg His 565 570 575Phe Pro Glu Leu Ala Ala Pro Leu His Asn Val Lys Asn Ala Phe Ala 580 585 590Pro Trp Thr Lys Leu Gly Gln Thr Ala Ala Tyr Ala Gly Pro Glu Thr 595 600 605Asn Lys Ala Lys Ser 61033653PRTFusarium verticillioides 33Met Ala Ser Val Leu Ser Lys Glu Ser Leu Ala Ile Ile Leu Ser Val1 5 10 15Val Thr Leu Leu Ile Gly Leu Ser His Phe Asn Met Ile Ser Leu Lys 20 25 30Ser Ile Phe Lys Ser Val Tyr Ile Arg Leu Trp Lys Leu Val Asn Val 35 40 45Phe Val His Trp His Lys Leu Pro Thr Trp Leu Gly Val Phe Asn Leu 50 55 60Leu Ala Leu Arg Tyr Glu Leu Arg Glu Lys Asn Leu His Asp Thr Tyr65 70 75 80Pro Asn Ala Glu Phe Gln Gly Thr Ala Ala Asp Cys Pro Met Lys Asn 85 90 95Ser Lys Phe Ile Ala Thr Arg Asn Ser Asp Gly Asp Phe Asn Asp Leu 100 105 110Ala Gln Pro Lys Met Gly Cys Ala Gly Met Arg Phe Gly Arg Asn Val 115 120 125Pro Arg Asn His Thr Thr Pro Pro Thr Gln Gln Glu Leu Leu Thr Pro 130 135 140Asn Pro Arg Leu Ile Ser Glu Lys Ile Leu Ala Arg Pro Glu Gly Gln145 150 155 160Phe Lys Pro Ala Glu Ile Val Asn Leu Leu Ala Ala Ala Trp Ile Gln 165 170 175Phe Gln Val His Asp Trp Ala Gln His Ser Leu Val Thr Asn Gly Asp 180 185 190Lys Asp Val Glu Ile Leu Leu Asp Lys Ala Asp Arg Trp Ser Glu Arg 195 200 205Ile Met Lys Ile Pro Arg Thr Lys Lys Asp Asp Pro Leu Ser Gln Gln 210 215 220Asp Ile Glu Thr Pro Ala Tyr Thr Asn Glu Cys Thr His Trp Trp Asp225 230 235 240Ala Ser Gln Ile Tyr Gly Ser Thr Glu Ala Glu Thr Lys Ala Leu Arg 245 250 255Ala Gln Cys Asp Lys Ser Tyr Pro Gly Gln Leu His Val Thr Arg Glu 260 265 270Asp Gly Val Gln Phe Leu Pro Arg Ser Asp Asp Gly Ile Pro Lys Thr 275 280 285Gly Phe Arg Gln Asn Trp Trp Leu Gly Leu Glu Leu Leu His Thr Leu 290 295 300Phe Ala Leu Glu His Asn Ala Ile Ala Thr Gln Leu His Leu Ser Asn305 310 315 320Pro Ser Trp Ser Ser Asp Gln Ile Phe Asp Thr Ala Arg Leu Ile Asn 325 330 335Cys Ala Leu Met Ala Lys Ile His Thr Val Glu Trp Thr Pro Gly Ile 340 345 350Leu Gln His Pro Ala Leu Gln Ile Gly Met Asn Ala Asn Trp Trp Gly 355 360 365Leu Leu Gly Asp Lys Leu Trp His Val Phe Gly Arg Val Phe Asp Asn 370 375 380Lys Ser Glu Val Ile Ser Gly Ile Pro Gly Ser Gly Val Asp His Asp385 390 395 400Asn Val Pro Tyr Cys Leu Thr Glu Glu Phe Val Ser Val Tyr Arg Leu 405 410 415His Pro Leu Ile Pro Asp Asn Val Ala Phe Phe Ser Ile Lys Asp Gly 420 425 430Gln His Lys Gly Thr Leu Pro Ile Lys Glu Val Ala Phe Lys Ser Ala 435 440 445Arg Lys Pro Phe Asp Glu Asp Lys Ser Gly Leu Gly Leu Ser Phe Ala 450 455 460Asp Val Phe Tyr Ser Phe Gly Val Asn Tyr Pro Gly Ala Ile Arg Ala465 470 475 480His Asn Met Pro Asn Phe Leu Arg Asp Leu Asn Ile Pro Gly Asp Lys 485 490 495Asp Phe Pro His Gly Arg His Leu Asp Leu Gly Thr Ile Asp Ile Leu 500 505 510Arg Asp Arg Glu Arg Gly Val Pro Arg Tyr Asn Ala Phe Arg Arg Leu 515 520 525Phe His Met Ala Pro Ala Lys Thr Phe Ile Asp Leu Thr Gly Gly Asp 530 535 540Ser Lys Leu Ala Ala Glu Leu Glu Glu Val Tyr Asp Gly Asp Leu Glu545 550 555 560Ala Val Asp Leu Leu Val Gly Thr Leu Ser Glu Pro Leu Pro Lys Gly 565 570 575Phe Gly Phe Ser Asp Thr Ala Phe Arg Val Phe Ile Leu Met Ala Thr 580 585 590Arg Arg Ile Lys Ser Asp Arg Phe Leu Ala Gly Asp Gly Trp Cys Pro 595 600 605Glu Val Tyr Thr Arg Glu Gly Ile Asn Trp Val Gln Asn Asn Thr Met 610 615 620Lys Asp Val Leu Cys Arg His Phe Pro Glu Leu Ala Ala Thr Leu His625 630 635 640Asn Val Lys Asn Leu Ser Val Ser Phe Ile Leu Ser Leu 645 65034668PRTFusarium oxysporum 34Met Ala Ser Val Leu Ser Lys Glu Ser Leu Ala Ile Ser Leu Ser Ile1 5 10 15Val Thr Leu Leu Ile Gly Leu Ser His Phe Asn Met Ile Ser Leu Lys 20 25 30Pro Ile Phe Lys Ser Val Tyr Ile Arg Leu Trp Lys Phe Val Asn Ile 35 40 45Phe Val His Trp His Lys Leu Pro Thr Trp Leu Gly Val Phe Asn Leu 50 55 60Leu Ala Leu Arg Tyr Glu Leu Arg Glu Lys Asn Leu His Asp Thr Tyr65 70 75 80Pro Asn Ala Glu Phe Gln Gly Thr Thr Ala Asp Cys Pro Met Lys Asn 85 90 95Ser Lys Phe Ile Ala Asn Arg Asn Ser Asp Gly Asp Phe Asn Asp Leu 100 105 110Ala Gln Pro Lys Met Gly Cys Ala Gly Met Arg Phe Gly Arg Asn Val 115 120 125Pro Arg Lys Tyr Thr Thr Pro Pro Thr Gln Gln Glu Leu Leu Thr Pro 130 135 140Asn Pro Arg Ile Ile Ser Glu Lys Ile Leu Ala Arg Pro Glu Gly

Gln145 150 155 160Phe Lys Pro Ala Glu Ile Val Asn Leu Leu Ala Ala Ala Trp Ile Gln 165 170 175Phe Gln Val His Asp Trp Ala Gln His Phe Leu Val Thr Asn Gly Asp 180 185 190Lys Asp Val Glu Ile Pro Leu Asp Lys Ala Asp Arg Trp Ser Glu Arg 195 200 205Ile Met Lys Ile Pro Arg Thr Lys Lys Asp Asp Ala Leu Ser Gln Gln 210 215 220Asp Ile Glu Thr Pro Ala Tyr Thr Asn Glu Cys Thr His Trp Trp Asp225 230 235 240Ala Ser Gln Ile Tyr Gly Ser Thr Glu Ala Glu Thr Lys Ala Leu Arg 245 250 255Ala Gln Cys Asp Lys Ser Tyr Pro Gly Gln Leu His Val Thr Arg Glu 260 265 270Asp Gly Val Gln Phe Leu Pro Arg Ser Asp Asp Gly Ile Pro Lys Thr 275 280 285Gly Phe Arg Gln Asn Trp Trp Leu Gly Leu Glu Leu Leu His Thr Leu 290 295 300Phe Ala Leu Glu His Asn Ala Ile Ala Thr Gln Leu His Leu Ser Asn305 310 315 320Pro Ser Trp Ser Ser Asp Gln Ile Phe Asp Thr Ala Arg Leu Ile Asn 325 330 335Cys Ala Leu Met Ala Lys Ile His Thr Val Glu Trp Thr Pro Gly Ile 340 345 350Leu Gln His Pro Ala Leu Gln Ile Gly Met Asn Ala Asn Trp Trp Gly 355 360 365Leu Leu Gly Asp Lys Leu Trp His Val Phe Gly Arg Val Phe Asp Asn 370 375 380Lys Ser Glu Val Ile Ser Gly Ile Pro Gly Ser Gly Val Asp His Asp385 390 395 400Asn Val Pro Tyr Cys Leu Thr Glu Glu Phe Val Ser Val Tyr Arg Leu 405 410 415His Pro Leu Ile Pro Asp Asn Val Ala Phe Phe Ser Ile Lys Asp Gly 420 425 430Gln His Lys Gly Thr Leu Pro Ile Lys Asp Val Ala Phe Glu Ser Ala 435 440 445Arg Lys Pro Phe Asp Glu Asp Lys Ser Gly Leu Gly Leu Ser Phe Ala 450 455 460Asp Val Phe Tyr Ser Phe Gly Val Asn Tyr Pro Gly Ala Ile Arg Ala465 470 475 480His Asn Met Pro Asn Phe Leu Arg Asp Leu Asn Ile Pro Gly Asp Lys 485 490 495Asp Phe Pro Gln Gly Arg His Leu Asp Leu Gly Thr Ile Asp Ile Leu 500 505 510Arg Asp Arg Glu Arg Gly Val Pro Arg Tyr Asn Ala Phe Arg Arg Leu 515 520 525Phe His Met Ala Pro Ala Lys Ser Phe Leu Asp Leu Thr Gly Gly Asp 530 535 540Ala Lys Leu Ala Ala Glu Leu Glu Asp Val Tyr Asp Gly Asp Leu Glu545 550 555 560Ala Val Asp Leu Leu Val Gly Thr Leu Ser Glu Pro Leu Pro Lys Gly 565 570 575Phe Gly Phe Ser Asp Thr Ala Phe Arg Val Phe Ile Leu Met Ala Thr 580 585 590Arg Arg Ile Lys Ser Asp Arg Phe Leu Ala Gly Asp Gly Trp Cys Pro 595 600 605Glu Val Tyr Thr Arg Glu Gly Ile Asn Trp Val Gln Asn Asn Thr Met 610 615 620Lys Asp Val Leu Cys Arg His Phe Pro Glu Leu Ala Ala Thr Leu His625 630 635 640Asn Val Lys Asn Ala Phe Ala Pro Trp Thr Lys Ile Gly Gln Thr Glu 645 650 655Ala Tyr Ala Gly Pro Glu Thr Asn Lys Ala Lys Asn 660 66535599PRTHomo sapiens 35Met Ser Arg Ser Leu Leu Leu Trp Phe Leu Leu Phe Leu Leu Leu Leu1 5 10 15Pro Pro Leu Pro Val Leu Leu Ala Asp Pro Gly Ala Pro Thr Pro Val 20 25 30Asn Pro Cys Cys Tyr Tyr Pro Cys Gln His Gln Gly Ile Cys Val Arg 35 40 45Phe Gly Leu Asp Arg Tyr Gln Cys Asp Cys Thr Arg Thr Gly Tyr Ser 50 55 60Gly Pro Asn Cys Thr Ile Pro Gly Leu Trp Thr Trp Leu Arg Asn Ser65 70 75 80Leu Arg Pro Ser Pro Ser Phe Thr His Phe Leu Leu Thr His Gly Arg 85 90 95Trp Phe Trp Glu Phe Val Asn Ala Thr Phe Ile Arg Glu Met Leu Met 100 105 110Arg Leu Val Leu Thr Val Arg Ser Asn Leu Ile Pro Ser Pro Pro Thr 115 120 125Tyr Asn Ser Ala His Asp Tyr Ile Ser Trp Glu Ser Phe Ser Asn Val 130 135 140Ser Tyr Tyr Thr Arg Ile Leu Pro Ser Val Pro Lys Asp Cys Pro Thr145 150 155 160Pro Met Gly Thr Lys Gly Lys Lys Gln Leu Pro Asp Ala Gln Leu Leu 165 170 175Ala Arg Arg Phe Leu Leu Arg Arg Lys Phe Ile Pro Asp Pro Gln Gly 180 185 190Thr Asn Leu Met Phe Ala Phe Phe Ala Gln His Phe Thr His Gln Phe 195 200 205Phe Lys Thr Ser Gly Lys Met Gly Pro Gly Phe Thr Lys Ala Leu Gly 210 215 220His Gly Val Asp Leu Gly His Ile Tyr Gly Asp Asn Leu Glu Arg Gln225 230 235 240Tyr Gln Leu Arg Leu Phe Lys Asp Gly Lys Leu Lys Tyr Gln Val Leu 245 250 255Asp Gly Glu Met Tyr Pro Pro Ser Val Glu Glu Ala Pro Val Leu Met 260 265 270His Tyr Pro Arg Gly Ile Pro Pro Gln Ser Gln Met Ala Val Gly Gln 275 280 285Glu Val Phe Gly Leu Leu Pro Gly Leu Met Leu Tyr Ala Thr Leu Trp 290 295 300Leu Arg Glu His Asn Arg Val Cys Asp Leu Leu Lys Ala Glu His Pro305 310 315 320Thr Trp Gly Asp Glu Gln Leu Phe Gln Thr Thr Arg Leu Ile Leu Ile 325 330 335Gly Glu Thr Ile Lys Ile Val Ile Glu Glu Tyr Val Gln Gln Leu Ser 340 345 350Gly Tyr Phe Leu Gln Leu Lys Phe Asp Pro Glu Leu Leu Phe Gly Val 355 360 365Gln Phe Gln Tyr Arg Asn Arg Ile Ala Met Glu Phe Asn His Leu Tyr 370 375 380His Trp His Pro Leu Met Pro Asp Ser Phe Lys Val Gly Ser Gln Glu385 390 395 400Tyr Ser Tyr Glu Gln Phe Leu Phe Asn Thr Ser Met Leu Val Asp Tyr 405 410 415Gly Val Glu Ala Leu Val Asp Ala Phe Ser Arg Gln Ile Ala Gly Arg 420 425 430Ile Gly Gly Gly Arg Asn Met Asp His His Ile Leu His Val Ala Val 435 440 445Asp Val Ile Arg Glu Ser Arg Glu Met Arg Leu Gln Pro Phe Asn Glu 450 455 460Tyr Arg Lys Arg Phe Gly Met Lys Pro Tyr Thr Ser Phe Gln Glu Leu465 470 475 480Val Gly Glu Lys Glu Met Ala Ala Glu Leu Glu Glu Leu Tyr Gly Asp 485 490 495Ile Asp Ala Leu Glu Phe Tyr Pro Gly Leu Leu Leu Glu Lys Cys His 500 505 510Pro Asn Ser Ile Phe Gly Glu Ser Met Ile Glu Ile Gly Ala Pro Phe 515 520 525Ser Leu Lys Gly Leu Leu Gly Asn Pro Ile Cys Ser Pro Glu Tyr Trp 530 535 540Lys Pro Ser Thr Phe Gly Gly Glu Val Gly Phe Asn Ile Val Lys Thr545 550 555 560Ala Thr Leu Lys Lys Leu Val Cys Leu Asn Thr Lys Thr Cys Pro Tyr 565 570 575Val Ser Phe Arg Val Pro Asp Ala Ser Gln Asp Asp Gly Pro Ala Val 580 585 590Glu Arg Pro Ser Thr Glu Leu 59536624PRTPseudomonas aeruginosa 36Met His Pro Thr Phe Ser Arg Val Leu Leu Ala Ala Ala Leu Ala Ala1 5 10 15Ala Gly Ser Pro Ala Val Ala Thr Glu Ile Gln Leu Glu Gln Gly Trp 20 25 30Asn Ala Glu Gln Arg Ala Ser Trp Tyr Asp Ala Ser Leu Gly Ser Arg 35 40 45Leu Leu Pro Leu Ala Trp Ala Gln Ala Leu Glu Arg Pro Asp Ser Glu 50 55 60Glu Arg Leu Phe Ser Glu Asp Asn Ala Arg Arg Leu Gly Phe Pro Leu65 70 75 80Arg Asn Trp Gln Gly Gly Glu Leu Arg Leu Pro Arg Gly Phe Ala Leu 85 90 95Asp Gln Gln Asp Asp Ser Gln Phe Ser Asp Thr Arg Leu Arg Trp Lys 100 105 110Ala Arg Gln Ser Ser Ser Glu Pro Trp Val Gly Leu Asn Cys Ala Gly 115 120 125Cys His Ser Thr Asp Ile Ser Tyr Arg Gly Ser Glu Leu Thr Val Asp 130 135 140Ala Gly Ala Thr Leu Ala Asn Val Gln Ala Ile Phe Asp Glu Val Leu145 150 155 160Ala Ala Leu Arg Arg Thr Ser Asp Asp Gly Asp Lys Phe Ala Arg Phe 165 170 175Ala Gly Asn Val Leu Gly Ser Glu Asp Ser Pro Ala Asn Arg Glu Leu 180 185 190Leu Lys Ala Ala Leu Val Lys Arg Ala Ala Leu Ile Asp Thr Leu Leu 195 200 205Ser Met Ser Ala Thr Asp Leu Gln Pro Gly Pro Gly Arg Leu Asp Ala 210 215 220Thr Gly Gln Ser Leu Asn Arg Ala Ala Ile Asn Ser Gly Ala Arg His225 230 235 240Leu Gln Ala Asn Pro Thr Asp Ala Pro Thr Ser Phe Pro Ala Leu Trp 245 250 255His Thr Leu Gln Met Asp Lys Leu Gln Ser Ser Gly Phe Val Pro Asn 260 265 270Val Lys Val Leu Asp Leu Asn Gly Gln Val Phe Asp Leu Gly Tyr Leu 275 280 285Ala Gly Asp Ile Gly Val Val Gln Gly Asp Tyr Gly Asp Val Val Ser 290 295 300His Pro Leu Ser Gly Leu Glu Gly Tyr Ile Ser Ser Ile Arg Val Asp305 310 315 320Asn Leu Thr Arg Val Glu Gly Leu Ile His Lys Leu Lys Ala Pro Ala 325 330 335Trp Pro Ser Gln Leu Phe Gly Ala Pro Asp Ser Ala Arg Leu Ala Gln 340 345 350Gly Lys Arg Leu Tyr Glu Glu Asn Cys Ala Ala Cys His Ala Ser Ile 355 360 365Gly Arg Asp Asp Leu Gln Thr Pro Ile Lys Val Arg Gln Val Arg Leu 370 375 380Lys Ala His Gly Asp Asp Ala Pro Ile Gly Thr Asp Pro Trp Met Ala385 390 395 400Cys Asn Thr Phe Thr Phe Ser Ser Pro Ser Gly Asn Tyr Phe Gly Leu 405 410 415Phe Arg Pro Ser Leu Gly Thr Pro Ser Gly Val Gly Ile Val Gly Arg 420 425 430Thr Ser Lys Ile Ala Asp Met Gln Val Pro Glu Val Phe Gln Ile Met 435 440 445Leu Gly Lys Lys Gly Gln Leu Ala Asp Gly Ile Ala Glu Ile Ile His 450 455 460Ala Ile Val Thr Gly Gln Gln Thr Leu Pro Gly Ser Asp Ser Leu Gln465 470 475 480Ala Val Pro Ala Gly Gln Leu Leu Leu Ala Gly Ala Ala Pro Ala Asp 485 490 495Ser Gln Ala Gln Ser Leu Ala Ala Gly Glu Val Pro Thr Asp Lys Ser 500 505 510Ala Arg Lys Asp Tyr Cys Leu Asn Thr Glu His Pro Phe Leu Gly Tyr 515 520 525Ile Ala Arg Pro Leu Asn Gly Ile Trp Ala Thr Ala Pro Tyr Leu His 530 535 540Asn Gly Ser Val Pro Ser Leu Tyr Asp Leu Leu Leu Pro Gln Glu Gln545 550 555 560Arg Pro Ala Thr Phe Tyr Thr Gly Ser His Glu Phe Asp Pro Ser Arg 565 570 575Val Gly Tyr Leu Thr Ala Pro Gly Pro Asp Asn Ala Phe Leu Phe Asp 580 585 590Thr His Leu Glu Gly Asn Ser Asn Ala Gly His Asp Phe Ala Arg Glu 595 600 605Tyr Asp Glu Ser Gln Arg Leu Ala Leu Leu Glu Tyr Leu Lys Thr Leu 610 615 62037624PRTPseudomonas aeruginosa 37Met His Pro Thr Phe Ser Arg Ile Leu Leu Ala Ala Ala Leu Ala Ser1 5 10 15Ala Gly Ser Pro Ala Val Ala Thr Glu Ile Gln Leu Glu Gln Gly Trp 20 25 30Asn Ala Glu Gln Arg Ala Ser Trp Tyr Asp Ala Ser Leu Gly Ser Arg 35 40 45Leu Leu Pro Leu Ala Trp Ala Gln Ala Leu Glu Arg Pro Asp Ser Glu 50 55 60Glu Arg Leu Phe Ser Glu Asp Asn Ala Arg Arg Leu Gly Phe Pro Leu65 70 75 80Arg Asn Trp Gln Gly Gly Glu Leu Arg Leu Pro Arg Gly Phe Ala Leu 85 90 95Asp Gln Gln Asp Asp Ser Gln Phe Ser Asp Thr Arg Leu Arg Trp Lys 100 105 110Ala Arg Gln Ser Ser Ser Glu Pro Trp Val Gly Leu Asn Cys Ala Gly 115 120 125Cys His Ser Thr Asp Ile Ser Tyr Arg Gly Ser Glu Leu Thr Val Asp 130 135 140Ala Gly Ala Thr Leu Ala Asn Val Gln Ala Ile Phe Asp Glu Val Leu145 150 155 160Ala Ala Leu Arg Arg Thr Ser Asp Asp Gly Asp Lys Phe Ala Arg Phe 165 170 175Ala Gly Asn Val Leu Gly Ser Glu Asp Ser Pro Ala Asn Arg Asp Leu 180 185 190Leu Lys Ala Ala Leu Ala Lys Cys Ala Ala Leu Ile Asp Thr Leu Leu 195 200 205Ser Met Ser Ala Thr Asp Leu Gln Pro Gly Pro Gly Arg Leu Asp Ala 210 215 220Thr Gly Gln Ser Leu Asn Arg Ala Ala Ile Asn Ser Gly Ala Arg His225 230 235 240Leu Gln Ala Asn Pro Thr Asp Ala Pro Thr Ser Phe Pro Ala Leu Trp 245 250 255His Thr Leu Gln Met Asp Lys Leu Gln Ser Ser Gly Phe Val Pro Asn 260 265 270Val Lys Val Leu Asp Leu Asn Gly Gln Val Phe Asp Leu Gly Tyr Leu 275 280 285Ala Gly Asp Ile Gly Val Val Gln Gly Asp Tyr Gly Asp Val Val Ser 290 295 300His Pro Leu Ser Gly Leu Glu Gly Tyr Ile Ser Ser Ile Arg Val Asp305 310 315 320Asn Leu Thr Arg Val Glu Gly Leu Ile His Lys Leu Lys Ala Pro Ala 325 330 335Trp Pro Ser Gln Leu Phe Gly Ala Pro Asp Ser Ala Arg Leu Ala Gln 340 345 350Gly Lys Arg Leu Tyr Glu Glu Asn Cys Ala Ala Cys His Ala Ser Ile 355 360 365Gly Arg Asp Asp Leu Gln Thr Pro Ile Lys Val Arg Gln Val Arg Leu 370 375 380Lys Ala His Gly Asp Asp Ala Pro Ile Gly Thr Asp Pro Trp Met Ala385 390 395 400Cys Asn Thr Phe Thr Phe Ser Ser Pro Ser Gly Asn Tyr Phe Gly Leu 405 410 415Phe Arg Pro Ser Leu Gly Thr Pro Ser Gly Val Gly Ile Val Gly Arg 420 425 430Thr Ser Lys Ile Ala Asp Met Gln Val Pro Glu Val Phe Gln Ile Met 435 440 445Leu Gly Lys Lys Gly Gln Leu Ala Asp Gly Ile Ala Glu Ile Ile His 450 455 460Ala Ile Val Thr Gly Gln Gln Thr Leu Pro Gly Ser Asp Ser Leu Gln465 470 475 480Ala Leu Pro Thr Gly Gln Leu Leu Leu Ala Gly Gly Asp Pro Ala Gly 485 490 495Ser Gln Ala Pro Ser Leu Ala Ala Gly Glu Val Pro Ala Asp Lys Ser 500 505 510Ala Arg Lys Asp Tyr Cys Leu Asn Thr Glu His Pro Phe Leu Gly Tyr 515 520 525Ile Ala Arg Pro Leu Asn Gly Ile Trp Ala Thr Ala Pro Tyr Leu His 530 535 540Asn Gly Ser Val Pro Ser Leu Tyr Asp Leu Leu Leu Pro Gln Glu Gln545 550 555 560Arg Pro Thr Thr Phe Tyr Thr Gly Ser His Glu Phe Asp Pro Ser Arg 565 570 575Val Gly Tyr Leu Thr Gly Pro Gly Pro Asp Asn Ala Phe Leu Phe Asp 580 585 590Thr His Leu Glu Gly Asn Ser Asn Ala Gly His Asp Phe Ala Arg Glu 595 600 605Tyr Asp Glu Ser Gln Arg Leu Ala Leu Leu Glu Tyr Leu Lys Thr Leu 610 615 62038604PRTPseudomonas aeruginosa 38Ala Val Ala Thr Glu Ile Gln Leu Glu Gln Gly Trp Asn Ala Glu Gln1 5 10 15Arg Ala Ser Trp Tyr Asp Ala Ser Leu Gly Ser Arg Leu Leu Pro Leu 20 25 30Ala Trp Ala Gln Ala Leu Glu Arg Pro Asp Ser Glu Glu Arg Leu Phe 35 40 45Ser Glu Asp Asn Ala Arg Arg Leu Gly Phe Pro Leu Arg Asn Trp Gln 50 55 60Gly Gly Glu Leu Arg Leu Pro Arg Gly Phe Ala Leu Asp Gln Gln Asp65 70 75 80Asp Ser Gln Phe Ser Asp Thr Arg Leu Arg Trp Lys Ala Arg Gln Ser 85 90 95Ser Ser Glu Pro Trp Val

