Anti-inflammatory peptides and their uses

Abstract

The present invention discloses an anti-inflammatory peptide, which comprises an anti-inflammatory fragment of a protein selected from SEQUENCE ID NO: 1-16, the anti-inflammatory fragment having a length of 7 to 37 amino acids and a charge of -9 to +3; wherein the C-terminal amino acid is not cysteine (C) or methionine (M), and the N-terminal amino acid is not cysteine (C), histidine (H), proline (P) or threonine (T). The anti-inflammatory fragment does not contain cysteine (C). The anti-inflammatory fragment is from a region of the protein of SEQUENCE ID NO: 1-16, the region being characterized by a length of 17 to 109 amino acids and a charge of -6 to +4, wherein the C-terminal amino acid of the region is not aspartic acid (D), phenylalanine (F), methionine (M) or tryptophan (W), and the N-terminal amino acid of the region is not aspartic acid (D), histidine (H), methionine (M), proline (P) or tryptophan (W). Examples of the peptide are provided in SEQUENCE ID NO: 71-221.

Description

[0001] Divisional application

[0002] This application is a divisional application of the application with the application number 201680051932.6, the filing date of July 18, 2016, and the title of "Anti-inflammatory peptides and their uses". Background art

[0003] It is estimated that a staggering two billion people worldwide suffer from some type of inflammation. Inflammation is a huge biological process and an essential part of our immune response. The inflammatory response can be acute (short-lived) or chronic (more persistent), and can occur in almost every part of the body, whether it is internal or external. Additionally, interestingly, regardless of the cause of the inflammation, the biological changes that occur in the body due to the inflammatory response are the same throughout the body, meaning that the pattern of reducing inflammation by different anti-inflammatory agents is the same in all parts of the body.

[0004] Generally, inflammation is a natural response and a necessary response to rid cells of the cause of injury, foreign invasion, or to remove dead cells. However, excessive inflammation has a great impact on the human body and can sometimes have adverse effects. In fact, the inflammatory response can have lasting adverse consequences, such as tissue damage. During the inflammatory response, the body releases lysosomal enzymes, which can damage tissues and even cause life-threatening hypersensitivity reactions. These conditions can have lasting effects both externally and internally, causing acute rashes and eczema externally and triggering diseases such as inflammatory bowel disease internally. Therefore, maintaining normal levels of inflammation is very important for our physical and mental health, both in the body and externally. Unfortunately, inflammation is on the rise. One of the main factors contributing to this increase comes from our exposure to an increasing number of external agents to which our bodies are not accustomed.

[0005] Most of the anti-inflammatory treatments used today are drugs. There are two main types of anti-inflammatory drugs, corticosteroids and non-steroidal anti-inflammatory drugs (NSAIDs). These include: immunosuppressants (methotrexate, cyclosporine); specific biopharmaceuticals (mainly TNF-α inhibitors, but also including inhibitors of, for example, cyclooxygenase); cytotoxic drugs; and oral retinoids (acitretin). Additionally, there are topical treatments that specifically reduce skin inflammation. Examples include creams and ointments (mainly based on cortisone), and physical therapies such as ultraviolet radiation. However, these drugs have strong side effects, such as gastrointestinal toxicity and anaphylactoid reactions. They can even suppress the immune system to the extent that it is vulnerable to other diseases and pathogens.

[0006] Thus, it is clear that there is a need to identify reagents with anti-inflammatory activity that do not immunosuppress and / or cause other adverse side effects. To this end, it is known that some very specific types of foods can reduce inflammation (Kiecolt-Glaser J.K. et al., 2010, Middleton E. et al., 2000, Chatterjee M. et al., 2005). In fact, the specific components of these special foods are present in low concentrations, are cryptic or "locked away", and once identified and unlocked, can be amplified in an approved manner to specifically target inflammation because our bodies recognize the components of food and can easily process these molecules. In fact, these specific food molecules can reduce inflammation without completely blocking this immune system response and leaving the body vulnerable. Similarly, for those individuals who are allergic to multiple foods, identifying and unlocking the specific components of foods that can reduce inflammation will allow these individuals to obtain the anti-inflammatory benefits of foods to which they would otherwise be allergic.

[0007] The object of the present invention is to overcome at least one of the above problems. Summary of the Invention

[0008] The pea genome encodes more than 70,000 different proteins. The Applicant has identified seven of these proteins, each of which contains one or more anti-inflammatory fragments. Similarly, among the more than 60,000 proteins encoded by the rice genome, the present Applicant has identified eight proteins, each of which contains one or more anti-inflammatory fragments. When incubated with LPS-stimulated human cells, the anti-inflammatory fragments of the 16 identified proteins have been shown to have anti-inflammatory activity ( Figures 1 to 19 ), do not cause problems with human cell viability ( Figure 20 ), and are not toxic to human cells ( Figure 21)。The specific plant proteins from which the native peptides are derived are provided in SEQUENCE ID NO:1-15 and 353-355, particularly regions from the proteins provided in SEQUENCE ID NO:17-69. The specific pea proteins from which the peptides are derived are provided in SEQUENCE ID NO:1-5, 8 and 9, while the specific rice proteins from which the peptides are derived are provided in SEQUENCE ID NO:6, 7 and 10-15. Homologues of these proteins are described in SEQUENCE ID NO:222-267. The specific peptides initially identified in pea proteins are shown in SEQUENCE ID NO:71-107 and 110-111. The specific peptides initially identified in rice proteins are shown in SEQUENCE ID NO:108-109 and 112-220. Additional peptides of the invention identified in pea and rice proteins are provided herein, such as those provided in SEQUENCE ID NO:320, 331-352 and 356-424. The peptides of the invention encompass peptides containing or consisting of any of the above peptides.

[0009] EWQINEK (SEQ ID 331) - fragment of rice protein of SEQ ID 7

[0010] FLPQHTD (SEQ ID 332) - fragment of pea protein of SEQ ID 1

[0011] GPQQYAEWQINEK (SEQ ID 333) - fragment of rice protein of SEQ ID 7

[0012] PGQLQSFLLSGN (SEQ ID 334) - fragment of pea protein of SEQ ID 1

[0013] PGQLQSFLLSGNQNQQNYLSGF (SEQ ID 335) - fragment of pea protein of SEQ ID 1

[0014] PQQYAEWQ (SEQ ID 336) - fragment of rice protein of SEQ ID 7

[0015] QLQSFLLSGNQNQQNYLSGFSK (SEQ ID 337) - fragment of pea protein of SEQ ID 1

[0016] QNQQNYLSGFSK (SEQ ID 338) - fragment of pea protein of SEQ ID 1

[0017] Fragment of pea protein of QSFLLSGNQNQQ (SEQ ID 339) - SEQ ID 1

[0018] QSFLLSGNQ (SEQ ID 340) - Fragment of pea protein of SEQ ID 1

[0019] RGPQQYA (SEQ ID 341) - Fragment of rice protein of SEQ ID 7

[0020] DALEPDNR (SEQ ID 342) - Fragment of pea protein of SEQ ID 354

[0021] SEEGYYGEQQQQPGMTR (SEQ ID 343) - Fragment of rice protein of SEQ ID 353

[0022] GYYGEQQQQPGMTR (SEQ ID 344) - Fragment of rice protein of SEQ ID 353

[0023] IDGYDTPVEGR (SEQ ID 345) - Fragment of rice protein of SEQ ID 15

[0024] NGVLRPGQL (SEQ ID 346) - Fragment of rice protein of SEQ ID 14

[0025] RHGEWGPSY (SEQ ID 347)

[0026] FWM (SEQ ID 348) - Fragment of pea protein of SEQ ID 3

[0027] TVFDGVLRPGQL [SEQ ID 349] - Fragment of rice protein of SEQ ID 10

[0028] RLQSQNDQRGEIIHVK [SEQ ID 350] - Fragment of rice protein of SEQ ID 10

[0029] HGPVEMPYTLLYPSSK [SEQ ID 351] - Fragment of pea protein of SEQ ID 355

[0030] LDALEPDNR [SEQ ID 352] - Fragment of pea protein of SEQ ID 354

[0031] RGPQQYAEWQINE [SEQ ID 320] - Fragment of rice protein of SEQ ID 7

[0032] The peptides of the present invention are mainly used to reduce inflammation, and thus can be used for preventing or treating inflammatory conditions and maintaining the intestinal health of mammals.

[0033] In a first aspect, the present invention provides a peptide having a length generally from 3 to 50 amino acids and comprising a fragment of a protein disclosed herein, such as a fragment selected from SEQUENCE ID NO: 1-16, 349 or 350 or homologues thereof, or a variant or fragment of said peptide (hereinafter referred to as "the peptide of the present invention"). In one embodiment, the peptide or its variant or fragment has biological activity. In one embodiment, the peptide or its variant or fragment has anti-inflammatory activity.

[0034] In one embodiment, the peptide of the present invention comprises a sequence selected from SEQUENCE ID NO: 17-220, 268-352 and 356-424.

[0035] In one embodiment, the peptide of the present invention consists essentially of a sequence selected from SEQUENCE ID NO: 17-220, 268-352 and 356-424.

[0036] In one embodiment, the peptide consists of 3-50 amino acids. In one embodiment, the peptide consists of 4-50 amino acids. In one embodiment, the peptide consists of 5-50 amino acids. In one embodiment, the peptide consists of 6-50 amino acids.

[0037] In one embodiment, the fragment has 7 to 37 amino acids and a charge between -9 and +3.

[0038] Preferably, the C-terminal amino acid is not cysteine (C) or methionine (M).

[0039] Preferably, the N-terminal amino acid is not cysteine (C), histidine (H), proline (P) or threonine (T).

[0040] Preferably, the C-terminal domain of the fragment does not contain cysteine (C).

[0041] Preferably, the N-terminal domain of the fragment does not contain cysteine (C).

[0042] Preferably, the fragment does not contain cysteine (C).

[0043] Preferably, the peptide does not contain cysteine (C).

[0044] Preferably, the fragment is from a region of the protein of SEQUENCE ID NO: 1-16, which is characterized by:

[0045] - ranging from 17 to 109 amino acids in length;

[0046] - having a charge between -6 and +4;

[0047] - the C-terminal amino acid is not aspartic acid (D), phenylalanine (F), methionine (M), or tryptophan (W);

[0048] - the N-terminal amino acid is not aspartic acid (D), histidine (H), methionine (M), proline (P), or tryptophan (W).

[0049] Preferably, the C-terminal domain of this region does not contain tryptophan (W).

[0050] Preferably, the region of the protein of SEQUENCE ID NO: 1-7 is selected from SEQUENCE ID NO: 17-33.

[0051] Preferably, the region of the protein of SEQUENCE ID NO: 8-16 is selected from SEQUENCE ID NO: 34-70.

[0052] Preferably, the region of the protein of SEQUENCE ID NO: 1-16 is selected from SEQUENCE ID NO: 17-70.

[0053] Preferably, the fragment is selected from SEQUENCE ID NO: 71-221, or a variant of the fragment.

[0054] Preferably, the peptide consists of a fragment selected from SEQUENCE ID NO: 71-221 or a variant of the fragment.

[0055] Preferably, the peptide consists of a sequence selected from SEQUENCE ID NO: 71-221.

[0056] In one embodiment, the peptide comprises a fragment of pea protein, wherein the fragment is selected from SEQUENCE ID NO: 71-107, 332, 334, 335, 337-340, 342, 348, and 351-352.

[0057] In one embodiment, the peptide comprises a fragment of pea protein, wherein the fragment is selected from SEQUENCE ID NO: 71-107, 332, 334, 335, 337-340, 342, 348, and 351-352. In one embodiment, the fragment is selected from 339, 352, 351, 93, 92, 75, 76, 105.

[0058] In one embodiment, the peptide comprises a fragment of rice protein, wherein the fragment is selected from SEQUENCE ID NO: 108-109, 112-220, 320, 331, 333, 336, 341, 343-346, 349-350. In one embodiment, the fragment is selected from 341, 144, 320, 349, 350, 177, 343-346.

[0059] In one embodiment, the peptide is a modified peptide. In one embodiment, the peptide is modified with a protecting group. In one embodiment, the peptide is modified to increase its lipophilicity. In one embodiment, the peptide is modified to increase its half-life. In one embodiment, the N-terminal or C-terminal amino acid of the peptide is modified. In one embodiment, the N-terminal or C-terminal amino acid of the peptide is modified with a protecting group.

[0060] The invention also provides a conjugate comprising the peptide of the invention conjugated to a binding partner. In one embodiment, the peptide of the invention is modified with a reactive group configured to allow conjugation to the binding partner.

[0061] [SEQUENCE ID NO: 1 (Pea Protein 1)]

[0062] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO: 1, or a homolog thereof, or a bioactive variant of the protein fragment.

[0063] Preferably, the peptide comprises a bioactive fragment of one of the seven regions of SEQUENCE ID NO: 1, namely SEQUENCE ID NO: 17-23, or a bioactive variant of the protein fragment.

[0064] Preferably, the peptide comprises a bioactive fragment selected from SEQUENCE ID NO: 71-91 or 360, or a bioactive variant of the protein fragment.

[0065] Preferably, the peptide comprises a fragment of the region of SEQUENCE ID NO: 17, such as SEQUENCE ID NO: 71, or a bioactive variant of the protein fragment.

[0066] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO: 18, such as SEQUENCE ID NO: 72, or a bioactive variant of the fragment.

[0067] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:19, such as any one or both of SEQUENCE ID NO:73 or 74, or a bioactive variant of the fragment.

[0068] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:20, such as any one or both of SEQUENCE ID NO:75 or 76, or a bioactive variant of the fragment.

[0069] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:21, such as one or more or all of SEQUENCE ID NO:77 - 84, or a bioactive variant of the fragment.

[0070] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:22, such as one or more or all of SEQUENCE ID NO:85 - 89, or a bioactive variant of the fragment.

[0071] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:23, such as SEQUENCE ID NO:90, or a bioactive variant of the fragment.

[0072] Preferably, the peptide comprises SEQUENCE ID NO:91, or a bioactive variant of the fragment.

[0073] The present invention also provides a composition comprising at least one peptide of the present invention, the peptide comprising a fragment of SEQUENCE ID NO:1 or its homolog. The present invention also provides a composition comprising at least 2, preferably 3, preferably 4, preferably 5, preferably 6, preferably 7, preferably 8, preferably 9 or preferably 10 peptides of the present invention, each of which comprises a different fragment of SEQUENCE ID NO:1 or its homolog. Preferably, the peptide or peptides are bioactive. Preferably, the peptide or peptides are anti - inflammatory. Preferably, the composition comprises a first peptide and a second peptide of the present invention, the first peptide comprising a fragment of a first region selected from SEQUENCE ID NO:17 - 23, and the second peptide comprising a fragment of a second region selected from SEQUENCE ID NO:17 - 23. Preferably, the composition comprises a first bioactive peptide (which comprises a first bioactive fragment selected from SEQUENCE ID NO:71 - 91 (or a bioactive variant of the fragment)), and a second bioactive peptide (which comprises a second bioactive fragment selected from SEQUENCE ID NO:71 - 91 (or a bioactive variant of the fragment)).

[0074] Homologs of pea protein 1 (SEQUENCE ID NO:1) include homologs from Vicia fabia, Cicer arietinum, and Lens culinaris (SEQ ID NO:222 - 224).

[0075] [SEQUENCE ID NO: 2 (Pea Protein 2)]

[0076] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:2, or a homolog thereof.

[0077] Preferably, the peptide comprises a bioactive fragment of one of the two regions of SEQUENCE ID NO:2, namely SEQUENCE ID NO:24 or 25.

[0078] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:24, such as SEQUENCE ID NO:92, or a bioactive variant of the fragment.

[0079] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:25, such as SEQUENCE ID NO:93, or a bioactive variant of the fragment.

[0080] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, wherein the peptide comprises a bioactive fragment of SEQUENCE ID NO:2 or a homolog thereof. The present invention also provides a composition comprising at least two bioactive peptides of the present invention, each peptide comprising a different bioactive fragment of SEQUENCE ID NO:2 or a homolog thereof. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment of the region containing SEQUENCE ID NO 24 and a second bioactive peptide comprising a bioactive fragment of the region containing SEQUENCE ID NO 25. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment of SEQUENCE ID NO 92 and a second bioactive peptide comprising a bioactive fragment of SEQUENCE ID NO 93.

[0081] Homologs of pea protein 2 (SEQUENCE ID NO:2) include Lens culinaris, Vicia narbonensis, and Glycine max (SEQ ID NO:225 - 227).

[0082] [SEQUENCE ID NO: 3 (Pea Protein 3)]

[0083] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:3, or a homolog thereof.

[0084] Preferably, the peptide comprises a bioactive fragment of one of the two regions of SEQUENCE ID NO:3, namely SEQUENCE ID NO:26 or 27.

[0085] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:26, such as SEQUENCE ID NO:94, or a bioactive variant of the fragment.

[0086] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:27, such as SEQUENCE ID NO:95, or a bioactive variant of the fragment.

[0087] The present invention also provides a composition comprising at least the bioactive peptide of the present invention, wherein the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:3 or a homolog thereof. The present invention also provides a composition comprising at least two bioactive peptides of the present invention, wherein each peptide comprises a different bioactive fragment of the protein of SEQUENCE ID NO:3 or a homolog thereof. Preferably, the composition comprises a first peptide comprising a bioactive fragment of the region containing SEQUENCE ID NO 26 and a second peptide comprising a bioactive fragment of SEQUENCE ID NO 27. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment of SEQUENCE ID NO94 (or a bioactive variant of the fragment) and a second bioactive peptide comprising a bioactive fragment of SEQUENCE ID NO95 (or a bioactive variant of the fragment).

[0088] Homologs of pea protein 3 (SEQUENCE ID NO:3) include Vicia sativa, Medicago truncatula, and Lotus japonicas (SEQ ID NO:228 - 230).

[0089] [SEQUENCE ID NO: 4 (Pea Protein 4)]

[0090] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:4, or a homolog thereof.

[0091] Preferably, the peptide comprises a bioactive fragment of one of the five regions of SEQUENCE ID NO:4, namely SEQUENCE ID NO:28 - 32. Preferably, the region is SEQUENCE ID NO:28, preferably SEQUENCE ID NO:29, preferably SEQUENCE ID NO:30, preferably SEQUENCE ID NO:31, preferably SEQUENCE ID NO:32.

[0092] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:28, such as SEQUENCE ID NO:96, or a bioactive variant of the fragment.

[0093] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:29, such as SEQUENCE ID NO:97 - 103, or a bioactive variant of the fragment.

[0094] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:30, such as SEQUENCE ID NO:104, or a bioactive variant of the fragment.

[0095] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:31, such as SEQUENCE ID NO:105, or a bioactive variant of the fragment.

[0096] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:32, such as SEQUENCE ID NO:106, or a bioactive variant of the fragment.

[0097] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, said peptide comprising a bioactive fragment of SEQUENCE ID NO:4 or a homolog thereof. The present invention also provides a composition comprising at least 2, preferably 3, preferably 4, preferably 5, preferably 6, preferably 7, preferably 8, preferably 9 or preferably 10 peptides containing different bioactive fragments of SEQUENCE ID NO:4 or homologs thereof. Preferably, the composition comprises a first peptide containing a bioactive fragment of a first region selected from SEQUENCE ID NO:28-32, and a second peptide containing a bioactive fragment of a second region selected from SEQUENCE ID NO:28-32. Preferably, the composition comprises a first bioactive peptide (which comprises a first bioactive fragment (or a bioactive variant of the fragment) selected from SEQUENCE ID NO:96-106), and a second bioactive peptide (which comprises a second bioactive fragment (or a bioactive variant of the fragment) selected from SEQUENCE ID NO:96-106).

[0098] Homologs of pea protein 4 (SEQUENCE ID NO:4) include Pisum abyssinicum, Lathyrus annuus, and Vicia villosa (SEQ ID 231-233).

[0099] [SEQUENCE ID NO: 5 (Pea Protein 5)]

[0100] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:5, or a homolog thereof.

[0101] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:5, i.e., the region of SEQUENCE ID NO 33, such as SEQUENCE ID NO:107, or a bioactive variant of the fragment.

[0102] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, said peptide comprising a bioactive fragment of SEQUENCE ID NO:5 or a homolog thereof. The present invention also provides a composition comprising at least two peptides of the present invention, which comprise at least one bioactive fragment of SEQUENCE ID NO:5 or a homolog thereof, such as SEQUENCE ID NO:107.

[0103] Homologs of pea protein 5 (SEQUENCE ID NO:5) include Medicago truncatula, Vicia peregrine, and Vicia lutea (SEQ ID NO:234 - 236).

[0104] [SEQUENCE ID NO: 6 (Rice Protein 7 - Q6K508)]

[0105] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:6, or a homolog thereof.

[0106] Preferably, the peptide comprises a bioactive fragment of SEQUENCE ID NO:108, or a bioactive variant of the fragment.

[0107] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, wherein the peptide comprises a bioactive fragment of SEQUENCE ID NO:6 or a homolog thereof. The present invention also provides a composition comprising at least two peptides of the present invention, which comprises at least one bioactive fragment of SEQUENCE ID NO:6 or a homolog thereof, such as SEQUENCE ID NO:108 (SP1).