Gly Leu Asn Cys Ala Gly Cys His Ser Thr 100 105 110Asp Ile Ser Tyr Arg Gly Ser Glu Leu Thr Val Asp Ala Gly Ala Thr 115 120 125Leu Ala Asn Val Gln Ala Ile Phe Asp Glu Val Leu Ala Ala Leu Arg 130 135 140Arg Thr Ser Asp Asp Gly Asp Lys Phe Ala Arg Phe Ala Gly Asn Val145 150 155 160Leu Gly Ser Glu Asp Ser Pro Ala Asn Arg Asp Leu Leu Lys Ala Ala 165 170 175Leu Ala Lys Cys Ala Ala Leu Ile Asp Thr Leu Leu Ser Met Ser Ala 180 185 190Thr Asp Leu Gln Pro Gly Pro Gly Arg Leu Asp Ala Thr Gly Gln Ser 195 200 205Leu Asn Arg Ala Ala Ile Asn Ser Gly Ala Arg His Leu Gln Ala Asn 210 215 220Pro Thr Asp Ala Pro Thr Ser Phe Pro Ala Leu Trp His Thr Leu Gln225 230 235 240Met Asp Lys Leu Gln Ser Ser Gly Phe Val Pro Asn Val Lys Val Leu 245 250 255Asp Leu Asn Gly Gln Val Phe Asp Leu Gly Tyr Leu Ala Gly Asp Ile 260 265 270Gly Val Val Gln Gly Asp Tyr Gly Asp Val Val Ser His Pro Leu Ser 275 280 285Gly Leu Glu Gly Tyr Ile Ser Ser Ile Arg Val Asp Asn Leu Thr Arg 290 295 300Val Glu Gly Leu Ile His Lys Leu Lys Ala Pro Ala Trp Pro Ser Gln305 310 315 320Leu Phe Gly Ala Pro Asp Ser Ala Arg Leu Ala Gln Gly Lys Arg Leu 325 330 335Tyr Glu Glu Asn Cys Ala Ala Cys His Ala Ser Ile Gly Arg Asp Asp 340 345 350Leu Gln Thr Pro Ile Lys Val Arg Gln Val Arg Leu Lys Ala His Gly 355 360 365Asp Asp Ala Pro Ile Gly Thr Asp Pro Trp Met Ala Cys Asn Thr Phe 370 375 380Thr Phe Ser Ser Pro Ser Gly Asn Tyr Phe Gly Leu Phe Arg Pro Ser385 390 395 400Leu Gly Thr Pro Ser Gly Val Gly Ile Val Gly Arg Thr Ser Lys Ile 405 410 415Ala Asp Met Gln Val Pro Glu Val Phe Gln Ile Met Leu Gly Lys Lys 420 425 430Gly Gln Leu Ala Asp Gly Ile Ala Glu Ile Ile His Ala Ile Val Thr 435 440 445Gly Gln Gln Thr Leu Pro Gly Ser Asp Ser Leu Gln Ala Leu Pro Thr 450 455 460Gly Gln Leu Leu Leu Ala Gly Gly Asp Pro Ala Gly Ser Gln Ala Pro465 470 475 480Ser Leu Ala Ala Gly Glu Val Pro Ala Asp Lys Ser Ala Arg Lys Asp 485 490 495Tyr Cys Leu Asn Thr Glu His Pro Phe Leu Gly Tyr Ile Ala Arg Pro 500 505 510Leu Asn Gly Ile Trp Ala Thr Ala Pro Tyr Leu His Asn Gly Ser Val 515 520 525Pro Ser Leu Tyr Asp Leu Leu Leu Pro Gln Glu Gln Arg Pro Thr Thr 530 535 540Phe Tyr Thr Gly Ser His Glu Phe Asp Pro Ser Arg Val Gly Tyr Leu545 550 555 560Thr Gly Pro Gly Pro Asp Asn Ala Phe Leu Phe Asp Thr His Leu Glu 565 570 575Gly Asn Ser Asn Ala Gly His Asp Phe Ala Arg Glu Tyr Asp Glu Ser 580 585 590Gln Arg Leu Ala Leu Leu Glu Tyr Leu Lys Thr Leu 595 60039711PRTHomo sapiens 39Met Ala Val Tyr Arg Leu Cys Val Thr Thr Gly Pro Tyr Leu Arg Ala1 5 10 15Gly Thr Leu Asp Asn Ile Ser Val Thr Leu Val Gly Thr Cys Gly Glu 20 25 30Ser Pro Lys Gln Arg Leu Asp Arg Met Gly Arg Asp Phe Ala Pro Gly 35 40 45Ser Val Gln Lys Tyr Lys Val Arg Cys Thr Ala Glu Leu Gly Glu Leu 50 55 60Leu Leu Leu Arg Val His Lys Glu Arg Tyr Ala Phe Phe Arg Lys Asp65 70 75 80Ser Trp Tyr Cys Ser Arg Ile Cys Val Thr Glu Pro Asp Gly Ser Val 85 90 95Ser His Phe Pro Cys Tyr Gln Trp Ile Glu Gly Tyr Cys Thr Val Glu 100 105 110Leu Arg Pro Gly Thr Ala Arg Thr Ile Cys Gln Asp Ser Leu Pro Leu 115 120 125Leu Leu Asp His Arg Thr Arg Glu Leu Arg Ala Arg Gln Glu Cys Tyr 130 135 140Arg Trp Lys Ile Tyr Ala Pro Gly Phe Pro Cys Met Val Asp Val Asn145 150 155 160Ser Phe Gln Glu Met Glu Ser Asp Lys Lys Phe Ala Leu Thr Lys Thr 165 170 175Thr Thr Cys Val Asp Gln Gly Asp Ser Ser Gly Asn Arg Tyr Leu Pro 180 185 190Gly Phe Pro Met Lys Ile Asp Ile Pro Ser Leu Met Tyr Met Glu Pro 195 200 205Asn Val Arg Tyr Ser Ala Thr Lys Thr Ile Ser Leu Leu Phe Asn Ala 210 215 220Ile Pro Ala Ser Leu Gly Met Lys Leu Arg Gly Leu Leu Asp Arg Lys225 230 235 240Gly Ser Trp Lys Lys Leu Asp Asp Met Gln Asn Ile Phe Trp Cys His 245 250 255Lys Thr Phe Thr Thr Lys Tyr Val Thr Glu His Trp Cys Glu Asp His 260 265 270Phe Phe Gly Tyr Gln Tyr Leu Asn Gly Val Asn Pro Val Met Leu His 275 280 285Cys Ile Ser Ser Leu Pro Ser Lys Leu Pro Val Thr Asn Asp Met Val 290 295 300Ala Pro Leu Leu Gly Gln Asp Thr Cys Leu Gln Thr Glu Leu Glu Arg305 310 315 320Gly Asn Ile Phe Leu Ala Asp Tyr Trp Ile Leu Ala Glu Ala Pro Thr 325 330 335His Cys Leu Asn Gly Arg Gln Gln Tyr Val Ala Ala Pro Leu Cys Leu 340 345 350Leu Trp Leu Ser Pro Gln Gly Ala Leu Val Pro Leu Ala Ile Gln Leu 355 360 365Ser Gln Thr Pro Gly Pro Asp Ser Pro Ile Phe Leu Pro Thr Asp Ser 370 375 380Glu Trp Asp Trp Leu Leu Ala Lys Thr Trp Val Arg Asn Ser Glu Phe385 390 395 400Leu Val His Glu Asn Asn Thr His Phe Leu Cys Thr His Leu Leu Cys 405 410 415Glu Ala Phe Ala Met Ala Thr Leu Arg Gln Leu Pro Leu Cys His Pro 420 425 430Ile Tyr Lys Leu Leu Leu Pro His Thr Arg Tyr Thr Leu Gln Val Asn 435 440 445Thr Ile Ala Arg Ala Thr Leu Leu Asn Pro Glu Gly Leu Val Asp Gln 450 455 460Val Thr Ser Ile Gly Arg Gln Gly Leu Ile Tyr Leu Met Ser Thr Gly465 470 475 480Leu Ala His Phe Thr Tyr Thr Asn Phe Cys Leu Pro Asp Ser Leu Arg 485 490 495Ala Arg Gly Val Leu Ala Ile Pro Asn Tyr His Tyr Arg Asp Asp Gly 500 505 510Leu Lys Ile Trp Ala Ala Ile Glu Ser Phe Val Ser Glu Ile Val Gly 515 520 525Tyr Tyr Tyr Pro Ser Asp Ala Ser Val Gln Gln Asp Ser Glu Leu Gln 530 535 540Ala Trp Thr Gly Glu Ile Phe Ala Gln Ala Phe Leu Gly Arg Glu Ser545 550 555 560Ser Gly Phe Pro Ser Arg Leu Cys Thr Pro Gly Glu Met Val Lys Phe 565 570 575Leu Thr Ala Ile Ile Phe Asn Cys Ser Ala Gln His Ala Ala Val Asn 580 585 590Ser Gly Gln His Asp Phe Gly Ala Trp Met Pro Asn Ala Pro Ser Ser 595 600 605Met Arg Gln Pro Pro Pro Gln Thr Lys Gly Thr Thr Thr Leu Lys Thr 610 615 620Tyr Leu Asp Thr Leu Pro Glu Val Asn Ile Ser Cys Asn Asn Leu Leu625 630 635 640Leu Phe Trp Leu Val Ser Gln Glu Pro Lys Asp Gln Arg Pro Leu Gly 645 650 655Thr Tyr Pro Asp Glu His Phe Thr Glu Glu Ala Pro Arg Arg Ser Ile 660 665 670Ala Ala Phe Gln Ser Arg Leu Ala Gln Ile Ser Arg Asp Ile Gln Glu 675 680 685Arg Asn Gln Gly Leu Ala Leu Pro Tyr Thr Tyr Leu Asp Pro Pro Leu 690 695 700Ile Glu Asn Ser Val Ser Ile705 71040393PRTNostoc punctiforme 40Met Lys Leu Phe Thr Glu Tyr Pro Glu Lys Asp Glu Leu Lys Tyr Cys1 5 10 15Asp Leu Met Ser Glu Leu Val Lys Lys Asn Met Glu Asn Leu Tyr Gly 20 25 30Gly Lys Lys Lys Lys Thr Ala Lys Arg Asp Thr His Ser Lys Thr His 35 40 45Ala Ala Val Gln Gly Thr Leu Glu Ile Phe Asp Phe Asp Glu Ala Ala 50 55 60Ile Lys Gln Glu Leu Ser Lys Arg Thr Ser Leu Ser Glu Ala Glu Leu65 70 75 80Ser Ala Ile Ser Leu Lys Gln Gly Leu Phe Ala Thr Pro Lys Gln Tyr 85 90 95Pro Val Trp Leu Arg Phe Ala Asn Gly Ala Phe Ser Val Lys Asn Asp 100 105 110Tyr Glu Gly Asp Thr Arg Ser Met Ala Val Lys Ala Ile Gly Val Glu 115 120 125Gly Glu Arg Leu Ser Gln Ser His Glu Leu Lys Thr Gln Asp Ile Ile 130 135 140Thr His Asn Thr Glu Phe Phe Phe Val Arg Thr Ile Lys Asp Phe His145 150 155 160Ser Phe Phe Leu Thr Val Tyr Arg Ala Gly Leu Phe Pro Leu Phe Lys 165 170 175Leu Leu Val Leu Phe Trp Leu Lys Leu His Pro Tyr Glu Ser Thr Leu 180 185 190Leu Gln Thr Ser Phe Lys Arg Phe Pro Lys Ser Leu Leu Lys Glu Arg 195 200 205Tyr Trp Ser Ala Ser Ala Phe Ser Val Gly Leu Lys Ser Gly Phe Asp 210 215 220Pro Ser Gln Pro Gly Arg Val Pro Val Glu Tyr Pro Ala Val Ile Lys225 230 235 240Tyr Gly Phe Thr Pro Val Ser Ser Gln Pro Pro His Gln Gln Phe Pro 245 250 255Leu Glu Ser Arg Ser Glu Ser Glu Leu Lys Leu Ala Lys Ala Ser Gly 260 265 270Ser Glu Asp Asn Tyr Tyr Arg Glu Asp Ile Ile Gln Ala Leu Ala Lys 275 280 285Pro Asp Ala Glu Tyr Tyr Trp Asp Phe Gln Ile Gln Phe Gln Thr Ser 290 295 300Pro Glu Met Ser Ile Asp Asp Thr Thr Ile Val Trp Asn Glu Glu Glu305 310 315 320Ser Pro Phe Phe Thr Val Gly Arg Leu Thr Ile Lys His Gln Lys Val 325 330 335Asn Tyr Pro Gln Ala Asn Asp Phe Gly Glu Asn Leu Ser Phe Ser Pro 340 345 350Gly Asn Gly Leu Ala Val His Arg Pro Val Gly Ala Ile Asn Arg Leu 355 360 365Arg Ser Ile Val Tyr Pro Ile Val Ala Asn Asp Arg His Gln Lys Arg 370 375 380Gly Val Lys Tyr Gln Glu Pro Thr Val385 390411143PRTAspergillus terreus 41Met Ser Ser Val Ile Val Ala Leu Ala Val Leu Val Leu Ser Leu Leu1 5 10 15Tyr Leu Thr Leu Phe Arg Asn Asp Leu Thr His Leu Ile Ile Glu Lys 20 25 30Leu Gln Ser Phe Arg Thr Gly Ser Gly Trp Glu Leu Ser Pro Arg Ser 35 40 45Arg Leu Leu Pro Arg Ala Thr Lys Ala Ala Leu Ser Ser Ile Thr Gly 50 55 60Thr Gly Val Gly Ile Trp Ser Arg Leu Tyr Ala Arg Ile Phe His Ser65 70 75 80Asp Glu Leu Ala Glu Glu Glu Asp Asp Glu Lys Tyr Gln Ala Gly Glu 85 90 95Ala Tyr Gly Asp Pro Lys Val Leu Ala Thr Ser Leu Ile Lys Asp Leu 100 105 110Arg Ala Leu Gly Val Lys Gly Arg Arg Ser Asp Leu Arg Thr Leu Ile 115 120 125Glu Met Val Lys Asn Lys Gly Lys Pro Met Asp Asp Arg Gln Met His 130 135 140Met Glu Lys Ile Ile Ala Ile Val Ala Met Leu Pro Arg Thr Ser Lys145 150 155 160Ala Arg Gln Arg Leu Thr Gly Val Leu Ile Asp Gln Leu Trp Arg Ser 165 170 175Leu Gln His Pro Pro Leu Ser Tyr Phe Gly Asn Lys Tyr Gln Tyr Arg 180 185 190Thr Pro Asp Gly Ser Tyr Asn Asn Pro Leu Glu Pro Asn Leu Gly Lys 195 200 205Ala Gly Ser Pro Tyr Ala Arg Ser Ile Pro Arg Ile Lys Thr Met His 210 215 220Gly Val Arg Pro Asp Pro Gly Leu Leu Phe Asp Leu Leu Met Ala Arg225 230 235 240Asp Asp Ser Thr Phe Lys Glu Asn Pro Ala Gly Ile Ser Ser Met Leu 245 250 255Phe Tyr His Ala Ser Ile Ile Ile His Asp Ile Phe Arg Thr Asn Arg 260 265 270Arg Asp Pro Asn Ile Ser Asp Thr Ser Ser Tyr Leu Asp Leu Ala Pro 275 280 285Leu Tyr Gly Ser Ser Leu Glu Asp Gln Leu Lys Val Arg Thr Met Glu 290 295 300Lys Gly Met Leu Lys Pro Asp Thr Phe His Glu Lys Arg Leu Leu Gly305 310 315 320Gln Pro Ala Gly Val Asn Val Ile Leu Val Met Tyr Ser Arg Phe His 325 330 335Asn Tyr Val Ala Asp Met Leu Leu Lys Ile Asn Glu Asn Gly Arg Phe 340 345 350Thr Leu Pro Pro Thr Ser Ser Glu Glu Ala Arg Lys Lys Ala Leu Ala 355 360 365Lys Gln Asp Glu Asp Leu Phe Gln Val Ala Arg Leu Val Val Asn Gly 370 375 380Leu Tyr Val Asn Ile Ser Leu His Asp Tyr Leu Arg Gly Leu Thr Asn385 390 395 400Thr His His Ser Ala Ser Asp Trp Thr Leu Asp Pro Arg Ile Ala Val 405 410 415Gly Arg Thr Phe Asp Pro Asp Gly Val Pro Arg Gly Ile Gly Asn Gln 420 425 430Ile Ser Ala Glu Phe Asn Leu Leu Tyr Arg Phe His Ser Val Ile Ser 435 440 445Arg Arg Asp Glu Lys Trp Thr Asn Glu Phe Leu Lys Ser Leu Phe Pro 450 455 460Asp Leu Asn Lys Pro Leu Asp Gln Leu Thr Pro Gln Glu Phe Met Met465 470 475 480Gly Leu Met Arg Tyr Glu Gln Ser Ile Asp Lys Asp Pro Ser Lys Arg 485 490 495Glu Phe Gly Gly Leu Lys Arg Ser Pro Asp Gly Lys Phe Asn Asp Ala 500 505 510Asp Leu Val Gln Ile Leu Lys Asp Ser Met Glu Asp Pro Ala Gly Leu 515 520 525Phe Gly Pro Arg Asn Val Pro Lys Ala Leu Arg Met Ile Glu Ile Ala 530 535 540Gly Ile Met Ser Ala Arg Lys Trp Asp Leu Gly Ser Leu Asn Glu Met545 550 555 560Arg Asp Phe Phe Lys Leu Lys Arg His Ala Thr Phe Glu Asp Ile Asn 565 570 575Pro Asp Pro Glu Ile Ala Asp Leu Leu Arg Lys Leu Tyr Asp His Pro 580 585 590Asp Met Val Glu Met Tyr Pro Gly Met Phe Leu Glu Asp Ala Lys Pro 595 600 605Arg Leu Asp Pro Gly Cys Gly Gly Cys Pro Pro Tyr Thr Val Gly Arg 610 615 620Ala Val Phe Ser Asp Ala Val Thr Leu Val Arg Ser Asp Arg Phe Leu625 630 635 640Thr Leu Asp Tyr Thr Ala Ser Asn Leu Thr Asn Trp Gly Phe Arg Glu 645 650 655Val Gln Gln Asp Tyr Asp Ile Leu Gly Gly Ser Met Phe His Lys Leu 660 665 670Ile Gln Arg Ala Leu Pro Gly Trp Phe Pro Tyr Asn Ser Leu His Ala 675 680 685Thr Gln Pro Met Phe Thr Arg Lys Met Asn Glu Gln Ile Ala Arg Glu 690 695 700Ile Gly Thr Ile Asp His Tyr Ser Leu Ala Asp Pro Ala Pro Pro Pro705 710 715 720Arg Lys Ile Val Leu Thr Asp Tyr Ala Thr Asn Ile Lys Val Leu Lys 725 730 735Asp Gln Ala Ser Phe Arg Val Pro Trp Ala Arg Tyr Leu Asn Asp Met 740 745 750Phe Pro Gly Lys Thr Tyr Asn Asp Tyr Met Leu Gly Gly Asp Asp Pro 755 760 765Ala Asn Ala Ala Gln Lys Lys Leu Val His Ser Ile Leu Phe Ser Pro 770 775 780Asp Gln Phe Leu Asp Leu Leu Ser Glu Thr Thr Thr Lys Leu Gly Ser785 790 795 800Glu Leu Leu Lys Ala Asn Thr Leu Trp Leu Thr Lys Asp Leu His Gln 805 810 815Val Asp Ile Ile Arg Asp Val Ala Ile Pro Leu Asn Ala Arg Ile Met 820 825 830Ala Asp Leu Phe Cys Leu Asp Met Lys Thr Pro Glu Asn Pro Thr Gly 835 840 845Ser Met Asn Ala Ala Thr Val Tyr Arg His Leu Met Asn Val Arg Ile 850

855 860Trp Gly Phe Asn Asn Asn Asp Pro Ala Leu Met Leu Gln Arg Arg Lys865 870 875 880Trp Ala Ile Glu Ser Ala Glu Ala Leu Ile Glu Thr Thr Arg Lys Leu 885 890 895Val Asn Glu Gln Ala Gln Pro Ala Gln Ser Gly Val Leu Lys Asn Leu 900 905 910Met Thr Arg Arg Gln Ala Thr Gly Thr Leu Arg Trp Tyr Gly Asn Asn 915 920 925Val Ala Lys Glu Met Met Glu Met Gly Met Ser Ala Glu Glu Val Ala 930 935 940Asp Ile Cys Trp Leu Thr Ala Ile Gly Gly Val Gly Thr Pro Ser Gly945 950 955 960Val Val Ala Asn Val Leu Gln Tyr Tyr Phe Arg Tyr Glu Asn Ile Gly 965 970 975His Trp Glu Glu Ile Gln Lys Leu Val Thr Gln Pro Asp Thr Pro Ala 980 985 990Ala Asp Arg Thr Leu Arg Gln Tyr Val Leu Glu Ala Asn Arg Leu Thr 995 1000 1005Ser Met Glu Cys Thr Val Arg Val Cys Ala Arg Pro Val Thr Val 1010 1015 1020Asp Gly His Asp Phe Lys Pro Gly Glu Val Ile Val Asn His Leu 1025 1030 1035Gly Leu Ala Cys Arg Asp Pro His Asn Ile Pro Asp Ala Asp Lys 1040 1045 1050Phe Arg Leu Asp Arg Pro Ala Ser Ala Tyr Ile Gln Trp Gly Tyr 1055 1060 1065Gly Ala His Glu Cys Leu Gly Lys Glu Ile Ala Ile Thr Phe Ala 1070 1075 1080Val Ser Met Ile Arg Ile Leu Ala Gly Leu Lys Tyr Leu Arg Pro 1085 1090 1095Ala Pro Gly Glu Met Gly Val Leu Lys Ser Val Met Ala Asp Gly 1100 1105 1110Arg Gln Ala Phe Leu Asn Asp Ser Trp Ser Trp Leu Thr Gln Asp 1115 1120 1125Pro Thr Ser Lys Ser Asn Met His Gly Lys Ala Ser Ala Val Asp 1130 1135 114042518PRTArabidopsis thaliana 42Met Ala Ser Ile Ser Thr Pro Phe Pro Ile Ser Leu His Pro Lys Thr1 5 10 15Val Arg Ser Lys Pro Leu Lys Phe Arg Val Leu Thr Arg Pro Ile Lys 20 25 30Ala Ser Gly Ser Glu Thr Pro Asp Leu Thr Val Ala Thr Arg Thr Gly 35 40 45Ser Lys Asp Leu Pro Ile Arg Asn Ile Pro Gly Asn Tyr Gly Leu Pro 50 55 60Ile Val Gly Pro Ile Lys Asp Arg Trp Asp Tyr Phe Tyr Asp Gln Gly65 70 75 80Ala Glu Glu Phe Phe Lys Ser Arg Ile Arg Lys Tyr Asn Ser Thr Val 85 90 95Tyr Arg Val Asn Met Pro Pro Gly Ala Phe Ile Ala Glu Asn Pro Gln 100 105 110Val Val Ala Leu Leu Asp Gly Lys Ser Phe Pro Val Leu Phe Asp Val 115 120 125Asp Lys Val Glu Lys Lys Asp Leu Phe Thr Gly Thr Tyr Met Pro Ser 130 135 140Thr Glu Leu Thr Gly Gly Tyr Arg Ile Leu Ser Tyr Leu Asp Pro Ser145 150 155 160Glu Pro Lys His Glu Lys Leu Lys Asn Leu Leu Phe Phe Leu Leu Lys 165 170 175Ser Ser Arg Asn Arg Ile Phe Pro Glu Phe Gln Ala Thr Tyr Ser Glu 180 185 190Leu Phe Asp Ser Leu Glu Lys Glu Leu Ser Leu Lys Gly Lys Ala Asp 195 200 205Phe Gly Gly Ser Ser Asp Gly Thr Ala Phe Asn Phe Leu Ala Arg Ala 210 215 220Phe Tyr Gly Thr Asn Pro Ala Asp Thr Lys Leu Lys Ala Asp Ala Pro225 230 235 240Gly Leu Ile Thr Lys Trp Val Leu Phe Asn Leu His Pro Leu Leu Ser 245 250 255Ile Gly Leu Pro Arg Val Ile Glu Glu Pro Leu Ile His Thr Phe Ser 260 265 270Leu Pro Pro Ala Leu Val Lys Ser Asp Tyr Gln Arg Leu Tyr Glu Phe 275 280 285Phe Leu Glu Ser Ala Gly Glu Ile Leu Val Glu Ala Asp Lys Leu Gly 290 295 300Ile Ser Arg Glu Glu Ala Thr His Asn Leu Leu Phe Ala Thr Cys Phe305 310 315 320Asn Thr Trp Gly Gly Met Lys Ile Leu Phe Pro Asn Met Val Lys Arg 325 330 335Ile Gly Arg Ala Gly His Gln Val His Asn Arg Leu Ala Glu Glu Ile 340 345 350Arg Ser Val Ile Lys Ser Asn Gly Gly Glu Leu Thr Met Gly Ala Ile 355 360 365Glu Lys Met Glu Leu Thr Lys Ser Val Val Tyr Glu Cys Leu Arg Phe 370 375 380Glu Pro Pro Val Thr Ala Gln Tyr Gly Arg Ala Lys Lys Asp Leu Val385 390 395 400Ile Glu Ser His Asp Ala Ala Phe Lys Val Lys Ala Gly Glu Met Leu 405 410 415Tyr Gly Tyr Gln Pro Leu Ala Thr Arg Asp Pro Lys Ile Phe Asp Arg 420 425 430Ala Asp Glu Phe Val Pro Glu Arg Phe Val Gly Glu Glu Gly Glu Lys 435 440 445Leu Leu Arg His Val Leu Trp Ser Asn Gly Pro Glu Thr Glu Thr Pro 450 455 460Thr Val Gly Asn Lys Gln Cys Ala Gly Lys Asp Phe Val Val Leu Val465 470 475 480Ala Arg Leu Phe Val Ile Glu Ile Phe Arg Arg Tyr Asp Ser Phe Asp 485 490 495Ile Glu Val Gly Thr Ser Pro Leu Gly Ser Ser Val Asn Phe Ser Ser 500 505 510Leu Arg Lys Ala Ser Phe 51543478PRTSolanum tuberosum 43Met Ser Ser Tyr Ser Glu Leu Ser Asn Leu Pro Ile Arg Glu Ile Pro1 5 10 15Gly Asp Tyr Gly Phe Pro Ile Ile Ser Ala Ile Lys Asp Arg Tyr Asp 20 25 30Tyr Phe Tyr Asn Gln Gly Glu Asp Ala Trp Phe His Asn Lys Ala Glu 35 40 45Lys Tyr Lys Ser Thr Val Val Lys Ile Asn Met Ala Pro Gly Pro Phe 50 55 60Thr Ser Asn Asp Tyr Lys Leu Val Ala Phe Leu Asp Ala Asn Ser Phe65 70 75 80Val Cys Met Phe Asp Asn Ser Leu Ile Asp Lys Thr Asp Thr Leu Gly 85 90 95Gly Thr Phe Lys Pro Gly Lys Glu Tyr Tyr Ser Gly Tyr Arg Pro Val 100 105 110Ala Phe Ile Asp Thr Lys Asp Pro Asn His Ala Ala Leu Lys Gly Tyr 115 120 125Ile Leu Ser Ala Phe Ala Lys Arg His Asn Leu Phe Ile Pro Leu Phe 130 135 140Arg Asn Ser Leu Ser Asp His Leu Phe Asn Asn Leu Glu Lys Gln Val145 150 155 160Thr Glu Gln Gly Lys Ser Asp Phe Asn Ala Leu Leu Pro Thr Met Thr 165 170 175Phe Asn Phe Ile Phe Arg Leu Leu Cys Asp Gln Thr Asn Pro Ser Asp 180 185 190Thr Val Leu Gly Ala Gln Gly Pro Glu His Leu Arg Lys Trp Leu Phe 195 200 205Pro Gln Leu Ile Pro Ser Leu Ser Ala Lys Lys Leu Pro Asn Ile Ile 210 215 220Glu Asp Thr Leu Phe His Asn Phe Leu Ile Pro Phe Gly Phe Ile Lys225 230 235 240Ser Asp Tyr Asn Lys Leu Val Asp Ala Phe Ser Lys Ser Ala Val Ser 245 250 255Ile Leu Asp Glu Ala Glu Lys Leu Gly Ile Lys Arg Glu Glu Ala Val 260 265 270Gln Asn Ile Leu Phe Leu Val Gly Ile Asn Met Phe Ala Gly Leu Asn 275 280 285Ala Phe Ser Pro His Leu Phe Arg Phe Val Gly Glu Ala Gly Ala Ser 290 295 300Leu His Thr Gln Leu Ala Lys Glu Ile Arg Thr Val Ile Lys Glu Glu305 310 315 320Gly Gly Ala Ile Thr Leu Ser Ala Ile Asn Lys Met Ser Leu Val Lys 325 330 335Ser Val Val Tyr Glu Thr Leu Arg Leu Arg Pro Pro Val Pro Leu Gln 340 345 350Tyr Gly Lys Ala Lys Lys Asp Phe Met Val Gln Ser His Asp Ala Ser 355 360 365Tyr Lys Ile Asn Lys Gly Gln Phe Val Val Gly Tyr Gln Pro Met Ala 370 375 380Ser Arg Asp Pro Lys Ile Phe Ala Asn Pro Asp Glu Phe Val Pro Asp385 390 395 400Arg Phe Met Asn Asp Gly Glu Lys Met Leu Lys His Val Leu Trp Ser 405 410 415Asn Gly Arg Glu Thr Glu Asn Pro Ala Pro Asp Asn Lys Gln Cys Pro 420 425 430Gly Lys Asp Leu Val His Leu Leu Gly Arg Leu Ile Leu Val Glu Phe 435 440 445Phe Met Arg Tyr Asp Thr Phe Thr Val Glu Ile Thr Pro Leu Phe Arg 450 455 460Ala Pro Asn Val Ala Phe Lys Thr Leu Thr Lys Ala Ser Lys465 470 47544472PRTAllium sativum 44Met Ser Thr Ser Asn Gly Ser Thr Glu Asn Ile Gln Lys Pro Leu Arg1 5 10 15Lys Ile Pro Asp Ile Thr Gly Thr Pro Ile Leu Thr Ala Ile Lys Asp 20 25 30Arg Leu Asp Phe Phe Tyr Asn Gln Gly Gln Tyr Glu Tyr Phe Gln Ser 35 40 45Arg Val Lys Lys Asn Asn Ser Thr Ile Leu Arg Met Asn Met Ile Pro 50 55 60Gly Pro Phe Ala Ser Asn Pro Lys Ile Val Ala Leu Cys Asp Ala Ala65 70 75 80Ser Phe Pro Thr Leu Phe Asp Pro Ser Lys Val Ser Lys Val Asn Ser 85 90 95Leu Thr Gly Asn Tyr Met Pro Ala Leu Ser Phe Thr Gly Gly Tyr Arg 100 105 110Val Cys Ala Tyr Leu Asp Pro Ser Glu Pro Thr His Thr Lys Ile Lys 115 120 125Gln Val Phe Phe Asn Ala Gln Ala Ala Lys Lys Asp Thr Phe Ile Pro 130 135 140Thr Phe Val Ser Thr Phe Asn Ser Met Phe Asp Lys Met Asp Ala Glu145 150 155 160Val Glu Ser Lys Lys Lys Ala Glu Phe Thr Lys Phe Asn Glu Ala Ala 165 170 175Val Phe Glu Phe Val Gly Leu Ala Leu Val Gly Pro Lys Pro Ala Arg 180 185 190Glu Val Phe Asp Ser Ala Lys Lys Ser Val Phe Phe Gln Phe His Pro 195 200 205Phe Ile Thr Ala Gly Leu Pro Ala Leu Val Glu Glu Leu Ala Phe His 210 215 220Met Phe Pro Phe Pro Ser Phe Val Ala Lys Ser Ser Tyr Lys Ile Leu225 230 235 240Tyr Glu Tyr Phe Ser Thr Gly Gly Ser Trp Ile Leu Asp Asn Ala Glu 245 250 255Glu Ile Gly Leu Ser Arg Glu Glu Ala Ile His His Leu Ile Phe Thr 260 265 270Trp Ala Ile Asn Ala Tyr Leu Gly Ile Arg Thr Cys Leu Met Arg Leu 275 280 285Phe Lys Trp Ile Val Ala Ser Gly Pro Asp Leu Gln Glu Lys Leu Ala 290 295 300Arg Glu Val Arg Ser Val Val Arg Ser Glu Glu Gly Lys Ile Thr Phe305 310 315 320Ala Gly Ile Glu Lys Met Glu Leu Val Lys Ser Val Ala Tyr Glu Ser 325 330 335Phe Arg Phe Asp Pro Pro Val Gln Val Gln Tyr Gly Thr Ala Lys Ser 340 345 350Asp Leu Ile Ile Glu Ser His Asp Gly Lys Tyr Gln Val Lys Lys Gly 355 360 365Glu Met Leu Cys Gly Phe Gln Pro Met Ala Thr Arg Asp Pro Lys Val 370 375 380Phe Asp Arg Ala Asp Glu Phe Val Pro Asp Arg Phe Met Gly Asp Gly385 390 395 400Lys Lys Leu Val Lys His Val Leu Trp Ala Asn Gly Tyr Gly Thr Asp 405 410 415Ala Pro Lys Ala Asp Asp Lys Ile Cys Ala Gly Lys Asp Leu Gly Val 420 425 430Leu Val Gly Arg Leu Leu Ile Ala Val Met Phe Leu Arg Tyr Asp Lys 435 440 445Ile Gly Gly Val Val Gly Lys Thr Met Glu Glu Val Asp Val Ile Val 450 455 460Asn Glu Leu Thr Lys Val Ala Val465 470451081PRTAsperigullus nidalus 45Met Gly Glu Asp Lys Glu Thr Asn Ile Leu Ala Gly Leu Gly Asn Thr1 5 10 15Ile Ser Gln Val Glu Asn Val Val Ala Ala Ser Leu Arg Pro Leu Pro 20 25 30Thr Ala Thr Gly Asp Gly Thr Tyr Val Ala Glu Ser Thr Gln Thr Gly 35 40 45Leu Ala Lys Asp Leu Ser His Val Asp Leu Lys Asp Val Arg Thr Leu 50 55 60Ala Glu Val Val Lys Ser Ala Ala Thr Gly Glu Pro Val Asp Asp Lys65 70 75 80Gln Tyr Ile Met Glu Arg Val Ile Gln Leu Ala Ala Gly Leu Pro Ser 85 90 95Thr Ser Arg Asn Ala Ala Glu Leu Thr Lys Ser Phe Leu Asn Met Leu 100 105 110Trp Asn Asp Leu Glu His Pro Pro Val Ser Tyr Leu Gly Ala Asp Ser 115 120 125Met His Arg Lys Ala Asp Gly Ser Gly Asn Asn Arg Phe Trp Pro Gln 130 135 140Leu Gly Ala Ala Gly Ser Ala Tyr Ala Arg Ser Val Arg Pro Lys Thr145 150 155 160Met Gln Ser Pro Ser Leu Pro Asp Pro Glu Thr Ile Phe Asp Cys Leu 165 170 175Leu Arg Arg Lys Glu Tyr Arg Glu His Pro Asn Lys Ile Ser Ser Val 180 185 190Leu Phe Tyr Leu Ala Ser Ile Ile Ile His Asp Leu Phe Gln Thr Asp 195 200 205Pro Lys Asp Asn Ser Val Ser Lys Thr Ser Ser Tyr Leu Asp Leu Ser 210 215 220Pro Leu Tyr Gly Asn Asn Gln Asp Glu Gln Asn Leu Val Arg Thr Phe225 230 235 240Lys Asp Gly Lys Leu Lys Pro Asp Cys Phe Ala Thr Lys Arg Val Leu 245 250 255Gly Phe Pro Pro Gly Val Gly Val Leu Leu Ile Met Phe Asn Arg Phe 260 265 270His Asn Tyr Val Val Asp Gln Leu Ala Ala Ile Asn Glu Cys Gly Arg 275 280 285Phe Thr Lys Pro Asp Glu Ser Asn Val Asp Glu Tyr Ala Lys Tyr Asp 290 295 300Asn Asn Leu Phe Gln Thr Gly Arg Leu Val Thr Cys Gly Leu Tyr Ala305 310 315 320Asn Ile Ile Leu Lys Asp Tyr Val Arg Thr Ile Leu Asn Ile Asn Arg 325 330 335Thr Asp Ser Thr Trp Ser Leu Asp Pro Arg Met Glu Met Lys Asp Gly 340 345 350Leu Leu Gly Glu Ala Ala Ala Met Ala Thr Gly Asn Gln Val Ser Ala 355 360 365Glu Phe Asn Val Val Tyr Arg Trp His Ala Cys Ile Ser Lys Arg Asp 370 375 380Glu Lys Trp Thr Glu Asp Phe His Arg Glu Ile Met Pro Gly Val Asp385 390 395 400Pro Ser Thr Leu Ser Met Gln Asp Phe Val Ala Gly Leu Gly Arg Trp 405 410 415Gln Ala Gly Leu Pro Gln Glu Pro Leu Glu Arg Pro Phe Ser Gly Leu 420 425 430Gln Arg Lys Pro Asp Gly Ala Phe Asn Asp Asp Asp Leu Val Asn Leu 435 440 445Phe Glu Lys Ser Val Glu Asp Cys Ala Gly Ala Phe Gly Ala Ser His 450 455 460Val Pro Ala Ile Phe Lys Ser Val Glu Ala Leu Gly Ile Met Gln Ala465 470 475 480Arg Arg Trp Asn Leu Gly Thr Leu Asn Glu Phe Arg Gln Tyr Phe Asn 485 490 495Leu Ala Pro His Lys Thr Phe Glu Asp Ile Asn Ser Asp Pro Tyr Ile 500 505 510Ala Asp Gln Leu Lys Arg Leu Tyr Asp His Pro Asp Leu Val Glu Ile 515 520 525Tyr Pro Gly Val Val Val Glu Glu Ala Lys Asp Ser Met Val Pro Gly 530 535 540Ser Gly Leu Cys Thr Asn Phe Thr Ile Ser Arg Ala Ile Leu Ser Asp545 550 555 560Ala Val Ala Leu Val Arg Gly Asp Arg Phe Tyr Thr Val Asp Tyr Thr 565 570 575Pro Lys His Leu Thr Asn Trp Ala Tyr Asn Glu Ile Gln Pro Asn Asn 580 585 590Ala Val Asp Gln Gly Gln Val Phe Tyr Lys Leu Val Leu Arg Ala Phe 595 600 605Pro Asn His Phe Asp Gly Asn Ser Ile Tyr Ala His Phe Pro Leu Val 610 615 620Val Pro Ser Glu Asn Glu Lys Ile Leu Lys Ser Leu Gly Val Ala Glu625 630 635 640Lys Tyr Ser Trp Glu Lys Pro Ser Arg Ile Ser His Pro Ile Phe Ile 645 650 655Ser Ser His Ala Ala Cys Met Ser Ile Leu Glu Asn Gln Glu Thr Phe 660 665 670Lys Val Thr Trp Gly Arg Lys Ile Glu Phe Leu Met Gln Arg Asp Lys 675 680 685His Gln Tyr Gly Lys Asp Phe Met Leu Ser Gly Asp Arg Pro Pro Asn 690 695 700Ala Ala Ser Arg Lys

Met Met Gly Ser Ala Leu Tyr Arg Asp Glu Trp705 710 715 720Glu Ala Glu Val Lys Asn Phe Tyr Glu Gln Thr Thr Leu Lys Leu Leu 725 730 735His Lys Asn Ser Tyr Lys Leu Ala Gly Val Asn Gln Val Asp Ile Val 740 745 750Arg Asp Val Ala Asn Leu Ala Gln Val His Phe Cys Ser Ser Val Phe 755 760 765Ser Leu Pro Leu Lys Thr Asp Ser Asn Pro Arg Gly Ile Phe Ala Glu 770 775 780Ser Glu Leu Tyr Lys Ile Met Ala Ala Val Phe Thr Ala Ile Phe Tyr785 790 795 800Asp Ala Asp Ile Gly Lys Ser Phe Glu Leu Asn Gln Ala Ala Arg Thr 805 810 815Val Thr Gln Gln Leu Gly Gln Leu Thr Met Ala Asn Val Glu Ile Ile 820 825 830Ala Lys Thr Gly Leu Ile Ala Asn Leu Val Asn Arg Leu His Arg Arg 835 840 845Asp Val Leu Ser Glu Tyr Gly Ile His Met Ile Gln Arg Leu Leu Asp 850 855 860Ser Gly Leu Pro Ala Thr Glu Ile Val Trp Thr His Ile Leu Pro Thr865 870 875 880Ala Gly Gly Met Val Ala Asn Gln Ala Gln Leu Phe Ser Gln Cys Leu 885 890 895Asp Tyr Tyr Leu Ser Glu Glu Gly Ser Gly His Leu Pro Glu Ile Asn 900 905 910Arg Leu Ala Lys Glu Asn Thr Pro Glu Ala Asp Glu Leu Leu Thr Arg 915 920 925Tyr Phe Met Glu Gly Ala Arg Leu Arg Ser Ser Val Ala Leu Pro Arg 930 935 940Val Ala Ala Gln Pro Thr Val Val Glu Asp Asn Gly Glu Lys Leu Thr945 950 955 960Ile Lys Ala Gly Gln Val Val Met Cys Asn Leu Val Ser Ala Cys Met 965 970 975Asp Pro Thr Ala Phe Pro Asp Pro Glu Lys Val Lys Leu Asp Arg Asp 980 985 990Met Asn Leu Tyr Ala His Phe Gly Phe Gly Pro His Lys Cys Leu Gly 995 1000 1005Leu Asp Leu Cys Lys Thr Gly Leu Ser Thr Met Leu Lys Val Leu 1010 1015 1020Gly Arg Leu Asp Asn Leu Arg Arg Ala Pro Gly Ala Gln Gly Gln 1025 1030 1035Leu Lys Lys Leu Ser Gly Pro Gly Gly Ile Ala Lys Tyr Met Asn 1040 1045 1050Glu Asp Gln Ser Gly Phe Thr Pro Phe Pro Ser Thr Met Lys Ile 1055 1060 1065Gln Trp Asp Gly Glu Leu Pro Gln Leu Lys Glu Asp Phe 1070 1075 1080461079PRTAspergillus fumigatus 46Met Ser Glu Lys Gln Thr Gly Ser Ala Asn Gly Gly Leu Gly Lys Thr1 5 10 15Leu Ala Gln Leu Glu Gln Val Val Ser Ala Ser Leu Arg Pro Leu Pro 20 25 30Cys Gln Thr Gly Asp Gly Thr Tyr Val Thr Glu Gln Val Lys Thr Gly 35 40 45Ile Leu Lys Asp Leu Ser His Val Asp Leu Gly Asp Leu Lys Thr Leu 50 55 60Val Asp Val Ser Lys Ser Ala Leu Thr Gly Glu Ala Leu Asp Asp Arg65 70 75 80Lys Tyr Ile Met Glu Arg Val Ile Gln Leu Ser Ala Gly Leu Pro Ser 85 90 95Thr Ser Gln Ile Gly Lys Glu Leu Thr Asn Thr Phe Leu Thr Thr Leu 100 105 110Trp Asn Asp Leu Glu His Pro Pro Ile Ser Tyr Leu Gly Arg Asp Ala 115 120 125Met Tyr Arg Arg Ala Asp Gly Ser Gly Asn Asn Val Leu Trp Pro His 130 135 140Ile Gly Ala Ala Gly Thr Pro Tyr Ala Arg Ser Val Gln Pro Lys Thr145 150 155 160Val Gln Ser Pro Asn Leu Pro Asp Pro Glu Thr Leu Phe Asp Cys Leu 165 170 175Leu Ala Arg Lys Glu Tyr Lys Glu His Pro Asn Lys Ile Ser Ser Val 180 185 190Leu Phe Tyr Ile Ala Ser Ile Ile Ile His Asp Leu Phe Glu Thr Asp 195 200 205Arg Lys Asp Pro Ala Ile Ser Leu Thr Ser Ser Tyr Leu Asp Leu Ser 210 215 220Pro Leu Tyr Gly Asn Asn Gln Gln Glu Gln Asp Leu Ile Arg Thr Phe225 230 235 240Lys Asp Gly Lys Leu Lys Pro Asp Cys Phe Ser Thr Lys Arg Val Leu 245 250 255Gly Phe Pro Pro Gly Val Gly Val Val Leu Ile Met Phe Asn Arg Phe 260 265 270His Asn Tyr Val Val Glu Lys Leu Ala Met Ile Asn Glu Gly Gly Arg 275 280 285Phe Thr Lys Pro Gln Glu Ser Asp Thr Ala Ala Tyr Ala Lys Tyr Asp 290 295 300Asn Asp Leu Phe Gln Thr Gly Arg Leu Val Thr Cys Gly Leu Tyr Val305 310 315 320Asn Ile Ile Leu Lys Asp Tyr Val Arg Thr Ile Leu Asn Ile Asn Arg 325 330 335Thr Asp Ser Ile Trp Ser Leu Asp Pro Arg Ser Glu Met Lys Asp Gly 340 345 350Leu Leu Gly Arg Ala Ala Ala Gln Ala Thr Gly Asn Gln Val Ala Ala 355 360 365Glu Phe Asn Leu Val Tyr Arg Trp His Ser Cys Ile Ser Gln Arg Asp 370 375 380Gln Lys Trp Thr Glu Asp Met Tyr Gln Glu Leu Phe Pro Gly Gln Asp385 390 395 400Pro Ser Lys Ile Ser Leu Gln Asp Phe Leu Arg Gly Leu Gly Arg Trp 405 410 415Glu Ala Lys Leu Pro Gly Glu Pro Arg Glu Arg Pro Phe Ala Gly Leu 420 425 430Gln Arg Lys Ala Asp Gly Ser Tyr Asp Asp Asn Asp Leu Val Lys Ile 435 440 445Phe Glu Glu Ser Val Glu Asp Cys Ala Gly Ala Phe Gly Ala Leu His 450 455 460Val Pro Thr Val Phe Arg Ser Ile Glu Ala Leu Gly Ile Gln Gln Ala465 470 475 480Arg Ser Trp Asn Leu Ala Thr Leu Asn Glu Phe Arg Lys Tyr Phe Asn 485 490 495Leu Ala Pro Tyr Lys Thr Phe Glu Glu Ile Asn Ser Asp Pro Tyr Val 500 505 510Ala Asp Gln Leu Lys Arg Leu Tyr Asp His Pro Asp Arg Val Glu Ile 515 520 525Tyr Pro Gly Ile Ile Val Glu Asp Ala Lys Glu Ser Met Ala Pro Gly 530 535 540Ser Gly Leu Cys Thr Asn Phe Thr Ile Ser Arg Ala Ile Leu Ser Asp545 550 555 560Ala Val Ala Leu Val Arg Gly Asp Arg Phe His Thr Val Asp Phe Thr 565 570 575Pro Lys His Leu Thr Asn Trp Ala Tyr Asn Glu Ile Gln Pro Gln Asp 580 585 590Ser Val Asp Gln Thr His Val Phe Tyr Lys Leu Val Leu Arg Ala Phe 595 600 605Pro Asn His Phe Arg Gly Asp Ser Ile Tyr Ala His Phe Pro Leu Val 610 615 620Val Pro Ser Glu Asn Lys Lys Ile Leu Thr Lys Leu Gly Thr Ala Asp625 630 635 640Lys Tyr Ser Trp Asp Arg Pro Asn Tyr Thr Pro Pro Pro Gln Phe Ile 645 650 655Asn Ser His Ser Ala Cys Met Ser Ile Leu Ser Asp Gln Glu Thr Phe 660 665 670Lys Val Thr Trp Gly Ser Lys Ile Glu Phe Leu Met Arg His Asn Asn 675 680 685Gln Pro Tyr Gly Arg Asp Phe Met Leu Ser Gly Asp Arg Thr Pro Asn 690 695 700Ala Met Ser Arg Gln Met Met Gly Lys Ala Leu Tyr Arg Asp Lys Trp705 710 715 720Glu Thr Glu Val Lys Arg Phe Tyr Glu Asn Ile Thr Leu Lys Leu Leu 725 730 735His Arg Tyr Ser Tyr Lys Leu Ala Gly Val Asn Gln Val Asp Val Val 740 745 750Arg Asp Ile Ala Asn Leu Ala Gln Val His Phe Cys Ala Ser Val Phe 755 760 765Ser Leu Pro Leu Lys Thr Glu Ser Asn Pro Arg Gly Ile Phe Thr Glu 770 775 780Ser Glu Leu Tyr Gln Ile Met Ala Val Val Phe Thr Ser Ile Phe Tyr785 790 795 800Asp Ala Asp Ile Gly Lys Ser Phe Glu Leu Asn Gln Ala Ala Arg Ala 805 810 815Val Thr Gln Gln Leu Gly Gln Leu Thr Leu Ala Asn Val Glu Leu Ile 820 825 830Ala Lys Thr Gly Phe Ile Ala Asn Leu Val Asn Ser Leu His Arg His 835 840 845Asp Val Leu Ser Glu Tyr Gly Val His Met Ile Gln Arg Leu Leu Asp 850 855 860Ser Gly Met Pro Ala Pro Glu Ile Val Trp Thr His Val Leu Pro Thr865 870 875 880Ala Gly Gly Met Val Ala Asn Gln Ala Gln Leu Phe Ser Gln Ser Leu 885 890 895Asp Tyr Tyr Leu Ser Glu Glu Gly Ser Val His Leu Pro Glu Ile Asn 900 905 910Arg Leu Ala Lys Glu Asp Thr Thr Glu Ala Asp Asp Leu Leu Leu Arg 915 920 925Tyr Phe Met Glu Gly Ala Arg Ile Arg Ser Ser Val Ala Leu Pro Arg 930 935 940Val Val Ala Gln Pro Thr Val Val Glu Asp Asn Gly Gln Lys Ile Thr945 950 955 960Leu Lys Gln Gly Gln His Ile Ile Cys Asn Leu Val Ser Ala Ser Met 965 970 975Asp Pro Val Thr Phe Pro Glu Pro Asp Lys Val Lys Leu Asp Arg Asp 980 985 990Met Asn Leu Tyr Ala His Phe Gly Phe Gly Pro His Gln Cys Leu Gly 995 1000 1005Leu Gly Leu Cys Lys Thr Ala Leu Thr Thr Met Leu Lys Val Ile 1010 1015 1020Gly Arg Leu Asp Asn Leu Arg Arg Ala Pro Gly Gly Gln Gly Lys 1025 1030 1035Leu Lys Lys Leu Ser Gly Pro Gly Gly Ile Ala Met Tyr Met Thr 1040 1045 1050Pro Asp Gln Thr Ala Phe Phe Pro Phe Pro Thr Thr Met Lys Ile 1055 1060 1065Gln Trp Asp Gly Asp Leu Pro Glu Val Lys Glu 1070 1075471066PRTPlexaura homomalla 47Met Thr Trp Lys Asn Phe Gly Phe Glu Ile Phe Gly Glu Lys Tyr Gly1 5 10 15Gln Glu Glu Leu Glu Lys Arg Ile Lys Asp Glu His Thr Pro Pro Pro 20 25 30Asp Ser Pro Val Phe Gly Gly Leu Lys Leu Lys Leu Lys Lys Glu Lys 35 40 45Phe Lys Thr Leu Phe Thr Leu Gly Thr Thr Leu Lys Gly Phe Arg Arg 50 55 60Ala Thr His Thr Val Gly Thr Gly Gly Ile Gly Glu Ile Thr Ile Val65 70 75 80Asn Asp Pro Lys Phe Pro Glu His Glu Phe Phe Thr Ala Gly Arg Thr 85 90 95Phe Pro Ala Arg Leu Arg His Ala Asn Leu Lys Tyr Pro Asp Asp Ala 100 105 110Gly Ala Asp Ala Arg Ser Phe Ser Ile Lys Phe Ala Asp Ser Asp Ser 115 120 125Asp Gly Pro Leu Asp Ile Val Met Asn Thr Gly Glu Ala Asn Ile Phe 130 135 140Trp Asn Ser Pro Ser Leu Glu Asp Phe Val Pro Val Glu Glu Gly Asp145 150 155 160Ala Ala Glu Glu Tyr Val Tyr Lys Asn Pro Tyr Tyr Tyr Tyr Asn Leu 165 170 175Val Glu Ala Leu Arg Arg Ala Pro Asp Thr Phe Ala His Leu Tyr Tyr 180 185 190Tyr Ser Gln Val Thr Met Pro Phe Lys Ala Lys Asp Gly Lys Val Arg 195 200 205Tyr Cys Arg Tyr Arg Ala Leu Pro Gly Asp Val Asp Ile Lys Glu Glu 210 215 220Asp Glu Ser Gly Arg Leu Thr Glu Glu Glu Gln Arg Lys Ile Trp Ile225 230 235 240Phe Ser Arg His Glu Asn Glu Lys Arg Pro Asp Asp Tyr Leu Arg Lys 245 250 255Glu Tyr Val Glu Arg Leu Gln Lys Gly Pro Val Asn Tyr Arg Leu Gln 260 265 270Ile Gln Ile His Glu Ala Ser Pro Asp Asp Thr Ala Thr Ile Phe His 275 280 285Ala Gly Ile Leu Trp Asp Lys Glu Thr His Pro Trp Phe Asp Leu Ala 290 295 300Lys Val Ser Ile Lys Thr Pro Leu Ser Pro Asp Val Leu Glu Lys Thr305 310 315 320Ala Phe Asn Ile Ala Asn Gln Pro Ala Ser Leu Gly Leu Leu Glu Ala 325 330 335Lys Ser Pro Glu Asp Tyr Asn Ser Ile Gly Glu Leu Arg Val Ala Val 340 345 350Tyr Thr Trp Val Gln His Leu Arg Lys Leu Lys Ile Gly Ser Leu Val 355 360 365Pro Ala Gly Gln Asn Ala Ile Tyr Asn Val Glu Val Glu Thr Gly Asp 370 375 380Arg Glu His Ala Gly Thr Asp Ala Thr Ile Thr Ile Arg Ile Thr Gly385 390 395 400Ala Lys Gly Arg Thr Asp Tyr Leu Lys Leu Asp Lys Trp Phe His Asn 405 410 415Asp Phe Glu Ala Gly Ser Lys Glu Gln Tyr Thr Val Gln Gly Phe Asp 420 425 430Val Gly Asp Ile Gln Leu Ile Glu Leu His Ser Asp Gly Gly Gly Tyr 435 440 445Trp Ser Gly Asp Pro Asp Trp Phe Val Asn Arg Val Ile Ile Ile Ser 450 455 460Ser Thr Gln Asp Arg Val Tyr Ser Phe Pro Cys Phe Arg Trp Val Ile465 470 475 480Lys Asp Met Val Leu Phe Pro Gly Glu Ala Thr Leu Pro Phe Asn Glu 485 490 495Val Pro Ala Ile Val Ser Glu Gln Arg Gln Lys Glu Leu Glu Gln Arg 500 505 510Lys Leu Thr Tyr Gln Trp Asp Tyr Val Ser Asp Asp Met Pro Gly Asn 515 520 525Ile Lys Ala Lys Thr His Asp Asp Leu Pro Arg Asp Val Gln Phe Thr 530 535 540Asp Glu Lys Ser Arg Ser Tyr Gln Glu Ser Arg Lys Ala Ala Leu Val545 550 555 560Asn Leu Gly Ile Gly Ser Leu Phe Thr Met Phe Glu Asn Trp Asp Ser 565 570 575Tyr Asp Asp Tyr His Ile Leu Tyr Arg Asn Trp Ile Leu Gly Gly Thr 580 585 590Pro Asn Met Ala Asp Arg Trp His Glu Asp Arg Trp Phe Gly Tyr Gln 595 600 605Phe Leu Asn Gly Ala Asn Pro Val Ile Leu Thr Arg Cys Asp Ala Leu 610 615 620Pro Ser Asn Phe Pro Val Thr Asn Glu His Val Asn Ala Ser Leu Asp625 630 635 640Arg Gly Lys Asn Leu Asp Glu Glu Ile Lys Asp Gly His Ile Tyr Ile 645 650 655Val Asp Phe Lys Val Leu Val Gly Ala Lys Ser Tyr Gly Gly Pro Val 660 665 670Leu Glu Asp Ile Gly Tyr Lys Val Pro Asp His Leu Lys His Asp Glu 675 680 685Ala Asp Ile Arg Tyr Cys Ala Ala Pro Leu Ala Leu Phe Tyr Val Asn 690 695 700Lys Leu Gly His Leu Met Pro Ile Ala Ile Gln Ile Asn Gln Glu Pro705 710 715 720Gly Pro Glu Asn Pro Ile Trp Thr Pro His Glu Glu Asn Glu His Asp 725 730 735Trp Met Met Ala Lys Phe Trp Leu Gly Val Ala Glu Ser Asn Phe His 740 745 750Gln Leu Asn Thr His Leu Leu Arg Thr His Leu Thr Thr Glu Ser Phe 755 760 765Ala Leu Ser Thr Trp Arg Asn Leu Ala Ser Ala His Pro Val Phe Lys 770 775 780Leu Leu Gln Pro His Ile Tyr Gly Val Leu Ala Ile Asp Thr Ile Gly785 790 795 800Arg Lys Glu Leu Ile Gly Ser Gly Gly Ile Val Asp Gln Ser Leu Ser 805 810 815Leu Gly Gly Gly Gly His Val Thr Phe Met Glu Lys Cys Phe Lys Glu 820 825 830Val Asn Leu Gln Asp Tyr His Leu Pro Asn Ala Leu Lys Lys Arg Gly 835 840 845Val Asp Asp Pro Ser Lys Leu Pro Gly Phe Tyr Tyr Arg Asp Asp Gly 850 855 860Leu Ala Leu Trp Glu Ala Ile Glu Thr Phe Ile Gly Glu Ile Ile Ala865 870 875 880Ile Phe Tyr Lys Asn Asp Asp Asp Val Lys Arg Asp Asn Glu Ile Gln 885 890 895Ser Trp Ile Tyr Asp Val His Lys Asn Gly Trp Arg Val Asn Pro Gly 900 905 910His Gln Asp His Gly Val Pro Ala Ser Phe Glu Ser Arg Glu Gln Leu 915 920 925Lys Glu Val Leu Thr Ser Leu Val Phe Thr Phe Ser Cys Gln His Ala 930 935 940Ala Val Asn Phe Ser Gln Lys Asp His Tyr Gly Phe Thr Pro Asn Ala945 950 955 960Pro Ala Val Leu Arg His Pro Pro Pro Lys Lys Lys Gly Glu Ala Thr 965 970 975Leu Gln Ser Ile Leu Ser Thr Leu Pro Ser Lys Ser Gln Ala Ala Lys 980 985 990Ala Ile Ala Thr Val Tyr Ile Leu Thr Lys Phe Ser Glu Asp Glu Arg 995 1000