[0108] Homologs of rice protein 7 (SEQUENCE ID NO:6) include Oryza brachyantha, Avena sativa, and Brachypodium distachyon (SEQ ID NO:237 - 239).

[0109] [SEQUENCE ID NO: 7 (Rice Protein 8 - Q6K7K6)]

[0110] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:7, or a homolog thereof.

[0111] Preferably, the peptide comprises a bioactive fragment of SEQUENCE ID NO:109 (SP2), or a bioactive variant of the fragment.

[0112] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, wherein the peptide comprises a bioactive fragment of SEQUENCE ID NO:7 or a homolog thereof. The present invention also provides a composition comprising at least two peptides of the present invention, which comprises at least one bioactive fragment of SEQUENCE ID NO:7 or a homolog thereof, such as SEQUENCE ID NO:109 (SP2).

[0113] Homologs of rice protein 8 (SEQUENCE ID NO:7) include rice of the Oryza sativa Japonica Group, rice of the Oryza sativa Indica Group, and Oryza brachyantha (SEQ ID NO:240 - 242).

[0114] [SEQUENCE ID NO: 8 (Pea Protein 6 - P13919)]

[0115] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:8 or a homolog thereof.

[0116] Preferably, the peptide comprises a bioactive fragment of SEQUENCE ID NO:110 (SP3), or a bioactive variant of the fragment.

[0117] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, wherein the peptide comprises a bioactive fragment of SEQUENCE ID NO:8 or a homolog thereof. The present invention also provides a composition comprising at least two peptides of the present invention, which comprises at least one bioactive fragment of SEQUENCE ID NO:8 or a homolog thereof, such as SEQUENCE ID NO:110 (SP3).

[0118] Homologs of pea protein 8 (SEQUENCE ID NO:8) include Pisum fulvum, Pisum abyssinicum, and Vicia villosa (SEQ ID NO:243 - 245).

[0119] [SEQUENCE ID NO: 9 (Pea Protein 7 - P02855)]

[0120] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:9, or a homolog thereof.

[0121] Preferably, the peptide comprises a bioactive fragment of SEQUENCE ID NO:111 (SP4), or a bioactive variant of the fragment.

[0122] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, wherein the peptide comprises a bioactive fragment of SEQUENCE ID NO:9 or a homolog thereof. The present invention also provides a composition comprising at least two peptides of the present invention, which comprises at least one bioactive fragment of SEQUENCE ID NO:9 or a homolog thereof, such as SEQUENCE ID NO:111 (SP4).

[0123] Homologs of pea protein 9 (SEQUENCE ID NO:9) include Lathyrus hirsutus, Lathyrus cicero, Lathyrus sativus (SEQ ID NO:246 - 248).

[0124] [SEQUENCE ID NO: 10 (Rice Protein 1 - P07728)]

[0125] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:10, or a homolog thereof.

[0126] Preferably, the peptide comprises a fragment of one of the nine regions of SEQUENCE ID NO:10, namely SEQUENCE ID NO:34 - 42. Preferably, the region is SEQUENCE ID NO:34, preferably SEQUENCE ID NO:35, preferably SEQUENCE ID NO:36, preferably SEQUENCE ID NO:37, preferably SEQUENCE ID NO:38, preferably SEQUENCE ID NO:39, preferably SEQUENCE ID NO:40, preferably SEQUENCE ID NO:41, preferably SEQUENCE ID NO:42.

[0127] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:34, such as SEQUENCE ID NO:112 or SEQUENCE ID NO:113, or a bioactive variant of the fragment.

[0128] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:35, such as SEQUENCE ID NO:114, or a bioactive variant of the fragment.

[0129] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:36, such as SEQUENCE ID NO:115 or SEQUENCE ID NO:116, or a bioactive variant of the fragment.

[0130] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:37, such as SEQUENCE ID NO:117 or SEQUENCE ID NO:118, or a bioactive variant of the fragment.

[0131] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:38, such as SEQUENCE ID NO:119, or a bioactive variant of such fragment.

[0132] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:39, such as SEQUENCE ID NO:120, 121 or 122, or a bioactive variant of such fragment.

[0133] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:40, such as SEQUENCE ID NO:123, or a bioactive variant of such fragment.

[0134] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:41, such as SEQUENCE ID NO:124, 125, 126, 127, 128 or 129, or a bioactive variant of such fragment.

[0135] Preferably, the peptide comprises a fragment of the region of SEQUENCE ID NO:42, such as SEQUENCE ID NO:130, 131 or 132, or a bioactive variant of such fragment.

[0136] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, wherein the peptide comprises a bioactive fragment of SEQUENCE ID NO:10 or its homolog. The present invention also provides a composition comprising at least 2, preferably 3, preferably 4, preferably 5, preferably 6, preferably 7, preferably 8, preferably 9 or preferably 10 peptides of the present invention, each peptide comprising a different bioactive fragment of SEQUENCE ID NO:10 or its homolog. Preferably, the composition comprises a first peptide containing a bioactive fragment of a first region selected from SEQUENCE ID NO:34-42, and a second peptide containing a bioactive fragment of a second region selected from SEQUENCE ID NO:34-42. Preferably, the composition comprises a first bioactive peptide (which comprises a first bioactive fragment (or a bioactive variant of such fragment) selected from SEQUENCE ID NO:112-132), and a second bioactive peptide (which comprises a second bioactive fragment (or a bioactive variant of such fragment) selected from SEQUENCE ID NO:112-132).

[0137] Homologs of rice protein 1 (SEQUENCE ID NO:10) include Oryza brachyantha and Zizania latifolia (SEQ ID NO:249 - 251).

[0138] [SEQUENCE ID NO: 11 (Rice Protein 2 - P07728)]

[0139] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:11, or a homolog thereof.

[0140] Preferably, the peptide comprises a bioactive fragment of one of the four regions of SEQUENCE ID NO:11, namely SEQUENCE ID NO:43 - 46. Preferably, the region is SEQUENCE ID NO:43, preferably SEQUENCE ID NO:44, preferably SEQUENCE ID NO:45, preferably SEQUENCE ID NO:46.

[0141] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:43, such as SEQUENCE ID NO:133, or a bioactive variant of the fragment.

[0142] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:44, such as SEQUENCE ID NO:134 - 137, or a bioactive variant of the fragment.

[0143] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:45, such as SEQUENCE ID NO:138 - 144, or a bioactive variant of the fragment.

[0144] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:46, such as SEQUENCE ID NO:145, or a bioactive variant of the fragment.

[0145] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, said peptide comprising a bioactive fragment of SEQUENCE ID NO:11 or a homolog thereof. The present invention also provides a composition comprising at least 2, preferably 3, preferably 4, preferably 5, preferably 6, preferably 7, preferably 8, preferably 9 or preferably 10 peptides of the present invention, wherein each peptide comprises a bioactive fragment of SEQUENCE ID NO:11 or a homolog thereof. Preferably, the composition comprises a first peptide containing a bioactive fragment of a first region selected from SEQUENCE ID NO:43-46, and a second peptide containing a bioactive fragment of a second region selected from SEQUENCE ID NO:43-46. Preferably, the composition comprises a first bioactive peptide (which comprises a first bioactive fragment selected from SEQUENCE ID NO:133-145 (or a bioactive variant of said fragment)), and a second bioactive peptide (which comprises a second bioactive fragment selected from SEQUENCE ID NO:133-145 (or a bioactive variant of said fragment)).

[0146] Homologs of rice protein 2 (SEQUENCE ID NO:11) include Oryza sativa Indica Group, Zizania latifolia, Avena sativa (SEQ ID NO:252-254).

[0147] [SEQUENCE ID NO: 12 (Rice Protein 3 - P07730)]

[0148] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:12, or a homolog thereof.

[0149] Preferably, the peptide comprises a bioactive fragment of one of the eight regions of SEQUENCE ID NO:12, namely SEQUENCE ID NO:47-54. Preferably, the region is SEQUENCE ID NO:47, preferably SEQUENCE ID NO:48, preferably SEQUENCE ID NO:49, preferably SEQUENCE ID NO:50, preferably SEQUENCE ID NO:51, preferably SEQUENCE ID NO:52, preferably SEQUENCE ID NO:53, preferably SEQUENCE ID NO:54.

[0150] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:47, such as SEQUENCE ID NO:146-150, or a bioactive variant of such fragment.

[0151] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:48, such as one of SEQUENCE ID NO:151-157, or a bioactive variant of such fragment.

[0152] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:49, such as one of SEQUENCE ID NO:158 or SEQUENCE ID NO:159, or a bioactive variant of such fragment.

[0153] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:50, such as one of SEQUENCE ID NO:160-162, or a bioactive variant of such fragment.

[0154] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:51, such as one of SEQUENCE ID NO:163 or 164, or a bioactive variant of such fragment.

[0155] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:52, such as SEQUENCE ID NO:165, or a bioactive variant of such fragment.

[0156] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:53, such as one of SEQUENCE ID NO:166-171, or a bioactive variant of such fragment.

[0157] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:54, such as one of SEQUENCE ID NO:172-176, or a bioactive variant of such fragment.

[0158] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, said peptide comprising a bioactive fragment of SEQUENCE ID NO:12 or a homolog thereof. The present invention also provides a composition comprising at least 2, preferably 3, preferably 4, preferably 5, preferably 6, preferably 7, preferably 8, preferably 9 or preferably 10 peptides of the present invention, wherein each peptide comprises a bioactive fragment of SEQUENCE ID NO:12 or a homolog thereof. Preferably, the composition comprises a first peptide containing a bioactive fragment of a first region selected from SEQUENCE ID NO:47-54, and a second peptide containing a bioactive fragment of a second region selected from SEQUENCE ID NO:47-54. Preferably, the composition comprises a first bioactive peptide (which comprises a first bioactive fragment (or a bioactive variant of the fragment) selected from SEQUENCE ID NO:146-172), and a second bioactive peptide (which comprises a second anti-inflammatory fragment (or a bioactive variant of the fragment) selected from SEQUENCE ID NO:146-172).

[0159] Homologs of rice protein 3 (SEQUENCE ID NO:12) include Oryza brachyantha and Brachypodium distachyon (SEQ ID NO:255-257).

[0160] [SEQUENCE ID NO: 13 (Rice Protein 4 - Q0D7S0)]

[0161] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:13, or a homolog thereof.

[0162] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:13, i.e., SEQUENCE ID NO55, such as SEQUENCE ID NO:177, or a bioactive variant of the fragment.

[0163] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, said peptide comprising a bioactive fragment of SEQUENCE ID NO:13 or a homolog thereof. The present invention also provides a composition comprising at least two peptides, wherein at least one of the peptides comprises a bioactive fragment of SEQUENCE ID NO:13 or a homolog thereof, such as SEQUENCE ID NO:177, or a bioactive variant of the fragment.

[0164] Homologs of rice protein 4 (SEQUENCE ID NO: 13) include Oryza sativa Indica Group, Zizania latifolia, and Avena sativa (SEQ ID NO: 252-254).

[0165] [SEQUENCE ID NO: 14 (Rice Protein 5 - P14614)]

[0166] Preferably, the peptide comprises a fragment of the protein of SEQUENCE ID NO: 14, or a homolog thereof.

[0167] Preferably, the peptide comprises a bioactive fragment of one of the seven regions of SEQUENCE ID NO: 14, namely SEQUENCE ID NO: 56-62. Preferably, the region is SEQUENCE ID NO: 56, preferably SEQUENCE ID NO: 57, preferably SEQUENCE ID NO: 58, preferably SEQUENCE ID NO: 59, preferably SEQUENCE ID NO: 60, preferably SEQUENCE ID NO: 61, preferably SEQUENCE ID NO: 62.

[0168] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO: 56, such as one of SEQUENCE ID NO: 178-180, or a bioactive variant of the fragment.

[0169] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO: 57, such as one of SEQUENCE ID NO: 181-182, or a bioactive variant of the fragment.

[0170] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO: 58, such as SEQUENCE ID NO: 183, or a bioactive variant of the fragment.

[0171] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO: 59, such as one of SEQUENCE ID NO: 184-190, or a bioactive variant of the fragment.

[0172] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO: 60, such as SEQUENCE ID NO: 191, or a bioactive variant of the fragment.

[0173] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:61, such as one of SEQUENCE ID NO:192-195, or a bioactive variant of such fragment.

[0174] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:62, such as one of SEQUENCE ID NO:196-197, or a bioactive variant of such fragment.

[0175] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, wherein the peptide comprises a bioactive fragment of SEQUENCE ID NO:14 or its homolog. The present invention also provides a composition comprising at least 2, preferably 3, preferably 4, preferably 5, preferably 6, preferably 7, preferably 8, preferably 9 or preferably 10 peptides of the present invention, wherein each peptide comprises a bioactive fragment of SEQUENCE ID NO:14 or its homolog. Preferably, the composition comprises a first peptide comprising a bioactive fragment of a first region selected from SEQUENCE ID NO:56-62, and a second peptide comprising a bioactive fragment of a second region selected from SEQUENCE ID NO:56-62. Preferably, the composition comprises a first bioactive peptide (which comprises a first bioactive fragment selected from SEQUENCE ID NO:178-197 (or a bioactive variant of such fragment)), and a second bioactive peptide (which comprises a second bioactive fragment selected from SEQUENCE ID NO:178-197 (or a bioactive variant of such fragment)).

[0176] Homologs of rice protein 5 (SEQUENCE ID NO:14) include Oryza sativa Japonica Group, Brachypodium distachyon (SEQ ID NO:261-263).

[0177] [SEQUENCE ID NO: 15 (Rice Protein 6 - Q0DEV5)]

[0178] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:15, or its homolog.

[0179] Preferably, the peptide comprises a bioactive fragment of one of the seven regions of SEQUENCE ID NO:15, namely SEQUENCE ID NO:63 - 67. Preferably, the region is SEQUENCE ID NO:63, preferably SEQUENCE ID NO:64, preferably SEQUENCE ID NO:65, preferably SEQUENCE ID NO:66, preferably SEQUENCE ID NO:67.

[0180] Preferably, the peptide comprises a fragment of the region of SEQUENCE ID NO:63, such as one of SEQUENCE ID NO:198 - 200, or a bioactive variant of the fragment.

[0181] Preferably, the peptide comprises a fragment of the region of SEQUENCE ID NO:64, such as one of SEQUENCE ID NO:201 - 203, or a bioactive variant of the fragment.

[0182] Preferably, the peptide comprises a fragment of the region of SEQUENCE ID NO:65, such as SEQUENCE ID NO:204, or a bioactive variant of the fragment.

[0183] Preferably, the peptide comprises a fragment of the region of SEQUENCE ID NO:66, such as one of SEQUENCE ID NO:205 - 208, or a bioactive variant of the fragment.

[0184] Preferably, the peptide comprises a fragment of the region of SEQUENCE ID NO:67, such as one of SEQUENCE ID NO:209 - 215, or a bioactive variant of the fragment.

[0185] Preferably, the peptide comprises a fragment of the region of SEQUENCE ID NO:68, such as one of SEQUENCE ID NO:216 - 219, or a bioactive variant of the fragment.

[0186] Preferably, the peptide comprises a fragment of the region of SEQUENCE ID NO:69, such as SEQUENCE ID NO:220, or a bioactive variant of the fragment.

[0187] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, said peptide comprising a bioactive fragment of SEQUENCE ID NO:15 or a homolog thereof. The present invention also provides a composition comprising at least 2, preferably 3, preferably 4, preferably 5, preferably 6, preferably 7, preferably 8, preferably 9, or preferably 10 peptides of the present invention, wherein each peptide comprises a bioactive fragment of SEQUENCE ID NO:15 or a homolog thereof. Preferably, the composition comprises a first peptide comprising a bioactive fragment of a first region selected from SEQUENCE ID NO:63-69, and a second peptide comprising a bioactive fragment of a second region selected from SEQUENCE ID NO:63-69. Preferably, the composition comprises a first bioactive peptide (which comprises a first bioactive fragment (or a bioactive variant of the fragment) selected from SEQUENCE ID NO:198-220), and a second bioactive peptide (which comprises a second bioactive fragment (or a bioactive variant of the fragment) selected from SEQUENCE ID NO:198-220).

[0188] Homologs of rice protein 6 (SEQUENCE ID NO:15) include common wild rice (Oryza rufipogon), medicinal wild rice (Oryza officinalis), and hulless barley (Hordeum vulgare subsp. vulgare) (SEQ ID NO:264-266).

[0189] [SEQUENCE ID NO: 16 (Bacterial Protein 1 - P0C1U8)]

[0190] Preferably, the peptide comprises a bioactive fragment of the protein of SEQUENCE ID NO:16, or a homolog thereof.

[0191] Preferably, the peptide comprises a bioactive fragment of the region of SEQUENCE ID NO:16, i.e., the region of SEQUENCE ID NO70. Generally, the peptide is SEQUENCE ID NO 221, or a bioactive variant of the fragment.

[0192] The present invention also provides a composition comprising at least one bioactive peptide of the present invention, said peptide comprising a bioactive fragment of SEQUENCE ID NO:16 or a homolog thereof. The present invention also provides a composition comprising at least two peptides of the present invention, wherein at least one of the peptides comprises a fragment of SEQUENCE ID NO:16 or a homolog thereof, such as SEQUENCE ID NO:212, or a bioactive variant of the fragment.

[0193] Homologs of bacterial protein 1 (SEQUENCE ID NO:16) include:

[0194] >gi|580560623|gb|EVF84961.1| Glutamyl endopeptidase [Staphylococcus aureus COAS6020]

[0195] >gi|580687002|gb|EVH10169.1| Glutamyl endopeptidase [Staphylococcus aureus UCIM6080]

[0196] >gi|751815683|gb|KIN24957.1| Glutamyl endopeptidase [Staphylococcus aureus MRSA_CVM43477]

[0197] >gi|781884797|dbj|BAR08486.1| Glutamyl endopeptidase precursor [Staphylococcus aureus subsp. aureus]

[0198] >gi|781887762|dbj|BAR11210.1| Glutamyl endopeptidase precursor [Staphylococcus aureus subsp. aureus]

[0199] The present invention also provides a bioactive composition comprising at least one, and preferably a plurality of, the bioactive peptides of the present invention, wherein each peptide of the present invention comprises a bioactive fragment of the protein described herein. In one embodiment, the protein is selected from SEQUENCE ID NO:1-16. Generally, the peptide or each peptide of the present invention is selected from, or comprises, a bioactive fragment selected from SEQUENCE ID NO:71-220, or a bioactive variant of said fragment.

[0200] In one embodiment, the composition comprises a peptide of the present invention, said peptide comprising a sequence selected from SEQUENCE ID NO:17-220, 268-352, and 356-424.

[0201] In one embodiment, the composition comprises a peptide of the present invention, said peptide consisting essentially of a sequence selected from SEQUENCE ID NO:17-220, 268-352, and 356-424.

[0202] Generally, the peptide or each peptide of the present invention is selected from, or comprises, a bioactive fragment selected from SEQUENCE ID NO:71-107 and 110-111, or a bioactive variant of said fragment.

[0203] Typically, the peptide or each peptide of the present invention is selected from, or comprises, an anti-inflammatory fragment selected from SEQUENCE ID NO: 108 - 109 and 112 - 220, or an anti-inflammatory variant of said fragment.

[0204] In one embodiment, the bioactive peptide, variant or fragment of the present invention is anti-inflammatory.

[0205] Preferably, the composition comprises at least two different peptides of the present invention.

[0206] Preferably, the composition comprises at least three different peptides of the present invention.

[0207] Preferably, the composition comprises at least four different peptides of the present invention.

[0208] Preferably, the composition comprises at least five different peptides of the present invention.

[0209] Preferably, the composition comprises at least six different peptides of the present invention.

[0210] Preferably, the composition comprises at least seven different peptides of the present invention.

[0211] Preferably, the composition comprises at least eight different peptides of the present invention.

[0212] Preferably, the composition comprises at least nine different peptides of the present invention.

[0213] Preferably, the composition comprises at least ten different peptides of the present invention.

[0214] In one embodiment, the present invention includes a composition comprising one or more of SEQUENCE ID NO: 71 - 107 and 110 - 111, or an anti-inflammatory variant of a fragment, or a mixture of anti-inflammatory fragments and variants.

[0215] In one embodiment, the composition comprises at least one, two, three, four, five or all of SEQUENCE ID NO 75, 91, 92, 93, 110 and 111.

[0216] In one embodiment, the composition comprises substantially all of the fragments SEQUENCE ID NO: 71 - 107 and 110 - 111.

[0217] In one embodiment, the present invention includes a composition comprising one or more of SEQUENCE ID NO: 108 - 109 and 112 - 220, or an anti-inflammatory variant of a fragment, or a mixture of anti-inflammatory fragments and variants.

[0218] In one embodiment, the composition comprises at least one, two, or three of SEQUENCE ID NO 108, 109, and 144.

[0219] In one embodiment, the composition of the present invention is rich in peptides with a molecular weight less than 10 KD. In one embodiment, the composition is depleted of cell debris.

[0220] In one embodiment, the composition of the present invention is a powder.

[0221] In one embodiment, the present invention includes a composition comprising substantially all fragments of SEQUENCE ID NO:108 - 109 and 112 - 220, or anti-inflammatory variants of the fragments, or a mixture of anti-inflammatory fragments and variants.