1005Tyr Leu Gly Asn Tyr Ser Ala Thr Ala Trp Glu Asp Lys Asp Ala 1010 1015 1020Leu Asp Ala Ile Asn Arg Phe Gln Asp Lys Leu Glu Asp Ile Ser 1025 1030 1035Lys Lys Ile Lys Gln Arg Asn Glu Asn Leu Glu Val Pro Tyr Ile 1040 1045 1050Tyr Leu Leu Pro Glu Arg Ile Pro Asn Gly Thr Ala Ile 1055 1060 1065481151PRTFusarium oxysporum 48Met Ser Phe Asn Glu Lys Phe Gln Ala Gly Glu Ser Tyr Gly Asp Ser1 5 10 15Lys Glu Asp Pro Ser Ser Leu Leu Asn Asn Pro Glu Lys Leu Val Ala 20 25 30Asp Leu Met Lys Asp Phe Ala Gly Val Arg Ser Gln Ala Ser Pro Ala 35 40 45Gln Leu Leu Gly Leu Val Lys Glu Leu Leu Gln Lys Gly Gln Pro Leu 50 55 60Asp Asp Lys Lys Gly Thr Thr Glu Leu Leu Ile Gly Ile Leu Thr Ala65 70 75 80Leu Pro Ala Thr Ser Lys Ala Arg Thr Ala Leu Thr Asn Lys Leu Ile 85 90 95Asp Thr Leu Trp Gly Asn Leu Gln His Pro Pro Leu Ser Tyr Met Gly 100 105 110Gly Asp Val Lys Tyr Asp Val Val Asn Ser Asp Lys Pro Ala His Lys 115 120 125His Asn Cys Glu Leu Tyr Asp Thr Ile Glu Phe Lys Val Pro Gly Thr 130 135 140Asp Val Leu Leu Arg Glu Gln Val Pro Gln Ala Pro Asp Gly Leu His145 150 155 160Gln Tyr Arg Met Pro Asp Gly Ser Phe Asn Asn Ile Leu Glu Pro Asn 165 170 175Leu Gly Arg Ala Gly Thr Pro Tyr Ala Lys Ser Val Lys Ser Glu Lys 180 185 190Arg Leu His Gly Val Lys Pro Asp Pro Gly Leu Leu Phe Asp Leu Leu 195 200 205Met Ala Arg Asp Glu Thr Thr Phe Gln Glu Asn Pro Ala Gly Ile Ser 210 215 220Ser Met Leu Phe Tyr His Ala Ala Ile Ile Ile His Asp Ile Phe Arg225 230 235 240Thr Asn Arg Thr Asp Met Asn Lys Ser Asp Thr Ser Ser Tyr Leu Asp 245 250 255Leu Ala Pro Leu Tyr Gly Ser Ser Leu Lys Asp Gln His Glu Ile Arg 260 265 270Thr Met Lys Glu Gly Lys Leu Lys Pro Asp Thr Phe His Glu Lys Arg 275 280 285Leu Leu Gly Gln Pro Ala Gly Val Asn Val Met Leu Val Leu Tyr Ser 290 295 300Arg Phe His Asn Tyr Val Ala Asp Ile Leu Leu Lys Ile Asn Glu Asn305 310 315 320Gly Arg Phe Ser Leu Ser Val Pro Pro Asn Ala Ser Glu Glu Asp Lys 325 330 335Ala Lys Ala Ile Ala Lys Gln Asp His Asp Leu Phe Asn Val Ala Arg 340 345 350Leu Ile Thr Gly Gly Leu Tyr Ile Asn Ile Cys Leu His Asp Tyr Leu 355 360 365Arg Ala Ile Thr Asn Thr His His Ser Ala Ser Asp Trp Thr Leu Asp 370 375 380Pro Arg Val Ala Ile Asp Lys Gln Phe Asp Gly Asp Gly Val Pro Arg385 390 395 400Gly Val Gly Asn Gln Val Ser Val Glu Phe Asn Leu Leu Tyr Arg Phe 405 410 415His Ser Cys Ile Ser Lys Arg Asp Glu Lys Trp Ile Asn Asn Phe Phe 420 425 430Leu Lys Leu Phe Pro Gly Arg Lys Ala Glu Asp Leu Gln Asp Val Ser 435 440 445Trp Thr Glu Leu Gly Gln Ala Leu Leu Ile Phe Glu Gln Asn Thr Pro 450 455 460Lys Asp Pro Ser Val Arg Thr Phe Asp Gly Leu Glu Arg Gln Ala Asp465 470 475 480Gly Thr Phe Lys Asp Glu Asp Leu Val Arg Ile Leu Lys Asp Ala Met 485 490 495Glu Asp Pro Ala Gly Thr Phe Gly Ala Arg Met Val Pro Lys Ala Leu 500 505 510Lys Val Val Glu Val Leu Gly Ile Ile Gln Gly Arg Lys Trp Gln Cys 515 520 525Ala Ser Leu Asn Glu Phe Arg Glu Phe Phe Gly Leu Lys Arg Tyr Asp 530 535 540Ser Phe Ser Glu Ile Asn Ser Asn Pro Asp Ile Ala Asn Ile Leu Glu545 550 555 560Lys Leu Tyr Thr Asp Pro Asp Met Val Glu Leu Tyr Pro Gly Leu Met 565 570 575Ile Glu Asp Ile Lys Pro Gln Arg Asn Pro Gly Ser Gly Ile Met Pro 580 585 590Thr Tyr Ser Val Gly Arg Ala Val Leu Ser Asp Ala Val Thr Leu Val 595 600 605Arg Ser Asp Arg Phe Asn Thr Ile Asp Tyr Thr Val Ser Asn Leu Thr 610 615 620Ala Trp Gly Tyr Asn Glu Val Gln Gln Asp Tyr Lys Thr Leu Gly Gly625 630 635 640Ser Met Leu Tyr Lys Leu Ile Gln Arg Gly Val Pro Asn Trp Phe Pro 645 650 655Phe Asn Ser Ile Ala Val Met Gln Pro Met Tyr Thr Lys Lys Ala Asn 660 665 670Glu Gln Ile Ala Lys Glu Ile Gly Thr Phe Asp Gln Tyr Thr Leu Asp 675 680 685Asp Pro Lys Ala Pro Pro Lys Val Ala Val Leu Thr Ser Gly Pro Ala 690 695 700Ile Lys Gln Ile Leu Ser Asn Thr Lys Gln Tyr Val Val Pro Trp Leu705 710 715 720Lys Pro Leu Asn Thr Leu Phe Pro Gly Lys Lys Asp Phe Gly Trp Phe 725 730 735Met Leu Ala Gly Asp Gln Pro Gln Asn Tyr Thr His Arg Ala Asn Phe 740 745 750Ser Lys Ala Met Ser Lys Ile Pro Asn Met His Asn Ala Val His Ala 755 760 765Phe Ile Glu Arg Glu Gly Thr Lys Leu Ile Asn Lys Glu Thr Phe Thr 770 775 780Leu Lys Lys Gly Leu Asp Gln Ile Asp Ile Ile Arg Asp Val Ala Ile785 790 795 800Pro Leu Asn Thr Gln Leu Leu Ala Asp Leu Phe Tyr Phe Asp Leu Arg 805 810 815Thr Glu Glu Asn Pro Asp Gly Lys Leu Gly Val Ala Glu Leu Tyr Arg 820 825 830Ser Leu Leu Asp Ile Arg Ile Trp Gly Val Asn Asn Asn Asp Pro Ala 835 840 845Gln Ala Trp Asn Arg Arg Arg Arg Ala Gln Glu Gly Ala Lys Arg Met 850 855 860Ile Glu Thr Thr Lys Thr Ile Val Ala Glu Ala Asp Ala Gly Arg Pro865 870 875 880Arg Gly Ile Gly Leu Val Ser Ala Val Ala Asn Arg Ile Gly Ala Arg 885 890 895Ser Tyr Leu Lys Lys Asp Ser Leu Arg Ser Cys Gly Leu Lys Leu Val 900 905 910Glu Glu Leu Leu Ala Gln Gly Asn Asn Val Asp Gln Val Thr Asp Asn 915 920 925Leu Trp Leu Thr Ala Phe Gly Gly Ile Gly Val Pro Val Thr Ala Phe 930 935 940Tyr Glu Val Leu Ser Phe Phe Leu Arg Pro Glu Asn Glu Ala Ile Trp945 950 955 960Ala Glu Val Gln Ala Ile Ala Gln Lys Gly Asp Asp Ala Thr Leu His 965 970 975Ala Tyr Val Ala Glu Ala Gln Arg Met Thr Ser Ser Gln Arg Asn Val 980 985 990Arg Val Ala Thr Ala Pro Gly Glu Val Gln Gly Gln Ala Ile Gln Pro 995 1000 1005Gly Thr Ala Val Val Leu Met Leu Gly Glu Ala Gly Arg Asn Pro 1010 1015 1020Lys Glu Val Pro Asp Ala Gly Lys Phe Asn Pro Gln Arg Lys Lys 1025 1030 1035Glu Asp Val Ser Ala Phe Ser Tyr Gly Gln His Glu Cys Ile Ala 1040 1045 1050Lys Asp Val Ala Leu Ala Phe Val Thr Gly Leu Ile Lys Leu Val 1055 1060 1065Ala Asp Leu Lys Glu Leu Arg Pro Ala Pro Gly Gln Met Gly Thr 1070 1075 1080Val Lys Thr Ile Gln Val Gly Thr Glu Lys Ala Tyr Leu Asn Asp 1085 1090 1095Ser Trp Ser Tyr Leu Gly Phe Asp Ala Ser Thr Trp Lys Val His 1100 1105 1110Phe Asn Gly His Gly Lys Gly Lys Phe Glu Gly Glu Arg Val Pro 1115 1120 1125Thr Lys Ser Thr Pro Ile Gln Glu Tyr Tyr Tyr Leu Leu Gln Lys 1130 1135 1140Arg Lys Asp Glu Ile Leu Gly Asn 1145 1150491162PRTColletotrichum graminicola 49Met Ser Phe Asp Gln Lys Phe Met Ala Gly Glu Thr Tyr Gly Asp Glu1 5 10 15Arg Lys Ser Ser Ala Asn Phe Phe Ser Asp Pro Thr Lys Val Ala Thr 20 25 30Asp Leu Leu Lys Asp Tyr Ala Gly Leu Arg Ser Gln Thr Ser Pro Ala 35 40 45Glu Leu Ala Gly Leu Ile Lys Glu Leu Leu Gln Lys Gly Gln Pro Leu 50 55 60Asp Asp Lys Lys Gly Thr Thr Glu Ile Leu Ile Gly Ile Leu Thr Ser65 70 75 80Leu Pro Ser Thr Ser Ser Thr Arg Val Gln Leu Thr Asn Lys Leu Ile 85 90 95Asp Thr Leu Trp Gly Thr Leu Gln His Pro Pro Leu Ser Tyr Val Gly 100 105 110Gly Asp Val Lys Tyr Glu Val Val Asn Pro Asn Glu Thr Ala Ser Lys 115 120 125Asp Lys Gln Gln Thr Glu Asp Ser Ile Glu Phe Lys Ala Pro Asp Ser 130 135 140Asp Val Ile Leu Arg Glu Gln Val Pro Arg Pro Pro Asp Gly Leu His145 150 155 160His Tyr Arg Met Pro Asp Gly Ser Tyr Asn Asn Ile Leu Glu Pro Asn 165 170 175Leu Gly Lys Ala Gly Thr Pro Tyr Ala Lys Thr Val Arg Thr Ser Lys 180 185 190Arg Leu His Gly Val Lys Pro Asp Pro Gly Leu Leu Phe Asp Leu Leu 195 200 205Met Ala Arg Asp Asp Ser Thr Phe Lys Glu Asn Pro Ala Gly Ile Ser 210 215 220Ser Met Leu Phe Tyr His Ala Ser Ile Ile Ile His Asp Ile Phe Arg225 230 235 240Thr Asn Arg Thr Asp Met Asn Lys Ser Asp Thr Ser Ser Tyr Leu Asp 245 250 255Leu Ala Pro Leu Tyr Gly Ser Ser Leu Lys Asp Gln Leu Glu Ile Arg 260 265 270Thr Met Lys Glu Gly Met Leu Lys Pro Asp Thr Phe His Glu Arg Arg 275 280 285Leu Leu Gly Gln Pro Ala Gly Val Asn Ala Met Leu Val Leu Tyr Asn 290 295 300Arg Phe His Asn Tyr Val Cys Asp Ile Leu Leu Lys Ile Asn Glu Asn305 310 315 320Gly Arg Phe Thr Leu Gln Cys Pro Ala Asp Ala Ser Pro Glu Asp Arg 325 330 335Ala Lys Ala Val Ala Lys Gln Asp His Asp Leu Phe Asn Thr Ala Arg 340 345 350Leu Ile Val Gly Gly Leu Tyr Ile Asn Ile Ser Leu His Asp Tyr Leu 355 360 365Arg Ala Ile Thr Asn Thr His His Ser Lys Ser Asp Trp Thr Leu Asp 370 375 380Pro Arg Val Glu Ile Gly Lys Gln Phe Asp Gly Glu Gly Val Pro Arg385 390 395 400Gly Val Gly Asn Gln Val Ser Val Glu Phe Asn Leu Leu Tyr Arg Phe 405 410 415His Ser Cys Ile Ser Lys Lys Asp Glu Arg Trp Ile Asp Asn Phe Phe 420 425 430Ala Lys Leu Phe Pro Asp Arg Lys Pro Glu Asp Leu Gln Asn Val Gly 435 440 445Met Ala Glu Leu Gly Gln Ala Leu Met Thr Phe Glu Gln Ser Ile Pro 450 455 460Lys Asp Pro Ser Ala Arg Thr Phe Asp Asn Leu Glu Arg Gln Ala Asp465 470 475 480Gly Lys Phe Lys Asp Glu Asp Leu Val Arg Val Leu Lys Glu Ala Met 485 490 495Asp Asp Pro Ala Gly Cys Phe Gly Ala Arg Met Val Pro Lys Ala Leu 500 505 510Lys Ile Val Glu Ile Leu Gly Ile Asn Gln Ala Arg Lys Trp Gln Val 515 520 525Ala Ser Leu Asn Glu Phe Arg Glu Phe Phe Gly Leu Lys Lys Tyr Asp 530 535 540Lys Phe Ala Glu Ile Asn Ser Asn Pro Glu Ile Ala Thr Leu Leu Glu545 550 555 560Lys Leu Tyr Thr Asp Pro Asp Met Val Glu Leu Tyr Pro Gly Leu Met 565 570 575Ile Glu Asp Ile Lys Pro Ala Arg Asn Thr Gly Ser Gly Ile Cys Pro 580 585 590Thr Tyr Ser Val Gly Arg Ala Val Leu Ser Asp Ala Val Thr Leu Val 595 600 605Arg Ser Asp Arg Phe Asn Thr Leu Asp Tyr Thr Val Ser Asn Leu Thr 610 615 620Ala Trp Gly Tyr Asn Glu Val Gln Gln Asp Tyr Lys Thr Leu Gly Gly625 630 635 640Ser Met Leu Tyr Lys Leu Ile Gln Arg Gly Leu Pro Asn Trp Phe Pro 645 650 655Tyr Asn Ser Val Ala Val Met Gln Pro Met Tyr Thr Lys Lys Ala Asn 660 665 670Glu Ser Ile Ala Lys Glu Leu Gly Thr Leu His Leu Tyr Thr Ser Asn 675 680 685Asp Pro Lys Pro Pro Pro Lys Ile Val Val Val Ala Thr Ser Val Ala 690 695 700Ile Lys Gln Val Leu Gly Asn Ser Lys Gln Phe Val Val Pro Trp Leu705 710 715 720Gln Pro Leu Asn Asp Leu Phe Thr Gly Thr Lys Lys Asp Ile Ser Trp 725 730 735Phe Met Leu Ala Gly Asp Glu Pro Lys Asn Tyr Gln His Arg Val Asn 740 745 750Leu Leu Lys Ala Met Gly Lys Ile Pro Asn Leu His Asn Ala Val His 755 760 765Glu Phe Val Asp Arg Val Gly Ala Lys Leu Ile Glu Lys Glu Thr Phe 770 775 780Lys Leu Lys Glu Gly Leu Cys Gln Met Asp Ile Ile Arg Asp Val Ala785 790 795 800Ile Pro Leu Asn Ala Gln Leu Leu Ala Asp Leu Phe Tyr Phe Asp Met 805 810 815Arg Thr Asp Glu Asn Pro Asn Gly Thr Leu Ser Ala Ala Asp Leu Tyr 820 825 830Arg His Leu Leu Asn Ile Arg Val Trp Gly Val Asn Asn Asn Asp Pro 835 840 845Ala Gln Ala Trp Asn Arg Arg Arg Arg Ala Thr Glu Ser Val Asn Ala 850 855 860Ile Ile Asp Ser Thr Arg Gly Leu Val Asn Glu Val Val Val Gly Arg865 870 875 880Gly Leu Gly Phe Gly Ile Ala Ser Thr Ile Ser Gly Val Val Gly Arg 885 890 895Lys Ser Asn Phe Lys Lys Asp Ser Leu Arg Ser Cys Gly His Lys Leu 900 905 910Val Glu Glu Leu Leu Ala Gln Gly Asn Ser Ala Glu Gln Val Val Asp 915 920 925Asn Met Trp Leu Thr Ala Phe Gly Gly Ile Gly Ala Pro Val Thr Ala 930 935 940Phe Tyr Glu Val Leu Glu Tyr Phe Leu Arg Arg Glu Asn Ala Ser Ile945 950 955 960Trp Ala Glu Val Gln Thr Leu Ala Gln Lys Asn Asp Asp Ala Gly Leu 965 970 975His Ala Tyr Val Lys Glu Ala Gln Arg Leu Thr Ser Ser Gln Arg Asn 980 985 990Val Arg Val Ala Thr Val Ala Ala Glu Val Asp Gly Lys Gln Val Gln 995 1000 1005Pro Gly Asn Val Val Val Met Leu Leu Gly Asp Ala Gly Arg Asn 1010 1015 1020Pro Lys Glu Val Ala Asn Pro Asp Lys Phe Asp Ala Lys Arg Lys 1025 1030 1035Thr Asp Pro Val Ser Ala Phe Ser Tyr Gly Gln His Glu Cys Leu 1040 1045 1050Ala Lys Asp Ile Ala Thr Thr Phe Ile Val Gly Leu Val Lys Leu 1055 1060 1065Val Ala Asp Leu Lys Gln Leu Arg Pro Ala Pro Gly Gln Met Gly 1070 1075 1080Leu Val Lys Thr Ile Arg Val Gly Ser Glu Lys Ala Tyr Leu Asn 1085 1090 1095Asp Ser Trp Ser Tyr Leu Gly Phe Asp Ala Ser Thr Trp Lys Val 1100 1105 1110His Phe Asp Gly His Gly Lys Gly Asn Phe Glu Gly Asp Val Gln 1115 1120 1125Pro Asn Lys Pro Ile Asp Leu Gly Gln Tyr Tyr Tyr Leu Leu Gln 1130 1135 1140Lys Arg Lys Glu Lys Leu Leu Asn Gly Asn Ser Ser Asn Gly Thr 1145 1150 1155Asn Gly Ser Ser 1160501161PRTGlomerella cingulate 50Met Ala Phe Asn Thr Lys Phe Gln Ala Gly Glu Ser Tyr Gly Asp Glu1 5 10 15Arg Lys Gly Ser Asn Asn Phe Phe Ala Asp Pro Lys Lys Val Ala Met 20 25 30Asp Ile Ile Lys Asp Leu Gly Gly Ala His Gly Gln Leu Asn Leu Leu 35 40 45Glu Val Thr Ala Leu Val Gln Gln Leu Leu Gln Lys Gly Glu Pro Leu 50 55 60Asp Asp Lys Lys Gly Thr Thr Glu Ala Leu Ile Gly Ile Leu Thr Ser65 70 75 80Leu Pro Ser Gly Ser

Asn Thr Arg Val Gln Leu Thr Asn Lys Leu Ile 85 90 95Asp Thr Leu Trp Gly Asn Leu Gln His Pro Pro Leu Ser Tyr Val Gly 100 105 110Gly Asp Val Lys Tyr Glu Val Val Lys Thr Lys Glu Gln Leu Ala Lys 115 120 125Glu Gln Ala Asp Leu Ala Ala Gln Gly Lys Ala Pro Gln Ser Pro Glu 130 135 140Glu Ser His Ile Thr Phe Lys Ala Pro Asp Phe Pro Asp Ile Thr Leu145 150 155 160Arg Glu His Leu Pro Thr Pro Pro Asp Asn Tyr Lys Met Pro Asp Gly 165 170 175Ser Tyr Asn Asn Ile Leu Glu Pro Asn Leu Gly Ala Ala Gly Thr Pro 180 185 190Tyr Ala Lys Thr Val Lys Thr Glu Lys Arg Leu Ala Gly Val Lys Pro 195 200 205Asp Pro Gly Leu Leu Phe Asp Leu Leu Leu Ala Arg Asp Asp Lys Lys 210 215 220Phe Thr Glu Asn Pro Ala Gly Ile Ser Ser Met Leu Phe Tyr His Ala225 230 235 240Ser Ile Ile Ile His Asp Ile Phe Arg Thr Asn Arg His Asp Leu Asn 245 250 255Lys Ser Asp Thr Ser Ser Tyr Leu Asp Leu Ala Pro Leu Tyr Gly Ser 260 265 270Ser Phe Lys Asp Gln Leu Glu Ile Arg Thr Met Lys Glu Gly Lys Leu 275 280 285Lys Pro Asp Thr Phe His Glu Lys Arg Leu Leu Gly Gln Pro Ala Gly 290 295 300Val Asn Val Met Leu Val Leu Ser Ser Arg Phe His Asn Tyr Val Ala305 310 315 320Asp Ile Leu Leu Lys Ile Asn Glu Asn Gly Arg Phe Thr Leu Gln Thr 325 330 335Ala Lys Asp Ala Ala Pro Glu Asp Gln Ala Lys Ala Val Ala Lys Gln 340 345 350Asp His Asp Leu Phe Asn Val Ala Arg Leu Val Thr Gly Gly Leu Tyr 355 360 365Ile Asn Ile Cys Leu His Asp Tyr Leu Arg Ala Ile Thr Asn Thr His 370 375 380His Ser Lys Ser Asp Trp Thr Leu Asp Pro Arg Val Glu Ile Gly Lys385 390 395 400Gln Phe Asp Gly Glu Gly Val Pro Arg Gly Val Gly Asn Gln Val Ser 405 410 415Val Glu Phe Asn Leu Leu Tyr Arg Phe His Ser Cys Ile Ser Lys Lys 420 425 430Asp Glu Arg Trp Ile Asp Gly Phe Phe Ala Lys Leu Phe Pro Gly Arg 435 440 445Lys Pro Glu Asp Leu Gln Asn Val Gly Met Glu Glu Leu Gly Ala Ala 450 455 460Leu Met Lys Phe Glu Met Gly Ile Asp Lys Asp Pro Ser Lys Arg Thr465 470 475 480Phe Asp Asp Leu Gln Arg Gly Glu Asp Gly Lys Phe Arg Asp Glu Asp 485 490 495Leu Val Arg Val Leu Lys Glu Ala Met Glu Asp Pro Ala Gly Thr Phe 500 505 510Gly Ala Arg Met Val Pro Lys Ala Leu Lys Ile Val Glu Ile Met Gly 515 520 525Ile Lys Gln Ala Arg Ala Trp Gln Val Ala Ser Leu Asn Glu Phe Arg 530 535 540Asp Phe Phe Gly Leu Lys Arg His Asp Thr Phe Lys Asp Ile Asn Ser545 550 555 560Asn Glu Glu Ile Ala Thr Leu Leu Glu Lys Leu Tyr Thr Asp Pro Asp 565 570 575Met Val Glu Leu Tyr Pro Gly Leu Met Ile Glu Asp Ile Lys Pro Val 580 585 590Arg Asn Thr Gly Ser Gly Ile Cys Pro Thr Tyr Ser Val Gly Arg Ala 595 600 605Val Leu Ser Asp Ala Val Thr Leu Val Arg Ser Asp Arg Phe Asn Thr 610 615 620Ile Asp Tyr Thr Val Ser Asn Leu Thr Ala Trp Gly Tyr Asn Glu Val625 630 635 640Gln Gln Asp Tyr Lys Thr Leu Gly Gly Ser Met Leu Tyr Lys Leu Ile 645 650 655Gln Arg Gly Leu Pro Gly Trp Phe Pro Phe Asn Ser Ile Ala Val Met 660 665 670Gln Pro Met Tyr Thr Lys Lys Ala Asn Glu Arg Ile Ala Arg Glu Ile 675 680 685Gly Thr Phe Asn Gln Phe Thr Leu Asp Asp Pro Lys Ala Pro Pro Lys 690 695 700Pro Val Val Val Ala Ser Ser Glu Gly Ile Lys Arg Val Leu Gly Ser705 710 715 720Pro Asp Lys Phe Val Val Pro Trp Leu Thr Pro Leu Asn Ala Leu Tyr 725 730 735Thr Asp Thr Lys Lys Asp Ile Ser Trp Phe Met Leu Ala Gly Asp Gly 740 745 750Ser Thr Asn Lys Gln Glu Lys Val Asn Phe Val Asn Ala Met Lys Lys 755 760 765Val Pro Asn Leu His Asn Ala Val His Gln Phe Ile Glu Arg Val Gly 770 775 780Arg Gln Leu Ile Glu Lys Glu Thr Phe Lys Leu Lys Glu Gly Leu Cys785 790 795 800Gln Met Asp Ile Ile Arg Asp Val Ala Ile Pro Leu Asn Ala Gln Leu 805 810 815Leu Ala Asp Leu Phe Tyr Phe Asp Leu Arg His Glu Glu Asn Pro Gly 820 825 830Gly Thr Leu Ser Ala Thr Asp Leu Tyr Arg His Leu Leu Asn Ile Arg 835 840 845Ile Trp Gly Val Asn Asn Asn Asp Pro Gly Gln Ala Trp Asn Arg Arg 850 855 860Arg Arg Ala Ala Glu Ser Ala Lys Val Ile Thr Asp Ser Thr Arg Lys865 870 875 880Leu Val Asp Glu Val Ser Arg Gly Arg Gly Leu Asn Leu Gly Phe Ile 885 890 895Ser Ala Ile Asn Glu Val Ala Ser Arg Lys Thr His Ile Lys Lys Asp 900 905 910Ser Leu Arg Ser Cys Gly Tyr Lys Leu Val Glu Glu Leu Leu Asn Gln 915 920 925Gly Gly Ser Pro Glu Lys Val Thr Asp Asn Val Trp Leu Thr Ala Phe 930 935 940Gly Gly Ile Gly Val Pro Val Thr Thr Phe Tyr Glu Val Met Glu Tyr945 950 955 960Phe Leu Arg Pro Glu Asn Lys Ser Ile Trp Gly Glu Val Gln Ala Leu 965 970 975Ala Gln Lys Asn Asp Glu Ala Gly Leu His Ala Tyr Val Asn Glu Ala 980 985 990Met Arg Leu Thr Ser Gly Gln Arg Asn Val Arg Ile Ala Thr Val Lys 995 1000 1005Asp Glu Ile Asp Gly Gln Lys Val Glu Pro Gly Asn Ala Val Val 1010 1015 1020Met Leu Leu Gly Ala Ala Gly Arg Asn Pro Lys Glu Val Pro Asn 1025 1030 1035Ala Asp Lys Phe Asp Ala Lys Arg Ser Thr Asp His Ile Lys Pro 1040 1045 1050Phe Ser Tyr Gly Gln His Glu Cys Val Gly Gln Asp Val Ala Arg 1055 1060 1065Ala Phe Val Thr Gly Leu Val Lys Leu Val Ala Asp Leu Arg Gln 1070 1075 1080Leu Arg Pro Ala Pro Gly Glu Met Gly Lys Val Lys Thr Ile Gln 1085 1090 1095Val Gly Thr Glu Arg Ala Tyr Leu Asn Asp Ser Trp Ser Tyr Leu 1100 1105 1110Gly Phe Asp Ala Ser Thr Trp Lys Val His Phe Asp Gly His Gly 1115 1120 1125Gln Gly Thr Tyr Glu Gly Asp Pro Glu Pro Asn Lys Pro Ile Asp 1130 1135 1140Met Gly Arg Tyr Tyr Tyr Ile Leu Gln Lys Arg Lys Glu Ser Leu 1145 1150 1155Leu Lys Gly 1160511251PRTAspergillus niger 51Met Gly Ser Ile Phe Ile Ala Leu Leu Leu Cys Leu Leu Ser Tyr Leu1 5 10 15Tyr Leu Arg Val Phe Ala Asp Asp Leu Thr Arg Pro Leu Gln Ile Leu 20 25 30Ala Lys Phe Phe Ser Ser His Gln His Pro Thr Trp Lys Leu Arg Pro 35 40 45Arg Phe Leu Pro Lys Ala Thr Arg Ala Ala Leu Ser Ser Ile Ala Gly 50 55 60Thr Gly Glu Gly Leu Trp Gln Arg Leu Tyr Ala Arg Thr Phe His Ala65 70 75 80Gln Glu Leu Ala Glu Val Glu Asp Asp Leu Lys Tyr Gln Ala Gly Glu 85 90 95Pro Tyr Gly Asp Pro Asp Val Leu Ala Thr Gly Leu Val Lys Asp Leu 100 105 110Ser Ala Leu Gly Leu Lys Gly Lys Arg Ser Asp Leu Arg Thr Leu Ile 115 120 125Gln Leu Val Lys Ala Lys Gly Lys Pro Ile Asp Asp Arg Gln Met Leu 130 135 140Met Glu Lys Val Ile Ala Ile Val Ser Met Leu Pro Arg Thr Ser Lys145 150 155 160Ser Arg Gln Arg Leu Thr Gly Ile Leu Val Asp Gln Leu Trp Gln Ser 165 170 175Leu Glu His Pro Pro Leu Ser Tyr Phe Gly Asn Lys Tyr Gln Tyr Arg 180 185 190Thr Pro Asp Gly Ser Tyr Asn Asn Pro Leu Glu Pro Asp Leu Gly Lys 195 200 205Ala Gly Ser Pro Tyr Ala Arg Ser Val Pro Arg Leu Lys Ala Leu His 210 215 220Gly Val Gln Pro Asp Pro Gly Leu Leu Phe Asp Leu Leu Met Ala Arg225 230 235 240Asp Asp Thr Thr Phe Arg Glu Asn Pro Ala Gly Ile Ser Ser Val Leu 245 250 255Phe Tyr His Ala Ser Ile Ile Ile His Asp Val Phe Cys Thr Asn Arg 260 265 270Arg Asp Pro Asn Ile Ser Asp Thr Ser Ser Tyr Leu Asp Leu Ala Pro 275 280 285Leu Tyr Gly Ser Ser Tyr Glu Asp Gln Leu Arg Val Arg Thr Met Gln 290 295 300Arg Gly Met Leu Lys Pro Asp Thr Phe His Glu Lys Arg Leu Leu Gly305 310 315 320Gln Pro Pro Gly Val Asn Val Ile Leu Val Met Tyr Asn Arg Phe His 325 330 335Asn Tyr Val Ala Asp Val Leu Leu Lys Ile Asn Glu Asn Gly Arg Phe 340 345 350Thr Leu Pro Pro Thr Thr Ser Glu Asp Ala Lys Arg Lys Ala Leu Ala 355 360 365Lys Gln Asp Glu Asp Leu Phe Gln Val Thr Arg Leu Ile Val Asn Gly 370 375 380Leu Tyr Val Asn Ile Ser Leu His Asp Tyr Leu Arg Gly Leu Thr Asn385 390 395 400Thr His His Ser Ala Ser Asp Trp Thr Leu Asp Pro Arg Val Ala Val 405 410 415Ser Arg Ala Phe Asp Ala Asp Gly Val Pro Arg Gly Val Gly Asn Gln 420 425 430Val Ser Ala Glu Phe Asn Leu Leu Tyr Arg Phe His Ser Val Ile Ser 435 440 445Arg Arg Asp Glu Gln Trp Thr Asn Glu Phe Leu Lys Ser Leu Phe Pro 450 455 460Asp Leu Lys Lys Pro Leu Glu Gln Leu Thr Pro Gln Glu Phe Met Gln465 470 475 480Gly Leu Ile Asn Tyr Glu Arg Ser Ile Asp Lys Asp Pro Ser Lys Arg 485 490 495Glu Phe Gly Gly Leu Lys Arg Asn Gln Asp Gly Arg Phe Asn Asp Ala 500 505 510Glu Leu Val Gln Ile Leu Lys Asp Ser Met Glu Asp Pro Ala Gly Leu 515 520 525Phe Gly Ala Arg Met Val Pro Lys Ala Leu Arg Met Val Glu Ile Ala 530 535 540Gly Ile Leu Thr Ala Arg Lys Trp Asn Leu Ala Ser Leu Asn Glu Met545 550 555 560Arg Asp Phe Phe Lys Leu Lys Arg His Ser Ser Phe Glu Asp Ile Asn 565 570 575Pro Asp Pro Lys Ile Ala Asp Leu Leu Arg Lys Leu Tyr Asp His Pro 580 585 590Asp Met Val Glu Met Tyr Pro Gly Ile Phe Leu Glu Asp Ala Lys Pro 595 600 605Ala Met Asp Pro Gly Cys Gly Gly Cys Pro Pro Tyr Thr Val Gly Arg 610 615 620Ala Val Phe Ser Asp Ala Val Thr Leu Val Arg Ser Asp Arg Phe Leu625 630 635 640Thr Leu Asp Tyr Thr Ala Ser Asn Leu Thr Asn Trp Gly Ile Arg Glu 645 650 655Val Gln Gln Asp Tyr Asp Ile Leu Gly Gly Ser Met Phe His Lys Leu 660 665 670Ile Gln Arg Ala Leu Pro Gly Trp Phe Pro Tyr Asn Ser Leu His Ala 675 680 685Thr Gln Pro Met Phe Thr Arg Lys Met Asn Glu Gln Ile Ala Lys Glu 690 695 700Ile Gly Thr Ile Asp Arg Tyr Ser Gln Glu Asp Pro Lys Pro Pro Pro705 710 715 720Arg Thr Val Met Leu Ala Asn His Ala Thr Ile Ile Glu Val Leu Lys 725 730 735Asp Gln Asp Thr Phe Arg Val Pro Trp Ala Arg Tyr Leu Asn Asp Met 740 745 750Ile Pro Gly Lys Arg Phe Asn Asp Tyr Met Leu Gly Gly Asp Gly Pro 755 760 765Val Asn Ala Ala Gln Lys Lys Leu Val Lys Ser Ile Leu Phe Ser Pro 770 775 780Asp Gln Phe Asn Gln Leu Leu Ser Gln Thr Thr Val Arg Leu Gly Lys785 790 795 800Glu Leu Leu Glu Leu Asn Thr Leu Gln Leu Ser Lys Asp Leu Asn Gln 805 810 815Val Asp Ile Ile Arg Asp Val Ala Ile Pro Leu Asn Ala Arg Ile Met 820 825 830Ala Asp Leu Phe Cys Leu Asp Met Lys Thr Pro Glu Asn Glu Ser Gly 835 840 845Ser Met Asn Ala Ala Thr Val Tyr Lys His Leu Met Asn Val Arg Thr 850 855 860Trp Gly Phe Asn Asn Thr Asp Pro Gly Leu Met Leu Gln Arg Arg Lys865 870 875 880Trp Ala Ser Glu Ser Ala Glu Ala Leu Val Lys Thr Thr Leu Lys Val 885 890 895Val Asn Glu Gln Ala Gln Pro Gln Lys Thr His Met Leu Lys Lys Leu 900 905 910Thr Gly Tyr Gln Arg Ser Glu Val Ser Thr Leu Arg Trp Tyr Gly Asn 915 920 925Asn Val Val Lys Gln Met Met Glu Met Asp Met Thr Ala Ala Glu Thr 930 935 940Ala Glu Val Cys Trp Leu Thr Ala Val Gly Gly Val Gly Ala Pro Val945 950 955 960Gly Leu Val Ala Asp Val Leu Gln Tyr Tyr Leu Arg Pro Glu Asn Ile 965 970 975Asp His Trp Lys Arg Ile Gln Asn Leu Val Ser Gln Pro Asp Asn Ser 980 985 990Gly Ser Ile Asp Lys Leu Leu Arg Gln Tyr Val Leu Glu Ala Gln Arg 995 1000 1005Leu Thr Ser Met Glu Cys Thr Val Arg Val Cys Arg Ala His Arg 1010 1015 1020Thr Ile Asn Asp Gln Glu Phe Lys Pro Gly Asp Val Val Ile Thr 1025 1030 1035Leu Leu Gly Pro Ala Cys Arg Asp Pro Thr Ser Ile Pro Asp Ala 1040 1045 1050Glu Thr Phe Lys Leu Asp Arg Pro Ser Asn Ala Tyr Ile His Phe 1055 1060 1065Gly Tyr Gly Ala His Glu Cys Leu Gly Lys Glu Ile Gly Leu Thr 1070 1075 1080Phe Ala Val Ser Met Leu Arg Val Leu Ala Gly Leu Lys Tyr Leu 1085 1090 1095Arg Pro Ala Pro Gly Asp Met Gly Met Leu Lys Ser Ile Ile Val 1100 1105 1110Asp Gly Arg Arg Val Tyr Leu Asn Asp Ser Trp Ser Trp Met Ile 1115 1120 1125Gln Asp Pro Thr Thr Trp Lys Leu His Phe Ala Gly Tyr Gly Gln 1130 1135 1140Gly Ala Tyr Glu Ala Pro Ala Pro Pro Pro Pro Ala Pro Thr Phe 1145 1150 1155Pro Val Ile Asp Gln Ser Pro Asp Thr Ser Asp Glu Asp Gly Val 1160 1165 1170Asp Asp Thr Ile Tyr Ser Thr Val Pro Thr Lys His His His His 1175 1180 1185Gly Asp Pro Glu Tyr Thr Arg Gln Glu Ser Tyr Thr Met Thr Asp 1190 1195 1200Gly Gly Ile Gly Met Ser Thr Gln Tyr Ser Phe Gly Gln His His 1205 1210 1215His His Gln Tyr His Glu Ile Thr Arg Thr Ser Ser Ser Ser Leu 1220 1225 1230Pro Ser Met Leu Gly Asp Asp Glu Ser Tyr Gly Arg Phe Ser Gly 1235 1240 1245Thr Leu Asn 1250521153PRTMagnaporthe oryzae 52Met Asp Gly Ala Val Arg Leu Asp Trp Thr Gly Leu Asp Leu Thr Gly1 5 10 15His Glu Ile His Asp Gly Val Pro Ile Ala Ser Arg Val Gln Val Met 20 25 30Val Ser Phe Pro Leu Phe Lys Asp Gln His Ile Ile Met Ser Ser Lys 35 40 45Glu Ser Pro Ser Arg Lys Ser Ser Thr Ile Gly Gln Ser Thr Arg Asn 50 55 60Gly Ser Cys Gln Ala Asp Thr Gln Lys Gly Gln Leu Pro Pro Val Gly65 70 75 80Glu Lys Pro Lys Pro Val Lys Glu Asn Pro Met Lys Lys Leu Lys Glu 85 90 95Met Ser Gln Arg Pro Leu Pro Thr Gln His Gly Asp Gly Thr Tyr Pro 100 105 110Thr Glu Lys Lys Leu Thr Gly Ile Gly Glu Asp Leu Lys His Ile Arg 115

120 125Gly Tyr Asp Val Lys Thr Leu Leu Ala Met Val Lys Ser Lys Leu Lys 130 135 140Gly Glu Lys Leu Lys Asp Asp Lys Thr Met Leu Met Glu Arg Val Met145 150 155 160Gln Leu Val Ala Arg Leu Pro Thr Glu Ser Lys Lys Arg Ala Glu Leu 165 170 175Thr Asp Ser Leu Ile Asn Glu Leu Trp Glu Ser Leu Asp His Pro Pro 180 185 190Leu Asn Tyr Leu Gly Pro Glu His Ser Tyr Arg Thr Pro Asp Gly Ser 195 200 205Tyr Asn His Pro Phe Asn Pro Gln Leu Gly Ala Ala Gly Ser Arg Tyr 210 215 220Ala Arg Ser Val Ile Pro Thr Val Thr Pro Pro Gly Ala Leu Pro Asp225 230 235 240Pro Gly Leu Ile Phe Asp Ser Ile Met Gly Arg Thr Pro Asn Ser Tyr 245 250 255Arg Lys His Pro Asn Asn Val Ser Ser Ile Leu Trp Tyr Trp Ala Thr 260 265 270Ile Ile Ile His Asp Ile Phe Trp Thr Asp Pro Arg Asp Ile Asn Thr 275 280 285Asn Lys Ser Ser Ser Tyr Leu Asp Leu Ala Pro Leu Tyr Gly Asn Ser 290 295 300Gln Glu Met Gln Asp Ser Ile Arg Thr Phe Lys Asp Gly Arg Met Lys305 310 315 320Pro Asp Cys Tyr Ala Asp Lys Arg Leu Ala Gly Met Pro Pro Gly Val 325 330 335Ser Val Leu Leu Ile Met Phe Asn Arg Phe His Asn His Val Ala Glu 340 345 350Asn Leu Ala Leu Ile Asn Glu Gly Gly Arg Phe Asn Lys Pro Ser Asp 355 360 365Leu Leu Glu Gly Glu Ala Arg Glu Ala Ala Trp Lys Lys Tyr Asp Asn 370 375 380Asp Leu Phe Gln Val Ala Arg Leu Val Thr Ser Gly Leu Tyr Ile Asn385 390 395 400Ile Thr Leu Val Asp Tyr Val Arg Asn Ile Val Asn Leu Asn Arg Val 405 410 415Asp Thr Thr Trp Thr Leu Asp Pro Arg Gln Asp Ala Gly Ala His Val 420 425 430Gly Thr Ala Asp Gly Ala Glu Arg Gly Thr Gly Asn Ala Val Ser Ala 435 440 445Glu Phe Asn Leu Cys Tyr Arg Trp His Ser Cys Ile Ser Glu Lys Asp 450 455 460Ser Lys Phe Val Glu Ala Gln Phe Gln Asn Ile Phe Gly Lys Pro Ala465 470 475 480Ser Glu Val Arg Pro Asp Glu Met Trp Lys Gly Phe Ala Lys Met Glu 485 490 495Gln Asn Thr Pro Ala Asp Pro Gly Gln Arg Thr Phe Gly Gly Phe Lys 500 505 510Arg Gly Pro Asp Gly Lys Phe Asp Asp Asp Asp Leu Val Arg Cys Ile 515 520 525Ser Glu Ala Val Glu Asp Val Ala Gly Ala Phe Gly Ala Arg Asn Val 530 535 540Pro Gln Ala Met Lys Val Val Glu Thr Met Gly Ile Ile Gln Gly Arg545 550 555 560Lys Trp Asn Val Ala Gly Leu Asn Glu Phe Arg Lys His Phe His Leu 565 570 575Lys Pro Tyr Ser Thr Phe Glu Asp Ile Asn Ser Asp Pro Gly Val Ala 580 585 590Glu Ala Leu Arg Arg Leu Tyr Asp His Pro Asp Asn Val Glu Leu Tyr 595 600 605Pro Gly Leu Val Ala Glu Glu Asp Lys Gln Pro Met Val Pro Gly Val 610 615 620Gly Ile Ala Pro Thr Tyr Thr Ile Ser Arg Val Val Leu Ser Asp Ala625 630 635 640Val Cys Leu Val Arg Gly Asp Arg Phe Tyr Thr Thr Asp Phe Thr Pro 645 650 655Arg Asn Leu Thr Asn Trp Gly Tyr Lys Glu Val Asp Tyr Asp Leu Ser 660 665 670Val Asn His Gly Cys Val Phe Tyr Lys Leu Phe Ile Arg Ala Phe Pro 675 680 685Asn His Phe Lys Gln Asn Ser Val Tyr Ala His Tyr Pro Met Val Val 690 695 700Pro Ser Glu Asn Lys Arg Ile Leu Glu Ala Leu Gly Arg Ala Asp Leu705 710 715 720Phe Asp Phe Glu Ala Pro Lys Tyr Ile Pro Pro Arg Val Asn Ile Thr 725 730 735Ser Tyr Gly Gly Ala Glu Tyr Ile Leu Glu Thr Gln Glu Lys Tyr Lys 740 745 750Val Thr Trp His Glu Gly Leu Gly Phe Leu Met Gly Glu Gly Gly Leu 755 760 765Lys Phe Met Leu Ser Gly Asp Asp Pro Leu His Ala Gln Gln Arg Lys 770 775 780Cys Met Ala Ala Gln Leu Tyr Lys Asp Gly Trp Thr Glu Ala Val Lys785 790 795 800Ala Phe Tyr Ala Gly Met Met Glu Glu Leu Leu Val Ser Lys Ser Tyr 805 810 815Phe Leu Gly Asn Asn Lys His Arg His Val Asp Ile Ile Arg Asp Val 820 825 830Gly Asn Met Val His Val His Phe Ala Ser Gln Val Phe Gly Leu Pro 835 840 845Leu Lys Thr Ala Lys Asn Pro Thr Gly Val Phe Thr Glu Gln Glu Met 850 855 860Tyr Gly Ile Leu Ala Ala Ile Phe Thr Thr Ile Phe Phe Asp Leu Asp865 870 875 880Pro Ser Lys Ser Phe Pro Leu Arg Thr Lys Thr Arg Glu Val Cys Gln 885 890 895Lys Leu Ala Lys Leu Val Glu Ala Asn Val Lys Leu Ile Asn Lys Ile 900 905 910Pro Trp Ser Arg Gly Met Phe Val Gly Lys Pro Ala Lys Asp Glu Pro 915 920 925Leu Ser Ile Tyr Gly Lys Thr Met Ile Lys Gly Leu Lys Ala His Gly 930 935 940Leu Ser Asp Tyr Asp Ile Ala Trp Ser His Val Val Pro Thr Ser Gly945 950 955 960Ala Met Val Pro Asn Gln Ala Gln Val Phe Ala Gln Ala Val Asp Tyr 965 970 975Tyr Leu Ser Pro Ala Gly Met His Tyr Ile Pro Glu Ile His Met Val 980 985 990Ala Leu Gln Pro Ser Thr Pro Glu Thr Asp Ala Leu Leu Leu Gly Tyr 995 1000 1005Ala Met Glu Gly Ile Arg Leu Ala Gly Thr Phe Gly Ser Tyr Arg 1010 1015 1020Glu Ala Ala Val Asp Asp Val Val Lys Glu Asp Asn Gly Arg Gln 1025 1030 1035Val Pro Val Lys Ala Gly Asp Arg Val Phe Val Ser Phe Val Asp 1040 1045 1050Ala Ala Arg Asp Pro Lys His Phe Pro Asp Pro Glu Val Val Asn 1055 1060 1065Pro Arg Arg Pro Ala Lys Lys Tyr Ile His Tyr Gly Val Gly Pro 1070 1075 1080His Ala Cys Leu Gly Arg Asp Ala Ser Gln Ile Ala Ile Thr Glu 1085 1090 1095Met Phe Arg Cys Leu Phe Arg Arg Arg Asn Val Arg Arg Val Pro 1100 1105 1110Gly Pro Gln Gly Glu Leu Lys Lys Val Pro Arg Pro Gly Gly Phe 1115 1120 1125Tyr Val Tyr Met Arg Glu Asp Trp Gly Gly Leu Phe Pro Phe Pro 1130 1135 1140Val Thr Met Arg Val Met Trp Asp Asp Glu 1145 1150531161PRTGlomerella cingulate 53Met Ala Phe Asn Thr Lys Phe Gln Ala Gly Glu Ser Tyr Gly Asp Glu1 5 10 15Arg Lys Gly Ser Asn Asn Phe Phe Ala Asp Pro Lys Lys Val Ala Met 20 25 30Asp Ile Ile Lys Asp Leu Gly Gly Ala His Gly Gln Leu Asn Leu Leu 35 40 45Glu Val Thr Ala Leu Val Gln Gln Leu Leu Gln Lys Gly Glu Pro Leu 50 55 60Asp Asp Lys Lys Gly Thr Thr Glu Ala Leu Ile Gly Ile Leu Thr Ser65 70 75 80Leu Pro Ser Gly Ser Asn Thr Arg Val Gln Leu Thr Asn Lys Leu Ile 85 90 95Asp Thr Leu Trp Gly Asn Leu Gln His Pro Pro Leu Ser Tyr Val Gly 100 105 110Gly Asp Val Lys Tyr Glu Val Val Lys Thr Lys Glu Gln Leu Ala Lys 115 120 125Glu Gln Ala Asp Leu Ala Ala Gln Gly Lys Ala Pro Gln Ser Pro Glu 130 135 140Glu Ser His Ile Thr Phe Lys Ala Pro Asp Phe Pro Asp Ile Thr Leu145 150 155 160Arg Glu His Leu Pro Thr Pro Pro Asp Asn Tyr Lys Met Pro Asp Gly 165 170 175Ser Tyr Asn Asn Ile Leu Glu Pro Asn Leu Gly Ala Ala Gly Thr Pro 180 185 190Tyr Ala Lys Thr Val Lys Thr Glu Lys Arg Leu Ala Gly Val Lys Pro 195 200 205Asp Pro Gly Leu Leu Phe Asp Leu Leu Leu Ala Arg Asp Asp Lys Lys 210 215 220Phe Thr Glu Asn Pro Ala Gly Ile Ser Ser Met Leu Phe Tyr His Ala225 230 235 240Ser Ile Ile Ile His Asp Ile Phe Arg Thr Asn Arg His Asp Leu Asn 245 250 255Lys Ser Asp Thr Ser Ser Tyr Leu Asp Leu Ala Pro Leu Tyr Gly Ser 260 265 270Ser Phe Lys Asp Gln Leu Glu Ile Arg Thr Met Lys Glu Gly Lys Leu 275 280 285Lys Pro Asp Thr Phe His Glu Lys Arg Leu Leu Gly Gln Pro Ala Gly 290 295 300Val Asn Val Met Leu Val Leu Ser Ser Arg Phe His Asn Tyr Val Ala305 310 315 320Asp Ile Leu Leu Lys Ile Asn Glu Asn Gly Arg Phe Thr Leu Gln Thr 325 330 335Ala Lys Asp Ala Ala Pro Glu Asp Gln Ala Lys Ala Val Ala Lys Gln 340 345 350Asp His Asp Leu Phe Asn Val Ala Arg Leu Val Thr Gly Gly Leu Tyr 355 360 365Ile Asn Ile Cys Leu His Asp Tyr Leu Arg Ala Ile Thr Asn Thr His 370 375 380His Ser Lys Ser Asp Trp Thr Leu Asp Pro Arg Val Glu Ile Gly Lys385 390 395 400Gln Phe Asp Gly Glu Gly Val Pro Arg Gly Val Gly Asn Gln Val Ser 405 410 415Val Glu Phe Asn Leu Leu Tyr Arg Phe His Ser Cys Ile Ser Lys Lys 420 425 430Asp Glu Arg Trp Ile Asp Gly Phe Phe Ala Lys Leu Phe Pro Gly Arg 435 440 445Lys Pro Glu Asp Leu Gln Asn Val Gly Met Glu Glu Leu Gly Ala Ala 450 455 460Leu Met Lys Phe Glu Met Gly Ile Asp Lys Asp Pro Ser Lys Arg Thr465 470 475 480Phe Asp Asp Leu Gln Arg Gly Glu Asp Gly Lys Phe Arg Asp Glu Asp 485 490 495Leu Val Arg Val Leu Lys Glu Ala Met Glu Asp Pro Ala Gly Thr Phe 500 505 510Gly Ala Arg Met Val Pro Lys Ala Leu Lys Ile Val Glu Ile Met Gly 515 520 525Ile Lys Gln Ala Arg Ala Trp Gln Val Ala Ser Leu Asn Glu Phe Arg 530 535 540Asp Phe Phe Gly Leu Lys Arg His Asp Thr Phe Lys Asp Ile Asn Ser545 550 555 560Asn Glu Glu Ile Ala Thr Leu Leu Glu Lys Leu Tyr Thr Asp Pro Asp 565 570 575Met Val Glu Leu Tyr Pro Gly Leu Met Ile Glu Asp Ile Lys Pro Val 580 585 590Arg Asn Thr Gly Ser Gly Ile Cys Pro Thr Tyr Ser Val Gly Arg Ala 595 600 605Val Leu Ser Asp Ala Val Thr Leu Val Arg Ser Asp Arg Phe Asn Thr 610 615 620Ile Asp Tyr Thr Val Ser Asn Leu Thr Ala Trp Gly Tyr Asn Glu Val625 630 635 640Gln Gln Asp Tyr Lys Thr Leu Gly Gly Ser Met Leu Tyr Lys Leu Ile 645 650 655Gln Arg Gly Leu Pro Gly Trp Phe Pro Phe Asn Ser Ile Ala Val Met 660 665 670Gln Pro Met Tyr Thr Lys Lys Ala Asn Glu Arg Ile Ala Arg Glu Ile 675 680 685Gly Thr Phe Asn Gln Phe Thr Leu Asp Asp Pro Lys Ala Pro Pro Lys 690 695 700Pro Val Val Val Ala Ser Ser Glu Gly Ile Lys Arg Val Leu Gly Ser705 710 715 720Pro Asp Lys Phe Val Val Pro Trp Leu Thr Pro Leu Asn Ala Leu Tyr 725 730 735Thr Asp Thr Lys Lys Asp Ile Ser Trp Phe Met Leu Ala Gly Asp Gly 740 745 750Ser Thr Asn Lys Gln Glu Lys Val Asn Phe Val Asn Ala Met Lys Lys 755 760 765Val Pro Asn Leu His Asn Ala Val His Gln Phe Ile Glu Arg Val Gly 770 775 780Arg Gln Leu Ile Glu Lys Glu Thr Phe Lys Leu Lys Glu Gly Leu Cys785 790 795 800Gln Met Asp Ile Ile Arg Asp Val Ala Ile Pro Leu Asn Ala Gln Leu 805 810 815Leu Ala Asp Leu Phe Tyr Phe Asp Leu Arg His Glu Glu Asn Pro Gly 820 825 830Gly Thr Leu Ser Ala Thr Asp Leu Tyr Arg His Leu Leu Asn Ile Arg 835 840 845Ile Trp Gly Val Asn Asn Asn Asp Pro Gly Gln Ala Trp Asn Arg Arg 850 855 860Arg Arg Ala Ala Glu Ser Ala Lys Val Ile Thr Asp Ser Thr Arg Lys865 870 875 880Leu Val Asp Glu Val Ser Arg Gly Arg Gly Leu Asn Leu Gly Phe Ile 885 890 895Ser Ala Ile Asn Glu Val Ala Ser Arg Lys Thr His Ile Lys Lys Asp 900 905 910Ser Leu Arg Ser Cys Gly Tyr Lys Leu Val Glu Glu Leu Leu Asn Gln 915 920 925Gly Gly Ser Pro Glu Lys Val Thr Asp Asn Val Trp Leu Thr Ala Phe 930 935 940Gly Gly Ile Gly Val Pro Val Thr Thr Phe Tyr Glu Val Met Glu Tyr945 950 955 960Phe Leu Arg Pro Glu Asn Lys Ser Ile Trp Gly Glu Val Gln Ala Leu 965 970 975Ala Gln Lys Asn Asp Glu Ala Gly Leu His Ala Tyr Val Asn Glu Ala 980 985 990Met Arg Leu Thr Ser Gly Gln Arg Asn Val Arg Ile Ala Thr Val Lys 995 1000 1005Asp Glu Ile Asp Gly Gln Lys Val Glu Pro Gly Asn Ala Val Val 1010 1015 1020Met Leu Leu Gly Ala Ala Gly Arg Asn Pro Lys Glu Val Pro Asn 1025 1030 1035Ala Asp Lys Phe Asp Ala Lys Arg Ser Thr Asp His Ile Lys Pro 1040 1045 1050Phe Ser Tyr Gly Gln His Glu Cys Val Gly Gln Asp Val Ala Arg 1055 1060 1065Ala Phe Val Thr Gly Leu Val Lys Leu Val Ala Asp Leu Arg Gln 1070 1075 1080Leu Arg Pro Ala Pro Gly Glu Met Gly Lys Val Lys Thr Ile Gln 1085 1090 1095Val Gly Thr Glu Arg Ala Tyr Leu Asn Asp Ser Trp Ser Tyr Leu 1100 1105 1110Gly Phe Asp Ala Ser Thr Trp Lys Val His Phe Asp Gly His Gly 1115 1120 1125Gln Gly Thr Tyr Glu Gly Asp Pro Glu Pro Asn Lys Pro Ile Asp 1130 1135 1140Met Gly Arg Tyr Tyr Tyr Ile Leu Gln Lys Arg Lys Glu Ser Leu 1145 1150 1155Leu Lys Gly 1160541283PRTFusarium oxysporum 54Met Ala Glu His Lys Asn Gly Val Ala Thr Asn Gly Tyr Glu Lys Lys1 5 10 15Ser Ser Pro Ala Ser Ser Ser Thr Lys Ser Glu Ala Lys Pro Leu Pro 20 25 30Asn Gly Asp Lys Lys Asp Gly Ile Val Lys Ser Phe Lys Gln Leu Arg 35 40 45Val Ala Ser Lys Arg Pro Leu Pro Lys Glu Met Gly Asp Gly Ser Tyr 50 55 60Arg Val Val Glu Asn Arg Pro Gly Leu Lys Gln Asp Ile Arg Arg Leu65 70 75 80Arg Gly Arg Asp Leu Lys Thr Leu Leu Glu Ile Val Lys Ala Lys Val 85 90 95Lys Gly Glu Thr Gln Gln Asp Asp Lys Thr Met Ile Met Glu Arg Thr 100 105 110Ile Gln Leu Val Ala Asn Leu Ser Asp His Ser Lys Val Gln Glu Ser 115 120 125Leu Thr Asn Ser Phe Ile Ser Gln Leu Trp Asn Ser Ile Asp His Pro 130 135 140Pro Met Leu Tyr Met Gly Asp Lys Phe Arg Phe Arg Gln Pro Asp Gly145 150 155 160Ser Asn Asn Asn Pro Tyr Leu Pro Gln Leu Gly Ala Ala Arg Thr Pro 165 170 175Tyr Ser Arg Thr Val Arg Pro Lys Gly Met Ser Leu Gly Ala Gln Pro 180 185 190Asp Pro Glu Ala Ile Phe Glu Ser Val Phe Ala Arg Asp Ala Phe Arg 195 200 205Lys Asn Pro Asn Asn Val Ser Ser Ile Leu Trp Tyr Trp Ala Thr Ile 210 215 220Ile Ile His Asp Leu Phe Trp Thr Asn Leu Gln Asp Pro Asn Gln Asn225 230 235 240Asp Ser Ser Ser Tyr Leu Asp Leu Ala Pro Leu Tyr Gly Ser Thr Glu 245 250 255Lys Asp Arg Asp Ser Ile Arg Thr Phe Lys Asp Gly Gln Leu Lys Pro 260 265

270Asp Cys Phe Ala Asp Lys Arg Leu Ile Gly Asn Pro Pro Gly Val Pro 275 280 285Ile Leu Leu Ile Met Phe Asn Arg Phe His Asn His Val Ala Thr Asn 290 295 300Leu Ala Asp Ile Asn Glu Gly Gly Arg Phe Ser Lys Pro Ala Glu His305 310 315 320Leu Ser Pro Glu Ala Ala Asp Ala Ala Trp Lys Lys Arg Asp Thr Glu 325 330 335Leu Phe Glu Thr Ala Arg Leu Val Thr Ser Gly Leu Tyr Ile Asn Ile 340 345 350Thr Leu Ile Asp Tyr Val Arg Asn Ile Ile Asn Leu Asn Arg Val Asp 355 360 365Thr Thr Trp Thr Leu Asp Pro Arg Gln Glu Met Gly Val Ser Val Gly 370 375 380Thr Lys Asp Leu Ser Glu Ser Gly Thr Gly Asn Val Val Ser Ala Glu385 390 395 400Phe Asn Leu Cys Tyr Arg Trp His Ser Cys Leu Ser Glu Met Asp Asp 405 410 415Lys Trp Val Gln Asp Phe Tyr Thr Glu Leu Leu Gly Glu Asn Tyr Gly 420 425 430Pro Met Asn Leu Gln Thr Met Met Lys Ala Leu Lys Ala Phe Glu Ala 435 440 445Ser Val Ala Asp Glu Pro Ser Glu Arg Thr Phe Gly Gly Phe Lys Arg 450 455 460Gly Pro Asp Gly Lys Phe Asn Asp Asp Glu Leu Val Glu Ala Leu Ala465 470 475 480Thr Ala Ile Glu Gln Pro Gly Gly Ala Phe Gly Gly Arg Asn Val Pro 485 490 495Arg Ile Met Lys Pro Ile Glu Met Leu Gly Ile Met Arg Gly Arg Lys 500 505 510Trp Asn Leu Ala Gly Leu Asn Glu Phe Arg Lys His Phe Gly Leu Lys 515 520 525Ala Tyr Glu Thr Phe Glu Asp Ile Asn Ser Asp Pro Ser Val Ala Asp 530 535 540Ala Leu Arg Asn Leu Tyr Gln His Pro Asp Tyr Val Glu Leu Tyr Pro545 550 555 560Gly Ile Val Ala Glu Glu Ala Lys Thr Pro Met Val Pro Gly Val Gly 565 570 575Ile Ala Pro Thr Tyr Thr Ile Ser Arg Val Val Leu Ser Asp Ala Val 580 585 590Ala Leu Val Arg Gly Asp Arg Tyr Tyr Thr Thr Asp Tyr Asn Pro Arg 595 600 605His Leu Thr Asn Trp Gly Tyr Lys Glu Val Asp Tyr Asp Leu Lys Val 610 615 620Asn His Gly Cys Val Phe Tyr Lys Leu Phe Leu Arg Ala Phe Pro Gln625 630 635 640His Phe Lys Gly Asn Ser Val Tyr Ala His Tyr Pro Met Val Ile Pro 645 650 655Ser Glu Asn Lys Lys Ile Leu Thr Asn Ile Lys Arg Ala Asp Arg Phe 660 665 670Asp Phe Ser Arg Pro Glu Pro Thr Ala Thr Arg Ile Asn Ile Ile Gly 675 680 685Tyr Asn Ala Ala Lys Tyr Ile Leu Glu Asp Gln Gln Lys Tyr Arg Val 690 695 700Cys Trp Glu Glu Gly Leu Lys His Leu Met Gly Glu Ala Gly Gly Arg705 710 715 720Phe Met Leu Ser Gly Asp Thr Ala Leu His Ala Gln Gln Arg Lys Cys 725 730 735Met Gly Lys Leu Leu Tyr Asn Asp Thr Trp Arg Asn Ala Val Lys Ser 740 745 750Phe Tyr Ala Thr Thr Ala Glu Lys Leu Leu Ala Glu Lys Ser Tyr Arg 755 760 765Leu Ala Gly Lys Met Gln Val Asp Val Val Arg Asp Val Gly Asn Val 770 775 780Ala His Thr His Phe Val Ala Arg Met Phe Asn Leu Pro Leu Lys Thr785 790 795 800Ser Glu Asn Pro Lys Gly Val Phe Ser Glu Gln Glu Leu Tyr Met Ile 805 810 815Leu Ala Val Ile Phe Val Cys Ile Phe Phe Asp Ile Asp Pro Ala Lys 820 825 830Ser Phe Pro Leu Arg Gln Gly Ala Arg Glu Val Ala Gln Lys Leu Gly 835 840 845Gly Ile Ile Glu Met Asn Val Lys Leu Ala Asn Ser Ile Gly Val Lys 850 855 860Gly Leu Phe Thr Ser Lys Pro Asp Lys Asn Asp Asp Pro Leu Ala Arg865 870 875 880Tyr Gly Glu Asn Met Ala Lys Gly Leu Lys Lys Ala Gly Leu Ser Thr 885 890 895Glu Asp Ile Val Trp Ser Gln Ile Leu Pro Thr Ala Gly Ala Met Val 900 905 910Pro Asn Gln Ala Gln Val Phe Ala Gln Thr Leu Asp Trp Tyr Leu Ser 915 920 925Pro Ala Gly Glu Lys Tyr Arg Pro Glu Leu Ala Arg Ile Ala Ala Leu 930 935 940Glu Thr Gly Asp Glu Thr Asp Ala Leu Leu Leu Gly Tyr Ala Met Glu945 950 955 960Gly Ile Arg Met Ala Gly Thr Phe Gly Leu Tyr Arg Glu Ala Thr Gly 965 970 975Pro Asp Thr Ile His Glu Asp Asp Gly Arg Ser Ile Pro Val Asn Ala 980 985 990Gly Asp Arg Val Phe Val Ser Phe Val Gln Ala Ala Gln Asp Pro Lys 995 1000 1005Ile Phe Pro Asn Pro Gly Val Val Asp Pro Lys Arg Pro Leu Asp 1010 1015 1020Lys Tyr Ile His Tyr Gly Val Gly Pro His Ala Cys Leu Gly Arg 1025 1030 1035Asp Ile Ser Gln Val Ala Leu Thr Glu Leu Phe Arg Ala Val Phe 1040 1045 1050Arg Lys Lys Gly Val Arg Arg Val Pro Gly Ala Gln Gly Glu Leu 1055 1060 1065Lys Lys Val Pro Arg Pro Gly Gly Phe Phe Val Tyr Met Thr Glu 1070 1075 1080Asp Trp Gly Ser Ile Trp Pro Phe Pro Thr Ser Met Lys Ile Thr 1085 1090 1095Trp Asp Asp Gly Cys Gly Thr Asp Leu Phe Thr Leu Leu Phe Trp 1100 1105 1110Cys Arg Ser Val Pro Trp Trp Asp Leu Leu Pro Glu Thr Thr Gln 1115 1120 1125Ala Ala Pro Phe Ile Ile Ser Ser Phe Gln Ser Gln Gln Ile Tyr 1130 1135 1140Ser Pro Ala Glu Ile Ala Ala Val Leu Ala Leu Met Ala Phe Glu 1145 1150 1155Ser Gly Asp Phe Gln Tyr Lys Arg Asn His Tyr Pro Gly Arg Pro 1160 1165 1170Gly Gln Gly Thr Ala Asn Met Gln Met Pro Asn Tyr Asn Leu Leu 1175 1180 1185Tyr Ala Lys Ser Ile Pro Glu Leu Ala Lys Gly Trp Gln Gly Ile 1190 1195 1200Glu Ser Val Glu Gly Leu Ser Asp Gln Glu Leu Gly Asp Leu Leu 1205 1210 1215Asp Asp Val Thr Val Asp Lys Tyr Asn Phe Gly Ser Gly Pro Trp 1220 1225 1230Phe Leu Lys Thr Gln Cys Lys Glu Asp Val Arg Gln Ala Phe Lys 1235 1240 1245Thr Asp Val Asp Thr Gly Phe Gln Lys Tyr Ile Glu Glu Cys Val 1250 1255 1260Gly Thr Asp Leu Gln Pro Arg Leu Glu Tyr Phe Gln Arg Ala Lys 1265 1270 1275Thr Ala Phe Gly Leu 1280551890DNAArtificial SequenceCodon optimized artificial DNA sequence 55aagcttggat ccggctcttc tggtagtgga gaaaacctgt attttcaggg cgacgatagc 60ggtgttgacc tggatcaggg ctggaaccag acccaaaaga ccgcgtggct ggaggcgggt 120caaggtagcc gtatgctgcc gctggcgtgg ctggttgcgc tggaacagcg tgcgagcgag 180gaaccgctga tgagcgacgc gctgatccgt caatacggtt atgtgccgca caccctgggt 240ggcagcagcg ttaaagtggt tcagggctat gcggtggacc gtagcgacga tagcgatctg 300acctttacca agctgcgttg gaaagcgctg caaggtagcc gtgagccgtg ggttggtccg 360acctgcagca tgtgccacac cagccacatt agctaccagg gtacccaact gaccgtgtat 420ggtggccaga ccatgggtga cctggcgggt ttccagctgg agattctggg tgcgctgcaa 480agcacccgtg cggataccgc gaagttcgaa cgttttgcgc gtaaagttct gggtgcggac 540ggcctggtta gcggttacaa cgatgcgaac aaagcgcgtc tgcaggcggc gctggatgcg 600accattgttc gtctgcgtga tggtagccac ttcaacctgc cgcatgaccc ggagtttggt 660ccgggccgtc tggatgcgat cggtagcatt tttaacagcg ttggctacga gctgcacgcg 720gacgaacaaa tctatggtgc ggaagatgcg ccggttagct acccgttcct gtggaacgtt 780ccgcagctgg accgtgtgca atggaccggt tttaacccga accacatcaa cgtggttgac 840attgataacc gtaagtttga tgtgggtgcg ctggcgcgta acgcgggcga ggcggttggc 900gtgtttgcgg atgttaaagt gctgagcccg atccagagcg cgctgcacat tggttatccg 960agcagcatca aggttgacaa cctgatccgt attgaggatc agttcggcca actgaaaccg 1020ccggcgtggc cgaaccagct gtttggtgcg ccggaaccga cccgtgtggc ggagggtcgt 1080gaactgtacc gtcaacattg cagcagctgc cacaccccgc tggaccgtaa cgatctgcgt 1140accccggtta aaaccgtgct gacccacctg caggcgcgtg gtgaagttgc gccgattggt 1200accgacccgt ggaccgcgtg caacagcatc gcgcaactga agaccggtta cgttcgtggc 1260aaaccgtatc tgagcttcgt gggtaccggc cagcgtggtt tttacggcaa acaagcgtat 1320gcggttgatg tgctgcagga agtggttgtt caggcgctgg cggcgcgtgg tctgagcgtt 1380gcgctgggtg cgttccagac cgcggcgctg ggtatttttg atggtcaact gccgccgctg 1440attagcccgg ttccggatag cccggatgcg gatagcgtgg aagcgaccgc ggcggatgcg 1500ccgggtgcgc tgctgctggc ggagaacgtg gcggcggaca gcgataaggc gcgtcgtctg 1560gaacagtgcc tggcgatgac cagcgatctg atggcgtaca aagcgcgtcc gctgaacggt 1620atttgggcga gcccgccgta tctgcacaac ggcagcgttg cgaccctgta tgacctgctg 1680ctgccgccgg atctgcgtcc gcgtaccttc tataccggta gcgtggaatt tgacccggtt 1740aacgtgggct acatcaccga tgcgggtggc gcgaaccgtt tcctgtttga cagcggcaag 1800ccgggtaacg cgaacggtgg ccacgattat ggtaacgcgc agttcaacga gcagcaacgt 1860cgtgcgctgg ttgagtacat gaaaaccctg 1890561017PRTPseudomonas aeruginosa 56Met Gly Ser Ser His His His His His His Gly Thr Lys Thr Glu Glu1 5 10 15Gly Lys Leu Val Ile Trp Ile Asn Gly Asp Lys Gly Tyr Asn Gly Leu 20 25 30Ala Glu Val Gly Lys Lys Phe Glu Lys Asp Thr Gly Ile Lys Val Thr 35 40 45Val Glu His Pro Asp Lys Leu Glu Glu Lys Phe Pro Gln Val Ala Ala 50 55 60Thr Gly Asp Gly Pro Asp Ile Ile Phe Trp Ala His Asp Arg Phe Gly65 70 75 80Gly Tyr Ala Gln Ser Gly Leu Leu Ala Glu Ile Thr Pro Asp Lys Ala 85 90 95Phe Gln Asp Lys Leu Tyr Pro Phe Thr Trp Asp Ala Val Arg Tyr Asn 100 105 110Gly Lys Leu Ile Ala Tyr Pro Ile Ala Val Glu Ala Leu Ser Leu Ile 115 120 125Tyr Asn Lys Asp Leu Leu Pro Asn Pro Pro Lys Thr Trp Glu Glu Ile 130 135 140Pro Ala Leu Asp Lys Glu Leu Lys Ala Lys Gly Lys Ser Ala Leu Met145 150 155 160Phe Asn Leu Gln Glu Pro Tyr Phe Thr Trp Pro Leu Ile Ala Ala Asp 165 170 175Gly Gly Tyr Ala Phe Lys Tyr Glu Asn Gly Lys Tyr Asp Ile Lys Asp 180 185 190Val Gly Val Asp Asn Ala Gly Ala Lys Ala Gly Leu Thr Phe Leu Val 195 200 205Asp Leu Ile Lys Asn Lys His Met Asn Ala Asp Thr Asp Tyr Ser Ile 210 215 220Ala Glu Ala Ala Phe Asn Lys Gly Glu Thr Ala Met Thr Ile Asn Gly225 230 235 240Pro Trp Ala Trp Ser Asn Ile Asp Thr Ser Lys Val Asn Tyr Gly Val 245 250 255Thr Val Leu Pro Thr Phe Lys Gly Gln Pro Ser Lys Pro Phe Val Gly 260 265 270Val Leu Ser Ala Gly Ile Asn Ala Ala Ser Pro Asn Lys Glu Leu Ala 275 280 285Lys Glu Phe Leu Glu Asn Tyr Leu Leu Thr Asp Glu Gly Leu Glu Ala 290 295 300Val Asn Lys Asp Lys Pro Leu Gly Ala Val Ala Leu Lys Ser Tyr Glu305 310 315 320Glu Glu Leu Ala Lys Asp Pro Arg Ile Ala Ala Thr Met Glu Asn Ala 325 330 335Gln Lys Gly Glu Ile Met Pro Asn Ile Pro Gln Met Ser Ala Phe Trp 340 345 350Tyr Ala Val Arg Thr Ala Val Ile Asn Ala Ala Ser Gly Arg Gln Thr 355 360 365Val Asp Glu Ala Leu Lys Asp Ala Gln Thr Gly Thr Asp Tyr Asp Ile 370 375 380Pro Thr Thr Lys Leu Gly Ser Gly Ser Ser Gly Ser Gly Glu Asn Leu385 390 395 400Tyr Phe Gln Gly Asp Asp Ser Gly Val Asp Leu Asp Gln Gly Trp Asn 405 410 415Gln Thr Gln Lys Thr Ala Trp Leu Glu Ala Gly Gln Gly Ser Arg Met 420 425 430Leu Pro Leu Ala Trp Leu Val Ala Leu Glu Gln Arg Ala Ser Glu Glu 435 440 445Pro Leu Met Ser Asp Ala Leu Ile Arg Gln Tyr Gly Tyr Val Pro His 450 455 460Thr Leu Gly Gly Ser Ser Val Lys Val Val Gln Gly Tyr Ala Val Asp465 470 475 480Arg Ser Asp Asp Ser Asp Leu Thr Phe Thr Lys Leu Arg Trp Lys Ala 485 490 495Leu Gln Gly Ser Arg Glu Pro Trp Val Gly Pro Thr Cys Ser Met Cys 500 505 510His Thr Ser His Ile Ser Tyr Gln Gly Thr Gln Leu Thr Val Tyr Gly 515 520 525Gly Gln Thr Met Gly Asp Leu Ala Gly Phe Gln Leu Glu Ile Leu Gly 530 535 540Ala Leu Gln Ser Thr Arg Ala Asp Thr Ala Lys Phe Glu Arg Phe Ala545 550 555 560Arg Lys Val Leu Gly Ala Asp Gly Leu Val Ser Gly Tyr Asn Asp Ala 565 570 575Asn Lys Ala Arg Leu Gln Ala Ala Leu Asp Ala Thr Ile Val Arg Leu 580 585 590Arg Asp Gly Ser His Phe Asn Leu Pro His Asp Pro Glu Phe Gly Pro 595 600 605Gly Arg Leu Asp Ala Ile Gly Ser Ile Phe Asn Ser Val Gly Tyr Glu 610 615 620Leu His Ala Asp Glu Gln Ile Tyr Gly Ala Glu Asp Ala Pro Val Ser625 630 635 640Tyr Pro Phe Leu Trp Asn Val Pro Gln Leu Asp Arg Val Gln Trp Thr 645 650 655Gly Phe Asn Pro Asn His Ile Asn Val Val Asp Ile Asp Asn Arg Lys 660 665 670Phe Asp Val Gly Ala Leu Ala Arg Asn Ala Gly Glu Ala Val Gly Val 675 680 685Phe Ala Asp Val Lys Val Leu Ser Pro Ile Gln Ser Ala Leu His Ile 690 695 700Gly Tyr Pro Ser Ser Ile Lys Val Asp Asn Leu Ile Arg Ile Glu Asp705 710 715 720Gln Phe Gly Gln Leu Lys Pro Pro Ala Trp Pro Asn Gln Leu Phe Gly 725 730 735Ala Pro Glu Pro Thr Arg Val Ala Glu Gly Arg Glu Leu Tyr Arg Gln 740 745 750His Cys Ser Ser Cys His Thr Pro Leu Asp Arg Asn Asp Leu Arg Thr 755 760 765Pro Val Lys Thr Val Leu Thr His Leu Gln Ala Arg Gly Glu Val Ala 770 775 780Pro Ile Gly Thr Asp Pro Trp Thr Ala Cys Asn Ser Ile Ala Gln Leu785 790 795 800Lys Thr Gly Tyr Val Arg Gly Lys Pro Tyr Leu Ser Phe Val Gly Thr 805 810 815Gly Gln Arg Gly Phe Tyr Gly Lys Gln Ala Tyr Ala Val Asp Val Leu 820 825 830Gln Glu Val Val Val Gln Ala Leu Ala Ala Arg Gly Leu Ser Val Ala 835 840 845Leu Gly Ala Phe Gln Thr Ala Ala Leu Gly Ile Phe Asp Gly Gln Leu 850 855 860Pro Pro Leu Ile Ser Pro Val Pro Asp Ser Pro Asp Ala Asp Ser Val865 870 875 880Glu Ala Thr Ala Ala Asp Ala Pro Gly Ala Leu Leu Leu Ala Glu Asn 885 890 895Val Ala Ala Asp Ser Asp Lys Ala Arg Arg Leu Glu Gln Cys Leu Ala 900 905 910Met Thr Ser Asp Leu Met Ala Tyr Lys Ala Arg Pro Leu Asn Gly Ile 915 920 925Trp Ala Ser Pro Pro Tyr Leu His Asn Gly Ser Val Ala Thr Leu Tyr 930 935 940Asp Leu Leu Leu Pro Pro Asp Leu Arg Pro Arg Thr Phe Tyr Thr Gly945 950 955 960Ser Val Glu Phe Asp Pro Val Asn Val Gly Tyr Ile Thr Asp Ala Gly 965 970 975Gly Ala Asn Arg Phe Leu Phe Asp Ser Gly Lys Pro Gly Asn Ala Asn 980 985 990Gly Gly His Asp Tyr Gly Asn Ala Gln Phe Asn Glu Gln Gln Arg Arg 995 1000 1005Ala Leu Val Glu Tyr Met Lys Thr Leu 1010 101557839PRTGlycine max 57Met Phe Ser Ala Gly His Lys Ile Lys Gly Thr Val Val Leu Met Pro1 5 10 15Lys Asn Glu Leu Glu Val Asn Pro Asp Gly Ser Ala Val Asp Asn Leu 20 25 30Asn Ala Phe Leu Gly Arg Ser Val Ser Leu Gln Leu Ile Ser Ala Thr 35 40 45Lys Ala Asp Ala His Gly Lys Gly Lys Val Gly Lys Asp Thr Phe Leu 50 55 60Glu Gly Ile Asn Thr Ser Leu Pro Thr Leu Gly Ala Gly Glu Ser Ala65 70 75 80Phe Asn Ile His Phe Glu Trp Asp Gly Ser Met Gly Ile Pro Gly Ala 85 90 95Phe Tyr Ile Lys Asn Tyr Met Gln Val Glu Phe Phe Leu Lys Ser Leu