[0222] In one embodiment, the composition is a personal care composition. In one embodiment, the composition is a pharmaceutical composition. In one embodiment, the composition is a solid. In one embodiment, the composition is a semi-solid (i.e., cream, gel, or lotion). In one embodiment, the composition is a liquid.

[0223] The present invention also relates to an artificial personal care composition comprising the peptide of the present invention.

[0224] The present invention also relates to an artificial personal care composition comprising a composition of the peptide of the present invention.

[0225] In one embodiment, the personal care composition is a skin care product. In one embodiment, the personal care composition is a hair care product. In one embodiment, the personal care composition is a toothpaste product. In one embodiment, the personal care composition is a fragrance product. In one embodiment, the personal care composition is a deodorant product. In one embodiment, the personal care composition is an antiperspirant product. In one embodiment, the personal care composition is a soap. In one embodiment, the personal care composition is a liquid soap. In one embodiment, the personal care composition is a cream. In one embodiment, the personal care composition is a lotion. In one embodiment, the personal care composition is a gel. In one embodiment, the personal care composition is a powder.

[0226] The present invention also relates to the peptide of the present invention for treating or preventing inflammation in mammals.

[0227] The present invention also relates to a composition of the peptide of the present invention for treating or preventing inflammation in mammals.

[0228] The present invention also relates to a peptide of the present invention for treating or preventing inflammatory disorders in mammals.

[0229] The present invention also relates to a composition of a peptide of the present invention for treating or preventing inflammatory disorders in mammals.

[0230] In one embodiment, the inflammation is symptomatic inflammation.

[0231] In one embodiment, the inflammatory disorder is an inflammatory disorder of the joints. In one embodiment, the inflammatory disease is an inflammatory disorder of the cardiovascular system. In one embodiment, the inflammatory disorder is an autoimmune disease. In one embodiment, the inflammatory disorder is a pulmonary and airway inflammatory disease. In one embodiment, the inflammatory disorder is an intestinal inflammatory disorder. In one embodiment, the inflammatory disorder is dermatitis. In one embodiment, the inflammatory disorder is acne vulgaris. In one embodiment, the inflammatory disorder is psoriasis. In one embodiment, the inflammatory disorder is rheumatoid arthritis. In one embodiment, the inflammatory disorder is cardiovascular disease. In one embodiment, the inflammatory disorder is atherosclerosis. In one embodiment, the inflammatory disorder is type I diabetes. In one embodiment, the inflammatory disorder is Graves disease. In one embodiment, the inflammatory disorder is Guillain-Barre disease. In one embodiment, the inflammatory disorder is lupus. In one embodiment, the inflammatory disorder is psoriatic arthritis. In one embodiment, the inflammatory disorder is ulcerative colitis. In one embodiment, the inflammatory disorder is asthma. In one embodiment, the inflammatory disorder is cystic fibrosis. In one embodiment, the inflammatory disorder is COPD. In one embodiment, the inflammatory disorder is emphysema. In one embodiment, the inflammatory disorder is acute respiratory distress syndrome. In one embodiment, the inflammatory disorder is colitis. In one embodiment, the inflammatory disorder is inflammatory bowel disease.

[0232] The present invention also relates to a peptide of the present invention for treating or preventing pain in mammals.

[0233] The present invention also relates to a composition of a peptide of the present invention for treating or preventing pain in mammals.

[0234] The present invention also relates to a peptide of the present invention for treating or preventing metabolic disorders in mammals.

[0235] The present invention also relates to a composition of a peptide of the present invention for treating or preventing metabolic disorders in mammals.

[0236] In one embodiment, the metabolic disorder is pre-diabetes. In one embodiment, the metabolic disorder is diabetes. In one embodiment, the metabolic disorder is type 1 diabetes. In one embodiment, the metabolic disorder is type 2 diabetes. In one embodiment, the metabolic disorder is metabolic syndrome. In one embodiment, the metabolic disorder is obesity. In one embodiment, the metabolic disorder is diabetic dyslipidemia. In one embodiment, the metabolic disorder is hyperlipidemia. In one embodiment, the metabolic disorder is hypertension. In one embodiment, the metabolic disorder is hypertriglyceridemia. In one embodiment, the metabolic disorder is hyperfattyacidemia. In one embodiment, the metabolic disorder is hypercholesterolemia. In one embodiment, the metabolic disorder is hyperinsulinemia. In one embodiment, the metabolic disorder is MODY.

[0237] The invention also relates to a peptide of the invention for maintaining or restoring intestinal health in a mammal.

[0238] The invention also relates to a composition of a peptide of the invention for maintaining or restoring intestinal health in a mammal.

[0239] The invention also relates to a peptide of the invention for maintaining or restoring muscle health (e.g., lean tissue mass) in a mammal.

[0240] The invention also relates to a composition of a peptide of the invention for maintaining or restoring muscle health (e.g., lean tissue mass) in a mammal.

[0241] The invention also relates to a pharmaceutical composition comprising a peptide of the invention and a pharmaceutically acceptable carrier.

[0242] The invention also relates to a pharmaceutical composition comprising a composition of a peptide of the invention and a pharmaceutically acceptable carrier.

[0243] Such peptides can be used in personal care and pharmaceutical products to treat and maintain the health level of inflammation throughout the body. The present invention meets the great demand for food-derived specific peptides and peptide compositions that reduce inflammation in a manner that can be processed by the body without completely blocking the immune response and causing autoimmune problems and other unwanted side effects. The present invention ultimately helps two billion patients with inflammation.

[0244] The peptides of the present invention are used in the topical cosmetic or pharmaceutical compositions of the present invention at a cosmetically or pharmaceutically effective concentration to achieve the desired effect; preferably in a form of from 0.00000001% (by weight) to 20% (by weight), more preferably from 0.000001% (by weight) to 15% (by weight), still more preferably from 0.0001% (by weight) to 10% (by weight), and even more preferably from 0.0001% (by weight) to 5% (by weight), relative to the total weight of the composition. Ideally, the peptides of the present invention are preferably used at about 0.00001% w / w to about 0.5% w / w [0.1 to 5000 ppm], more preferably at 0.00005 w / w to about 0.05 w / w [0.5 to 500 ppm], and most preferably at about 0.0001 w / w to about 0.01 w / w [1 to 100 ppm] of the composition. Ideally, the peptides of the present invention are preferably used at about 0.0001% w / w to about 0.004% w / w of the composition.

[0245] For the compositions of the peptides of the present invention, a typical daily dose can be from 0.2 g to 100 g.

[0246] The peptides and compositions of the present invention can also be used for non-therapeutic treatment of inflammation. Examples of non-therapeutic treatment of inflammation include for reducing normal non-pathological inflammation, such as inflammation within muscles and joints after exercise.

[0247] The present invention also provides a topical composition comprising the peptides of the present invention. It should be understood that the topical composition can comprise a plurality of peptides, fragments and / or variants. In one embodiment, the topical composition comprises substantially all of the peptides. In one embodiment, the topical composition comprises substantially all of the variants. The topical compositions of the present invention can be present in formulations selected from the group consisting of creams, multiple emulsions, anhydrous compositions, aqueous dispersions, oils, milks, balms, foams, lotions, gels, gel creams, hydroalcoholic solutions, hydroxyglycolic acid solutions, cosmetics, personal care products, hydrogels, liniments, sera, soaps, dusting powders, pastes, semi-solid formulations, liniments, serum, shampoos, conditioners, ointments, any rinses, talc, mousses, powders, sprays, aerosols, solutions, suspensions, emulsions, syrups, elixirs, polysaccharide films, patches, gel patches, bandages, adhesive systems, water-in-oil emulsions, oil-in-water emulsions and silicone emulsions.

[0248] In one embodiment of the present invention, the emulsion contains lipids or oils. The emulsion can be, but is not limited to, oil-in-water, water-in-oil, water-in-oil-in-water, and silicone-in-water-in-oil emulsions. The emulsion can contain a humectant. The emulsion can contain an antifoaming agent such as silicone. The emulsion can have any suitable viscosity. The emulsion can also contain an emulsifier and / or an antifoaming agent. Methods for preparing emulsions are known to those skilled in the art.

[0249] The topical compositions of the present invention can be incorporated into a medical device for administration. Such devices can include, but are not limited to, fabrics, patches, bandages, meters, socks, corsets, underwear, dressings, gloves, masks, adhesive patches, non-adhesive patches, occlusive patches, and microelectrode patches or suitable adhesive systems. In such an embodiment, the device is in direct contact with the stratum corneum such as the skin, thereby releasing the peptides of the present invention. It should be understood that the topical compositions can be incorporated in any suitable form detailed herein. For example, the topical compositions or peptides of the present invention can be incorporated into the device or present on the surface of the device, or can be a cream, gel, or wax formulation or any suitable formulation defined herein and incorporated into the device or on the surface of the device. The device can be adapted to adhere or attach to the skin.

[0250] In one embodiment, the device is adapted to release a constant amount of the composition or peptide of the present invention. It should be understood that the amount of the composition contained in the sustained release system depends on, for example, where the composition will be administered, the kinetics and duration of the release of the composition of the present invention, and the nature of the condition, disorder, and / or disease to be treated and / or cared for. The device can be such that the composition is released due to body moisture, the pH of the skin, or body temperature, or by biodegradation of the device or by friction between the device and the body.

[0251] In one embodiment of the present invention, the topical composition can also contain at least one cosmetic or pharmaceutically acceptable excipient. Excipients can be used interchangeably with functional ingredients or additives. It should be understood that although the topical compositions of the present invention can be administered alone, they are generally administered in admixture with cosmetic or pharmaceutical excipients. Cosmetic or pharmaceutically acceptable excipients are well known in the art and are any known excipient that can be used as long as it is suitable for topical administration and is dermatologically acceptable without undue toxicity, incompatibility, and / or allergic reactions.

[0252] Preferably, any excipient included is present in trace amounts. The amount of the excipient included will depend on many factors, including the type of excipient used, the nature of the excipient, the components of the topical composition, the amount of the active ingredient or peptide in the topical composition, and / or the intended use of the topical composition. The nature and amount of any excipient should not unacceptably alter the benefits of the peptides of the present invention.

[0253] In one embodiment of the present invention, the excipient can be a suitable diluent, carrier, binder, lubricant, suspending agent, coating agent, preservative, stabilizer, dye, carrier, solubilizer, base, emollient, emulsifier, fragrance, humectant, and / or surfactant.

[0254] Examples of suitable diluents include, but are not limited to, any diluents disclosed in US2014120131 or US2004132667. Examples include ethanol, glycerol, and water.

[0255] Examples of suitable carriers include, but are not limited to, lactose, starch, glucose, methylcellulose, magnesium stearate, mannitol, sorbitol, and any suitable carrier disclosed in US2014120131 or US2004132667.

[0256] Examples of suitable binders include, but are not limited to, starch, gelatin, natural sugars such as glucose, anhydrous lactose, free-flowing lactose, β-lactose, corn sweeteners, natural and synthetic gums such as gum arabic, tragacanth, or sodium alginate, carboxymethylcellulose, and polyethylene glycol, and any suitable binder disclosed in US2014120131 or US2004132667.

[0257] Examples of suitable lubricants include, but are not limited to, sodium oleate, sodium stearate, magnesium stearate, sodium benzoate, sodium acetate, and sodium chloride, and any suitable lubricant disclosed in US2014120131 or US2004132667.

[0258] The carrier can be any suitable carrier known in the art or any suitable carrier disclosed in US2014120131 or US2004132667. In some embodiments, the carrier can include, but is not limited to, liquids such as water, oil, or surfactants, including those of petroleum, animal, vegetable, or synthetic origin, polymers, oils such as peanut oil, mineral oil, castor oil, soybean oil, alcohols, polysorbates, sorbitan esters, ether sulfates, sulfates, betaines, glycosides, maltosides, fatty alcohols, nonoxynols, poloxamers, polyoxyethylene, polyethylene glycol, dextrose, glycerol, or digitonin. It should be understood that the carrier will be dermatologically acceptable. Preferred carriers comprise emulsions, such as oil-in-water, water-in-oil, water-in-oil-in-water, and oil-in-water-in-silicone emulsions. The emulsions can also contain emulsifiers and / or defoamers.

[0259] In one embodiment of the present invention, the topical composition may further comprise one or more additional ingredients. The topical composition of the present invention may be administered continuously, simultaneously or sequentially with one or more other additional agents. Such additional ingredients may be those that are beneficial when included in the topical composition or are beneficial depending on the intended use of the topical composition. The additional ingredients may be active or functional or both.

[0260] Examples of such additional ingredients include, but are not limited to, one or more of the following: detergents, conditioners, sunscreens, pigments, moisturizers, thickening agents, gelling agents, essential oils, astringents, pigments, anti-caking agents, defoamers, binders, additives, buffers, chelating agents, topical analgesics, film-forming agents or materials, fillers, polymers, emulsifiers, pH regulators, propellants, reducing agents, sequestrants, skin lightening and brightening agents, skin conditioners, aloe vera, repair agents, soothing agents, smoothing agents, pantothenic acid, treating agents, thickeners, vitamins, colorants, drugs, preservatives, defoamers, buffers, astringents, polymers, pH regulators, deodorants or any other dermatologically acceptable carrier or surfactant.

[0261] It should be understood that the listed additional ingredients may provide more than one benefit. The classification given herein is for clarity and convenience only and is not intended to limit the additional ingredients to the specific applications or categories listed.

[0262] Any additional ingredient should be suitable for application to the skin without undue toxicity, incompatibility and / or allergic reaction.

[0263] In some embodiments, the additional ingredient has glucose transport activity or contributes to glucose transport activity. In some embodiments, the additional ingredient has anti-inflammatory activity or contributes to anti-inflammatory activity. In some embodiments, the additional ingredient has anti-aging activity or contributes to anti-aging activity. In some embodiments, the additional ingredient is for stratum corneum health and / or development, skin health and / or development, and / or muscle health, recovery and / or development. The active agent may be a pharmacological enhancer. Such active agents are known and commercially available. In such cases, the topical composition of the present invention may be administered continuously, simultaneously or sequentially with one or more other active agents.

[0264] In some embodiments, the additional ingredients can be farnesol ([2E,6E],-3,7,11,-trimethyl-2,6,10,dodecatrien-1-ol), phytantriol (3,7,11,15,tetramethylhexadecane-1,2,3,-triol), exfoliating active, enzyme, enzyme inhibitor, enzyme activator, plant extract and marine extract, anti-acne active, anti-wrinkle or anti-atrophy active, antioxidant / free radical scavenger, chelating agent, flavonoid, anti-inflammatory agent, anti-cellulite agent, local anesthetic, tanning active, skin brightener, skin repair agent, bisabolol, anti-microbial or anti-fungal active, sun protection active, particulate material, conditioning agent, structuring agent, thickening agent.

[0265] The exfoliating active can be any suitable reagent that enhances the appearance or texture of the skin and is as disclosed in US2014120131 or US2004132667.

[0266] Examples of anti-acne actives are as disclosed in US2014120131 or US2004132667 and include resorcinol, salicylic acid, erythromycin, zinc, sulfur, benzoyl peroxide.

[0267] Examples of thickening agents are as disclosed in US2014120131 or US2004132667 and include carboxylic acid polymers, crosslinked polyacrylate polymers, polyacrylamide polymers, polysaccharides.

[0268] Examples of conditioning agents are as disclosed in US2014120131 or US2004132667 and include humectants, emollients or skin conditioners.

[0269] Examples of structuring agents are as disclosed in US2014120131 or US2004132667 and include any reagent that provides rheological properties to the composition and contributes to the stability of the composition.

[0270] Any suitable anti-microbial or anti-fungal active can be used and examples are as disclosed in US2014120131 or US2004132667. These actives are capable of destroying microorganisms, preventing the growth or action of microorganisms. Examples include but are not limited to β-lactam drugs, quinolone drugs, tetracyclines, erythromycin, streptomycin sulfate, salicylic acid, benzoyl peroxide.

[0271] Examples of particulate materials include metal oxides. Examples of anti-lipid agents include xanthine agents. Examples of tanning actives include 1,3-dihydroxy-2-acetone and those disclosed in US2014120131 or US2004132667. Examples of local anesthetics include benzocaine, lidocaine, and bupivacaine, and those disclosed in US2014120131 or US2004132667.

[0272] Examples of skin brighteners include any agent known in the art such as kojic acid, ascorbic acid, and those disclosed in US2014120131 or US2004132667.

[0273] Examples of sunscreen actives include any suitable organic or inorganic sunscreen active. Examples include metal oxides, 2-ethylhexyl-p-methoxycinnamate, and those disclosed in US2014120131 or US2004132667.

[0274] Examples of skin repair agents include pantothenic acid as disclosed in US2014120131 or US2004132667.

[0275] Examples of anti-inflammatory agents include any agent that enhances the appearance, complexion, or color of the skin and includes, but is not limited to, corticosteroids, hydrocortisone, non-steroidal agents such as ibuprofen and aspirin, and those disclosed in US2014120131 or US2004132667.

[0276] Examples of flavonoids include flavanones, methoxyflavones, unsubstituted chalcones, and mixtures thereof, and those disclosed in US2014120131 or US2004132667.

[0277] Examples of enzymes include lipase, protease, catalase, superoxide dismutase, amylase, peroxidase, glucuronidase, ceramidase, hyaluronidase. Examples of enzyme inhibitors include trypsin inhibitors, Bowmann-Birk inhibitors, chymotrypsin inhibitors, plant extracts, flavonoids, quercetin chalcones, and those disclosed in US2014120131 or US2004132667 and mixtures thereof. Examples of enzyme activators include coenzyme A, Q10 (ubiquinone), glycyrrhizin, berberine, chrysin, and those disclosed in US2014120131 or US2004132667 and mixtures thereof.

[0278] Examples of anti-wrinkle or anti-atrophy actives include sulfur-containing D and L amino acids, particularly N-acyl derivatives such as N-acetyl-L-cysteine, hydroxy acids, phytic acid, lipoic acid, lysophosphatidic acid, skin peeling agents, vitamin B 3, retinoids and those disclosed in US2014120131 or US2004132667 and mixtures thereof.

[0279] The antioxidant / free radical scavenger can be any reagent used to provide protection against ultraviolet radiation or other environmental agents that may cause skin damage, such as those disclosed in US2014120131 or US2004132667. Examples of antioxidant / free radical scavengers include ascorbic acid, its salts and derivatives (vitamin C), tocopherols and their salts and derivatives (vitamin E), butylated hydroxybenzoic acid and its salts, peroxides, gallic acid and alkyl esters, sorbic acid, lipoic acid, amines, picolinic acid betaine, arginine oxyproline, nordihydroguaiaretic acid, bioflavonoids, curcumin, lysine, methionine, proline, superoxide dismutase, silymarin, tea extracts and mixtures thereof.

[0280] Examples of chelating agents include EDTA, NTA, hydroxamic acid, phytic acid, lactoferrin and those disclosed in US2014120131 or US2004132667 and mixtures thereof. A chelating agent refers to a reagent that can remove metal ions by forming complexes so that the metal ions cannot participate in chemical reactions or catalyze chemical reactions. Chelating agents can be used to prevent ultraviolet radiation or other environmental factors that may cause skin damage.

[0281] It should be understood that a variety of additional ingredients can be added. The amount of the additional ingredient can be from about 0.001% to about 50% by weight of the composition, preferably from about 0.01% to about 20%, preferably from about 0.1% to about 10%, from about 0.5% to about 10%, from about 1% to about 5%, preferably 2% by weight of the composition. The amount of the additional ingredient included will depend on many factors, including the type of additional ingredient used, the nature of the additional ingredient, the (multiple) components of the topical composition, the amount of the active ingredient or peptide in the topical composition, and / or the intended use of the topical composition. The nature and amount of any additional ingredient should not unacceptably alter the benefits of the peptides of the present invention.

[0282] The topical composition can be alcohol-free.

[0283] In some embodiments of the present invention, in addition to the peptides of the present invention (also referred to as the active agents of the composition), the composition further comprises one or more additional active agents. Additionally or alternatively, the composition may be administered in combination with one or more other additional active agents. Typically, the additional active agents are present only in trace amounts. In some embodiments, no additional active agents may be present in the composition. The amount of additional active agents included will depend on a number of factors, including the type of additional active agent used, the nature of the additional active agent, the (multiple) components of the topical composition, the amount of the active agent or peptide in the topical composition, and / or the intended use of the topical composition. The nature and amount of any additional active agent should not unacceptably alter the benefits of the peptides of the present invention.

[0284] It should be understood that a component that is considered an "active" ingredient in one product may be a "functional" or "excipient" ingredient in another product, and vice versa. It should also be understood that some components serve a dual role as both an active ingredient and as a functional or excipient ingredient.

[0285] Examples of additional active agents include glucose transport promoting drugs, skin supplements, skin treatment and / or care agents, anti-inflammatory agents, anti-aging agents, cell growth promoting agents, and pharmacological enhancers. These agents are well known in the art, and it is understood that any suitable additional active agent may be used. Additional active agents for treating and / or caring for the skin may include collagen synthesis agents, retinoids, exfoliants, lipolytic agents, elastase inhibitors, melanin synthesis stimulants or inhibitors, self-tanning agents, anti-aging agents, anti-microbial agents, anti-fungal agents, fungistatic agents, bactericidal agents, and repair agents. The active agents also include anti-inflammatory agents.