100 105 110Thr Leu Glu Ala Ile Ser Asn Gln Gly Thr Ile Arg Phe Val Cys Asn 115 120 125Ser Trp Val Tyr Asn Thr Lys Leu Tyr Lys Ser Val Arg Ile Phe Phe 130 135 140Ala Asn His Thr Tyr Val Pro Ser Glu Thr Pro Ala Pro Leu Val Ser145 150 155 160Tyr Arg Glu Glu Glu Leu Lys Ser Leu Arg Gly Asn Gly Thr Gly Glu 165 170 175Arg Lys Glu Tyr Asp Arg Ile Tyr Asp Tyr Asp Val Tyr Asn Asp Leu 180 185 190Gly Asn Pro Asp Lys Ser Glu Lys Leu Ala Arg Pro Val Leu Gly Gly 195 200 205Ser Ser Thr Phe Pro Tyr Pro Arg Arg Gly Arg Thr Gly Arg Gly Pro 210 215 220Thr Val Thr Asp Pro Asn Thr Glu Lys Gln Gly Glu Val Phe Tyr Val225 230 235 240Pro Arg Asp Glu Asn Leu Gly His Leu Lys Ser Lys Asp Ala Leu Glu 245 250 255Ile Gly Thr Lys Ser Leu Ser Gln Ile Val Gln Pro Ala Phe Glu Ser 260 265 270Ala Phe Asp Leu Lys Ser Thr Pro Ile Glu Phe His Ser Phe Gln Asp 275 280 285Val His Asp Leu Tyr Glu Gly Gly Ile Lys Leu Pro Arg Asp Val Ile 290 295 300Ser Thr Ile Ile Pro Leu Pro Val Ile Lys Glu Leu Tyr Arg Thr Asp305 310 315 320Gly Gln His Ile Leu Lys Phe Pro Gln Pro His Val Val Gln Val Ser 325 330 335Gln Ser Ala Trp Met Thr Asp Glu Glu Phe Ala Arg Glu Met Ile Ala 340 345 350Gly Val Asn Pro Cys Val Ile Arg Gly Leu Glu Glu Phe Pro Pro Lys 355 360 365Ser Asn Leu Asp Pro Ala Ile Tyr Gly Asp Gln Ser Ser Lys Ile Thr 370 375 380Ala Asp Ser Leu Asp Leu Asp Gly Tyr Thr Met Asp Glu Ala Leu Gly385 390 395 400Ser Arg Arg Leu Phe Met Leu Asp Tyr His Asp Ile Phe Met Pro Tyr 405 410 415Val Arg Gln Ile Asn Gln Leu Asn Ser Ala Lys Thr Tyr Ala Thr Arg 420 425 430Thr Ile Leu Phe Leu Arg Glu Asp Gly Thr Leu Lys Pro Val Ala Ile 435 440 445Glu Leu Ser Leu Pro His Ser Ala Gly Asp Leu Ser Ala Ala Val Ser 450 455 460Gln Val Val Leu Pro Ala Lys Glu Gly Val Glu Ser Thr Ile Trp Leu465 470 475 480Leu Ala Lys Ala Tyr Val Ile Val Asn Asp Ser Cys Tyr His Gln Leu 485 490 495Met Ser His Trp Leu Asn Thr His Ala Ala Met Glu Pro Phe Val Ile 500 505 510Ala Thr His Arg His Leu Ser Val Leu His Pro Ile Tyr Lys Leu Leu 515 520 525Thr Pro His Tyr Arg Asn Asn Met Asn Ile Asn Ala Leu Ala Arg Gln 530 535 540Ser Leu Ile Asn Ala Asn Gly Ile Ile Glu Thr Thr Phe Leu Pro Ser545 550 555 560Lys Tyr Ser Val Glu Met Ser Ser Ala Val Tyr Lys Asn Trp Val Phe 565 570 575Thr Asp Gln Ala Leu Pro Ala Asp Leu Ile Lys Arg Gly Val Ala Ile 580 585 590Lys Asp Pro Ser Thr Pro His Gly Val Arg Leu Leu Ile Glu Asp Tyr 595 600 605Pro Tyr Ala Ala Asp Gly Leu Glu Ile Trp Ala Ala Ile Lys Thr Trp 610 615 620Val Gln Glu Tyr Val Pro Leu Tyr Tyr Ala Arg Asp Asp Asp Val Lys625 630 635 640Asn Asp Ser Glu Leu Gln His Trp Trp Lys Glu Ala Val Glu Lys Gly 645 650 655His Gly Asp Leu Lys Asp Lys Pro Trp Trp Pro Lys Leu Gln Thr Leu 660 665 670Glu Asp Leu Val Glu Val Cys Leu Ile Ile Ile Trp Ile Ala Ser Ala 675 680 685Leu His Ala Ala Val Asn Phe Gly Gln Tyr Pro Tyr Gly Gly Leu Ile 690 695 700Met Asn Arg Pro Thr Ala Ser Arg Arg Leu Leu Pro Glu Lys Gly Thr705 710 715 720Pro Glu Tyr Glu Glu Met Ile Asn Asn His Glu Lys Ala Tyr Leu Arg 725 730 735Thr Ile Thr Ser Lys Leu Pro Thr Leu Ile Ser Leu Ser Val Ile Glu 740 745 750Ile Leu Ser Thr His Ala Ser Asp Glu Val Tyr Leu Gly Gln Arg Asp 755 760 765Asn Pro His Trp Thr Ser Asp Ser Lys Ala Leu Gln Ala Phe Gln Lys 770 775 780Phe Gly Asn Lys Leu Lys Glu Ile Glu Glu Lys Leu Val Arg Arg Asn785 790 795 800Asn Asp Pro Ser Leu Gln Gly Asn Arg Leu Gly Pro Val Gln Leu Pro 805 810 815Tyr Thr Leu Leu Tyr Pro Ser Ser Glu Glu Gly Leu Thr Phe Arg Gly 820 825 830Ile Pro Asn Ser Ile Ser Ile 83558865PRTGlycine max 58Met Phe Ser Val Pro Gly Val Ser Gly Ile Leu Asn Arg Gly Gly Gly1 5 10 15His Lys Ile Lys Gly Thr Val Val Leu Met Arg Lys Asn Val Leu Asp 20 25 30Phe Asn Ser Val Ala Asp Leu Thr Lys Gly Asn Val Gly Gly Leu Ile 35 40 45Gly Thr Gly Leu Asn Val Val Gly Ser Thr Leu Asp Asn Leu Thr Ala 50 55 60Phe Leu Gly Arg Ser Val Ala Leu Gln Leu Ile Ser Ala Thr Lys Pro65 70 75 80Leu Ala Asn Gly Lys Gly Lys Val Gly Lys Asp Thr Phe Leu Glu Gly 85 90 95Ile Ile Val Ser Leu Pro Thr Leu Gly Ala Gly Glu Ser Ala Phe Asn 100 105 110Ile Gln Phe Glu Trp Asp Glu Ser Met Gly Ile Pro Gly Ala Phe Tyr 115 120 125Ile Lys Asn Tyr Met Gln Val Glu Phe Tyr Leu Lys Ser Leu Thr Leu 130 135 140Glu Asp Val Pro Asn Gln Gly Thr Ile Arg Phe Val Cys Asn Ser Trp145 150 155 160Val Tyr Asn Thr Lys Leu Tyr Lys Ser Val Arg Ile Phe Phe Ala Asn 165 170 175His Thr Tyr Val Pro Ser Glu Thr Pro Ala Ala Leu Val Gly Tyr Arg 180 185 190Glu Glu Glu Leu Lys Asn Leu Arg Gly Asp Gly Lys Gly Glu Arg Lys 195 200 205Glu His Asp Arg Ile Tyr Asp Tyr Asp Val Tyr Asn Asp Leu Gly Asn 210 215 220Pro Asp His Gly Glu Asn Phe Ala Arg Pro Ile Leu Gly Gly Ser Ser225 230 235 240Thr His Pro Tyr Pro Arg Arg Gly Arg Thr Gly Arg Tyr Pro Thr Arg 245 250 255Lys Asp Gln Asn Ser Glu Lys Pro Gly Glu Val Tyr Val Pro Arg Asp 260 265 270Glu Asn Phe Gly His Leu Lys Ser Ser Asp Phe Leu Ala Tyr Gly Ile 275 280 285Lys Ser Leu Ser Gln Tyr Val Leu Pro Ala Phe Glu Ser Val Phe Asp 290 295 300Leu Asn Phe Thr Pro Asn Glu Phe Asp Ser Phe Gln Asp Val Arg Asp305 310 315 320Leu His Glu Gly Gly Ile Lys Leu Pro Thr Glu Val Ile Ser Thr Ile 325 330 335Met Pro Leu Pro Val Val Lys Glu Leu Phe Arg Thr Asp Gly Glu Gln 340 345 350Val Leu Lys Phe Pro Pro Pro His Val Ile Gln Val Ser Lys Ser Ala 355 360 365Trp Met Thr Asp Glu Glu Phe Ala Arg Glu Met Val Ala Gly Val Asn 370 375 380Pro Cys Val Ile Arg Gly Leu Gln Glu Phe Pro Pro Lys Ser Asn Leu385 390 395 400Asp Pro Thr Ile Tyr Gly Glu Gln Thr Ser Lys Ile Thr Ala Asp Ala 405 410 415Leu Asp Leu Asp Gly Tyr Thr Val Asp Glu Ala Leu Ala Ser Arg Arg 420 425 430Leu Phe Met Leu Asp Tyr His Asp Val Phe Met Pro Tyr Ile Arg Arg 435 440 445Ile Asn Gln Thr Tyr Ala Lys Ala Tyr Ala Thr Arg Thr Ile Leu Phe 450 455 460Leu Arg Glu Asn Gly Thr Leu Lys Pro Val Ala Ile Glu Leu Ser Leu465 470 475 480Pro His Pro Ala Gly Asp Leu Ser Gly Ala Val Ser Gln Val Ile Leu 485 490 495Pro Ala Lys Glu Gly Val Glu Ser Thr Ile Trp Leu Leu Ala Lys Ala 500 505 510Tyr Val Val Val Asn Asp Ser Cys Tyr His Gln Leu Met Ser His Trp 515 520 525Leu Asn Thr His Ala Val Ile Glu Pro Phe Ile Ile Ala Thr Asn Arg 530 535 540His Leu Ser Ala Leu His Pro Ile Tyr Lys Leu Leu Thr Pro His Tyr545 550 555 560Arg Asp Thr Met Asn Ile Asn Ala Leu Ala Arg Gln Ser Leu Ile Asn 565 570 575Ala Asp Gly Ile Ile Glu Lys Ser Phe Leu Pro Ser Lys His Ser Val 580 585 590Glu Met Ser Ser Ala Val Tyr Lys Asn Trp Val Phe Thr Asp Gln Ala 595 600 605Leu Pro Ala Asp Leu Ile Lys Arg Gly Val Ala Ile Lys Asp Pro Ser 610 615 620Ala Pro His Gly Leu Arg Leu Leu Ile Glu Asp Tyr Pro Tyr Ala Val625 630 635 640Asp Gly Leu Glu Ile Trp Ala Ala Ile Lys Thr Trp Val Gln Glu Tyr 645 650 655Val Ser Leu Tyr Tyr Ala Arg Asp Asp Asp Val Lys Pro Asp Ser Glu 660 665 670Leu Gln Gln Trp Trp Lys Glu Ala Val Glu Lys Gly His Gly Asp Leu 675 680 685Lys Asp Lys Pro Trp Trp Pro Lys Leu Gln Thr Ile Glu Glu Leu Val 690 695 700Glu Ile Cys Thr Ile Ile Ile Trp Thr Ala Ser Ala Leu His Ala Ala705 710 715 720Val Asn Phe Gly Gln Tyr Pro Tyr Gly Gly Phe Ile Leu Asn Arg Pro 725 730 735Thr Ser Ser Arg Arg Leu Leu Pro Glu Lys Gly Thr Pro Glu Tyr Glu 740 745 750Glu Met Val Lys Ser His Gln Lys Ala Tyr Leu Arg Thr Ile Thr Ser 755 760 765Lys Phe Gln Thr Leu Val Asp Leu Ser Val Ile Glu Ile Leu Ser Arg 770 775 780His Ala Ser Asp Glu Val Tyr Leu Gly Gln Arg Asp Asn Pro His Trp785 790 795 800Thr Ser Asp Ser Lys Ala Leu Gln Ala Phe Gln Lys Phe Gly Asn Lys 805 810 815Leu Lys Glu Ile Glu Glu Lys Leu Ala Arg Lys Asn Asn Asp Gln Ser 820 825 830Leu Ser Asn Arg Leu Gly Pro Val Gln Leu Pro Tyr Thr Leu Leu His 835 840 845Pro Asn Ser Glu Gly Leu Thr Cys Arg Gly Ile Pro Asn Ser Ile Ser 850 855 860Ile86559857PRTGlycine max 59Met Leu Gly Gly Leu Leu His Arg Gly His Lys Ile Lys Gly Thr Val1 5 10 15Val Leu Met Arg Lys Asn Val Leu His Val Asn Ser Val Thr Ser Val 20 25 30Gly Gly Ile Ile Gly Gln Gly Leu Asp Leu Val Gly Ser Thr Leu Asp 35 40 45Thr Leu Thr Ala Phe Leu Gly Arg Pro Val Ser Leu Gln Leu Ile Ser 50 55 60Ala Thr Lys Ala Asp Ala Asn Gly Lys Gly Lys Leu Gly Lys Ala Thr65 70 75 80Phe Leu Glu Gly Ile Ile Thr Ser Leu Pro Thr Leu Gly Ala Gly Gln 85 90 95Ser Ala Phe Lys Ile Asn Phe Glu Trp Asp Asp Gly Ser Gly Ile Leu 100 105 110Gly Ala Phe Tyr Ile Lys Asn Phe Met Gln Thr Glu Phe Phe Leu Val 115 120 125Ser Leu Thr Leu Glu Asp Ile Pro Asn His Gly Ser Ile His Phe Val 130 135 140Cys Asn Ser Trp Ile Tyr Asn Ala Lys Leu Phe Lys Ser Asp Arg Ile145 150 155 160Phe Phe Ala Asn Gln Thr Tyr Leu Pro Ser Glu Thr Pro Ala Pro Leu 165 170 175Val Lys Tyr Arg Glu Glu Glu Leu His Asn Leu Arg Gly Asp Gly Thr 180 185 190Gly Glu Arg Lys Glu Trp Glu Arg Val Tyr Asp Tyr Asp Val Tyr Asn 195 200 205Asp Leu Gly Asp Pro Asp Lys Gly Glu Asn His Ala Arg Pro Val Leu 210 215 220Gly Gly Asn Asp Thr Phe Pro Tyr Pro Arg Arg Gly Arg Thr Gly Arg225 230 235 240Lys Pro Thr Arg Lys Asp Pro Asn Ser Glu Ser Arg Ser Asn Asp Val 245 250 255Tyr Leu Pro Arg Asp Glu Ala Phe Gly His Leu Lys Ser Ser Asp Phe 260 265 270Leu Thr Tyr Gly Leu Lys Ser Val Ser Gln Asn Val Leu Pro Leu Leu 275 280 285Gln Ser Ala Phe Asp Leu Asn Phe Thr Pro Arg Glu Phe Asp Ser Phe 290 295 300Asp Glu Val His Gly Leu Tyr Ser Gly Gly Ile Lys Leu Pro Thr Asp305 310 315 320Ile Ile Ser Lys Ile Ser Pro Leu Pro Val Leu Lys Glu Ile Phe Arg 325 330 335Thr Asp Gly Glu Gln Ala Leu Lys Phe Pro Pro Pro Lys Val Ile Gln 340 345 350Val Ser Lys Ser Ala Trp Met Thr Asp Glu Glu Phe Ala Arg Glu Met 355 360 365Leu Ala Gly Val Asn Pro Asn Leu Ile Arg Cys Leu Lys Glu Phe Pro 370 375 380Pro Arg Ser Lys Leu Asp Ser Gln Val Tyr Gly Asp His Thr Ser Gln385 390 395 400Ile Thr Lys Glu His Leu Glu Pro Asn Leu Glu Gly Leu Thr Val Asp 405 410 415Glu Ala Ile Gln Asn Lys Arg Leu Phe Leu Leu Gly His His Asp Pro 420 425 430Ile Met Pro Tyr Leu Arg Arg Ile Asn Ala Thr Ser Thr Lys Ala Tyr 435 440 445Ala Thr Arg Thr Ile Leu Phe Leu Lys Asn Asp Gly Thr Leu Arg Pro 450 455 460Leu Ala Ile Glu Leu Ser Leu Pro His Pro Gln Gly Asp Gln Ser Gly465 470 475 480Ala Phe Ser Gln Val Phe Leu Pro Ala Asp Glu Gly Val Glu Ser Ser 485 490 495Ile Trp Leu Leu Ala Lys Ala Tyr Val Val Val Asn Asp Ser Cys Tyr 500 505 510His Gln Leu Val Ser His Trp Leu Asn Thr His Ala Val Val Glu Pro 515 520 525Phe Ile Ile Ala Thr Asn Arg His Leu Ser Val Val His Pro Ile Tyr 530 535 540Lys Leu Leu His Pro His Tyr Arg Asp Thr Met Asn Ile Asn Gly Leu545 550 555 560Ala Arg Leu Ser Leu Val Asn Asp Gly Gly Val Ile Glu Gln Thr Phe 565 570 575Leu Trp Gly Arg Tyr Ser Val Glu Met Ser Ala Val Val Tyr Lys Asp 580 585 590Trp Val Phe Thr Asp Gln Ala Leu Pro Ala Asp Leu Ile Lys Arg Gly 595 600 605Met Ala Ile Glu Asp Pro Ser Cys Pro His Gly Ile Arg Leu Val Ile 610 615 620Glu Asp Tyr Pro Tyr Ala Val Asp Gly Leu Glu Ile Trp Asp Ala Ile625 630 635 640Lys Thr Trp Val His Glu Tyr Val Phe Leu Tyr Tyr Lys Ser Asp Asp 645 650 655Thr Leu Arg Glu Asp Pro Glu Leu Gln Ala Cys Trp Lys Glu Leu Val 660 665 670Glu Val Gly His Gly Asp Lys Lys Asn Glu Pro Trp Trp Pro Lys Met 675 680 685Gln Thr Arg Glu Glu Leu Val Glu Ala Cys Ala Ile Ile Ile Trp Thr 690 695 700Ala Ser Ala Leu His Ala Ala Val Asn Phe Gly Gln Tyr Pro Tyr Gly705 710 715 720Gly Leu Ile Leu Asn Arg Pro Thr Leu Ser Arg Arg Phe Met Pro Glu 725 730 735Lys Gly Ser Ala Glu Tyr Glu Glu Leu Arg Lys Asn Pro Gln Lys Ala 740 745 750Tyr Leu Lys Thr Ile Thr Pro Lys Phe Gln Thr Leu Ile Asp Leu Ser 755 760 765Val Ile Glu Ile Leu Ser Arg His Ala Ser Asp Glu Val Tyr Leu Gly 770 775 780Glu Arg Asp Asn Pro Asn Trp Thr Ser Asp Thr Arg Ala Leu Glu Ala785 790 795 800Phe Lys Arg Phe Gly Asn Lys Leu Ala Gln Ile Glu Asn Lys Leu Ser 805 810 815Glu Arg Asn Asn Asp Glu Lys Leu Arg Asn Arg Cys Gly Pro Val Gln 820 825 830Met Pro Tyr Thr Leu Leu Leu Pro Ser Ser Lys Glu Gly Leu Thr Phe 835 840 845Arg Gly Ile Pro Asn Ser Ile Ser Ile 850 85560853PRTGlycine max 60Met Phe Pro Phe Gly Gln Lys Gly Gln Lys Ile Lys Gly Thr Met Val1 5 10

15Val Met Gln Lys Asn Val Leu Asp Ile Asn Ser Ile Thr Ser Val Gly 20 25 30Gly Ile Val Asp Gln Gly Leu Gly Phe Ile Gly Ser Ala Val Asp Ala 35 40 45Leu Thr Phe Ala Ala Thr Lys Ile Ser Ile Gln Leu Ile Ser Ala Thr 50 55 60Lys Ala Asp Gly Gly Lys Gly Lys Ile Gly Lys Ser Thr Asn Leu Arg65 70 75 80Gly Lys Ile Thr Leu Pro Thr Leu Gly Ala Gly Glu Gln Ala Tyr Asp 85 90 95Val Asn Phe Glu Trp Asp Ser Asp Phe Gly Ile Pro Gly Ala Phe Tyr 100 105 110Ile Lys Asn Phe Met Gln Asn Glu Phe Tyr Leu Lys Ser Leu Ile Leu 115 120 125Glu Asp Ile Pro Asn His Gly Thr Ile His Phe Val Cys Asn Ser Trp 130 135 140Val Tyr Asn Ser Lys Asn Tyr Lys Thr Asp Arg Ile Phe Phe Ala Asn145 150 155 160Asn Thr Tyr Leu Pro Ser Glu Thr Pro Ala Pro Leu Leu Lys Tyr Arg 165 170 175Glu Glu Glu Leu Lys Asn Val Arg Gly Asp Gly Thr Gly Glu Arg Lys 180 185 190Glu Trp Asp Arg Ile Tyr Asp Tyr Asp Val Tyr Asn Asp Leu Gly Asn 195 200 205Pro Asp Ser Gly Asp Lys Tyr Ala Arg Pro Val Leu Gly Gly Ser Ala 210 215 220Leu Pro Tyr Pro Arg Arg Glu Arg Thr Gly Arg Gly Lys Thr Arg Lys225 230 235 240Asp Pro Asn Ser Glu Lys Pro Ser Asp Phe Val Tyr Leu Pro Arg Asp 245 250 255Glu Ala Phe Gly His Leu Lys Ser Ser Asp Phe Leu Ala Tyr Gly Ile 260 265 270Lys Ser Val Ser Gln Asp Val Leu Pro Val Leu Thr Asp Ala Phe Asp 275 280 285Gly Asn Ile Leu Ser Leu Glu Phe Asp Asn Phe Ala Glu Val His Lys 290 295 300Leu Tyr Glu Gly Gly Val Thr Leu Pro Thr Asn Phe Leu Ser Lys Ile305 310 315 320Ala Pro Ile Pro Val Ile Lys Glu Ile Phe Arg Thr Asp Gly Glu Gln 325 330 335Phe Leu Lys Tyr Pro Pro Pro Lys Val Met Gln Val Asp Lys Ser Ala 340 345 350Trp Met Thr Asp Glu Glu Phe Ala Arg Glu Thr Ile Ala Gly Leu Asn 355 360 365Pro Asn Val Ile Lys Ile Ile Glu Glu Phe Pro Leu Ser Ser Lys Leu 370 375 380Asp Thr Gln Ala Tyr Gly Asp His Thr Cys Ile Ile Ala Lys Glu His385 390 395 400Leu Glu Pro Asn Leu Gly Gly Leu Thr Val Glu Gln Ala Ile Gln Asn 405 410 415Lys Lys Leu Phe Ile Leu Asp His His Asp Tyr Leu Ile Pro Tyr Leu 420 425 430Arg Lys Ile Asn Ala Asn Thr Thr Lys Thr Tyr Ala Thr Arg Thr Ile 435 440 445Phe Phe Leu Lys Asp Asp Gly Thr Leu Thr Pro Leu Ala Ile Glu Leu 450 455 460Ser Lys Pro His Pro Gln Gly Glu Glu Tyr Gly Pro Val Ser Glu Val465 470 475 480Tyr Val Pro Ala Ser Glu Gly Val Glu Ala Tyr Ile Trp Leu Leu Ala 485 490 495Lys Ala Tyr Val Val Val Asn Asp Ala Cys Tyr His Gln Ile Ile Ser 500 505 510His Trp Leu Ser Thr His Ala Ile Val Glu Pro Phe Val Ile Ala Thr 515 520 525Asn Arg Gln Leu Ser Val Val His Pro Ile Tyr Lys Leu Leu Phe Pro 530 535 540His Tyr Arg Asp Thr Met Asn Ile Asn Ser Leu Ala Arg Lys Ala Leu545 550 555 560Val Asn Ala Asp Gly Ile Ile Glu Lys Thr Phe Leu Trp Gly Arg Tyr 565 570 575Ser Met Glu Met Ser Ala Val Ile Tyr Lys Asp Trp Val Phe Thr Asp 580 585 590Gln Ala Leu Pro Asn Asp Leu Val Lys Arg Gly Val Ala Val Lys Asp 595 600 605Pro Ser Ala Pro His Gly Val Arg Leu Leu Ile Glu Asp Tyr Pro Tyr 610 615 620Ala Ser Asp Gly Leu Glu Ile Trp Asp Ala Ile Lys Ser Trp Val Gln625 630 635 640Glu Tyr Val Ser Phe Tyr Tyr Lys Ser Asp Glu Glu Leu Gln Lys Asp 645 650 655Pro Glu Leu Gln Ala Trp Trp Lys Glu Leu Val Glu Val Gly His Gly 660 665 670Asp Leu Lys Asp Lys Pro Trp Trp Gln Lys Met Gln Thr Arg Glu Glu 675 680 685Leu Val Glu Ala Ser Ala Ile Leu Ile Trp Ile Ala Ser Ala Leu His 690 695 700Ala Ala Val Asn Phe Gly Gln Tyr Pro Tyr Gly Gly Leu Ile Leu Asn705 710 715 720Arg Pro Thr Ile Ser Arg Arg Phe Met Pro Glu Lys Gly Ser Pro Glu 725 730 735Tyr Asp Ala Leu Ala Lys Asn Pro Glu Lys Glu Phe Leu Lys Thr Ile 740 745 750Thr Gly Lys Lys Glu Thr Leu Ile Asp Leu Thr Val Ile Glu Ile Leu 755 760 765Ser Arg His Ala Ser Asp Glu Phe Tyr Leu Gly Gln Arg Asp Gly Gly 770 775 780Asp Tyr Trp Thr Ser Asp Ala Gly Pro Leu Glu Ala Phe Lys Arg Phe785 790 795 800Gly Lys Lys Leu Glu Glu Ile Glu Lys Lys Leu Ile Glu Lys Asn Lys 805 810 815Asp Glu Thr Leu Arg Asn Arg Tyr Gly Pro Ala Lys Met Pro Tyr Thr 820 825 830Leu Leu Tyr Pro Ser Ser Glu Glu Gly Leu Thr Phe Arg Gly Ile Pro 835 840 845Asn Ser Ile Ser Ile 85061864PRTGlycine max 61Met Phe Gly Ile Phe Asp Lys Gly Gln Lys Ile Lys Gly Thr Val Val1 5 10 15Leu Met Pro Lys Asn Val Leu Asp Phe Asn Ala Ile Thr Ser Ile Gly 20 25 30Lys Gly Gly Val Ile Asp Thr Ala Thr Gly Ile Leu Gly Gln Gly Val 35 40 45Ser Leu Val Gly Gly Val Ile Asp Thr Ala Thr Ser Phe Leu Gly Arg 50 55 60Asn Ile Ser Met Gln Leu Ile Ser Ala Thr Gln Thr Asp Gly Ser Gly65 70 75 80Asn Gly Lys Val Gly Lys Glu Val Tyr Leu Glu Lys His Leu Pro Thr 85 90 95Leu Pro Thr Leu Gly Ala Arg Gln Asp Ala Phe Ser Ile Phe Phe Glu 100 105 110Trp Asp Ala Ser Phe Gly Ile Pro Gly Ala Phe Tyr Ile Lys Asn Phe 115 120 125Met Thr Asp Glu Phe Phe Leu Val Ser Val Lys Leu Glu Asp Ile Pro 130 135 140Asn His Gly Thr Ile Glu Phe Val Cys Asn Ser Trp Val Tyr Asn Phe145 150 155 160Arg Ser Tyr Lys Lys Asn Arg Ile Phe Phe Val Asn Asp Thr Tyr Leu 165 170 175Pro Ser Ala Thr Pro Ala Pro Leu Leu Lys Tyr Arg Lys Glu Glu Leu 180 185 190Glu Val Leu Arg Gly Asp Gly Thr Gly Lys Arg Lys Asp Phe Asp Arg 195 200 205Ile Tyr Asp Tyr Asp Val Tyr Asn Asp Leu Gly Asn Pro Asp Gly Gly 210 215 220Asp Pro Arg Pro Ile Leu Gly Gly Ser Ser Ile Tyr Pro Tyr Pro Arg225 230 235 240Arg Val Arg Thr Gly Arg Glu Arg Thr Arg Thr Asp Pro Asn Ser Glu 245 250 255Lys Pro Gly Glu Val Tyr Val Pro Arg Asp Glu Asn Phe Gly His Leu 260 265 270Lys Ser Ser Asp Phe Leu Thr Tyr Gly Ile Lys Ser Leu Ser His Asp 275 280 285Val Ile Pro Leu Phe Lys Ser Ala Ile Phe Gln Leu Arg Val Thr Ser 290 295 300Ser Glu Phe Glu Ser Phe Glu Asp Val Arg Ser Leu Tyr Glu Gly Gly305 310 315 320Ile Lys Leu Pro Thr Asp Ile Leu Ser Gln Ile Ser Pro Leu Pro Ala 325 330 335Leu Lys Glu Ile Phe Arg Thr Asp Gly Glu Asn Val Leu Gln Phe Pro 340 345 350Pro Pro His Val Ala Lys Val Ser Lys Ser Gly Trp Met Thr Asp Glu 355 360 365Glu Phe Ala Arg Glu Val Ile Ala Gly Val Asn Pro Asn Val Ile Arg 370 375 380Arg Leu Gln Glu Phe Pro Pro Lys Ser Thr Leu Asp Pro Thr Leu Tyr385 390 395 400Gly Asp Gln Thr Ser Thr Ile Thr Lys Glu Gln Leu Glu Ile Asn Met 405 410 415Gly Gly Val Thr Val Glu Glu Ala Leu Ser Thr Gln Arg Leu Phe Ile 420 425 430Leu Asp Tyr Gln Asp Ala Phe Ile Pro Tyr Leu Thr Arg Ile Asn Ser 435 440 445Leu Pro Thr Ala Lys Ala Tyr Ala Thr Arg Thr Ile Leu Phe Leu Lys 450 455 460Asp Asp Gly Thr Leu Lys Pro Leu Ala Ile Glu Leu Ser Lys Pro His465 470 475 480Pro Asp Gly Asp Asn Leu Gly Pro Glu Ser Ile Val Val Leu Pro Ala 485 490 495Thr Glu Gly Val Asp Ser Thr Ile Trp Leu Leu Ala Lys Ala His Val 500 505 510Ile Val Asn Asp Ser Gly Tyr His Gln Leu Val Ser His Trp Leu Asn 515 520 525Thr His Ala Val Met Glu Pro Phe Ala Ile Ala Thr Asn Arg His Leu 530 535 540Ser Val Leu His Pro Ile Tyr Lys Leu Leu Tyr Pro His Tyr Arg Asp545 550 555 560Thr Ile Asn Ile Asn Gly Leu Ala Arg Gln Ser Leu Ile Asn Ala Asp 565 570 575Gly Ile Ile Glu Lys Ser Phe Leu Pro Gly Lys Tyr Ser Ile Glu Met 580 585 590Ser Ser Ser Val Tyr Lys Asn Trp Val Phe Thr Asp Gln Ala Leu Pro 595 600 605Ala Asp Leu Val Lys Arg Gly Leu Ala Ile Glu Asp Pro Ser Ala Pro 610 615 620His Gly Leu Arg Leu Val Ile Glu Asp Tyr Pro Tyr Ala Val Asp Gly625 630 635 640Leu Glu Ile Trp Asp Ala Ile Lys Thr Trp Val His Glu Tyr Val Ser 645 650 655Leu Tyr Tyr Pro Thr Asp Ala Ala Val Gln Gln Asp Thr Glu Leu Gln 660 665 670Ala Trp Trp Lys Glu Ala Val Glu Lys Gly His Gly Asp Leu Lys Glu 675 680 685Lys Pro Trp Trp Pro Lys Met Gln Thr Thr Glu Asp Leu Ile Gln Ser 690 695 700Cys Ser Ile Ile Val Trp Thr Ala Ser Ala Leu His Ala Ala Val Asn705 710 715 720Phe Gly Gln Tyr Pro Tyr Gly Gly Leu Ile Leu Asn Arg Pro Thr Leu 725 730 735Ala Arg Arg Phe Ile Pro Ala Glu Gly Thr Pro Glu Tyr Asp Glu Met 740 745 750Val Lys Asn Pro Gln Lys Ala Tyr Leu Arg Thr Ile Thr Pro Lys Phe 755 760 765Glu Thr Leu Ile Asp Leu Ser Val Ile Glu Ile Leu Ser Arg His Ala 770 775 780Ser Asp Glu Ile Tyr Leu Gly Glu Arg Glu Thr Pro Asn Trp Thr Thr785 790 795 800Asp Lys Lys Ala Leu Glu Ala Phe Lys Arg Phe Gly Ser Lys Leu Thr 805 810 815Gly Ile Glu Gly Lys Ile Asn Ala Arg Asn Ser Asp Pro Ser Leu Arg 820 825 830Asn Arg Thr Gly Pro Val Gln Leu Pro Tyr Thr Leu Leu His Arg Ser 835 840 845Ser Glu Glu Gly Leu Thr Phe Lys Gly Ile Pro Asn Ser Ile Ser Ile 850 855 860621242DNAArtificial sequenceCodon optimized artificial DNA sequence 62aagcttggat ccggctcttc tggtagtgga gaaaatctat attttcaagg aatgaaacta 60ttcacagaat accccgaaaa ggatgaacta aagtactgtg atctgatgag cgaactggtt 120aagaaaaaca tggagaacct gtatggtggc aagaaaaaga aaaccgcgaa acgtgacacc 180cacagcaaaa cccatgcggc ggtgcaaggt accctggaga tctttgactt cgatgaagcg 240gcgattaaac aggagctgag caagcgtacc agcctgagcg aagcggagct gagcgcgatc 300agcctgaaac aaggtctgtt cgcgaccccg aagcagtacc cggtgtggct gcgttttgcg 360aacggtgcgt tcagcgttaa aaacgactat gaaggcgata cccgtagcat ggcggtgaag 420gcgatcggtg ttgaaggcga gcgtctgagc caaagccacg aactgaaaac ccaggacatc 480attacccaca acaccgagtt ctttttcgtg cgtaccatta aggattttca cagctttttc 540ctgaccgttt accgtgcggg cctgtttccg ctgttcaaac tgctggtgct gttctggctg 600aagctgcacc cgtatgaaag caccctgctg caaaccagct ttaagcgttt cccgaaaagc 660ctgctgaagg agcgttactg gagcgcgagc gcgtttagcg ttggtctgaa aagcggcttc 720gatccgagcc aaccgggtcg tgtgccggtt gaatacccgg cggtgatcaa gtatggcttt 780accccggtta gcagccagcc gccgcaccag caattcccgc tggagagccg tagcgaaagc 840gagctgaagc tggcgaaagc gagcggtagc gaagacaact actatcgtga ggatatcatt 900caggcgctgg cgaagccgga cgcggaatac tattgggatt ttcagatcca attccagacc 960agcccggaga tgagcatcga cgataccacc attgtgtgga acgaggaaga gagcccgttt 1020ttcaccgtgg gtcgtctgac cattaagcac caaaaagtta actacccgca ggcgaacgac 1080tttggcgaaa acctgagctt cagcccgggt aacggtctgg cggtgcaccg tccggttggt 1140gcgattaacc gtctgcgtag catcgtgtac ccgattgttg cgaacgatcg tcaccaaaaa 1200cgtggcgtga agtatcagga gccgaccgtt taatgactcg ag 124263797PRTNostoc punctiforme 63Met Gly Ser Ser His His His His His His Gly Thr Lys Thr Glu Glu1 5 10 15Gly Lys Leu Val Ile Trp Ile Asn Gly Asp Lys Gly Tyr Asn Gly Leu 20 25 30Ala Glu Val Gly Lys Lys Phe Glu Lys Asp Thr Gly Ile Lys Val Thr 35 40 45Val Glu His Pro Asp Lys Leu Glu Glu Lys Phe Pro Gln Val Ala Ala 50 55 60Thr Gly Asp Gly Pro Asp Ile Ile Phe Trp Ala His Asp Arg Phe Gly65 70 75 80Gly Tyr Ala Gln Ser Gly Leu Leu Ala Glu Ile Thr Pro Asp Lys Ala 85 90 95Phe Gln Asp Lys Leu Tyr Pro Phe Thr Trp Asp Ala Val Arg Tyr Asn 100 105 110Gly Lys Leu Ile Ala Tyr Pro Ile Ala Val Glu Ala Leu Ser Leu Ile 115 120 125Tyr Asn Lys Asp Leu Leu Pro Asn Pro Pro Lys Thr Trp Glu Glu Ile 130 135 140Pro Ala Leu Asp Lys Glu Leu Lys Ala Lys Gly Lys Ser Ala Leu Met145 150 155 160Phe Asn Leu Gln Glu Pro Tyr Phe Thr Trp Pro Leu Ile Ala Ala Asp 165 170 175Gly Gly Tyr Ala Phe Lys Tyr Glu Asn Gly Lys Tyr Asp Ile Lys Asp 180 185 190Val Gly Val Asp Asn Ala Gly Ala Lys Ala Gly Leu Thr Phe Leu Val 195 200 205Asp Leu Ile Lys Asn Lys His Met Asn Ala Asp Thr Asp Tyr Ser Ile 210 215 220Ala Glu Ala Ala Phe Asn Lys Gly Glu Thr Ala Met Thr Ile Asn Gly225 230 235 240Pro Trp Ala Trp Ser Asn Ile Asp Thr Ser Lys Val Asn Tyr Gly Val 245 250 255Thr Val Leu Pro Thr Phe Lys Gly Gln Pro Ser Lys Pro Phe Val Gly 260 265 270Val Leu Ser Ala Gly Ile Asn Ala Ala Ser Pro Asn Lys Glu Leu Ala 275 280 285Lys Glu Phe Leu Glu Asn Tyr Leu Leu Thr Asp Glu Gly Leu Glu Ala 290 295 300Val Asn Lys Asp Lys Pro Leu Gly Ala Val Ala Leu Lys Ser Tyr Glu305 310 315 320Glu Glu Leu Ala Lys Asp Pro Arg Ile Ala Ala Thr Met Glu Asn Ala 325 330 335Gln Lys Gly Glu Ile Met Pro Asn Ile Pro Gln Met Ser Ala Phe Trp 340 345 350Tyr Ala Val Arg Thr Ala Val Ile Asn Ala Ala Ser Gly Arg Gln Thr 355 360 365Val Asp Glu Ala Leu Lys Asp Ala Gln Thr Gly Thr Asp Tyr Asp Ile 370 375 380Pro Thr Thr Lys Leu Gly Ser Gly Ser Ser Gly Ser Gly Glu Asn Leu385 390 395 400Tyr Phe Gln Gly Met Lys Leu Phe Thr Glu Tyr Pro Glu Lys Asp Glu 405 410 415Leu Lys Tyr Cys Asp Leu Met Ser Glu Leu Val Lys Lys Asn Met Glu 420 425 430Asn Leu Tyr Gly Gly Lys Lys Lys Lys Thr Ala Lys Arg Asp Thr His 435 440 445Ser Lys Thr His Ala Ala Val Gln Gly Thr Leu Glu Ile Phe Asp Phe 450 455 460Asp Glu Ala Ala Ile Lys Gln Glu Leu Ser Lys Arg Thr Ser Leu Ser465 470 475 480Glu Ala Glu Leu Ser Ala Ile Ser Leu Lys Gln Gly Leu Phe Ala Thr 485 490 495Pro Lys Gln Tyr Pro Val Trp Leu Arg Phe Ala Asn Gly Ala Phe Ser 500 505 510Val Lys Asn Asp Tyr Glu Gly Asp Thr Arg Ser Met Ala Val Lys Ala 515 520 525Ile Gly Val Glu Gly Glu Arg Leu Ser Gln Ser His Glu Leu Lys Thr 530 535 540Gln Asp Ile Ile Thr His Asn Thr Glu Phe

Phe Phe Val Arg Thr Ile545 550 555 560Lys Asp Phe His Ser Phe Phe Leu Thr Val Tyr Arg Ala Gly Leu Phe 565 570 575Pro Leu Phe Lys Leu Leu Val Leu Phe Trp Leu Lys Leu His Pro Tyr 580 585 590Glu Ser Thr Leu Leu Gln Thr Ser Phe Lys Arg Phe Pro Lys Ser Leu 595 600 605Leu Lys Glu Arg Tyr Trp Ser Ala Ser Ala Phe Ser Val Gly Leu Lys 610 615 620Ser Gly Phe Asp Pro Ser Gln Pro Gly Arg Val Pro Val Glu Tyr Pro625 630 635 640Ala Val Ile Lys Tyr Gly Phe Thr Pro Val Ser Ser Gln Pro Pro His 645 650 655Gln Gln Phe Pro Leu Glu Ser Arg Ser Glu Ser Glu Leu Lys Leu Ala 660 665 670Lys Ala Ser Gly Ser Glu Asp Asn Tyr Tyr Arg Glu Asp Ile Ile Gln 675 680 685Ala Leu Ala Lys Pro Asp Ala Glu Tyr Tyr Trp Asp Phe Gln Ile Gln 690 695 700Phe Gln Thr Ser Pro Glu Met Ser Ile Asp Asp Thr Thr Ile Val Trp705 710 715 720Asn Glu Glu Glu Ser Pro Phe Phe Thr Val Gly Arg Leu Thr Ile Lys 725 730 735His Gln Lys Val Asn Tyr Pro Gln Ala Asn Asp Phe Gly Glu Asn Leu 740 745 750Ser Phe Ser Pro Gly Asn Gly Leu Ala Val His Arg Pro Val Gly Ala 755 760 765Ile Asn Arg Leu Arg Ser Ile Val Tyr Pro Ile Val Ala Asn Asp Arg 770 775 780His Gln Lys Arg Gly Val Lys Tyr Gln Glu Pro Thr Val785 790 795643489DNAArtificial sequenceCodon optimized artificial DNA sequence 64catatgcacc accaccacca ccacatgagt ttcaacgaaa agttccaagc tggcgaaagc 60tacggtgaca gcaaggaaga tccgagcagc ctgctgaaca acccggagaa actggtggcg 120gacctgatga aggattttgc gggtgttcgt agccaggcga gcccggcgca actgctgggt 180ctggttaaag aactgctgca gaagggtcaa ccgctggacg ataagaaagg caccaccgag 240ctgctgattg gtattctgac cgcgctgccg gcgaccagca aagcgcgtac cgcgctgacc 300aacaagctga tcgacaccct gtggggtaac ctgcagcacc cgccgctgag ctatatgggt 360ggcgacgtta aatacgatgt ggttaacagc gataaaccgg cgcacaagca caactgcgag 420ctgtatgaca ccattgaatt caaggtgccg ggtaccgatg ttctgctgcg tgagcaggtg 480ccgcaagcgc cggacggcct gcaccaatat cgtatgccgg atggtagctt taacaacatc 540ctggaaccga acctgggtcg tgcgggtacc ccgtacgcga agagcgtgaa aagcgagaag 600cgtctgcacg gcgttaaacc ggacccgggt ctgctgttcg atctgctgat ggcgcgtgac 660gagaccacct ttcaggaaaa cccggcgggt attagcagca tgctgttcta ccacgcggcg 720atcattatcc acgacatctt tcgtaccaac cgtaccgaca tgaacaaaag cgataccagc 780agctatctgg acctggcgcc gctgtatggt agcagcctga aagatcaaca cgagatccgt 840accatgaagg aaggtaagct gaaaccggac accttccatg aaaagcgtct gctgggtcag 900ccggcgggtg tgaacgttat gctggtgctg tatagccgtt tccacaacta cgttgcggac 960attctgctga aaatcaacga gaacggtcgt tttagcctga gcgttccgcc gaacgcgagc 1020gaggaagata aggcgaaagc gattgcgaag caggaccacg acctgttcaa cgtggcgcgt 1080ctgatcaccg gtggcctgta tattaacatc tgcctgcacg actacctgcg tgcgattacc 1140aacacccatc atagcgcgag cgactggacc ctggatccgc gtgttgcgat cgataaacaa 1200tttgacggtg atggcgtgcc gcgtggtgtt ggcaaccaag tgagcgttga attcaacctg 1260ctgtaccgtt ttcacagctg cattagcaaa cgtgacgaga agtggatcaa caacttcttt 1320ctgaaactgt tcccgggccg taaggcggag gacctgcaag atgtgagctg gaccgaactg 1380ggtcaggcgc tgctgatttt tgagcaaaac accccgaagg atccgagcgt tcgtaccttc 1440gacggcctgg aacgtcaggc ggatggtacc tttaaagacg aggatctggt gcgtatcctg 1500aaggacgcga tggaagatcc ggcgggtacc tttggtgcgc gtatggtgcc gaaagcgctg 1560aaggtggttg aggttctggg cattatccag ggtcgtaaat ggcaatgcgc gagcctgaac 1620gagttccgtg aattctttgg tctgaagcgt tatgacagct ttagcgaaat caacagcaac 1680ccggatattg cgaacatcct ggagaaactg tataccgacc cggatatggt ggagctgtac 1740ccgggcctga tgattgaaga catcaagccg cagcgtaacc cgggtagcgg cattatgccg 1800acctatagcg tgggtcgtgc ggttctgagc gatgcggtga ccctggttcg tagcgatcgt 1860ttcaacacca tcgactacac cgtgagcaac ctgaccgcgt ggggctataa cgaagttcag 1920caagactaca aaaccctggg tggcagcatg ctgtacaagc tgattcagcg tggtgtgccg 1980aactggttcc cgtttaacag catcgcggtt atgcagccga tgtataccaa gaaagcgaac 2040gagcaaattg cgaaagaaat cggcaccttc gaccagtaca ccctggacga tccgaaagct 2100ccgccgaagg tggcggttct gaccagcggt ccggcgatta aacagatcct gagcaacacc 2160aagcaatatg tggttccgtg gctgaagccg ctgaacaccc tgttcccggg caagaaagac 2220ttcggttggt ttatgctggc gggtgatcag ccgcaaaact acacccaccg tgcgaacttt 2280agcaaagcga tgagcaagat cccgaacatg cacaacgcgg ttcacgcgtt cattgagcgt 2340gaaggcacca aactgatcaa caaggagacc tttaccctga agaaaggtct ggaccaaatt 2400gatattatcc gtgacgtggc gatcccgctg aacacccagc tgctggcgga cctgttctat 2460tttgatctgc gtaccgagga aaacccggat ggcaaactgg gtgtggcgga actgtaccgt 2520agcctgctgg acattcgtat ctggggcgtt aacaacaacg atccggcgca ggcgtggaac 2580cgtcgtcgtc gtgcgcaaga gggtgcgaaa cgtatgattg aaaccaccaa gaccattgtt 2640gcggaggcgg atgcgggtcg tccgcgtggt attggcctgg ttagcgcggt tgcgaaccgt 2700atcggtgcgc gtagctatct gaagaaagat agcctgcgta gctgcggcct gaaactggtg 2760gaggaactgc tggcgcaggg taacaacgtg gaccaagtta ccgataacct gtggctgacc 2820gcgttcggtg gcattggcgt gccggttacc gcgttttatg aagtgctgag cttctttctg 2880cgtccggaga acgaagcgat ttgggcggaa gtgcaggcga tcgcgcaaaa gggtgacgat 2940gcgaccctgc atgcgtacgt ggcggaagcg cagcgtatga ccagcagcca acgtaacgtg 3000cgtgttgcga ccgcgccggg cgaggttcaa ggtcaagcga ttcaaccggg taccgcggtg 3060gttctgatgc tgggtgaagc gggtcgtaac ccgaaagaag tgccggacgc gggcaagttc 3120aacccgcaac gtaagaaaga agatgttagc gcgtttagct acggccagca cgagtgcatt 3180gcgaaggacg tggcgctggc gttcgttacc ggtctgatca aactggtggc ggatctgaaa 3240gaactgcgtc cggcgccggg tcagatgggt accgtgaaaa ccatccaagt tggcaccgag 3300aaggcgtatc tgaacgacag ctggagctac ctgggttttg atgcgagcac ctggaaagtg 3360cacttcaacg gtcacggcaa gggtaaattt gagggcgaac gtgttccgac caagagcacc 3420ccgattcagg aatactatta cctgctgcaa aagcgtaaag acgagatcct gggtaactaa 3480tgaaagctt 3489651158PRTFusarium oxysporum 65Met His His His His His His Met Ser Phe Asn Glu Lys Phe Gln Ala1 5 10 15Gly Glu Ser Tyr Gly Asp Ser Lys Glu Asp Pro Ser Ser Leu Leu Asn 20 25 30Asn Pro Glu Lys Leu Val Ala Asp Leu Met Lys Asp Phe Ala Gly Val 35 40 45Arg Ser Gln Ala Ser Pro Ala Gln Leu Leu Gly Leu Val Lys Glu Leu 50 55 60Leu Gln Lys Gly Gln Pro Leu Asp Asp Lys Lys Gly Thr Thr Glu Leu65 70 75 80Leu Ile Gly Ile Leu Thr Ala Leu Pro Ala Thr Ser Lys Ala Arg Thr 85 90 95Ala Leu Thr Asn Lys Leu Ile Asp Thr Leu Trp Gly Asn Leu Gln His 100 105 110Pro Pro Leu Ser Tyr Met Gly Gly Asp Val Lys Tyr Asp Val Val Asn 115 120 125Ser Asp Lys Pro Ala His Lys His Asn Cys Glu Leu Tyr Asp Thr Ile 130 135 140Glu Phe Lys Val Pro Gly Thr Asp Val Leu Leu Arg Glu Gln Val Pro145 150 155 160Gln Ala Pro Asp Gly Leu His Gln Tyr Arg Met Pro Asp Gly Ser Phe 165 170 175Asn Asn Ile Leu Glu Pro Asn Leu Gly Arg Ala Gly Thr Pro Tyr Ala 180 185 190Lys Ser Val Lys Ser Glu Lys Arg Leu His Gly Val Lys Pro Asp Pro 195 200 205Gly Leu Leu Phe Asp Leu Leu Met Ala Arg Asp Glu Thr Thr Phe Gln 210 215 220Glu Asn Pro Ala Gly Ile Ser Ser Met Leu Phe Tyr His Ala Ala Ile225 230 235 240Ile Ile His Asp Ile Phe Arg Thr Asn Arg Thr Asp Met Asn Lys Ser 245 250 255Asp Thr Ser Ser Tyr Leu Asp Leu Ala Pro Leu Tyr Gly Ser Ser Leu 260 265 270Lys Asp Gln His Glu Ile Arg Thr Met Lys Glu Gly Lys Leu Lys Pro 275 280 285Asp Thr Phe His Glu Lys Arg Leu Leu Gly Gln Pro Ala Gly Val Asn 290 295 300Val Met Leu Val Leu Tyr Ser Arg Phe His Asn Tyr Val Ala Asp Ile305 310 315 320Leu Leu Lys Ile Asn Glu Asn Gly Arg Phe Ser Leu Ser Val Pro Pro 325 330 335Asn Ala Ser Glu Glu Asp Lys Ala Lys Ala Ile Ala Lys Gln Asp His 340 345 350Asp Leu Phe Asn Val Ala Arg Leu Ile Thr Gly Gly Leu Tyr Ile Asn 355 360 365Ile Cys Leu His Asp Tyr Leu Arg Ala Ile Thr Asn Thr His His Ser 370 375 380Ala Ser Asp Trp Thr Leu Asp Pro Arg Val Ala Ile Asp Lys Gln Phe385 390 395 400Asp Gly Asp Gly Val Pro Arg Gly Val Gly Asn Gln Val Ser Val Glu 405 410 415Phe Asn Leu Leu Tyr Arg Phe His Ser Cys Ile Ser Lys Arg Asp Glu 420 425 430Lys Trp Ile Asn Asn Phe Phe Leu Lys Leu Phe Pro Gly Arg Lys Ala 435 440 445Glu Asp Leu Gln Asp Val Ser Trp Thr Glu Leu Gly Gln Ala Leu Leu 450 455 460Ile Phe Glu Gln Asn Thr Pro Lys Asp Pro Ser Val Arg Thr Phe Asp465 470 475 480Gly Leu Glu Arg Gln Ala Asp Gly Thr Phe Lys Asp Glu Asp Leu Val 485 490 495Arg Ile Leu Lys Asp Ala Met Glu Asp Pro Ala Gly Thr Phe Gly Ala 500 505 510Arg Met Val Pro Lys Ala Leu Lys Val Val Glu Val Leu Gly Ile Ile 515 520 525Gln Gly Arg Lys Trp Gln Cys Ala Ser Leu Asn Glu Phe Arg Glu Phe 530 535 540Phe Gly Leu Lys Arg Tyr Asp Ser Phe Ser Glu Ile Asn Ser Asn Pro545 550 555 560Asp Ile Ala Asn Ile Leu Glu Lys Leu Tyr Thr Asp Pro Asp Met Val 565 570 575Glu Leu Tyr Pro Gly Leu Met Ile Glu Asp Ile Lys Pro Gln Arg Asn 580 585 590Pro Gly Ser Gly Ile Met Pro Thr Tyr Ser Val Gly Arg Ala Val Leu 595 600 605Ser Asp Ala Val Thr Leu Val Arg Ser Asp Arg Phe Asn Thr Ile Asp 610 615 620Tyr Thr Val Ser Asn Leu Thr Ala Trp Gly Tyr Asn Glu Val Gln Gln625 630 635 640Asp Tyr Lys Thr Leu Gly Gly Ser Met Leu Tyr Lys Leu Ile Gln Arg 645 650 655Gly Val Pro Asn Trp Phe Pro Phe Asn Ser Ile Ala Val Met Gln Pro 660 665 670Met Tyr Thr Lys Lys Ala Asn Glu Gln Ile Ala Lys Glu Ile Gly Thr 675 680 685Phe Asp Gln Tyr Thr Leu Asp Asp Pro Lys Ala Pro Pro Lys Val Ala 690 695 700Val Leu Thr Ser Gly Pro Ala Ile Lys Gln Ile Leu Ser Asn Thr Lys705 710 715 720Gln Tyr Val Val Pro Trp Leu Lys Pro Leu Asn Thr Leu Phe Pro Gly 725 730 735Lys Lys Asp Phe Gly Trp Phe Met Leu Ala Gly Asp Gln Pro Gln Asn 740 745 750Tyr Thr His Arg Ala Asn Phe Ser Lys Ala Met Ser Lys Ile Pro Asn 755 760 765Met His Asn Ala Val His Ala Phe Ile Glu Arg Glu Gly Thr Lys Leu 770 775 780Ile Asn Lys Glu Thr Phe Thr Leu Lys Lys Gly Leu Asp Gln Ile Asp785 790 795 800Ile Ile Arg Asp Val Ala Ile Pro Leu Asn Thr Gln Leu Leu Ala Asp 805 810 815Leu Phe Tyr Phe Asp Leu Arg Thr Glu Glu Asn Pro Asp Gly Lys Leu 820 825 830Gly Val Ala Glu Leu Tyr Arg Ser Leu Leu Asp Ile Arg Ile Trp Gly 835 840 845Val Asn Asn Asn Asp Pro Ala Gln Ala Trp Asn Arg Arg Arg Arg Ala 850 855 860Gln Glu Gly Ala Lys Arg Met Ile Glu Thr Thr Lys Thr Ile Val Ala865 870 875 880Glu Ala Asp Ala Gly Arg Pro Arg Gly Ile Gly Leu Val Ser Ala Val 885 890 895Ala Asn Arg Ile Gly Ala Arg Ser Tyr Leu Lys Lys Asp Ser Leu Arg 900 905 910Ser Cys Gly Leu Lys Leu Val Glu Glu Leu Leu Ala Gln Gly Asn Asn 915 920 925Val Asp Gln Val Thr Asp Asn Leu Trp Leu Thr Ala Phe Gly Gly Ile 930 935 940Gly Val Pro Val Thr Ala Phe Tyr Glu Val Leu Ser Phe Phe Leu Arg945 950 955 960Pro Glu Asn Glu Ala Ile Trp Ala Glu Val Gln Ala Ile Ala Gln Lys 965 970 975Gly Asp Asp Ala Thr Leu His Ala Tyr Val Ala Glu Ala Gln Arg Met 980 985 990Thr Ser Ser Gln Arg Asn Val Arg Val Ala Thr Ala Pro Gly Glu Val 995 1000 1005Gln Gly Gln Ala Ile Gln Pro Gly Thr Ala Val Val Leu Met Leu 1010 1015 1020Gly Glu Ala Gly Arg Asn Pro Lys Glu Val Pro Asp Ala Gly Lys 1025 1030 1035Phe Asn Pro Gln Arg Lys Lys Glu Asp Val Ser Ala Phe Ser Tyr 1040 1045 1050Gly Gln His Glu Cys Ile Ala Lys Asp Val Ala Leu Ala Phe Val 1055 1060 1065Thr Gly Leu Ile Lys Leu Val Ala Asp Leu Lys Glu Leu Arg Pro 1070 1075 1080Ala Pro Gly Gln Met Gly Thr Val Lys Thr Ile Gln Val Gly Thr 1085 1090 1095Glu Lys Ala Tyr Leu Asn Asp Ser Trp Ser Tyr Leu Gly Phe Asp 1100 1105 1110Ala Ser Thr Trp Lys Val His Phe Asn Gly His Gly Lys Gly Lys 1115 1120 1125Phe Glu Gly Glu Arg Val Pro Thr Lys Ser Thr Pro Ile Gln Glu 1130 1135 1140Tyr Tyr Tyr Leu Leu Gln Lys Arg Lys Asp Glu Ile Leu Gly Asn 1145 1150 1155663522DNAArtificial SequenceCodon optimized artificial DNA sequence 66aagcttggat ccggctcttc tggtagtgga gaaaatctat attttcaagg aatggatggg 60gcagttaggc tagattggac cggcctggat ctgaccggtc acgagatcca cgacggtgtg 120ccgattgcga gccgtgtgca ggttatggtg agcttcccgc tgtttaagga ccaacacatc 180attatgagca gcaaagaaag cccgagccgt aagagcagca ccatcggcca gagcacccgt 240aacggtagct gccaagcgga tacccagaaa ggccaactgc cgccggttgg cgagaagccg 300aaaccggtga aagaaaaccc gatgaagaaa ctgaaggaga tgagccaacg tccgctgccg 360acccaacatg gtgatggtac ctatccgacc gagaagaaac tgaccggtat cggcgaagac 420ctgaaacaca ttcgtggcta cgatgttaag accctgctgg cgatggtgaa gagcaaactg 480aagggcgaga aactgaagga cgataagacc atgctgatgg aacgtgttat gcagctggtt 540gcgcgtctgc cgaccgagag caagaaacgt gcggaactga ccgacagcct gatcaacgag 600ctgtgggaaa gcctggatca cccgccgctg aactacctgg gcccggaaca cagctatcgt 660accccggacg gtagctacaa ccacccgttt aacccgcaac tgggtgcggc gggtagccgt 720tatgcgcgta gcgttatccc gaccgttacc ccgccgggtg cgctgccgga cccgggtctg 780attttcgata gcatcatggg tcgtaccccg aacagctatc gtaagcaccc gaacaacgtt 840agcagcattc tgtggtactg ggcgaccatc attatccacg atatcttttg gaccgacccg 900cgtgatatta acaccaacaa aagcagcagc tatctggacc tggcgccgct gtacggcaac 960agccaggaga tgcaagacag catccgtacc ttcaaagatg gtcgtatgaa gccggactgc 1020tatgcggata aacgtctggc gggtatgccg ccgggcgtta gcgtgctgct gatcatgttc 1080aaccgttttc acaaccacgt ggcggagaac ctggcgctga ttaacgaagg tggccgtttt 1140aacaaaccga gcgatctgct ggagggtgaa gcgcgtgaag cggcgtggaa gaaatacgac 1200aacgacctgt tccaggttgc gcgtctggtg accagcggtc tgtatattaa catcaccctg 1260gttgactacg tgcgtaacat cgttaacctg aaccgtgtgg ataccacctg gaccctggac 1320ccgcgtcaag atgcgggtgc gcatgttggt accgcggatg gtgcggagcg tggtaccggt 1380aacgctgtga gcgcggaatt taacctgtgc taccgttggc acagctgcat cagcgagaaa 1440gatagcaagt tcgttgaagc gcagttccaa aacatttttg gtaaaccggc gagcgaggtg 1500cgcccggacg aaatgtggaa aggcttcgcg aaaatggaac aaaacacccc ggcggacccg 1560ggtcaacgta ccttcggtgg ctttaaacgt ggtccggatg gcaagtttga cgatgacgat 1620ctggttcgtt gcatcagcga ggcggtggaa gatgttgcgg gtgcgtttgg tgcgcgtaac 1680gtgccgcagg cgatgaaggt ggttgagacc atgggcatta tccaaggtcg taaatggaac 1740gttgcgggtc tgaacgaatt ccgtaaacac tttcacctga agccgtatag caccttcgag 1800gacattaaca gcgatccggg cgtggcggaa gcgctgcgtc gtctgtatga ccacccggat 1860aacgttgagc tgtacccggg tctggtggcg gaggaagata agcaaccgat ggttccgggt 1920gtgggtattg cgccgaccta taccattagc cgtgtggttc tgagcgatgc ggtttgcctg 1980gtgcgtggcg accgtttcta caccaccgat tttaccccgc gtaacctgac caactggggc 2040tacaaagaag ttgactatga tctgagcgtt aaccacggtt gcgtgttcta caagctgttt 2100atccgtgcgt tcccgaacca ctttaaacag aacagcgtgt acgcgcacta tccgatggtg 2160gttccgagcg agaacaagcg tattctggaa gcgctgggtc gtgcggacct gttcgatttt 2220gaggcgccga aatatatccc gccgcgtgtt aacattacca gctacggtgg cgcggaatat 2280atcctggaga cccaggaaaa atacaaggtg acctggcacg agggtctggg cttcctgatg 2340ggcgaaggtg gcctgaaatt tatgctgagc ggtgacgatc cgctgcacgc gcagcaacgt 2400aaatgcatgg cggcgcaact gtataaggac ggctggaccg aagcggttaa agcgttttac 2460gcgggtatga tggaggaact gctggttagc aagagctatt tcctgggtaa caacaaacac 2520cgtcacgttg acattatccg tgatgtgggc aacatggttc acgtgcactt cgcgagccag 2580gtttttggtc tgccgctgaa aaccgcgaag aacccgaccg gcgtgttcac cgagcaagaa 2640atgtacggta ttctggcggc gatctttacc accattttct ttgacctgga tccgagcaag 2700agcttcccgc tgcgtaccaa gacccgtgag gtttgccaga aactggcgaa gctggttgaa 2760gcgaacgtga aactgattaa caagatcccg tggagccgtg