[0286] Any additional active agent should be suitable for administration to the skin without undue toxicity, incompatibility, and / or allergic reaction.

[0287] It should be understood that the classifications given herein are for clarity and convenience only and are not intended to limit the additional components, excipients, or active agents to the specific applications or categories listed.

[0288] In a particularly preferred embodiment, the methods and uses of the present invention include administering the peptides or compositions of the present invention in combination with one or more other active agents (e.g., commercially available existing growth promoting drugs or pharmacological enhancers). In such cases, the compounds of the present invention may be administered continuously, simultaneously, or sequentially with one or more other active agents.

[0289] The effects of the present invention are achieved by topically applying or administering the topical compositions of the present invention described herein to a human, animal or patient in need of treatment or care. Topical delivery preferably means delivery to the stratum corneum such as the skin, hair and / or nails, but can also mean delivery to body cavities lined with epithelial cells, such as the lungs or airways, the gastrointestinal tract, the buccal cavity. The effects can be confined to the skin surface or can be within the skin or a combination of both.

[0290] The topical compositions of the present invention are administered in a cosmetically or pharmaceutically effective amount. In other words, in an amount that is non-toxic but sufficient to provide the desired effect. It should be understood that those skilled in the art will be able to determine a suitable dosage for administering the topical compositions of the present invention without undue experimentation. Alternatively, a physician will determine the actual dosage most suitable for the patient based on the particular situation, the disease or disorder to be treated or cared for, and the age, weight and / or health status of the individual. This will depend on a variety of factors, including the activity of the specific compound employed, the metabolic stability and duration of action of the compound, age, weight, general health, sex, diet, mode and time of administration, rate of excretion, drug combination, severity of the particular medical condition, and the individual being treated. Of course, there can be individual cases where higher or lower dosage ranges are appropriate, and this is also within the scope of the present invention. For example, the composition can be administered at a dosage of 0.01 to 50 mg / kg body weight, such as 0.1 to 30 mg / kg, more preferably 0.1 to 20 mg / kg body weight, more preferably 0.1 to 10 mg / kg body weight, preferably 0.1 to 5 mg / kg body weight. In one exemplary embodiment, one or more doses of 10 to 300 mg / day or more preferably 10 to 150 mg / day will be administered to the patient. The amount and frequency are most suitable for the purpose. Depending on the needs of each subject, the frequency of application or administration can vary widely, and the recommended range of application or administration is from once a month to ten times a day, preferably from once a week to four times a day, more preferably from three times a week to three times a day, and even more preferably once or twice a day.

[0291] In a preferred embodiment, repeated use of the topical composition is provided.

[0292] The topical composition can be applied by, but not limited to, rubbing or massaging into the horny tissue, skin or body area to be treated or cared for. In some embodiments, the composition remains on the area of the body or is not removed from the area of the body. In other embodiments, after a period of time, such as but not limited to about 2 minutes to 60 minutes, about 5 minutes to about 30 minutes, preferably about 10 minutes to about 20 minutes, the composition is removed. The composition can be removed immediately after application. In some embodiments of the present invention, the composition of the present invention can be applied to the area to be treated by methods that achieve greater penetration of the composition and / or peptide of the present invention, such as but not limited to iontophoresis, sonophoresis, electroporation, microelectropatch, mechanical pressure, osmotic pressure gradient, occlusive treatment, microinjection by means of pressure or needleless injection such as injection through oxygen partial pressure, or any combination thereof.

[0293] The peptides of the present invention are used in the topical cosmetic or pharmaceutical compositions of the present invention at a cosmetically or pharmaceutically effective concentration to achieve the desired effect; preferably in the form of 0.00000001% (by weight) to 20% (by weight) relative to the total weight of the composition; preferably 0.000001% (by weight) to 15% (by weight), more preferably 0.0001% (by weight) to 10% (by weight), and even more preferably 0.0001% (by weight) to 5% (by weight).

[0294] In some embodiments of the present invention, the composition can be delivered via any of the following: liposomes, mixed liposomes, oleosomes, niosomes, ethosomes, microcapsules, capsules, macrocapsules, nanocapsules, nanostructured lipid carriers, sponges, cyclodextrins, vesicles, micelles, mixed micelles of surfactants, surfactant-phospholipid mixed micelles, microspheres, spheres, lipid spheres, particles, nanospheres, nanoparticles, microparticles, solid nanoparticles and microemulsions including water-in-oil microemulsions and nanoemulsion microspheres with an internal structure of reverse micelles, microparticles.

[0295] A variety of methods can be used to prepare liposomes. See, e.g., Szoka et al., Ann. Rev. Biophys. Bioeng. 9:467 (1980), U.S. Patent Nos. 4,186,183, 4,217,344, 4,235,871, 4,261,975, 4,485,054, 4,501,728, 4,774,085, 4,837,028, 4,235,871, 4,261,975, 4,485,054, 4,501,728, 4,774,085, 4,837,028, 4,946,787, PCT Publication No. WO 91 / 17424, Deamer & Bangham, Biochim. Biophys. Acta 443:629 - 634 (1976); Fraley, et al., PNAS 76:3348 - 3352 (1979); Hope et al., Biochim. Biophys. Acta 812:55 - 65 (1985); Mayer et al., Biochim. Biophys. Acta 858:161 - 168 (1986); Williams et al., PNAS 85:242 - 246 (1988); Liposomes (Ostro (ed.), 1983, Chapter 1); Hope et al., Chem. Phys. Lip. 40:89 (1986); Gregoriadis, Liposome Technology (1984) and Lasic, Liposomes: from Physics to Applications (1993)). Suitable methods include, for example, sonication, extrusion, high pressure / homogenization, microfluidization, detergent dialysis, calcium-induced fusion of small lipid carriers, and ether fusion methods, all of which are well known in the art.

[0296] These delivery systems can be suitable for achieving greater penetration of the compounds and / or peptides of the present invention. This can improve pharmacokinetic and pharmacodynamic properties. The delivery system can be a sustained release system, in which the compound or peptide of the present invention is gradually released over a period of time and preferably has a constant release rate over a period of time. The delivery system is prepared by methods known in the art. The amount of peptide contained in the sustained release system will depend on where the composition is to be delivered, the duration of release, and the type of condition, disease, and / or disorder to be treated or cared for.

[0297] The topical compositions of the present invention can be used for human or veterinary use in humans or animals.

[0298] The topical compositions of the present invention can be used for pharmaceutical, personal care, and / or cosmetic uses.

[0299] The composition can be used for treating or caring for any disease, disorder or condition of the skin, including but not limited to psoriasis, dermatitis, atopic dermatitis, eczema, spongiotic edema, edema, skin cancer, ulcers, acne, scars, cellulitis, elastosis, keratosis, rosacea, varicose veins, inflammatory diseases.

[0300] The topical composition can be used for treating or caring for visible signs of aging, including but not limited to wrinkles, stretch marks and dark circles under the eyes, dryness, fine lines, age spots, red spots, skin sagging, and conditions caused by sun exposure including sunburn, stress, pollution, and / or diet. The topical composition can also be used to delay, slow down or inhibit the occurrence of skin aging. The composition can be administered via a medical device such as a plaster or patch as described herein.

[0301] The topical composition can be used for treating or caring for wounds in mammals. In another embodiment, the topical composition is used for treating or preventing diseases or conditions characterized by damaged epithelial cells or tissues, and / or damaged dermal or epithelial cells or tissues. The diseases may be but are not limited to cancer and trauma.

[0302] The topical composition can be used for treating or caring for any muscle condition to improve the muscle state of a mammal, generally promote muscle recovery after exercise, maintain or restore the muscle health of a mammal (e.g., lean tissue mass), enhance physical performance, treat or prevent diseases or conditions characterized by lethargy or low energy levels.

[0303] The topical composition can be used to promote tissue growth, promote epithelial tissue growth, promote skin growth, promote organ growth, promote organism growth. The skin can have normal pathology and / or abnormal pathology.

[0304] The topical composition can also be used for treating or caring for any inflammatory disorder.

[0305] Other aspects of the invention relate to a pharmaceutical composition comprising a peptide of the invention or a composition of a peptide of the invention admixed with one or more pharmaceutically acceptable diluents, excipients or carriers. Although the peptides and compositions of the invention may be administered alone, they are generally administered in admixture with a pharmaceutical carrier, excipient or diluent, particularly for human therapy. The pharmaceutical compositions may be for human or animal use in human or veterinary medicine. Examples of such suitable excipients for the various different forms of pharmaceutical compositions described herein may be found in "Handbook of Pharmaceutical Excipients", 2nd Edition, (1994), edited by A Wade and PJ Weller. In particular, formulations for topical delivery are described in Topical drug delivery formulations, edited by David Osborne and Antonio Aman, Taylor & Francis, the entire contents of which are incorporated herein by reference. Acceptable carriers or diluents for therapeutic use are well known in the pharmaceutical art and are described, for example, in Remington's Pharmaceutical Sciences, Mack Publishing Co. (edited by A.R. Gennaro, 1985). Examples of suitable carriers include lactose, starch, glucose, methylcellulose, magnesium stearate, mannitol, sorbitol, etc. Examples of suitable diluents include ethanol, glycerol and water. The choice of pharmaceutical carrier, excipient or diluent can be selected according to the intended route of administration and standard pharmaceutical practice. The pharmaceutical composition may contain any suitable binder, lubricant, suspending agent, coating agent, solubilizer as a carrier, excipient or diluent, or in addition to the carrier, excipient or diluent. Examples of suitable binders include starch, gelatin, natural sugars such as glucose, anhydrous lactose, free-flowing lactose, β-lactose, corn sweeteners, natural and synthetic gums such as gum arabic, tragacanth or sodium alginate, carboxymethylcellulose and polyethylene glycol. Examples of suitable lubricants include sodium oleate, sodium stearate, magnesium stearate, sodium benzoate, sodium acetate, sodium chloride, etc. Preservatives, stabilizers, dyes and even flavoring agents may be provided in the pharmaceutical composition. Examples of preservatives include sodium benzoate, sorbic acid and esters of p-hydroxybenzoic acid. Antioxidants and suspending agents may also be used.

[0306] The peptides or compositions of the present invention are applicable to routes of administration such as topical, oral, rectal, parenteral, intramuscular, intraperitoneal, intraarterial, intratracheal, subcutaneous, intradermal, intravenous, nasal, vaginal, buccal or sublingual. For oral administration, the special uses consist of compressed tablets, pills, tablets, gels, drops and capsules. Preferably, these compositions contain 1 - 250 mg, and more preferably 10 - 100 mg of the active ingredient per dose. Other forms of administration include solutions or emulsions that can be injected intravenously, intraarterially, subcutaneously, intradermally, intraperitoneally or intramuscularly, and are prepared from sterile or sterilizable solutions. The pharmaceutical compositions of the present invention can also be in the form of suppositories, vaginal rings, pessaries, suspensions, emulsions, lotions, ointments, creams, gels, sprays, solutions or dusting powders. The compositions of the present invention can be formulated for topical delivery. Topical delivery generally means delivery to the skin, but can also mean delivery to body cavities lined with epithelial cells, such as the lungs or airways, the gastrointestinal tract, the buccal cavity. In particular, the formulations for topical delivery are described in Topical drug delivery formulations edited by David Osborne and Antonio Aman, Taylor & Francis, the entire content of which is incorporated herein by reference. The compositions or formulations for delivery to the airways are described in O'Riordan et al. (Respir Care, 2002, Nov. 47), EP2050437, WO2005023290, US2010098660 and US20070053845. The compositions and formulations for delivering the active agent to the ileum, especially the proximal ileum, include microparticles and microcapsules, wherein the active agent is encapsulated within a protective matrix formed from a polymer or milk protein, which is acid-resistant but readily soluble in the more alkaline environment of the ileum. Examples of such delivery systems are described in EP1072600.2 and EP13171757.1. An alternative method of transdermal administration is by using a skin patch. For example, the active ingredient can be incorporated into a cream consisting of an aqueous emulsion of polyethylene glycol or liquid paraffin. The active ingredient can also be incorporated into an ointment consisting of a white wax or white soft paraffin matrix and stabilizers and preservatives as may be required, at a concentration of 1 to 10% by weight.

[0307] The injectable form can contain 10 - 1000 mg, preferably 10 - 250 mg of the active ingredient per dose.

[0308] The compositions can be formulated in unit dosage form, i.e., in the form of discrete portions containing a unit dose or multiple or sub-units of a unit dose.

[0309] One of ordinary skill in the art can readily determine the appropriate dose of one of the compositions of the present invention to be administered to a subject without undue experimentation. Generally, a physician will determine the actual dose most suitable for an individual patient, and this will depend on a variety of factors, including the activity of the specific compound used, the metabolic stability and duration of action of the compound, age, body weight, general health, sex, diet, mode and time of administration, rate of excretion, drug combination, the severity of the particular condition, and the individual being treated. The doses disclosed herein are examples of average cases. Of course, there can be individual cases where higher or lower dose ranges are appropriate, and these are also within the scope of the present invention. The reagent can be administered at a dose of from 0.01 to 30 mg / kg body weight, such as from 0.1 to 10 mg / kg, more preferably from 0.1 to 1 mg / kg body weight. In one exemplary embodiment, for the treatment of an inflammatory disease, one or more doses of from 10 to 300 milligrams per day or more preferably from 10 to 150 milligrams per day will be administered to a patient.

[0310] In a particularly preferred embodiment, the methods and uses of the present invention include co-administering the peptides or compositions of the present invention with one or more other active agents (e.g., commercially available existing anti-inflammatory drugs or pharmacological enhancers). In such cases, the compositions of the present invention can be administered continuously, simultaneously, or sequentially with one or more other active agents.

[0311] In one embodiment of the present invention, the peptides of the present invention can be administered in the form of conjugates comprising the peptides and can optionally include a linker and a conjugate molecule, such as a protein like an antibody molecule designed to increase the half-life of the conjugate in vivo. In one embodiment, the peptide can be modified to replace with one or more amino acids, wherein the amino acids are used to link the conjugate molecule. For example, for the purpose of conjugating a conjugate molecule such as a PEG molecule, an amino acid can be replaced with a lysine residue.

[0312] Definition

[0313] For all purposes, all publications, patents, patent applications, and other references mentioned herein are hereby incorporated by reference in their entirety as if each individual publication, patent, or patent application was specifically and individually indicated to be incorporated by reference and the content thereof was fully recited.

[0314] As used herein, unless otherwise expressly indicated, the following terms are intended to have the following meanings in addition to any broader (or narrower) meanings they may have in the art:

[0315] Unless the context otherwise requires, the use of the singular herein shall be construed to include the plural and vice versa. The term "a" or "an" when used in reference to an entity shall be construed to mean one or more of that entity. Thus, the terms "a" (or "an"), "one or more", and "at least one" are used interchangeably herein.

[0316] As used herein, the term "comprise" or variations thereof such as "comprises" or "comprising" shall be understood to imply the inclusion of any recited integer (e.g., a feature, element, characteristic, property, method / process step, or limitation) or group of integers (e.g., a feature, element, characteristic, property, method / process step, or limitation) but not the exclusion of any other integer or group of integers. Thus, as used herein, the term "comprising" is inclusive or open-ended and does not exclude additional, unrecited integers or method / process steps.

[0317] As used herein, the term "disease" is used to define any abnormal condition that impairs physiological function and is associated with specific symptoms. The term is used broadly to encompass any disorder, affliction, abnormality, pathology, illness, condition, or syndrome in which physiological function is impaired regardless of the nature of the cause (or indeed whether the etiological basis of the disease is determined). Thus, it encompasses conditions caused by infection, trauma, injury, surgery, radioablation, poisoning, or nutritional deficiency.

[0318] As used herein, the term "treatment" or "treating" refers to an intervention (e.g., administering a reagent to a subject) that cures, ameliorates, or alleviates the symptoms of a disease or eliminates its cause (or alleviates the effects of its cause) (e.g., reducing the accumulation of pathological levels of lysosomal enzymes). In this context, the term is used synonymously with the term "therapy".

[0319] In addition, the term "treatment" or "treating" refers to an intervention (e.g., administering a reagent to a subject) that prevents or delays the onset or progression of a disease or reduces (or eradicates) its incidence in the treated population. In this context, the term treatment is used synonymously with the term "prophylaxis".

[0320] As used herein, an effective amount or therapeutically effective amount of a reagent defines an amount that can be administered to a subject without undue toxicity, irritation, allergic response, or other problems or complications commensurate with a reasonable benefit / risk ratio, but is sufficient to provide the desired effect, such as treatment or prophylaxis manifested as a permanent or transient improvement in the condition of the subject. This amount varies from subject to subject and depends on the individual's age and general condition, the mode of administration, and other factors. Thus, while it is not possible to specify an exact effective amount, those skilled in the art can determine the appropriate "effective" amount in any individual case using routine experimentation and general knowledge of the background. Therapeutic outcomes in such cases include eradication or alleviation of symptoms, relief of pain or discomfort, extended survival, improved mobility, and other markers of clinical improvement. Therapeutic outcomes are not necessarily complete cures.

[0321] The term "mammal" should be understood to refer to higher mammals, particularly humans. However, the term also includes non-mammals, such as fish.

[0322] As used herein, the term "peptide" refers to a polymer composed of up to 50 amino acid monomers that are typically linked by peptide bonds. The length of the peptide can be from 3 to 50 amino acids. The length of the peptide can be from 4 to 50 amino acids. The length of the peptide can be from 5 to 50 amino acids. The length of the peptide can be from 7 to 50 amino acids. Peptides (including fragments and variants thereof) of the present invention and for use in the present invention can be produced in whole or in part by chemical synthesis or by expression from nucleic acids. For example, the peptides of the present invention and the peptides for use in the present invention can be readily prepared according to well-established standard liquid or preferably solid-phase peptide synthesis methods known in the art (see, e.g., J.M. Stewart and J.D. Young, Solid Phase Peptide Synthesis, 2nd ed., Pierce Chemical Company, Rockford, Illinois in M. Bodanzsky and A. Bodanzsky, The Practice of Peptide Synthesis, Springer Verlag, New York (1984)). If necessary, any peptide used in the present invention can be chemically modified to increase their stability. Chemically modified peptides or peptide analogs include any functional chemical equivalents of peptides, which are characterized by an increase in their stability and / or efficacy in vivo or in vitro relative to the practice of the present invention. The term peptide analog also refers to any amino acid derivative of a peptide as described herein. Peptide analogs can be prepared by procedures including, but not limited to, modification of side chains, incorporation of unnatural amino acids and / or their derivatives during peptide synthesis, and the use of cross-linking agents and other methods that impose conformational constraints on the peptide or its analog. Examples of side chain modifications include modification of amino groups, such as reductive alkylation, by reaction with an aldehyde followed by reduction with NaBH 4 reduction; amidation with methyl acetimidate; acetylation with acetic anhydride; carbamylation of amino groups with cyanate esters; trinitrobenzylation of amino groups with 2,4,6-trinitrobenzenesulfonic acid (TNBS); alkylation of amino groups with succinic anhydride and tetrahydrophthalic anhydride; and pyridoxylation of lysine with pyridoxal-5'-phosphate followed by reduction with NABH 4Reduction. The guanidino group of arginine residues can be modified by forming heterocyclic condensation products with reagents such as 2,3-butanedione, benzoylformaldehyde, and glyoxal. The carboxyl group can be modified by activation with carbodiimide via O-acylisourea followed by subsequent derivatization such as to the corresponding amide. The sulfhydryl group can be modified by (a variety of) methods such as carboxymethylation with iodoacetic acid or iodoacetamide; oxidation with performic acid to sulfoalanine; formation of mixed disulfides with other thiol compounds; reaction with maleimide; maleic anhydride or other substituted maleimides; formation of mercury derivatives using 4-chloromercuribenzoic acid, 4-chloromercuribenzene sulfonic acid, phenylmercuric chloride, 2-chloromercuri-4-nitrophenol, and other mercury preparations; carbamylation with cyanate at alkaline pH. Tryptophan residues can be modified by oxidation with, for example, N-bromosuccinimide or alkylation of the indole ring with 2-hydroxy-5-nitrobenzyl bromide or sulfonyl halides. Tyrosine residues can be altered by nitration with tetranitromethane to form 3-nitrotyrosine derivatives. Modification of the imidazole ring of histidine residues can be accomplished by alkylation with iodoacetic acid derivatives or N-ethoxycarbonylation with diethyl pyrocarbonate. Examples of incorporation of unnatural amino acids and derivatives during peptide synthesis include, but are not limited to, the use of norleucine, 4-aminobutyric acid, 4-amino-3-hydroxy-5-phenylpentanoic acid, 6-aminohexanoic acid, tert-butylglycine, norvaline, phenylglycine, ornithine, sarcosine, 4-amino-3-hydroxy-6-methylheptanoic acid, 2-thienylalanine, and / or D-isomers of amino acids. Peptide structure modification includes the production of retro-inverso peptides containing reverse sequences encoded by D-amino acids.

[0323] "Modified Peptide": In one embodiment of the present invention, the peptide is a modified peptide. The term "modified peptide" is used interchangeably with the term "peptide derivative". A modified peptide includes a peptide that has been replaced by one or more groups as defined herein. The modification can be any modification that provides the peptide and / or composition of the present invention with increased ability to penetrate cells. The modification can be any modification that increases the half-life of the composition or peptide of the present invention. In one embodiment, the group is a protecting group. The protecting group can be an N-terminal protecting group, a C-terminal protecting group, or a side chain protecting group. The peptide can have one or more of these protecting groups. Those skilled in the art know the appropriate techniques for reacting amino acids with these protecting groups. These groups can be added by methods known in the art, such as those outlined in paragraphs

[0104] to

[0107] of US2014120141. These groups may remain on the peptide or may be removed. The protecting group can be added during the synthesis process. In one embodiment of the present invention, the peptide can be replaced by a group selected from: one or more straight-chain or branched-chain, long-chain or short-chain, saturated or unsaturated, substituted or unsubstituted by hydroxyl, amino, aminoacyl, sulfate or sulfide groups, having 1 to 29 carbon atoms. N-acyl derivatives include those derived from acetic acid, capric acid, lauric acid, myristic acid, caprylic acid, palmitic acid, stearic acid, behenic acid, linoleic acid, linolenic acid, lipoic acid, oleic acid, isostearic acid, elaidic acid, 2-ethylhexanoic acid, coconut oil fatty acids, tallow fatty acids, hardened tallow fatty acids, palm kernel fatty acids, lanolin fatty acids or similar acids. These can be substituted or unsubstituted. When substituted, they are preferably substituted by hydroxyl or sulfur-containing groups, such as but not limited to SO 3 H, SH or S-S. In one embodiment of the present invention, the peptide is R 1 -X-R 2 . R 1 and / or R 2 groups are respectively bound to the amino terminus (N-terminus) and carboxyl terminus (C-terminus) of the peptide sequence. In one embodiment, the peptide is R 1 -X. Alternatively, the peptide is X-R 2 . Preferably, R 1 is H, C 1-4 alkyl, acetyl, benzoyl or trifluoroacetyl. X is the peptide of the present invention; R 2 is OH or NH 2 . In one embodiment, R 1 is selected from the group consisting of H, acyclic substituted or unsubstituted aliphatic groups, substituted or unsubstituted cycloaliphatic, substituted or unsubstituted heterocyclic groups, substituted or unsubstituted heteroarylalkyl, substituted or unsubstituted aryl, substituted or unsubstituted aralkyl, tert-butoxycarbonyl, 9-fluorenylmethoxycarbonyl (Fmoc) and R5 -CO - formed group, where R 5 is selected from the group consisting of H, acyclic substituted or unsubstituted aliphatic groups, substituted or unsubstituted cycloaliphatic groups, substituted or unsubstituted aryl groups, substituted or unsubstituted aralkyl groups, substituted or unsubstituted heterocyclic groups, and substituted or unsubstituted heteroarylalkyl groups; R 2 is selected from the group consisting of -NR 3 R 4 , -OR 3 and -SR 3 formed group, where R 3 and R 4 are independently selected from the group consisting of H, acyclic substituted or unsubstituted aliphatic groups, substituted or unsubstituted cycloaliphatic groups, substituted or unsubstituted heterocyclic groups, substituted or unsubstituted heteroarylalkyl groups, substituted or unsubstituted aryl groups, and substituted or unsubstituted aralkyl groups; and provided that R 1 and R 2 are not α - amino acids. According to another preferred embodiment, R 2 is -NR 3 R 4 , -OR 3 or -SR 3 , where R 3 and R 4 are independently selected from the group consisting of: H, substituted or unsubstituted C 1 -C 24 alkyl, substituted or unsubstituted C 2 -C 24 alkenyl, tert - butoxycarbonyl, 9 - fluorenylmethoxycarbonyl (Fmoc), substituted or unsubstituted C 2 -C 24 alkynyl, substituted or unsubstituted C 3 -C 24 cycloalkyl, substituted or unsubstituted C 5 -C 24 cycloalkenyl, substituted or unsubstituted C 8 -C 24 cycloalkynyl, substituted or unsubstituted C 6 -C 30 aryl, substituted or unsubstituted C 7 -C 24 aralkyl, 3 - 10 - membered substituted or unsubstituted heterocyclic rings, and substituted or unsubstituted heteroarylalkyl groups with 2 - 24 carbon atoms and 1 - 3 non - carbon atoms, where the alkyl chain has 1 - 6 carbon atoms. Optionally, R 3 and R 4 can be bonded through a saturated or unsaturated carbon - carbon bond to form a ring with the nitrogen atom. More preferably, R2 is -NR 3 R 4 or -OR 3 , wherein R 3 and R 4 are independently selected from the group consisting of: H, substituted or unsubstituted C 1 -C 24 alkyl, substituted or unsubstituted C 2 -C 24 alkenyl, substituted or unsubstituted C 2 -C 24 alkynyl, substituted or unsubstituted C 3 -C 10 cycloalkyl, substituted or unsubstituted C 6 -C 15 aryl and 3 - 10 membered substituted or unsubstituted heterocyclic group, substituted or unsubstituted heteroarylalkyl having an alkyl chain with 3 to 10 members in the ring and 1 to 6 carbon atoms. More preferably, R 3 and R 4 are selected from the group consisting of: H, methyl, ethyl, hexyl, dodecyl or hexadecyl. Even more preferably, R 3 is H and R 4 is selected from the group consisting of H, methyl, ethyl, hexyl, dodecyl or hexadecyl. According to an even more preferred embodiment, R 2 is selected from -OH and -NH 2 . According to another embodiment of the present invention, R 1 is selected from the group consisting of H, acetyl, lauroyl, myristoyl or palmitoyl, and R 2 is -NR 3 R 4 or -OR 3 , wherein R 3 and R 4 are independently selected from H, methyl, ethyl, hexyl, dodecyl and hexadecyl, preferably R 2 is -OH or -NH 2 . More preferably, R 1 is acetyl or palmitoyl, and R 2 is -NH 2。In a preferred embodiment, the acyl group is bonded to the N-terminus of at least one amino acid of the peptide. In one embodiment of the invention, the peptide is modified to include side chain protecting groups. The side chain protecting groups can be one or more of a group including benzyl or benzyl-based groups, tert-butyl-based groups, benzyloxy-carbonyl (Z) groups, and allyloxycarbonyl (alloc) protecting groups. The side chain protecting groups can be derived from achiral amino acids such as achiral glycine. The use of achiral amino acids helps to stabilize the resulting peptide and also facilitates a simple synthetic route for the present invention. Preferably, the peptide also contains a modified C-terminus, preferably an amidated C-terminus. The achiral residue can be α-aminoisobutyric acid (methylalanine). It should be understood that the particular side chain protecting group used will depend on the sequence of the peptide and the type of N-terminus protecting group used.

[0324] "Conjugate": In one embodiment of the present invention, a peptide is conjugated, linked or fused to a binding partner, such as one or more polyethylene glycol polymers or other compounds, such as a molecular weight increasing compound or a lipophilic group. A molecular weight increasing compound is any compound that increases the molecular weight of the resulting conjugate by generally 10% to 90% or 20% to 50%, and may have a molecular weight of 200 to 20,000, preferably 500 to 10,000. The molecular weight increasing compound can be PEG, any water-soluble (amphiphilic or hydrophilic) polymer moiety, a homopolymer or copolymer of PEG, a monomethyl-substituted polymer of PEG (mPEG) and polyoxyethylene glycerol (POG), polyamino acids such as polylysine, polyglutamic acid, polyaspartic acid, especially those in the L configuration, pharmacologically inactive proteins such as albumin, gelatin, fatty acids, polysaccharides, lipid amino acids, and dextrans. The polymer moiety can be linear or branched, and it can have a molecular weight of 500 to 40,000 Da, 5000 to 10,000 Da, 10,000 to 5000 Da. The compound (binding partner) can be any suitable cell-penetrating compound, such as the tat peptide, a cell-penetrating peptide, pep-1. The compound (binding partner) can be an antibody molecule. The compound (binding partner) can be a lipophilic moiety or a polymer moiety. Lipophilic substituents and polymer substituents are known in the art. Lipophilic substituents include acyl groups, sulfonyl groups, N atoms, O atoms or S atoms that form part of an ester, sulfonyl ester, thioester, amide or sulfonamide. The lipophilic moiety can include a hydrocarbon chain having 4 to 30 C atoms, preferably 8 to 12 C atoms. It can be linear or branched, saturated or unsaturated. The hydrocarbon chain can be further substituted. It can be a cycloalkane or a heterocycloalkane. The peptide can be modified at the N-terminus, C-terminus or both. The polymer or compound (binding partner) is preferably linked to an amino group, a carboxyl group or a sulfhydryl group, and can be linked through the N-terminus or C-terminus of the side chain of any amino acid residue. The polymer or compound (binding partner) can be conjugated to the side chain of any suitable residue. The polymer or compound (binding partner) can be conjugated through a spacer. The spacer can be a natural or unnatural amino acid, succinic acid, lysyl, glutamyl, aspartyl, glycyl, β-alanyl, γ-aminobutyryl. The polymer or compound (binding partner) can be conjugated through an ester, sulfonyl ester, thioester, amide, carbamate, urea, sulfonamide. Those skilled in the art know suitable methods for preparing the conjugates.

[0325] "Fragment" means a protein fragment, usually selected from SEQUENCE ID NO: 1-16 and 353-355, and particularly from regions of those proteins selected from SEQUENCE ID NO: 17-70. In one embodiment, the fragment typically has a length of 3 to 37 contiguous amino acids. In one embodiment, the fragment typically has a length of 5 to 37 contiguous amino acids. In one embodiment, the fragment typically has a length of 5 to 37 contiguous amino acids. The fragment typically has a charge of -9 to +3; the C-terminal amino acid is typically not cysteine (C) or methionine (M); and the N-terminal amino acid is typically not cysteine (C), histidine (H), proline (P) or threonine (T). The charge of a peptide, fragment or region is determined using the method of Cameselle, J.C., Ribeiro, J.M. and Sillero, A. (1986). Derivation and use of a formula to calculate the net charge of acid-base compounds. Its application to amino acids, proteins and nucleotides. Biochem. Educ. 14, 131-136.

[0326] The term "native" as applied to a peptide means a peptide that comprises (a) a fragment of a plant protein, the plant protein typically being rice or pea protein, or variants of pea protein including lentil, sweet pea or chickpea, or variants of rice protein including oats, grass, corn, wild rice and banana, or (b) a variant of a fragment of a plant protein, such as a fragment of a homolog of a plant protein. The peptides or fragments of the invention can be isolated or synthetically prepared from plant proteins.

[0327] The "C-terminal domain" as applied to a fragment means the first three amino acids at the C-terminus of the fragment.

[0328] The "N-terminal domain" as applied to a fragment means the last three amino acids at the N-terminus of the fragment.

[0329] "Bioactivity" as applied to a peptide or fragment means having a health-promoting effect when administered to a mammal, such as promoting glucose transport, antibacterial, anti-inflammatory or promoting cell growth or proliferation. In one embodiment, the term "bioactivity" means anti-inflammatory.

[0330] "Glucose transport promotion" or "glucose transport promoting activity" as applied to a peptide or variant or fragment means a peptide, variant or fragment that, when used at a concentration of 2 μM in the following in vitro assay, is capable of increasing GLUT4 translocation into skeletal muscle as compared to an untreated control. L6-GLUT4myc cells are cultured in 10% FBS and 2 μg / ml blasticidin. The cells are allowed to grow for 48 - 72 hours and then seeded at 15,000 cells per well in 2% FBS in a 24-well plate and allowed to differentiate for 6 to 8 days prior to the experiment. The L6-GLUT4myc cells are serum-starved for 3 hours and then incubated with 100 nM insulin for 30 minutes or with 200, 20, 2.0, and 0.2 μM SP and 2, 1, 0.5, and 0.25 mg / ml peptide composition for 3 hours. A 3-hour incubation period was selected based on previous findings that determined that incubation with a dipeptide containing branched-chain amino acids for 3 hours increased glucose uptake in L6 myotubes 1. To determine GLUT4myc translocation at the same time point, the treatments were staggered. The amount of myc-tagged GLUT4 on the cell surface was measured by antibody-conjugated colorimetric assay. Briefly, after incubation with insulin for 30 minutes or with synthetic peptide or peptide composition for 3 hours, the L6-GLUT4myc cells were fixed by incubation with 3% paraformaldehyde (PFA). Then, a 0.1 M glycine solution was added to quench the PFA and the cells were blocked with 5% goat serum. The myotube monolayer was exposed to anti-myc antibody and then incubated with peroxidase-conjugated donkey anti-mouse IgG. 1 mL of o-phenylenediamine dihydrochloride (OPD) reagent was added to each well and the reaction was terminated by adding 250 μl / well of 3 M HCl. To determine GLUT4 translocation to the cell surface, the measured aliquots for each condition were determined spectrophotometrically on a microplate reader using the absorbance at 492 nm. Preferably, the peptide or fragment is capable of increasing GLUT4 translocation by at least 50% as compared to an untreated control (i.e., the relative unit increase in GLUT4 translocation is 1% - 1.5%).

[0331] "Antibacterial" or "antibacterial activity" as applied to a peptide or fragment means a peptide or fragment that is capable of visibly inhibiting bacterial growth in the following agar plate-based growth inhibition assay: Peptide stock solution dissolved in DMSO = 5 mg / mL. The bacterial inoculum was adjusted to a McFarland 0.5 standard and the MHA plates were swabbed. Blank disks were placed on the plates and 10 μL of each compound (at 64 μg / mL - maximum test concentration) was added. The plates were incubated at 37 °C for 16 - 18 hours. Appropriate controls were also performed (DMSO; Mueller-Hinton medium alone; and two antibiotic disks - ciprofloxacin and tetracycline).

[0332] "Anti-inflammatory" applied to a peptide or fragment means a peptide or fragment that, when used to treat LPS-stimulated J774.2 macrophages at 100 μM, is capable of significantly reducing the TNFα secretion of the macrophages (compared to untreated LPS-stimulated J774.2 macrophages). The J774.2 macrophages were treated with 100 μM of the synthetic peptide for 24 hours, and then stimulated with (A) LPS (10 ng / ml) for 5 hours or (B) LPS (10 ng / ml) for 5 hours and then with ATP (5 mM) for 1 hour. The supernatant was collected and the level of TNFα was determined by ELISA.

[0333] "Cell growth promotion" or "cell growth or proliferation promotion" applied to a peptide or fragment means a peptide or fragment that, in the following assay, is capable of increasing the elastin production or cell proliferation of human skin treated with a solution of 20 μM of the peptide or fragment. Skin explants were prepared from abdominoplasty. Some of the explants were degreased with alcohol to obtain dehydrated skin. These explants were maintained in a maintenance medium provided by the supplier Bioprédic International for 5 days. The test item was applied twice a day, 5 μL for each explant. At the end of the test, a viability control was achieved with MTT on two of the explants, and the third explant was fixed in 4% formaldehyde for histological and cell staining. For each analysis (D1 and D5), histological analysis was performed on the degreased explants, the explants treated with the test item, the 0.3% DMSO control, and the water control. After receipt in the laboratory, each skin explant in the maintenance medium was degreased with 5 μL of alcohol over a 3-hour period. After 3 hours, all skin explants were treated twice a day with the test item and were incubated at 37 °C ± 2 °C, 5% CO 2Incubate for 1 day or 5 days. At day 1 and day 5, MTT is used to achieve the integrity of the system with viability controls. Histological analysis is performed by laboratory Gredeco, and immunohistochemistry of elastin and Ki67 is performed by the same laboratory. Immunohistochemistry of filaggrin is performed by laboratory Intertek. Detection of elastin (rabbit monoclonal antibody, clone P15502, LSBio) is performed using the immunoperoxidase technique in two layers (ABC kit, Vector Laboratories) and is visualized by AEC (3-amino-9-ethylcarbazole). The immunohistochemical staining intensity in elastic fibers is evaluated using semi-quantitative histological scoring. Epithelial cell proliferation is analyzed immunohistochemically using an anti-Ki67 antibody. Immunodetection is performed in three layers using the indirect immunoperoxidase technique, amplified (DAKO kit) and visualized by AEC (3-amino-9-ethylcarbazole). The number of labeled cells (keratinocytes in the basal layer of the epidermis) is counted, and the total number of basal cells is provided to calculate the percentage of labeled cells. Specific staining of filaggrin is performed by immunoperoxidase staining (ABC kit, Fisher). The intensity of immunohistochemical labeling in the epidermis is evaluated relative to the negative control of the solvent (water or 0.3% DMSO).

[0334] "Peptides enriched with a molecular weight of less than 10 KD" applied to the compositions of the present invention means that the dry weight percentage of peptides with a molecular weight of less than 10 KD in the composition is greater than the dry weight percentage of polypeptides / proteins with a molecular weight of 10 KD or higher in the composition.

[0335] "Homologues" of a reference protein should be understood to mean proteins from different plant species that have at least 60% sequence homology with the reference protein. Thus, for example, homologues of the pea protein P13918 include:

[0336] >gi|137584|sp|P08438.1|VCL_VICFA RecName: Full = Vicilin; Flags: Precursor [Broad bean]

[0337] >gi|22057|emb|CAA68559.1|Vicilin [Broad bean]>gi|383931031|gb|AFH56916.1|Vicilin [Broad bean]

[0338] >gi|502105533|ref|XP_004492829.1|Predicted: Vicilin-like isoform X1 [Chickpea (Cicer arietinum)] ChickPea

[0339] >gi|29539109|emb|CAD87730.1|Allergen Len c 1.0101[Lens culinaris]Lentil

[0340] A "variant" of an anti-inflammatory fragment should be taken to mean a fragment having an amino acid sequence substantially the same as that of the anti-inflammatory fragment and having the anti-inflammatory activity as defined above. Thus, for example, the term should be taken to include a fragment in which one or more amino acid residues are altered. Preferably, such alterations involve the insertion, addition, deletion, and / or substitution of 5 or fewer amino acids, more preferably 4 or fewer, even more preferably 3 or fewer, and most preferably only 1 or 2 amino acids. Insertions, additions, and substitutions with natural and modified amino acids are contemplated. Variants may have conservative amino acid changes, where the amino acid introduced is structurally, chemically, or functionally similar to the amino acid being replaced. Generally, a variant has at least 70% amino acid sequence homology with the parental anti-inflammatory fragment, preferably at least 80% sequence homology, more preferably at least 90% sequence homology, and desirably at least 95%, 96%, 97%, 98%, or 99% sequence homology.

[0341] In this specification, the term "sequence identity" should be understood to encompass both sequence identity and similarity, i.e., a variant (or homolog) that shares 70% sequence identity with a reference sequence is one in which any 70% of the aligned residues of the variant (or homolog) are identical to or are conservative substitutions for the corresponding residues in the reference sequence over the entire sequence length. Sequence identity is the amount of characters that exactly match between two different sequences. Thus, gaps are not counted and the measurement is related to the shorter of the two sequences. In terms of "sequence homology", the term should be understood to mean a variant (or homolog) that shares a defined percentage similarity or identity with a reference sequence when the percentage of aligned residues of the variant (or homolog) is identical to or is a conservative substitution for the corresponding residues in the reference sequence and where the variant (or homolog) and the reference sequence share the same function. The alignment and percentage homology or sequence identity can be determined using software programs known in the art, for example, one alignment program is BLAST using default parameters. Details of these programs can be obtained at the following Internet URL: http: / / www.ncbi.nlm.nih.gov / blast / Blast.cgi.

[0342] Variant of SEQUENCE ID NO: 109 (Anti - inflammatory Peptide (I_37)

[0343] Variants of SEQUENCE ID NO:109 (RGPQQYAEWQINEK) are provided below, including variants with 1, 2 or 3 conservative amino acid substitutions, 1, 2 to 3 non-conservative amino acid substitutions, 1 - 2 amino acid additions, 1, 2 or 3 amino acid deletions:

[0344] One conservative amino acid substitution:

[0345] RGPQQYAEWQINER, RGPQQYAEWQINDK, RGPQQFAEWQINEK,KGPQQYAEWQINEK,RGPEQYAEWQINEK, RGPQEYAEWQINEK,RGPQQYADWQINEK,RGPQQYAEYQINEK (SEQ ID NO268-275)

[0346] Two conservative amino acid substitutions:

[0347] KGPEQYAEWQINEK, KGPQEYAEWQNEK, KGPQQFAEWQINEK,

[0348] RGPEQFAEWQINEK, KGPQQYAEWQINER, RGPQQYAEWQINDR,

[0349] RGPQQYADWQINDK,RGPQQFAEWQINER (SEQ ID NO276–283)

[0350] Three conservative amino acid substitutions:

[0351] RGPQQYAEWQVNEK, RGPQQFAEWQINEK, KGPQQFAEWQNER,

[0352] KGPQQFAEWQVNEK, RGPQQFAEWQVNDK, RGPQQYADWQINDR,

[0353] KGPQQYADWQINDK,RGPQQFADYQINEK(SEQ ID NO284-291)

[0354] One non-conservative amino acid substitution

[0355] RGPQQYARWQINEK, RGPQQYAEWQINEE, HGPQQYAEWQINEK,,

[0356] RGPYQYAEWQINEK, RGPQQYMEWQINEK, RGPQQYAEWCINEK,

[0357] RGPQPYAEWQINEK (SEQ ID NO292 - 298)

[0358] Two non - conservative amino acid substitutions

[0359] RGGQQYAEWQINED, RGPQQYARWKINEK, RGGQQYAETQINEK,

[0360] RGPLQYAEWQNNEK, EGPQQYAEWQINED, RGPQQYAEWQINLL,

[0361] RGPQQGGEWQINEK (SEQ ID NO 299 - 305)

[0362] Three non - conservative amino acid substitutions

[0363] RGPQQYAEWQIGGG, RGPQQKYEWQINEK, RGPQAQYEWQINEK,

[0364] RPHQQYAEWQINEK, RGPQHHHEWQINEK, RGPPQYAPPQINEK,

[0365] RGPQCYYEWCINEK, RGPTQYAEGQINEG (SEQ ID NO 306 - 313)

[0366] One or two amino acid additions

[0367] RGPQQYAEWQINEKG, RGPQQYAEWQINEKY, RGPQQYAFTEWQINEK,

[0368] RGPQSQYAEWQINEKPM, RGPQQYAEWQINEKKK, RRRRGPQQYAEWQINEK (SEQ ID NO314–319).