gcatgtttgt gggtaaaccg 2820gcgaaggacg agccgctgag catctatggc aagaccatga ttaaaggcct gaaggcgcac 2880ggtctgagcg actacgatat tgcgtggagc catgtggttc cgaccagcgg tgcgatggtt 2940ccgaaccagg cgcaagtttt cgcgcaggcg gtggattact atctgagccc ggcgggtatg 3000cactacattc cggaaatcca catggtggcg ctgcaaccga gcaccccgga gaccgatgcg 3060ctgctgctgg gctatgcgat ggaaggtatt cgtctggcgg gtacctttgg cagctaccgt 3120gaggcggcgg ttgacgatgt ggttaaggaa gacaacggcc gtcaggttcc ggtgaaagcg 3180ggtgatcgtg ttttcgtgag ctttgtggac gcggcgcgtg atccgaaaca cttcccggat 3240ccggaagtgg ttaacccgcg tcgtccggcg aagaaataca tccactatgg tgttggtccg 3300catgcgtgcc tgggtcgtga tgcgagccag attgcgatca ccgaaatgtt ccgttgcctg 3360tttcgtcgtc gtaacgttcg tcgtgtgccg ggtccgcaag gtgaactgaa gaaagttccg 3420cgtccgggtg gcttctacgt gtatatgcgt gaagactggg gtggcctgtt cccgtttccg 3480gttaccatgc gtgtgatgtg ggacgatgag taatgactcg ag 3522671557PRTMagnaporthe oryzae 67Met Gly Ser Ser His His His His His His Gly Thr Lys Thr Glu Glu1 5 10 15Gly Lys Leu Val Ile Trp Ile Asn Gly Asp Lys Gly Tyr Asn Gly Leu 20 25 30Ala Glu Val Gly Lys Lys Phe Glu Lys Asp Thr Gly Ile Lys Val Thr 35 40 45Val Glu His Pro Asp Lys Leu Glu Glu Lys Phe Pro Gln Val Ala Ala 50 55 60Thr Gly Asp Gly Pro Asp Ile Ile Phe Trp Ala His Asp Arg Phe Gly65 70 75 80Gly Tyr Ala Gln Ser Gly Leu Leu Ala Glu Ile Thr Pro Asp Lys Ala 85 90 95Phe Gln Asp Lys Leu Tyr Pro Phe Thr Trp Asp Ala Val Arg Tyr Asn 100 105 110Gly Lys Leu Ile Ala Tyr Pro Ile Ala Val Glu Ala Leu Ser Leu Ile 115 120 125Tyr Asn Lys Asp Leu Leu Pro Asn Pro Pro Lys Thr Trp Glu Glu Ile 130 135 140Pro Ala Leu Asp Lys Glu Leu Lys Ala Lys Gly Lys Ser Ala Leu Met145 150 155 160Phe Asn Leu Gln Glu Pro Tyr Phe Thr Trp Pro Leu Ile Ala Ala Asp 165 170 175Gly Gly Tyr Ala Phe Lys Tyr Glu Asn Gly Lys Tyr Asp Ile Lys Asp 180 185 190Val Gly Val Asp Asn Ala Gly Ala Lys Ala Gly Leu Thr Phe Leu Val 195 200 205Asp Leu Ile Lys Asn Lys His Met Asn Ala Asp Thr Asp Tyr Ser Ile 210 215 220Ala Glu Ala Ala Phe Asn Lys Gly Glu Thr Ala Met Thr Ile Asn Gly225 230 235 240Pro Trp Ala Trp Ser Asn Ile Asp Thr Ser Lys Val Asn Tyr Gly Val 245 250 255Thr Val Leu Pro Thr Phe Lys Gly Gln Pro Ser Lys Pro Phe Val Gly 260 265 270Val Leu Ser Ala Gly Ile Asn Ala Ala Ser Pro Asn Lys Glu Leu Ala 275 280 285Lys Glu Phe Leu Glu Asn Tyr Leu Leu Thr Asp Glu Gly Leu Glu Ala 290 295 300Val Asn Lys Asp Lys Pro Leu Gly Ala Val Ala Leu Lys Ser Tyr Glu305 310 315 320Glu Glu Leu Ala Lys Asp Pro Arg Ile Ala Ala Thr Met Glu Asn Ala 325 330 335Gln Lys Gly Glu Ile Met Pro Asn Ile Pro Gln Met Ser Ala Phe Trp 340 345 350Tyr Ala Val Arg Thr Ala Val Ile Asn Ala Ala Ser Gly Arg Gln Thr 355 360 365Val Asp Glu Ala Leu Lys Asp Ala Gln Thr Gly Thr Asp Tyr Asp Ile 370 375 380Pro Thr Thr Lys Leu Gly Ser Gly Ser Ser Gly Ser Gly Glu Asn Leu385 390 395 400Tyr Phe Gln Gly Met Asp Gly Ala Val Arg Leu Asp Trp Thr Gly Leu 405 410 415Asp Leu Thr Gly His Glu Ile His Asp Gly Val Pro Ile Ala Ser Arg 420 425 430Val Gln Val Met Val Ser Phe Pro Leu Phe Lys Asp Gln His Ile Ile 435 440 445Met Ser Ser Lys Glu Ser Pro Ser Arg Lys Ser Ser Thr Ile Gly Gln 450 455 460Ser Thr Arg Asn Gly Ser Cys Gln Ala Asp Thr Gln Lys Gly Gln Leu465 470 475 480Pro Pro Val Gly Glu Lys Pro Lys Pro Val Lys Glu Asn Pro Met Lys 485 490 495Lys Leu Lys Glu Met Ser Gln Arg Pro Leu Pro Thr Gln His Gly Asp 500 505 510Gly Thr Tyr Pro Thr Glu Lys Lys Leu Thr Gly Ile Gly Glu Asp Leu 515 520 525Lys His Ile Arg Gly Tyr Asp Val Lys Thr Leu Leu Ala Met Val Lys 530 535 540Ser Lys Leu Lys Gly Glu Lys Leu Lys Asp Asp Lys Thr Met Leu Met545 550 555 560Glu Arg Val Met Gln Leu Val Ala Arg Leu Pro Thr Glu Ser Lys Lys 565 570 575Arg Ala Glu Leu Thr Asp Ser Leu Ile Asn Glu Leu Trp Glu Ser Leu 580 585 590Asp His Pro Pro Leu Asn Tyr Leu Gly Pro Glu His Ser Tyr Arg Thr 595 600 605Pro Asp Gly Ser Tyr Asn His Pro Phe Asn Pro Gln Leu Gly Ala Ala 610 615 620Gly Ser Arg Tyr Ala Arg Ser Val Ile Pro Thr Val Thr Pro Pro Gly625 630 635 640Ala Leu Pro Asp Pro Gly Leu Ile Phe Asp Ser Ile Met Gly Arg Thr 645 650 655Pro Asn Ser Tyr Arg Lys His Pro Asn Asn Val Ser Ser Ile Leu Trp 660 665 670Tyr Trp Ala Thr Ile Ile Ile His Asp Ile Phe Trp Thr Asp Pro Arg 675 680 685Asp Ile Asn Thr Asn Lys Ser Ser Ser Tyr Leu Asp Leu Ala Pro Leu 690 695 700Tyr Gly Asn Ser Gln Glu Met Gln Asp Ser Ile Arg Thr Phe Lys Asp705 710 715 720Gly Arg Met Lys Pro Asp Cys Tyr Ala Asp Lys Arg Leu Ala Gly Met 725 730 735Pro Pro Gly Val Ser Val Leu Leu Ile Met Phe Asn Arg Phe His Asn 740 745 750His Val Ala Glu Asn Leu Ala Leu Ile Asn Glu Gly Gly Arg Phe Asn 755 760 765Lys Pro Ser Asp Leu Leu Glu Gly Glu Ala Arg Glu Ala Ala Trp Lys 770 775 780Lys Tyr Asp Asn Asp Leu Phe Gln Val Ala Arg Leu Val Thr Ser Gly785 790 795 800Leu Tyr Ile Asn Ile Thr Leu Val Asp Tyr Val Arg Asn Ile Val Asn 805 810 815Leu Asn Arg Val Asp Thr Thr Trp Thr Leu Asp Pro Arg Gln Asp Ala 820 825 830Gly Ala His Val Gly Thr Ala Asp Gly Ala Glu Arg Gly Thr Gly Asn 835 840 845Ala Val Ser Ala Glu Phe Asn Leu Cys Tyr Arg Trp His Ser Cys Ile 850 855 860Ser Glu Lys Asp Ser Lys Phe Val Glu Ala Gln Phe Gln Asn Ile Phe865 870 875 880Gly Lys Pro Ala Ser Glu Val Arg Pro Asp Glu Met Trp Lys Gly Phe 885 890 895Ala Lys Met Glu Gln Asn Thr Pro Ala Asp Pro Gly Gln Arg Thr Phe 900 905 910Gly Gly Phe Lys Arg Gly Pro Asp Gly Lys Phe Asp Asp Asp Asp Leu 915 920 925Val Arg Cys Ile Ser Glu Ala Val Glu Asp Val Ala Gly Ala Phe Gly 930 935 940Ala Arg Asn Val Pro Gln Ala Met Lys Val Val Glu Thr Met Gly Ile945 950 955 960Ile Gln Gly Arg Lys Trp Asn Val Ala Gly Leu Asn Glu Phe Arg Lys 965 970 975His Phe His Leu Lys Pro Tyr Ser Thr Phe Glu Asp Ile Asn Ser Asp 980 985 990Pro Gly Val Ala Glu Ala Leu Arg Arg Leu Tyr Asp His Pro Asp Asn 995 1000 1005Val Glu Leu Tyr Pro Gly Leu Val Ala Glu Glu Asp Lys Gln Pro 1010 1015 1020Met Val Pro Gly Val Gly Ile Ala Pro Thr Tyr Thr Ile Ser Arg 1025 1030 1035Val Val Leu Ser Asp Ala Val Cys Leu Val Arg Gly Asp Arg Phe 1040 1045 1050Tyr Thr Thr Asp Phe Thr Pro Arg Asn Leu Thr Asn Trp Gly Tyr 1055 1060 1065Lys Glu Val Asp Tyr Asp Leu Ser Val Asn His Gly Cys Val Phe 1070 1075 1080Tyr Lys Leu Phe Ile Arg Ala Phe Pro Asn His Phe Lys Gln Asn 1085 1090 1095Ser Val Tyr Ala His Tyr Pro Met Val Val Pro Ser Glu Asn Lys 1100 1105 1110Arg Ile Leu Glu Ala Leu Gly Arg Ala Asp Leu Phe Asp Phe Glu 1115 1120 1125Ala Pro Lys Tyr Ile Pro Pro Arg Val Asn Ile Thr Ser Tyr Gly 1130 1135 1140Gly Ala Glu Tyr Ile Leu Glu Thr Gln Glu Lys Tyr Lys Val Thr 1145 1150 1155Trp His Glu Gly Leu Gly Phe Leu Met Gly Glu Gly Gly Leu Lys 1160 1165 1170Phe Met Leu Ser Gly Asp Asp Pro Leu His Ala Gln Gln Arg Lys 1175 1180 1185Cys Met Ala Ala Gln Leu Tyr Lys Asp Gly Trp Thr Glu Ala Val 1190 1195 1200Lys Ala Phe Tyr Ala Gly Met Met Glu Glu Leu Leu Val Ser Lys 1205 1210 1215Ser Tyr Phe Leu Gly Asn Asn Lys His Arg His Val Asp Ile Ile 1220 1225 1230Arg Asp Val Gly Asn Met Val His Val His Phe Ala Ser Gln Val 1235 1240 1245Phe Gly Leu Pro Leu Lys Thr Ala Lys Asn Pro Thr Gly Val Phe 1250 1255 1260Thr Glu Gln Glu Met Tyr Gly Ile Leu Ala Ala Ile Phe Thr Thr 1265 1270 1275Ile Phe Phe Asp Leu Asp Pro Ser Lys Ser Phe Pro Leu Arg Thr 1280 1285 1290Lys Thr Arg Glu Val Cys Gln Lys Leu Ala Lys Leu Val Glu Ala 1295 1300 1305Asn Val Lys Leu Ile Asn Lys Ile Pro Trp Ser Arg Gly Met Phe 1310 1315 1320Val Gly Lys Pro Ala Lys Asp Glu Pro Leu Ser Ile Tyr Gly Lys 1325 1330 1335Thr Met Ile Lys Gly Leu Lys Ala His Gly Leu Ser Asp Tyr Asp 1340 1345 1350Ile Ala Trp Ser His Val Val Pro Thr Ser Gly Ala Met Val Pro 1355 1360 1365Asn Gln Ala Gln Val Phe Ala Gln Ala Val Asp Tyr Tyr Leu Ser 1370 1375 1380Pro Ala Gly Met His Tyr Ile Pro Glu Ile His Met Val Ala Leu 1385 1390 1395Gln Pro Ser Thr Pro Glu Thr Asp Ala Leu Leu Leu Gly Tyr Ala 1400 1405 1410Met Glu Gly Ile Arg Leu Ala Gly Thr Phe Gly Ser Tyr Arg Glu 1415 1420 1425Ala Ala Val Asp Asp Val Val Lys Glu Asp Asn Gly Arg Gln Val 1430 1435 1440Pro Val Lys Ala Gly Asp Arg Val Phe Val Ser Phe Val Asp Ala 1445 1450 1455Ala Arg Asp Pro Lys His Phe Pro Asp Pro Glu Val Val Asn Pro 1460 1465 1470Arg Arg Pro Ala Lys Lys Tyr Ile His Tyr Gly Val Gly Pro His 1475 1480 1485Ala Cys Leu Gly Arg Asp Ala Ser Gln Ile Ala Ile Thr Glu Met 1490 1495 1500Phe Arg Cys Leu Phe Arg Arg Arg Asn Val Arg Arg Val Pro Gly 1505 1510 1515Pro Gln Gly Glu Leu Lys Lys Val Pro Arg Pro Gly Gly Phe Tyr 1520 1525 1530Val Tyr Met Arg Glu Asp Trp Gly Gly Leu Phe Pro Phe Pro Val 1535 1540 1545Thr Met Arg Val Met Trp Asp Asp Glu 1550 1555

Claims

1. A detergent composition comprising: a) one or more hydroperoxy fatty acid producing enzyme capable of converting one or more fatty acids into one or more hydroperoxy fatty acids, wherein the hydroperoxy fatty acid producing enzymes are selected from the group consisting of oleate lipoxygenases, linoleate lipoxygenases, arachidonate lipoxygenases, and mixtures thereof; b) one or more hydroperoxy fatty acid converting enzyme capable of converting said hydroperoxy fatty acids into one or more derivatives of hydroperoxy fatty acids, wherein the hydroperoxy fatty acid converting enzymes are selected from the group consisting of cyclooxygenases (EC 1.14.99.1), allene oxide synthases (EC 4.2.1.92), hydroperoxide isomerases (EC 4.2.1.92, EC 5.3.99.1, EC 5.4.4.5, EC 5.4.4.6), hydroperoxide lyases (EC 4.2.1.92), hydroperoxide dehydratases (EC 4.2.1.92), divinyl ether synthases (EC 4.2.1.121, EC 4.2.1.B8, EC 4.2.1.B9), 9,12-octadecadienoate 8-hydroperoxide 8R-isomerases (EC 5.4.4.5), 9,12-octadecadienoate 8-hydroperoxide 8S-isomerases (EC 5.4.4.6), 7,10-hydroperoxide diol synthases, epoxy alcohol synthases, and mixtures therefore; and c) a surfactant system.

2. The composition according to claim 1, wherein the hydroperoxy fatty acid producing enzymes are selected from the group consisting of oleate 10S-lipoxygenases (EC 1.13.11.77), linoleate 8R-lipoxygenases (EC 1.13.11.60), linoleate 9R-lipoxygenases (EC 1.13.11.61), linoleate 9S-lipoxygenases (EC 1.13.11.58), linoleate 10R-lipoxygenases (EC 1.13.11.62), linoleate 10S-lipoxygenases, linoleate 13S-lipoxygenases (EC 1.13.11.12), and mixtures thereof

3. The composition according to claim 1, wherein the hydroperoxy fatty acid converting enzymes are selected from the group consisting of allene oxide synthases (EC 4.2.1.92), hydroperoxide isomerases (EC 4.2.1.92, EC 5.3.99.1, EC 5.4.4.5, EC 5.4.4.6), hydroperoxide lyases (EC 4.2.1.92), hydroperoxide dehydratases (EC 4.2.1.92), 7,10-hydroperoxide diol synthases, epoxy alcohol synthases, and mixtures thereof.

4. The composition according to claim 1, further comprising one or more co-enzymes selected from the group consisting of fatty-acid peroxidases (EC 1.11.1.3), unspecific peroxygenases (EC 1.11.2.1), plant seed peroxygenases (EC 1.11.2.3), fatty acid peroxygenases (EC1.11.2.4), linoleate diol synthases (EC 1.13.11.44), 5,8-linoleate diol synthases (EC 1.13.11.60 and EC 5.4.4.5), 7,8-linoleate diol synthases (EC 1.13.11.60 and EC 5.4.4.6), 9,14-linoleate diol synthases (EC 1.13.11.B1), 8,11-linoleate diol synthases, oleate diol synthases, other linoleate diol synthases, unspecific monooxygenase (EC 1.14.14.1), alkane 1-monooxygenase (EC 1.14.15.3), oleate 12-hydroxylases (EC 1.14.18.4), alpha-dioxygenases, fatty acid amide hydrolase (EC 3.5.1.99), oleate hydratases (EC 4.2.1.53), linoleate isomerases (EC 5.2.1.5), linoleate (10E,12Z)-isomerases (EC 5.3.3.B2), fatty acid decarboxylases (OleT-like), iron-dependent decarboxylases (UndA-like), amylases, lipases, proteases, cellulases, and mixtures thereof.

5. The composition according to claim 1, wherein each of the hydroperoxy fatty acid producing enzymes and the hydroperoxy fatty acid converting enzymes are present in an amount of from about 0.001 wt % to about 0.2 wt %, by weight of the composition, based on active protein.

6. The composition according to claim 1, wherein the surfactant system is present in an amount of from about 5 wt % to about 50 wt %, by weight of the composition.

7. The composition according to claim 1, wherein: a) hydroperoxy fatty acid producing enzymes which are selected from the group consisting of oleate 10S-lipoxygenases (EC 1.13.11.77) and linoleate 105-lipoxygenases, and mixtures thereof, having at least 60% identity as calculated over the entire length of a sequence aligned against the entire length of at least one reference sequence selected from a wild-type Pseudomonas aeruginosa 10S-dioxygenase selected from the group consisting of: SEQ ID NO: 16, SEQ ID NO: 17, or SEQ ID NO: 18, and the wild-type Nostoc punctiforme linoleate 10S-lipoxygenases SEQ ID NO: 15; and b) the hydroperoxy fatty acid converting enzymes are 7,10-hydroperoxide diol synthases having at least about 60% identity as calculated over the entire length of a sequence aligned against the entire length of at least one reference sequence selected from the group consisting of a wild-type Pseudomonas aeruginosa 7,10-oleate diol synthase selected from the group consisting of: SEQ ID NO: 36, SEQ ID NO: 37, or SEQ ID NO: 38.

8. A method of manually washing dishware, comprising the step of: delivering a composition according to claim 1 into a volume of water to form a wash solution and immersing the soiled articles in the wash solution, wherein the soil on the soiled articles comprises at least one unsaturated fatty acid selected from the group consisting of: mono unsaturated fatty acids, di unsaturated fatty acids, tri unsaturated fatty acids, tetra unsaturated fatty acids, penta unsaturated fatty acids, hexa unsaturated fatty acids, and mixtures thereof.

9. The method according to claim 8, wherein the soil on the soiled articles comprises at least one unsaturated fatty acid selected from the group consisting of: palmitoleic acid, oleic acid, linoleic acid, .alpha.-linolenic acid, .gamma.-linolenic acid, and mixtures thereof.

10. A detergent composition comprising: a) at least one fatty acid processing fusion enzyme, wherein the at least one fatty acid processing fusion enzyme comprises at least two catalytic domains: a. a hydroperoxy fatty acid producing domain capable of converting one or more fatty acids into one or more hydroperoxy fatty acids; b. a hydroperoxy fatty acid converting domain capable of converting said hydroperoxy fatty acids into one or more derivatives of hydroperoxy fatty acids; and b) a surfactant system.

11. The detergent composition according to claim 10, wherein the hydroperoxy fatty acid producing catalytic domain of the fusion enzyme exhibits at least one activity selected from the group consisting of: oleate lipoxygenases, linoleate lipoxygenases, arachidonate lipoxygenases, and mixtures thereof.

12. The detergent composition according to claim 11 wherein the hydroperoxy fatty acid producing catalytic domain of the fusion enzyme exhibits at least one activity selected from the group consisting of: oleate 10S-lipoxygenases (EC 1.13.11.77), linoleate 8R-lipoxygenases (EC 1.13.11.60), linoleate 9R-lipoxygenases (EC 1.13.11.61), linoleate 9S-lipoxygenases (EC 1.13.11.58), linoleate 10R-lipoxygenases (EC 1.13.11.62), linoleate 10S-lipoxygenases), linoleate 13S-lipoxygenases (EC 1.13.11.12), alpha-dioxygenases (EC 1.14.99), and mixtures thereof.

13. The detergent composition according to claim 12, wherein the hydroperoxy fatty acid producing catalytic domain of the fusion enzyme exhibits at least one activity selected from the group consisting of: linoleate 9S-lipoxygenases (EC 1.13.11.58), linoleate 10R-lipoxygenases (EC 1.13.11.62), and mixtures thereof.

14. The detergent composition according to claim 10, wherein the hydroperoxy fatty acid converting catalytic domain of the fusion enzyme exhibits at least one activity selected from the group consisting of: cyclooxygenases (EC 1.14.99.1), allene oxide synthases (AOS--EC 4.2.1.92), hydroperoxide isomerases (EC 4.2.1.92, EC 5.3.99.1, EC 5.4.4.5, EC 5.4.4.6), hydroperoxide lyases (HPL--EC 4.2.1.92), hydroperoxide dehydratases (EC 4.2.1.92), divinyl ether synthases (DES--EC 4.2.1.121, EC 4.2.1.B8, EC 4.2.1.B9), 9,12-octadecadienoate 8-hydroperoxide 8R-isomerases (EC 5.4.4.5), 9,12-octadecadienoate 8-hydroperoxide 8S-isomerases (EC 5.4.4.6), 7,10-hydroperoxide diol synthases), epoxy alcohol synthases (EAS), and mixtures thereof.

15. The detergent composition according to claim 14, wherein the hydroperoxy fatty acid converting catalytic domain of the fusion enzyme exhibits at least one activity selected from the group consisting of: allene oxide synthases (AOS--EC 4.2.1.92), epoxy alcohol synthases (EAS), and mixtures thereof.

16. The detergent composition according to claim 10, wherein the fusion enzyme has at least about 60% identity as calculated over the entire length of a sequence aligned against the entire length of at least one reference sequence selected from the wild-type multi-domain enzymes selected from the group consisting of: Plexaura homomalla 8R-DOX-AOS (SEQ ID NO: 47), Fusarium oxysporum 9S-DOX-AOS (SEQ ID NO: 48), Colletotrichum graminicola 9S-DOX-AOS (SEQ ID NO: 49), Glomerella cingulate 9S-DOX-AOS (SEQ ID NO: 50), Aspergillus niger 9R-DOX-AOS (SEQ ID NO: 51), Magnaporthe oryzae 10R-DOX-EAS (SEQ ID NO: 52), Glomerella cingulate 10R-DOX-EAS (SEQ ID NO: 53), or Fusarium oxysporum 10R-DOX-EAS (SEQ ID NO: 54).

17. The detergent composition according to claim 10, wherein the at least one fatty acid processing fusion enzyme is present in an amount of from about 0.001 wt % to about 0.2 wt %, by weight of the composition, based on active protein.

18. The detergent composition according to claim 10, further comprising one or more co-enzymes selected from the group consisting of: fatty-acid peroxidases (EC 1.11.1.3), unspecific peroxygenases (EC 1.11.2.1), plant seed peroxygenases (EC 1.11.2.3), fatty acid peroxygenases (EC1.11.2.4), linoleate diol synthases (EC 1.13.11.44), 5,8-linoleate diol synthases (EC 1.13.11.60 and EC 5.4.4.5), 7,8-linoleate diol synthases (EC 1.13.11.60 and EC 5.4.4.6), 9,14-linoleate diol synthases (EC 1.13.11.B1), 8,11-linoleate diol synthases, oleate diol synthases, other linoleate diol synthases, unspecific monooxygenase (EC 1.14.14.1), alkane 1-monooxygenase (EC 1.14.15.3), alpha-dioxygenases, oleate 12-hydroxylases (EC 1.14.18.4), fatty acid amide hydrolase (EC 3.5.1.99), oleate hydratases (EC 4.2.1.53), linoleate isomerases (EC 5.2.1.5), linoleate (10E,12Z)-isomerases (EC 5.3.3.B2), fatty acid decarboxylases (OleT-like), iron-dependent decarboxylases (UndA-like), amylases, lipases, proteases, cellulases, and mixtures thereof.

19. The detergent composition according to claim 10, wherein the surfactant system is present in an amount of from about 5 wt % to about 50 wt %, by weight of the composition.

20. A method of manually washing dishware, comprising the step of: delivering a composition according to claim 10 into a volume of water to form a wash solution and immersing the soiled articles in the wash solution, wherein the soil on the soiled articles comprise at least one saturated or unsaturated fatty acid, and mixtures thereof; and wherein the at least one fatty acid processing fusion enzyme is present at a concentration of from about 0.005 ppm to about 15 ppm, based on active protein, in the wash solution during the washing step.