[0369] The term "variant" generally encompasses fragments of the peptides of the present invention. "Fragment of a peptide of the present invention" or "peptide fragment" means a fragment of one of the peptides of the present invention having at least 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 or 22 amino acids and usually having biological activity, such as anti-inflammatory activity, cell growth or proliferation promoting activity, glucose transport promoting activity or antibacterial activity. In one embodiment, the fragment consists of at least 30%, 40%, 50%, 60%, 70%, 80% or 90% of a reference sequence. Examples of fragments of the present invention are provided in SEQUENCE ID NO 320 - 330.

[0370] RGPQQYAEWQINE, RGPQQYAEWQIN, RGPQQYAEWQI, GPQQYAEWQINEK, PQQYAEWQINEK, QQYAEWQINEK, QQYAEWQI, PQQYAEWQINE, PQQYAEWQIN, RGPQQYA, EWQINEK (SEQ ID NO 320 - 330)

[0371] "Inflammatory disorder" means an immune-mediated inflammatory condition affecting humans and is typically characterized by dysregulated expression of one or more cytokines. Examples of inflammatory disorders include skin inflammatory disorders, arthritis inflammatory disorders, inflammatory disorders of the cardiovascular system, certain autoimmune diseases, lung and airway inflammatory disorders, intestinal inflammatory disorders. Examples of skin inflammatory disorders include dermatitis, such as atopic dermatitis and contact dermatitis, acne vulgaris and psoriasis. Examples of arthritis inflammatory disorders include rheumatoid arthritis. Examples of inflammatory disorders of the cardiovascular system are cardiovascular diseases and atherosclerosis. Examples of autoimmune diseases include type 1 diabetes, Graves' disease, Guillain - Barré disease, lupus, psoriatic arthritis and ulcerative colitis. Examples of lung and airway inflammatory disorders include asthma, cystic fibrosis, COPD, emphysema and acute respiratory distress syndrome. Examples of intestinal inflammatory disorders include colitis and inflammatory bowel disease. Other inflammatory disorders include cancer, hay fever, periodontitis, allergy, hypersensitivity, ischemia, depression, systemic diseases, post - infectious inflammation and bronchitis.

[0372] In the present specification, the term "metabolic disorder" should be understood to include prediabetes, diabetes; type 1 diabetes; type 2 diabetes; metabolic syndrome; obesity; diabetic dyslipidemia; hyperlipidemia; hypertension; hypertriglyceridemia; hyperfattyacidemia; hypercholesterolemia; hyperinsulinemia and MODY.

[0373] "Maintaining or restoring intestinal health" means reducing and / or modulating the pro-inflammatory response in the intestine and more specifically in epithelial cells. A healthy microbiome provides a certain protection against pathogenic viruses and bacteria, and their presence is required to guide the development of our immune system. It has been shown that these bacteria can respond to signals of stress, illness or age in the human body, which can manifest as inflammation and thus switch on their pathogenic genes and cause or contribute to disease. The ability to reduce the inflammatory response and maintain it at a healthy level can help maintain healthy bacteria. Digestive problems, including the number one health problem in North America, seem to occur more frequently in recent years. One way to maintain digestive health is to maintain appropriate inflammation and gut flora.

[0374] "Maintaining or restoring muscle health" means helping to maintain or restore mammalian muscle health caused by injuries that occur during exercise. By reducing inflammation, peptides promote the recovery from injuries during exercise and relieve muscle soreness / pain and exercise-related injuries. They can also be used to reduce and prevent muscle cramps and allow for a faster recovery from muscle cramps. Cramps can be caused by physical stress, psychological stress and / or repetitive strain stress. By reducing inflammation, peptides help reduce muscle myopathy and help prevent sarcopenia in mammals, promote the recovery from injuries during exercise, and relieve muscle soreness / exercise-related pain and injuries. They can also be used to reduce and prevent muscle cramps and allow for a rapid recovery from muscle cramps. Cramps may be caused by physical stress, psychological stress and / or repetitive compression injury stress. By reducing inflammation, peptides help reduce muscle myopathy and help prevent sarcopenia in mammals.

[0375] In this specification, the term "composition" should be understood to mean something made by hand by a human and does not exclude naturally occurring compositions. Exemplary compositions include personal care compositions and pharmaceutical compositions.

[0376] In this specification, the term "substantially all" applied to a list of peptides or fragments should be understood to mean at least 60%, 70%, 80%, 90% or 95% of the peptide or fragment.

[0377] In this specification, the term "personal care composition" should be understood to mean a composition formulated for the cleansing or treatment of the human body, particularly the skin, teeth, nails, feet and hair. Examples include shampoos, conditioners, skin creams and lotions, powders, toothpastes, shower gels or creams, body lotions, deodorants and antiperspirants. Description of the Drawings

[0378] Figures 1 to 18: Effects of the eighteen synthetic peptides of the present invention on TNF- secretion in THP1 cells. All experiments were prepared in triplicate (6 wells / condition) on three plates. Significance was calculated using Students t-test (*p < 0.05 compared to control, **p < 0.01 compared to control, ***p < 0.001 compared to control)

[0379] Figure 19 . Viability of J774.2 macrophages after treatment with synthetic peptides. J774.2 macrophages were treated with 100 μM synthetic peptides for 24 hours before performing the alamar blue assay. Data are presented as the mean of n = 3 + / - SEM.

[0380] Figure 20 . Effects of peptide compositions on cell survival. J774.2 macrophages were treated with (A) 1 mg / ml or (B) 0.5 mg / ml peptide compositions for 24 hours before performing the alamar blue assay. Data are shown as (A) n = 1 + / - SEM and (B) n = 3 + / - SEM.

[0381] Figure 21 : Effects of DMSO vehicle on TNFα and IL-1β secretion from J774.2 macrophages. J774.2 macrophages were treated with DMSO at final concentrations of 0.3% and 1% (equivalent to the amount used to dissolve the peptides) for 24 hours, and the effects on TNFα and IL-1β after stimulation were determined. Data are presented as the mean of n = 3 + / - SEM. (***p < 0.001 w.r.t LPS).

[0382] Figure 22 . Effects of six peptides of the present invention on TNFα and IL-1β secretion from J774.2 macrophages. J774.2 macrophages were treated with 100 μM synthetic peptides for 24 hours, then stimulated with (A) LPS (10 ng / ml) for 5 hours or (B) LPS (10 ng / ml) for 5 hours and then with ATP (5 mM) for 1 hour. Supernatants were collected and the levels of (A) TNFα and (B) IL-1β were determined by ELISA. ( *** p < 0.001 w.r.t LPS, ** p < 0.01 w.r.t LPS, * p < 0.05, ### p < 0.001 w.r.t.LPS / ATP, ## p < 0.01 w.r.t LPS / ATP and #p < 0.05 with respect to LPS / ATP). Final concentration of DMSO in the wells: SP1 - 0.3%, SP2 - 0%, SP3 - 0.3%, SP4 - 1%, SP5 - 1%, SP6 - 0.3%, positive control - 0%. Data are represented as mean ± SEM, n = 3.

[0383] Figure 23 : Effect of the peptide composition of the present invention on TNFα and IL-1β secretion. J774.2 macrophages were treated with 0.5 mg / ml of the peptide composition for 24 hours, and then stimulated with (A) LPS (10 ng / ml) for 5 hours or (B) LPS (10 ng / ml) for 5 hours and then with ATP (5 mM) for 1 hour. Supernatants were collected and the levels of (A) TNFα and (B) IL-1β were determined by ELISA. ( *** p < 0.001 with respect to untreated + LPS, ### p < 0.001 with respect to untreated + LPS / ATP). Data are represented as mean ± SEM, n = 3.

[0384] Figure 24 . Effect of synthetic peptides and DMSO vehicle on TNFα. J774.2 macrophages were treated with 100 μM of synthetic peptides for 24 hours and then with LPS (10 ng / ml) for 5 hours. Supernatants were collected and the levels of TNFα were determined by ELISA. p < 0.001 with respect to 0.3% DMSO + LPS, ## p < 0.01 with respect to 0.3% DMSO + LPS, +++ p < 0.001 with respect to 1% DMSO + LPS, ++ p < 0.01 with respect to 1% DMSO + LPS / ATP). Final concentration of DMSO in the wells: positive control - 0%, SP1 - 0.3%, SP2 - 0%, SP3 - 0.3%, SP4 - 1%, SP5 - 1%, SP6 - 0.3%.

[0385] Figure 25 . THP-1 differentiated macrophages treated with the composition (I_2_HR) of the rice peptide of the present invention for 24 hours were compared with untreated cells before LPS stimulation. Compared with untreated cells, TNF-α secretion in I_2_HR-treated cells was reduced by 92%. Significant results were observed at concentrations of 100 μg / ml and 500 μg / ml of I_2_HR, indicating the potency of I_2_HR.

[0386] Figures 26 to 28. Effects of three synthetic peptides of the present invention on TNF- secretion in THP1 cells. All experiments were prepared in duplicate (6 wells / condition) on three plates. Significance was calculated using the Students t-test (*p < 0.05 compared to control, **p < 0.01 compared to control, ***p < 0.001 compared to control). Detailed implementation

[0387] Example 1 - Inflammatory Response

[0388] In response to stimulation by endotoxins such as lipopolysaccharide (LPS), macrophages secrete TNF-α. TNF-α is considered to be related to systemic inflammation, and abnormal regulation of TNF-α production is considered to be related to many diseases. The Biolegend assay is a sandwich ELISA kit designed to precisely quantify human TNF-α from cell culture supernatants, sera, or plasma.

[0389] In RPMI containing 10% fetal bovine serum (FCS), 1% penicillin / streptomycin (Pen / strep), 1% L-glutamine, and 100 nM PMA, THP-1 monocytes were seeded at 10,000 cells / well in a 96-well plate and allowed to differentiate for 72 hours before the experiment.

[0390] After differentiation, the cells were incubated with synthetic peptides at 100 ng / ml, 10 ng / ml, or 1 ng / ml for 24 hours, respectively.

[0391] After treatment, the cells were stimulated with 10 ng / ml LPS for 5 hours, and the amount of TNF-α in the supernatant was determined using the Biolegend assay ELISA kit.

[0392] The results were calculated as a percentage of the untreated control. An increase in the optical density reading indicates a greater amount of TNF-α released into the cell culture supernatant.

[0393] The results are provided in Figures 1 to 21 and summarized in Table 1 below. All experiments were prepared in duplicate (6 wells / condition) on three plates. Significance was calculated using the Student t-test (*p < 0.05 compared to control, **p < 0.01 compared to control, ***p < 0.001 compared to control).

[0394] Table 1

[0395] Figure Number SEQ ID TNF - α Reduction Figure 1 339 26％ Figure 2 352 23％ Figure 3 341 21％ Figure 4 351 18％ Figure 5 144 16％ Figure 6 93 14％ Figure 7 320 13％ Figure 8 92 13％ Figure 9 75 11％ Figure 10 76 9％ Figure 11 349 6％ Figure 12 350 Figure 13 105 9％ Figure 14 177 Figure 15 345 23％ Figure 16 353 20％ Figure 17 344 20％ Figure 18 346 18％ Figure 26 85 80％ Figure 27 91 80％ Figure 28 420 80％

[0396] Example 2 - Inflammatory Response

[0397] Determine the effects of six synthetic peptides SP1 to SP6 (SEQUENCE ID NO: 108, 109, 110, 111, 85 and 91) of the present invention and four peptide compositions on the in vitro inflammatory response using cell lines.

[0398] Peptide composition I_1_HR (rice) contains the following peptides (determined by SEQ ID): 116, 197, 207, 112, 211, 158, 201, 203, 114, 183, 130, 113, 182, 167, 166, 152, 220, 213, 215, 154, 219, 218, 165, 123, 185, 190, 209, 181, 198, 200, 147, 172, 184, 124, 153, 205, 115, 196, 151, 161, 160, 216, 210, 208, 146, 133, 204, 212, 206.

[0399] Peptide composition I_2_HR (rice) contains the following peptides (determined by SEQ ID): 189, 177, 174, 129, 176, 202, 193, 195, 194, 192, 182, 128, 220, 127, 134, 136, 135, 180, 179, 178, 219, 218, 145, 120, 175, 190, 149, 126, 187, 191, 121, 122, 159, 132, 162, 137, 150, 186, 188, 164, 118, 125, 163, 157, 156, 117.

[0400] Peptide composition E_1_HR (pea) contains the following peptides (determined by SEQ ID): 74, 76, 106, 102, 101, 100, 92, 96, 83, 89, 90, 104, 82, 75, 79, 78, 77, 99, 103, 72, 86, 105, 94, 93, 81, 97, 80, 88, 85, 87, 71, 107, 73, 84, 98, 95.

[0401] Peptide composition E_2_HR (pea) contains homologs of the peptides of the present invention.

[0402] The J774.2 mouse macrophage cell line was treated with each synthetic peptide (Sp) at 100 μM and each peptide composition at 0.5 mg / ml, and the effects on two pro-inflammatory markers - tumor necrosis factor α (TNFα) and interleukin-1β (IL-1β) were determined after inducing inflammation using lipopolysaccharide (LPS) as an inflammatory stimulant. One-way ANOVA was used together with the Dunnett's test for multiple comparisons, and each mean was compared with a single control mean.

[0403] Example 3 - Synthetic Peptide: Cell Viability

[0404] First, dilute the synthetic peptides in a suitable solvent. Dimethyl sulfoxide (DMSO) is the solvent chosen for peptides with poor predicted water solubility. The final concentration of DMSO in each well: SP1(1_155_HR) - 0.3%, SP2(1_374_HR) - 0%, SP3(E_155_HR) - 0.3%, SP4(E_54_HR) - 1%, SP5(E_41_HR) - 1%, SP6(E_788_HR) - 0.3%, positive control - 0%. Before performing the alamar blue assay, first treat the cells with 100 μM of each SP for 24 hours. No viability issues were found with any of the peptides.

[0405] Example 4 - Peptide Composition: Preparation and Toxicity

[0406] Prepare the peptide composition by adjusting the pH to 6 - 7 and sterile filtering. Determine the effect of the peptide composition on cell viability. J774.2 macrophages are treated with 1 mg / ml and 0.5 mg / ml of each peptide composition, treated with hydrogen peroxide to induce cell death as a positive control, and treated with a peptide known to be non-toxic as a negative control. Then, perform the alamar blue assay, and cell survival is shown as a percentage of untreated (100%). Since the 1 mg / ml peptide impairs cell survival, the 0.5 mg / ml peptide composition is used for further assays. Figure 19 as a percentage of untreated (100%). Since the 1 mg / ml peptide impairs cell survival, the 0.5 mg / ml peptide composition is used for further assays.

[0407] Example 5 - Inflammatory Markers

[0408] Determine the effect of DMSO on TNFα and IL-1β secretion. 1% DMSO significantly increases the level of TNFα ( Figure 3 A, ***p < 0.001 w.r.t LPS), and this is taken into account when analyzing the effect of the peptides on TNFα. No significant effect was observed for DMSO and IL-1β secretion.

[0409] Example 6 - Inflammatory Response

[0410] THP-1 differentiated macrophages treated with the composition (I_2_HR) of the rice peptides of the present invention for 24 hours are then stimulated with LPS and compared with untreated cells. Compared with untreated cells, TNF-α secretion in I_2_HR-treated cells is reduced by 92%. Significant results were observed at 100 μg / ml and 500 μg / ml concentrations of I_2_HR, indicating the potency of I_2_HR.

[0411] The present invention is not limited to the embodiments described above, and can be changed in structure and details without departing from the spirit of the present invention.

[0412]

[0413]

[0414]

[0415]

[0416]

[0417]

[0418]

[0419]

[0420]

[0421]

[0422]

[0423]

[0424]

[0425]

[0426]

[0427]

[0428] Sequence Listing <110> Nuritas Limited <120> Anti-inflammatory Peptides and Their Uses <130> P11683EPDIV1 <140> EP20165063.7 <141> 2016-07-18 <150> 15177013.8 <151> 2015-07-16 <160> 425 <170> PatentIn version 3.5 <210> 1 <211> 459 <212> PRT <213> Pea <400> 1 Met Ala Ala Thr Thr Met Lys Ala Ser Phe Pro Leu Leu Met Leu Met 1 5 10 15 Gly Ile Ser Phe Leu Ala Ser Val Cys Val Ser Ser Arg Ser Asp Pro 20 25 30 Gln Asn Pro Phe Ile Phe Lys Ser Asn Lys Phe Gln Thr Leu Phe Glu 35 40 45 Asn Glu Asn Gly His Ile Arg Leu Leu Gln Lys Phe Asp Gln Arg Ser 50 55 60 Lys Ile Phe Glu Asn Leu Gln Asn Tyr Arg Leu Leu Glu Tyr Lys Ser 65 70 75 80 Lys Pro His Thr Ile Phe Leu Pro Gln His Thr Asp Ala Asp Tyr Ile 85 90 95 Leu Val Val Leu Ser Gly Lys Ala Ile Leu Thr Val Leu Lys Pro Asp 100 105 110 Asp Arg Asn Ser Phe Asn Leu Glu Arg Gly Asp Thr Ile Lys Leu Pro 115 120 125 Ala Gly Thr Ile Ala Tyr Leu Val Asn Arg Asp Asp Asn Glu Glu Leu 130 135 140 Arg Val Leu Asp Leu Ala Ile Pro Val Asn Arg Pro Gly Gln Leu Gln 145 150 155 160 Ser Phe Leu Leu Ser Gly Asn Gln Asn Gln Gln Asn Tyr Leu Ser Gly 165 170 175 Phe Ser Lys Asn Ile Leu Glu Ala Ser Phe Asn Thr Asp Tyr Glu Glu 180 185 190 Ile Glu Lys Val Leu Leu Glu Glu His Glu Lys Glu Thr Gln His Arg 195 200 205 Arg Ser Leu Lys Asp Lys Arg Gln Gln Ser Gln Glu Glu Asn Val Ile 210 215 220 Val Lys Leu Ser Arg Gly Gln Ile Glu Glu Leu Ser Lys Asn Ala Lys 225 230 235 240 Ser Thr Ser Lys Lys Ser Val Ser Ser Glu Ser Glu Pro Phe Asn Leu 245 250 255 Arg Ser Arg Gly Pro Ile Tyr Ser Asn Glu Phe Gly Lys Phe Phe Glu 260 265 270 Ile Thr Pro Glu Lys Asn Pro Gln Leu Gln Asp Leu Asp Ile Phe Val 275 280 285 Asn Ser Val Glu Ile Lys Glu Gly Ser Leu Leu Leu Pro His Tyr Asn 290 295 300 Ser Arg Ala Ile Val Ile Val Thr Val Asn Glu Gly Lys Gly Asp Phe 305 310 315 320 Glu Leu Val Gly Gln Arg Asn Glu Asn Gln Gln Glu Gln Arg Lys Glu 325 330 335 Asp Asp Glu Glu Glu Glu Gln Gly Glu Glu Glu Ile Asn Lys Gln Val 340 345 350 Gln Asn Tyr Lys Ala Lys Leu Ser Ser Gly Asp Val Phe Val Ile Pro 355 360 365 Ala Gly His Pro Val Ala Val Lys Ala Ser Ser Asn Leu Asp Leu Leu 370 375 380 Gly Phe Gly Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly 385 390 395 400 Asp Glu Asp Asn Val Ile Ser Gln Ile Gln Arg Pro Val Lys Glu Leu 405 410 415 Ala Phe Pro Gly Ser Ala Gln Glu Val Asp Arg Ile Leu Glu Asn Gln 420 425 430 Lys Gln Ser His Phe Ala Asp Ala Gln Pro Gln Gln Arg Glu Arg Gly 435 440 445 Ser Arg Glu Thr Arg Asp Arg Leu Ser Ser Val 450 455 <210> 2 <211> 124 <212> PRT <213> Pea <400> 2 Asp Arg Arg Gln Glu Leu Ser Asn Glu Asn Val Leu Val Lys Val Ser 1 5 10 15 Arg Arg Gln Leu Glu Glu Leu Ser Lys Asn Ala Lys Ser Ser Ser Arg 20 25 30 Arg Ser Val Ser Ser Glu Ser Gly Pro Phe Asn Leu Arg Ser Glu Asp 35 40 45 Pro Leu Tyr Ser Asn Asn Ser Gly Lys Phe Phe Glu Leu Thr Pro Glu 50 55 60 Lys Asn Gln Gln Leu Gln Asp Leu Asp Leu Phe Val Asn Ser Val Asp 65 70 75 80 Leu Lys Glu Gly Ser Leu Leu Leu Pro Asn Tyr Asn Ser Arg Ala Leu 85 90 95 Leu Val Leu Val Leu Val Val Asn Glu Gly Lys Gly Asp Phe Glu Leu 100 105 110 Val Gly Gln Arg Asn Glu Asn Gln Gly Lys Glu Asn 115 120 <210> 3 <211> 520 <212> PRT <213> Pea <400> 3 Met Ala Thr Lys Leu Leu Ala Leu Ser Leu Ser Phe Cys Phe Leu Leu 1 5 10 15 Leu Gly Gly Cys Phe Ala Leu Arg Glu Gln Pro Glu Gln Asn Glu Cys 20 25 30 Gln Leu Glu Arg Leu Asn Ala Leu Glu Pro Asp Asn Arg Ile Glu Ser 35 40 45 Glu Gly Gly Leu Ile Glu Thr Trp Asn Pro Asn Asn Lys Gln Phe Arg 50 55 60 Cys Ala Gly Val Ala Leu Ser Arg Ala Thr Leu Gln His Asn Ala Leu 65 70 75 80 Arg Arg Pro Tyr Tyr Ser Asn Ala Pro Gln Glu Ile Phe Ile Gln Gln 85 90 95 Gly Asn Gly Tyr Phe Gly Met Val Phe Pro Gly Cys Pro Glu Thr Phe 100 105 110 Glu Glu Pro Gln Glu Ser Glu Gln Gly Glu Gly Arg Arg Tyr Arg Asp 115 120 125 Arg His Gln Lys Val Asn Arg Phe Arg Glu Gly Asp Ile Ile Ala Val 130 135 140 Pro Thr Gly Ile Val Phe Trp Met Tyr Asn Asp Gln Asp Thr Pro Val 145 150 155 160 Ile Ala Val Ser Leu Thr Asp Ile Arg Ser Ser Asn Asn Gln Leu Asp 165 170 175 Gln Met Pro Arg Arg Phe Tyr Leu Ala Gly Asn His Glu Gln Glu Phe 180 185 190 Leu Arg Tyr Gln His Gln Gln Gly Gly Lys Gln Glu Gln Glu Asn Glu 195 200 205 Gly Asn Asn Ile Phe Ser Gly Phe Lys Arg Asp Phe Leu Glu Asp Ala 210 215 220 Phe Asn Val Asn Arg His Ile Val Asp Arg Leu Gln Gly Arg Asn Glu 225 230 235 240 Asp Glu Glu Lys Gly Ala Ile Val Lys Val Lys Gly Gly Leu Ser Ile 245 250 255 Ile Ser Pro Pro Glu Lys Gln Ala Arg His Gln Arg Gly Ser Arg Gln 260 265 270 Glu Glu Asp Glu Asp Glu Asp Glu Glu Arg Gln Pro Arg His Gln Arg 275 280 285 Gly Ser Arg Gln Glu Glu Glu Glu Asp Glu Asp Glu Glu Arg Gln Pro 290 295 300 Arg His Gln Arg Arg Arg Gly Glu Glu Glu Glu Glu Asp Lys Lys Glu 305 310 315 320 Arg Arg Gly Ser Gln Lys Gly Lys Ser Arg Arg Gln Gly Asp Asn Gly 325 330 335 Leu Glu Glu Thr Val Cys Thr Ala Lys Leu Arg Leu Asn Ile Gly Pro 340 345 350 Ser Ser Ser Pro Asp Ile Tyr Asn Pro Glu Ala Gly Arg Ile Lys Thr 355 360 365 Val Thr Ser Leu Asp Leu Pro Val Leu Arg Trp Leu Lys Leu Ser Ala 370 375 380 Glu His Gly Ser Leu His Lys Asn Ala Met Phe Val Pro His Tyr Asn 385 390 395 400 Leu Asn Ala Asn Ser Ile Ile Tyr Ala Leu Lys Gly Arg Ala Arg Leu 405 410 415 Gln Val Val Asn Cys Asn Gly Asn Thr Val Phe Asp Gly Glu Leu Glu 420 425 430 Ala Gly Arg Ala Leu Thr Val Pro Gln Asn Tyr Ala Val Ala Ala Lys 435 440 445 Ser Leu Ser Asp Arg Phe Ser Tyr Val Ala Phe Lys Thr Asn Asp Arg 450 455 460 Ala Gly Ile Ala Arg Leu Ala Gly Thr Ser Ser Val Ile Asn Asn Leu 465 470 475 480 Pro Leu Asp Val Val Ala Ala Thr Phe Asn Leu Gln Arg Asn Glu Ala 485 490 495 Arg Gln Leu Lys Ser Asn Asn Pro Phe Lys Phe Leu Val Pro Ala Arg 500 505 510 Gln Ser Glu Asn Arg Ala Ser Ala 515 520 <210> 4 <211> 613 <212> PRT <213> Pea <400> 4 Met Ala Thr Thr Ile Lys Ser Arg Phe Pro Leu Leu Leu Leu Leu Gly 1 5 10 15 Ile Ile Phe Leu Ala Ser Val Val Cys Val Thr Tyr Ala Asn Tyr Asp 20 25 30 Glu Gly Ser Glu Pro Arg Val Pro Ala Gln Arg Glu Arg Gly Arg Gln 35 40 45 Glu Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Arg Pro Ser Tyr 50 55 60 Glu Lys Glu Glu Asp Glu Glu Glu Gly Gln Arg Glu Arg Gly Arg Gln 65 70 75 80 Glu Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Arg Pro Ser Tyr 85 90 95 Glu Lys Gln Glu Asp Glu Glu Glu Lys Gln Lys Tyr Arg Tyr Gln Arg 100 105 110 Glu Lys Glu Asp Glu Glu Glu Lys Gln Lys Tyr Gln Tyr Gln Arg Glu 115 120 125 Lys Lys Glu Gln Lys Glu Val Gln Pro Gly Arg Glu Arg Trp Glu Arg 130 135 140 Glu Glu Asp Glu Glu Gln Val Asp Glu Glu Trp Arg Gly Ser Gln Arg 145 150 155 160 Arg Glu Asp Pro Glu Glu Arg Ala Arg Leu Arg His Arg Glu Glu Arg 165 170 175 Thr Lys Arg Asp Arg Arg His Gln Arg Glu Gly Glu Glu Glu Glu Arg 180 185 190 Ser Ser Glu Ser Gln Glu Arg Arg Asn Pro Phe Leu Phe Lys Ser Asn 195 200 205 Lys Phe Leu Thr Leu Phe Glu Asn Glu Asn Gly His Ile Arg Leu Leu 210 215 220 Gln Arg Phe Asp Lys Arg Ser Asp Leu Phe Glu Asn Leu Gln Asn Tyr 225 230 235 240 Arg Leu Val Glu Tyr Arg Ala Lys Pro His Thr Ile Phe Leu Pro Gln 245 250 255 His Ile Asp Ala Asp Leu Ile Leu Val Val Leu Ser Gly Lys Ala Ile 260 265 270 Leu Thr Val Leu Ser Pro Asn Asp Arg Asn Ser Tyr Asn Leu Glu Arg 275 280 285 Gly Asp Thr Ile Lys Leu Pro Ala Gly Thr Thr Ser Tyr Leu Val Asn 290 295 300 Gln Asp Asp Glu Glu Asp Leu Arg Leu Val Asp Leu Val Ile Pro Val 305 310 315 320 Asn Gly Pro Gly Lys Phe Glu Ala Phe Asp Leu Ala Lys Asn Lys Asn 325 330 335 Gln Tyr Leu Arg Gly Phe Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asn 340 345 350 Thr Arg Tyr Glu Thr Ile Glu Lys Val Leu Leu Glu Glu Gln Glu Lys 355 360 365 Asp Arg Lys Arg Arg Gln Gln Gly Glu Glu Thr Asp Ala Ile Val Lys 370 375 380 Val Ser Arg Glu Gln Ile Glu Glu Leu Lys Lys Leu Ala Lys Ser Ser 385 390 395 400 Ser Lys Lys Ser Leu Pro Ser Glu Phe Glu Pro Ile Asn Leu Arg Ser 405 410 415 His Lys Pro Glu Tyr Ser Asn Lys Phe Gly Lys Leu Phe Glu Ile Thr 420 425 430 Pro Glu Lys Lys Tyr Pro Gln Leu Gln Asp Leu Asp Leu Phe Val Ser 435 440 445 Cys Val Glu Ile Asn Glu Gly Ala Leu Met Leu Pro His Tyr Asn Ser 450 455 460 Arg Ala Ile Val Val Leu Leu Val Asn Glu Gly Lys Gly Asn Leu Glu 465 470 475 480 Leu Leu Gly Leu Lys Asn Glu Gln Gln Glu Arg Glu Asp Arg Lys Glu 485 490 495 Arg Asn Asn Glu Val Gln Arg Tyr Glu Ala Arg Leu Ser Pro Gly Asp 500 505 510 Val Val Ile Ile Pro Ala Gly His Pro Val Ala Ile Thr Ala Ser Ser 515 520 525 Asn Leu Asn Leu Leu Gly Phe Gly Ile Asn Ala Glu Asn Asn Glu Arg 530 535 540 Asn Phe Leu Ser Gly Ser Asp Asp Asn Val Ile Ser Gln Ile Glu Asn 545 550 555 560 Pro Val Lys Glu Leu Thr Phe Pro Gly Ser Val Gln Glu Ile Asn Arg 565 570 575 Leu Ile Lys Asn Gln Lys Gln Ser His Phe Ala Asn Ala Glu Pro Glu 580 585 590 Gln Lys Glu Gln Gly Ser Gln Gly Lys Arg Ser Pro Leu Ser Ser Ile 595 600 605 Leu Gly Thr Phe Tyr 610 <210> 5 <211> 438 <212> PRT <213> Pea <400> 5 Met Ala Ala Thr Pro Ile Lys Pro Leu Met Leu Leu Ala Ile Ala Phe 1 5 10 15 Leu Ala Ser Val Cys Val Ser Ser Arg Ser Asp Gln Glu Asn Pro Phe 20 25 30 Ile Phe Lys Ser Asn Arg Phe Gln Thr Leu Tyr Glu Asn Glu Asn Gly 35 40 45 His Ile Arg Leu Leu Gln Lys Phe Asp Lys Arg Ser Lys Ile Phe Glu 50 55 60 Asn Leu Gln Asn Tyr Arg Leu Leu Glu Tyr Lys Ser Lys Pro Arg Thr 65 70 75 80 Leu Phe Leu Pro Gln Tyr Thr Asp Ala Asp Phe Ile Leu Val Val Leu 85 90 95 Ser Gly Lys Ala Thr Leu Thr Val Leu Lys Ser Asn Asp Arg Asn Ser 100 105 110 Phe Asn Leu Glu Arg Gly Asp Thr Ile Lys Leu Pro Ala Gly Thr Ile 115 120 125 Ala Tyr Leu Ala Asn Arg Asp Asp Asn Glu Asp Leu Arg Val Leu Asp 130 135 140 Leu Thr Ile Pro Val Asn Lys Pro Gly Gln Leu Gln Ser Phe Leu Leu 145 150 155 160 Ser Gly Thr Gln Asn Gln Pro Ser Leu Leu Ser Gly Phe Ser Lys Asn 165 170 175 Ile Leu Glu Ala Ala Phe Asn Thr Asn Tyr Glu Glu Ile Glu Lys Val 180 185 190 Leu Leu Glu Gln Gln Glu Gln Glu Pro Gln His Arg Arg Ser Leu Lys 195 200 205 Asp Arg Arg Gln Glu Ile Asn Glu Glu Asn Val Ile Val Lys Val Ser 210 215 220 Arg Glu Gln Ile Glu Glu Leu Ser Lys Asn Ala Lys Ser Ser Ser Lys 225 230 235 240 Lys Ser Val Ser Ser Glu Ser Gly Pro Phe Asn Leu Arg Ser Arg Asn 245 250 255 Pro Ile Tyr Ser Asn Lys Phe Gly Lys Phe Phe Glu Ile Thr Pro Glu 260 265 270 Lys Asn Gln Gln Leu Gln Asp Leu Asp Ile Phe Val Asn Ser Val Asp 275 280 285 Ile Lys Glu Gly Ser Leu Leu Leu Pro Asn Tyr Asn Ser Arg Ala Ile 290 295 300 Val Ile Val Thr Val Thr Glu Gly Lys Gly Asp Phe Glu Leu Val Gly 305 310 315 320 Gln Arg Asn Glu Asn Gln Gly Lys Glu Asn Asp Lys Glu Glu Glu Gln 325 330 335 Glu Glu Glu Thr Ser Lys Gln Val Gln Leu Tyr Arg Ala Lys Leu Ser 340 345 350 Pro Gly Asp Val Phe Val Ile Pro Ala Gly His Pro Val Ala Ile Asn 355 360 365 Ala Ser Ser Asp Leu Asn Leu Ile Gly Phe Gly Ile Asn Ala Glu Asn 370 375 380 Asn Glu Arg Asn Phe Leu Ala Gly Glu Glu Asp Asn Val Ile Ser Gln 385 390 395 400 Val Glu Arg Pro Val Lys Glu Leu Ala Phe Pro Gly Ser Ser His Glu 405 410 415 Val Asp Arg Leu Leu Lys Asn Gln Lys Gln Ser Tyr Phe Ala Asn Ala 420 425 430 Gln Pro Leu Gln Arg Glu 435 <210> 6 <211> 484 <212> PRT <213> Rice <400> 6 Met Ala Thr Thr Thr Ser Leu Leu Ser Ser Cys Leu Cys Ala Leu Leu 1 5 10 15 Leu Ala Pro Leu Phe Ser Gln Gly Val Asp Ala Trp Glu Ser Arg Gln 20 25 30 Gly Ala Ser Arg Gln Cys Arg Phe Asp Arg Leu Gln Ala Phe Glu Pro 35 40 45 Leu Arg Lys Val Arg Ser Glu Ala Gly Asp Thr Glu Tyr Phe Asp Glu 50 55 60 Arg Asn Glu Gln Phe Arg Cys Ala Gly Val Phe Val Ile Arg Arg Val 65 70 75 80 Ile Glu Pro Gln Gly Leu Val Val Pro Arg Tyr Ser Asn Thr Pro Ala 85 90 95 Leu Ala Tyr Ile Ile Gln Gly Lys Gly Tyr Val Gly Leu Thr Phe Pro 100 105 110 Gly Cys Pro Ala Thr His Gln Gln Gln Phe Gln Leu Phe Glu Gln Arg 115 120 125 Gln Ser Asp Gln Ala His Lys Phe Arg Asp Glu His Gln Lys Ile His 130 135 140 Glu Phe Arg Gln Gly Asp Val Val Ala Leu Pro Ala Ser Val Ala His 145 150 155 160 Trp Phe Tyr Asn Gly Gly Asp Thr Pro Ala Val Val Val Tyr Val Tyr 165 170 175 Asp Ile Lys Ser Phe Ala Asn Gln Leu Glu Pro Arg Gln Lys Glu Phe 180 185 190 Leu Leu Ala Gly Asn Asn Gln Arg Gly Gln Gln Ile Phe Glu His Ser 195 200 205 Ile Phe Gln His Ser Gly Gln Asn Ile Phe Ser Gly Phe Asn Thr Glu 210 215 220 Val Leu Ser Glu Ala Leu Gly Ile Asn Thr Glu Ala Ser Lys Arg Leu 225 230 235 240 Gln Ser Gln Asn Asp Gln Arg Gly Asp Ile Ile Arg Val Lys His Gly 245 250 255 Leu Gln Leu Leu Lys Pro Thr Leu Thr Gln Arg Gln Glu Glu His Arg 260 265 270 Gln Tyr Gln Gln Val Gln Tyr Arg Glu Gly Gln Tyr Asn Gly Leu Asp 275 280 285 Glu Asn Phe Cys Thr Ile Lys Ala Arg Val Asn Ile Glu Asn Pro Ser 290 295 300 Arg Ala Asp Tyr Tyr Asn Pro Arg Ala Gly Arg Ile Thr Leu Leu Asn 305 310 315 320 Asn Gln Lys Phe Pro Ile Leu Asn Leu Ile Gly Met Gly Ala Ala Arg 325 330 335 Val Asn Leu Tyr Gln Asn Ala Leu Leu Ser Pro Phe Trp Asn Ile Asn 340 345 350 Ala His Ser Val Val Tyr Ile Ile Gln Gly Ser Val Arg Val Gln Val 355 360 365 Ala Asn Asn Gln Gly Arg Ser Val Phe Asn Gly Val Leu His Gln Gly 370 375 380 Gln Leu Leu Ile Ile Pro Gln Asn His Ala Val Ile Lys Lys Ala Glu 385 390 395 400 His Asn Gly Cys Gln Tyr Val Ala Ile Lys Thr Ile Ser Asp Pro Thr 405 410 415 Val Ser Trp Val Ala Gly Lys Asn Ser Ile Leu Arg Ala Leu Pro Val 420 425 430 Asp Val Ile Ala Asn Ala Tyr Arg Ile Ser Arg Asp Glu Ala Arg Arg 435 440 445 Leu Lys Asn Asn Arg Ala Asp Glu Ile Gly Pro Phe Thr Pro Arg Phe 450 455 460 Pro Gln Lys Ser Gln Arg Gly Tyr Gln Phe Leu Thr Glu Gly Leu Ser 465 470 475 480 Leu Ile Gly Met <210> 7 <211> 510 <212> PRT <213> Rice <400> 7 Met Ala Ser Met Ser Thr Ile Leu Pro Leu Cys Leu Gly Leu Leu Leu 1 5 10 15 Phe Phe Gln Val Ser Met Ala Gln Phe Ser Phe Gly Gly Ser Pro Leu 20 25 30 Gln Ser Pro Arg Gly Phe Arg Gly Asp Gln Asp Ser Arg His Gln Cys 35 40 45 Arg Phe Glu His Leu Thr Ala Leu Glu Ala Thr His Gln Gln Arg Ser 50 55 60 Glu Ala Gly Phe Thr Glu Tyr Tyr Asn Ile Glu Ala Arg Asn Glu Phe 65 70 75 80 Arg Cys Ala Gly Val Ser Val Arg Arg Leu Val Val Glu Ser Lys Gly 85 90 95 Leu Val Leu Pro Met Tyr Ala Asn Ala His Lys Leu Val Tyr Ile Val 100 105 110 Gln Gly Arg Gly Val Phe Gly Met Ala Leu Pro Gly Cys Pro Glu Thr 115 120 125 Phe Gln Ser Val Arg Ser Pro Phe Glu Gln Glu Val Ala Thr Ala Gly 130 135 140 Glu Ala Gln Ser Ser Ile Gln Lys Met Arg Asp Glu His Gln Gln Leu 145 150 155 160 His Gln Phe His Gln Gly Asp Val Ile Ala Val Pro Ala Gly Val Ala 165 170 175 His Trp Leu Tyr Asn Asn Gly Asp Ser Pro Val Val Ala Phe Thr Val 180 185 190 Ile Asp Thr Ser Asn Asn Ala Asn Gln Leu Asp Pro Lys Arg Arg Glu 195 200 205 Phe Phe Leu Ala Gly Lys Pro Arg Ser Ser Trp Gln Gln Gln Ser Tyr 210 215 220 Ser Tyr Gln Thr Glu Gln Leu Ser Arg Asn Gln Asn Ile Phe Ala Gly 225 230 235 240 Phe Ser Pro Asp Leu Leu Ser Glu Ala Leu Ser Val Ser Lys Gln Thr 245 250 255 Val Leu Arg Leu Gln Gly Leu Ser Asp Pro Arg Gly Ala Ile Ile Arg 260 265 270 Val Glu Asn Gly Leu Gln Ala Leu Gln Pro Ser Leu Gln Val Glu Pro 275 280 285 Val Lys Glu Glu Gln Thr Gln Ala Tyr Leu Pro Thr Lys Gln Leu Gln 290 295 300 Pro Thr Trp Leu Arg Ser Gly Gly Ala Cys Gly Gln Gln Asn Val Leu 305 310 315 320 Asp Glu Ile Met Cys Ala Phe Lys Leu Arg Lys Asn Ile Asp Asn Pro 325 330 335 Gln Ser Ser Asp Ile Phe Asn Pro His Gly Gly Arg Ile Thr Arg Ala 340 345 350 Asn Ser Gln Asn Phe Pro Ile Leu Asn Ile Ile Gln Met Ser Ala Thr 355 360 365 Arg Ile Val Leu Gln Asn Asn Ala Leu Leu Thr Pro His Trp Thr Val 370 375 380 Asn Ala His Thr Val Met Tyr Val Thr Ala Gly Gln Gly His Ile Gln 385 390 395 400 Val Val Asp His Arg Gly Arg Ser Val Phe Asp Gly Glu Leu His Gln 405 410 415 Gln Gln Ile Leu Leu Ile Pro Gln Asn Phe Ala Val Val Val Lys Ala 420 425 430 Arg Arg Glu Gly Phe Ala Trp Val Ser Phe Lys Thr Asn His Asn Ala 435 440 445 Val Asp Ser Gln Ile Ala Gly Lys Ala Ser Ile Leu Arg Ala Leu Pro 450 455 460 Val Asp Val Val Ala Asn Ala Tyr Arg Leu Ser Arg Glu Asp Ser Arg 465 470 475 480 His Val Lys Phe Asn Arg Gly Asp Glu Met Ala Val Phe Ala Pro Arg 485 490 495 Arg Gly Pro Gln Gln Tyr Ala Glu Trp Gln Ile Asn Glu Lys 500 505 510 <210> 8 <211> 386 <212> PRT <213> Pea <400> 8 Met Ala Thr Thr Ile Lys Ser Arg Phe Pro Leu Leu Leu Leu Leu Gly 1 5 10 15 Ile Ile Phe Leu Ala Ser Val Val Ser Val Thr Tyr Ala Asn Tyr Asp 20 25 30 Glu Gly Ser Glu Pro Arg Val Pro Ala Gln Arg Glu Arg Gly Arg Gln 35 40 45 Glu Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Arg Pro Ser Tyr 50 55 60 Glu Lys Glu Glu Asp Glu Glu Glu Gly Gln Arg Glu Arg Gly Arg Gln 65 70 75 80 Glu Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Gly Pro Ser Tyr 85 90 95 Glu Lys Gln Glu Asp Glu Glu Glu Lys Gln Lys Tyr Arg Tyr Gln Arg 100 105 110 Glu Lys Glu Asp Glu Glu Glu Lys Gln Lys Tyr Gln Tyr Gln Arg Glu 115 120 125 Lys Lys Glu Gln Lys Glu Val Gln Pro Gly Arg Glu Arg Trp Glu Arg 130 135 140 Glu Glu Asp Glu Glu Gln Val Asp Glu Glu Trp Arg Gly Ser Gln Arg 145 150 155 160 Arg Glu Asp Pro Glu Glu Arg Ala Arg Leu Arg His Arg Glu Glu Arg 165 170 175 Thr Lys Arg Asp Arg Arg His Gln Arg Glu Gly Glu Glu Glu Glu Arg 180 185 190 Ser Ser Glu Ser Gln Glu Arg Arg Asn Pro Phe Leu Phe Lys Ser Asn 195 200 205 Lys Phe Leu Thr Leu Phe Glu Asn Glu Asn Gly His Ile Arg Leu Leu 210 215 220 Gln Arg Phe Asp Lys Arg Ser Asp Leu Phe Glu Asn Leu Gln Asn Tyr 225 230 235 240 Arg Leu Val Glu Tyr Arg Ala Lys Pro His Thr Ile Phe Leu Pro Gln 245 250 255 His Ile Asp Ala Asp Leu Ile Leu Val Val Leu Ser Gly Lys Ala Ile 260 265 270 Leu Thr Val Leu Ser Pro Asn Asp Arg Asn Ser Tyr Asn Leu Glu Arg 275 280 285 Gly Asp Thr Ile Lys Leu Pro Ala Gly Thr Thr Ser Tyr Leu Val Asn 290 295 300 Gln Asp Asp Glu Glu Asp Leu Arg Leu Val Asp Leu Val Ile Pro Val 305 310 315 320 Asn Gly Pro Gly Lys Phe Glu Ala Phe Asp Leu Ala Lys Asn Lys Asn 325 330 335 Gln Tyr Leu Arg Gly Phe Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asn 340 345 350 Thr Arg Tyr Glu Thr Ile Glu Lys Val Leu Leu Glu Glu Gln Glu Lys 355 360 365 Asp Arg Lys Arg Arg Gln Gln Gly Glu Glu Thr Asp Ala Ile Val Lys 370 375 380 Val Ser 385 <210> 9 <211> 386 <212> PRT <213> Pea <400> 9 Met Ala Thr Thr Ile Lys Ser Arg Phe Pro Leu Leu Leu Leu Leu Gly 1 5 10 15 Ile Ile Phe Leu Ala Ser Val Val Ser Val Thr Tyr Ala Asn Tyr Asp 20 25 30 Glu Gly Ser Glu Pro Arg Val Pro Ala Gln Arg Glu Arg Gly Arg Gln 35 40 45 Glu Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Arg Pro Ser Tyr 50 55 60 Glu Lys Glu Glu Asp Glu Glu Glu Gly Gln Arg Glu Arg Gly Arg Gln 65 70 75 80 Glu Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Gly Pro Ser Tyr 85 90 95 Glu Lys Gln Glu Asp Glu Glu Glu Lys Gln Lys Tyr Arg Tyr Gln Arg 100 105 110 Glu Lys Glu Asp Glu Glu Glu Lys Gln Lys Tyr Gln Tyr Gln Arg Glu 115 120 125 Lys Lys Glu Gln Lys Glu Val Gln Pro Gly Arg Glu Arg Trp Glu Arg 130 135 140 Glu Glu Asp Glu Glu Gln Val Asp Glu Glu Trp Arg Gly Ser Gln Arg 145 150 155 160 Arg Glu Asp Pro Glu Glu Arg Ala Arg Leu Arg His Arg Glu Glu Arg 165 170 175 Thr Lys Arg Asp Arg Arg His Gln Arg Glu Gly Glu Glu Glu Glu Arg 180 185 190 Ser Ser Glu Ser Gln Glu Arg Arg Asn Pro Phe Leu Phe Lys Ser Asn 195 200 205 Lys Phe Leu Thr Leu Phe Glu Asn Glu Asn Gly His Ile Arg Leu Leu 210 215 220 Gln Arg Phe Asp Lys Arg Ser Asp Leu Phe Glu Asn Leu Gln Asn Tyr 225 230 235 240 Arg Leu Val Glu Tyr Arg Ala Lys Pro His Thr Ile Phe Leu Pro Gln 245 250 255 His Ile Asp Ala Asp Leu Ile Leu Val Val Leu Ser Gly Lys Ala Ile 260 265 270 Leu Thr Val Leu Ser Pro Asn Asp Arg Asn Ser Tyr Asn Leu Glu Arg 275 280 285 Gly Asp Thr Ile Lys Leu Pro Ala Gly Thr Thr Ser Tyr Leu Val Asn 290 295 300 Gln Asp Asp Glu Glu Asp Leu Arg Leu Val Asp Leu Val Ile Pro Val 305 310 315 320 Asn Gly Pro Gly Lys Phe Glu Ala Phe Asp Leu Ala Lys Asn Lys Asn 325 330 335 Gln Tyr Leu Arg Gly Phe Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asn 340 345 350 Thr Arg Tyr Glu Thr Ile Glu Lys Val Leu Leu Glu Glu Gln Glu Lys 355 360 365 Asp Arg Lys Arg Arg Gln Gln Gly Glu Glu Thr Asp Ala Ile Val Lys 370 375 380 Val Ser 385 <210> 10 <211> 499 <212> PRT <213> Rice <400> 10 Met Ala Ser Ser Val Phe Ser Arg Phe Ser Ile Tyr Phe Cys Val Leu 1 5 10 15 Leu Leu Cys His Gly Ser Met Ala Gln Leu Phe Asn Pro Ser Thr Asn 20 25 30 Pro Trp His Ser Pro Arg Gln Gly Ser Phe Arg Glu Cys Arg Phe Asp 35 40 45 Arg Leu Gln Ala Phe Glu Pro Leu Arg Lys Val Arg Ser Glu Ala Gly 50 55 60 Val Thr Glu Tyr Phe Asp Glu Lys Asn Glu Leu Phe Gln Cys Thr Gly 65 70 75 80 Thr Phe Val Ile Arg Arg Val Ile Gln Pro Gln Gly Leu Leu Val Pro 85 90 95 Arg Tyr Thr Asn Ile Pro Gly Val Val Tyr Ile Ile Gln Gly Arg Gly 100 105 110 Ser Met Gly Leu Thr Phe Pro Gly Cys Pro Ala Thr Tyr Gln Gln Gln 115 120 125 Phe Gln Gln Phe Ser Ser Gln Gly Gln Ser Gln Ser Gln Lys Phe Arg 130 135 140 Asp Glu His Gln Lys Ile His Gln Phe Arg Gln Gly Asp Ile Val Ala 145 150 155 160 Leu Pro Ala Gly Val Ala His Trp Phe Tyr Asn Asp Gly Asp Ala Pro 165 170 175 Ile Val Ala Val Tyr Val Tyr Asp Val Asn Asn Asn Ala Asn Gln Leu 180 185 190 Glu Pro Arg Gln Lys Glu Phe Leu Leu Ala Gly Asn Asn Asn Arg Ala 195 200 205 Gln Gln Gln Gln Val Tyr Gly Ser Ser Ile Glu Gln His Ser Gly Gln 210 215 220 Asn Ile Phe Ser Gly Phe Gly Val Glu Met Leu Ser Glu Ala Leu Gly 225 230 235 240 Ile Asn Ala Val Ala Ala Lys Arg Leu Gln Ser Gln Asn Asp Gln Arg 245 250 255 Gly Glu Ile Ile His Val Lys Asn Gly Leu Gln Leu Leu Lys Pro Thr 260 265 270 Leu Thr Gln Gln Gln Glu Gln Ala Gln Ala Gln Asp Gln Tyr Gln Gln 275 280 285 Val Gln Tyr Ser Glu Arg Gln Gln Thr Ser Ser Arg Trp Asn Gly Leu 290 295 300 Glu Glu Asn Phe Cys Thr Ile Lys Val Arg Val Asn Ile Glu Asn Pro 305 310 315 320 Ser Arg Ala Asp Ser Tyr Asn Pro Arg Ala Gly Arg Ile Thr Ser Val 325 330 335 Asn Ser Gln Lys Phe Pro Ile Leu Asn Leu Ile Gln Met Ser Ala Thr 340 345 350 Arg Val Asn Leu Tyr Gln Asn Ala Ile Leu Ser Pro Phe Trp Asn Val 355 360 365 Asn Ala His Ser Leu Val Tyr Met Ile Gln Gly Arg Ser Arg Val Gln 370 375 380 Val Val Ser Asn Phe Gly Lys Thr Val Phe Asp Gly Val Leu Arg Pro 385 390 395 400 Gly Gln Leu Leu Ile Ile Pro Gln His Tyr Ala Val Leu Lys Lys Ala 405 410 415 Glu Arg Glu Gly Cys Gln Tyr Ile Ala Ile Lys Thr Asn Ala Asn Ala 420 425 430 Phe Val Ser His Leu Ala Gly Lys Asn Ser Val Phe Arg Ala Leu Pro 435 440 445 Val Asp Val Val Ala Asn Ala Tyr Arg Ile Ser Arg Glu Gln Ala Arg 450 455 460 Ser Leu Lys Asn Asn Arg Gly Glu Glu His Gly Ala Phe Thr Pro Arg 465 470 475 480 Phe Gln Gln Gln Tyr Tyr Pro Gly Leu Ser Asn Glu Ser Glu Ser Glu 485 490 495 Thr Ser Glu <210> 11 <211> 499 <212> PRT <213> Rice <400> 11 Met Ala Ser Ile Asn Arg Pro Ile Val Phe Phe Thr Val Cys Leu Phe 1 5 10 15 Leu Leu Cys Asn Gly Ser Leu Ala Gln Gln Leu Leu Gly Gln Ser Thr 20 25 30 Ser Gln Trp Gln Ser Ser Arg Arg Gly Ser Pro Arg Glu Cys Arg Phe 35 40 45 Asp Arg Leu Gln Ala Phe Glu Pro Ile Arg Ser Val Arg Ser Gln Ala 50 55 60 Gly Thr Thr Glu Phe Phe Asp Val Ser Asn Glu Gln Phe Gln Cys Thr 65 70 75 80 Gly Val Ser Val Val Arg Arg Val Ile Glu Pro Arg Gly Leu Leu Leu 85 90 95 Pro His Tyr Thr Asn Gly Ala Ser Leu Val Tyr Ile Ile Gln Gly Arg 100 105 110 Gly Ile Thr Gly Pro Thr Phe Pro Gly Cys Pro Glu Ser Tyr Gln Gln 115 120 125 Gln Phe Gln Gln Ser Gly Gln Ala Gln Leu Thr Glu Ser Gln Ser Gln 130 135 140 Ser Gln Lys Phe Lys Asp Glu His Gln Lys Ile His Arg Phe Arg Gln 145 150 155 160 Gly Asp Val Ile Ala Leu Pro Ala Gly Val Ala His Trp Cys Tyr Asn 165 170 175 Asp Gly Glu Val Pro Val Val Ala Ile Tyr Val Thr Asp Leu Asn Asn 180 185 190 Gly Ala Asn Gln Leu Asp Pro Arg Gln Arg Asp Phe Leu Leu Ala Gly 195 200 205 Asn Lys Arg Asn Pro Gln Ala Tyr Arg Arg Glu Val Glu Glu Arg Ser 210 215 220 Gln Asn Ile Phe Ser Gly Phe Ser Thr Glu Leu Leu Ser Glu Ala Leu 225 230 235 240 Gly Val Ser Ser Gln Val Ala Arg Gln Leu Gln Cys Gln Asn Asp Gln 245 250 255 Arg Gly Glu Ile Val Arg Val Glu His Gly Leu Ser Leu Leu Gln Pro 260 265 270 Tyr Ala Ser Leu Gln Glu Gln Glu Gln Gly Gln Val Gln Ser Arg Glu 275 280 285 Arg Tyr Gln Glu Gly Gln Tyr Gln Gln Ser Gln Tyr Gly Ser Gly Cys 290 295 300 Ser Asn Gly Leu Asp Glu Thr Phe Cys Thr Leu Arg Val Arg Gln Asn 305 310 315 320 Ile Asp Asn Pro Asn Arg Ala Asp Thr Tyr Asn Pro Arg Ala Gly Arg 325 330 335 Val Thr Asn Leu Asn Thr Gln Asn Phe Pro Ile Leu Ser Leu Val Gln 340 345 350 Met Ser Ala Val Lys Val Asn Leu Tyr Gln Asn Ala Leu Leu Ser Pro 355 360 365 Phe Trp Asn Ile Asn Ala His Ser Val Val Tyr Ile Thr Gln Gly Arg 370 375 380 Ala Arg Val Gln Val Val Asn Asn Asn Gly Lys Thr Val Phe Asn Gly 385 390 395 400 Glu Leu Arg Arg Gly Gln Leu Leu Ile Ile Pro Gln His Tyr Ala Val 405 410 415 Val Lys Lys Ala Gln Arg Glu Gly Cys Ala Tyr Ile Ala Phe Lys Thr 420 425 430 Asn Pro Asn Ser Met Val Ser His Ile Ala Gly Lys Ser Ser Ile Phe 435 440 445 Arg Ala Leu Pro Asn Asp Val Leu Ala Asn Ala Tyr Arg Ile Ser Arg 450 455 460 Glu Glu Ala Gln Arg Leu Lys His Asn Arg Gly Asp Glu Phe Gly Ala 465 470 475 480 Phe Thr Pro Ile Gln Tyr Lys Ser Tyr Gln Asp Val Tyr Asn Ala Ala 485 490 495 Glu Ser Ser <210> 12 <211> 499 <212> PRT <213> Rice <400> 12 Met Ala Ser Ile Asn Arg Pro Ile Val Phe Phe Thr Val Cys Leu Phe 1 5 10 15 Leu Leu Cys Asp Gly Ser Leu Ala Gln Gln Leu Leu Gly Gln Ser Thr 20 25 30 Ser Gln Trp Gln Ser Ser Arg Arg Gly Ser Pro Arg Gly Cys Arg Phe 35 40 45 Asp Arg Leu Gln Ala Phe Glu Pro Ile Arg Ser Val Arg Ser Gln Ala 50 55 60 Gly Thr Thr Glu Phe Phe Asp Val Ser Asn Glu Leu Phe Gln Cys Thr 65 70 75 80 Gly Val Ser Val Val Arg Arg Val Ile Glu Pro Arg Gly Leu Leu Leu 85 90 95 Pro His Tyr Thr Asn Gly Ala Ser Leu Val Tyr Ile Ile Gln Gly Arg 100 105 110 Gly Ile Thr Gly Pro Thr Phe Pro Gly Cys Pro Glu Thr Tyr Gln Gln 115 120 125 Gln Phe Gln Gln Ser Gly Gln Ala Gln Leu Thr Glu Ser Gln Ser Gln 130 135 140 Ser His Lys Phe Lys Asp Glu His Gln Lys Ile His Arg Phe Arg Gln 145 150 155 160 Gly Asp Val Ile Ala Leu Pro Ala Gly Val Ala His Trp Cys Tyr Asn 165 170 175 Asp Gly Glu Val Pro Val Val Ala Ile Tyr Val Thr Asp Ile Asn Asn 180 185 190 Gly Ala Asn Gln Leu Asp Pro Arg Gln Arg Asp Phe Leu Leu Ala Gly 195 200 205 Asn Lys Arg Asn Pro Gln Ala Tyr Arg Arg Glu Val Glu Glu Trp Ser 210 215 220 Gln Asn Ile Phe Ser Gly Phe Ser Thr Glu Leu Leu Ser Glu Ala Phe 225 230 235 240 Gly Ile Ser Asn Gln Val Ala Arg Gln Leu Gln Cys Gln Asn Asp Gln 245 250 255 Arg Gly Glu Ile Val Arg Val Glu Arg Gly Leu Ser Leu Leu Gln Pro 260 265 270 Tyr Ala Ser Leu Gln Glu Gln Glu Gln Gly Gln Met Gln Ser Arg Glu 275 280 285 His Tyr Gln Glu Gly Gly Tyr Gln Gln Ser Gln Tyr Gly Ser Gly Cys 290 295 300 Pro Asn Gly Leu Asp Glu Thr Phe Cys Thr Met Arg Val Arg Gln Asn 305 310 315 320 Ile Asp Asn Pro Asn Arg Ala Asp Thr Tyr Asn Pro Arg Ala Gly Arg 325 330 335 Val Thr Asn Leu Asn Ser Gln Asn Phe Pro Ile Leu Asn Leu Val Gln 340 345 350 Met Ser Ala Val Lys Val Asn Leu Tyr Gln Asn Ala Leu Leu Ser Pro 355 360 365 Phe Trp Asn Ile Asn Ala His Ser Ile Val Tyr Ile Thr Gln Gly Arg 370 375 380 Ala Gln Val Gln Val Val Asn Asn Asn Gly Lys Thr Val Phe Asn Gly 385 390 395 400 Glu Leu Arg Arg Gly Gln Leu Leu Ile Val Pro Gln His Tyr Val Val 405 410 415 Val Lys Lys Ala Gln Arg Glu Gly Cys Ala Tyr Ile Ala Phe Lys Thr 420 425 430 Asn Pro Asn Ser Met Val Ser His Ile Ala Gly Lys Ser Ser Ile Phe 435 440 445 Arg Ala Leu Pro Thr Asp Val Leu Ala Asn Ala Tyr Arg Ile Ser Arg 450 455 460 Glu Glu Ala Gln Arg Leu Lys His Asn Arg Gly Asp Glu Phe Gly Ala 465 470 475 480 Phe Thr Pro Leu Gln Tyr Lys Ser Tyr Gln Asp Val Tyr Asn Val Ala 485 490 495 Glu Ser Ser <210> 13 <211> 160 <212> PRT <213> Rice <400> 13 Met Ala Ser Asn Lys Val Val Phe Ser Val Leu Leu Leu Ala Val Val 1 5 10 15 Ser Val Leu Ala Ala Thr Ala Thr Met Ala Glu Tyr His His Gln Asp 20 25 30 Gln Val Val Tyr Thr Pro Gly Pro Leu Cys Gln Pro Gly Met Gly Tyr 35 40 45 Pro Met Tyr Pro Leu Pro Arg Cys Arg Ala Leu Val Lys Arg Gln Cys 50 55 60 Val Gly Arg Gly Thr Ala Ala Ala Ala Glu Gln Val Arg Arg Asp Cys 65 70 75 80 Cys Arg Gln Leu Ala Ala Val Asp Asp Ser Trp Cys Arg Cys Glu Ala 85 90 95 Ile Ser His Met Leu Gly Gly Ile Tyr Arg Glu Leu Gly Ala Pro Asp 100 105 110 Val Gly His Pro Met Ser Glu Val Phe Arg Gly Cys Arg Arg Gly Asp 115 120 125 Leu Glu Arg Ala Ala Ala Ser Leu Pro Ala Phe Cys Asn Val Asp Ile 130 135 140 Pro Asn Gly Gly Gly Gly Val Cys Tyr Trp Leu Ala Arg Ser Gly Tyr 145 150 155 160 <210> 14 <211> 500 <212> PRT <213> Rice <400> 14 Met Ala Thr Ile Ala Phe Ser Arg Leu Ser Ile Tyr Phe Cys Val Leu 1 5 10 15 Leu Leu Cys His Gly Ser Met Ala Gln Leu Phe Gly Pro Asn Val Asn 20 25 30 Pro Trp His Asn Pro Arg Gln Gly Gly Phe Arg Glu Cys Arg Phe Asp 35 40 45 Arg Leu Gln Ala Phe Glu Pro Leu Arg Arg Val Arg Ser Glu Ala Gly 50 55 60 Val Thr Glu Tyr Phe Asp Glu Lys Asn Glu Gln Phe Gln Cys Thr Gly 65 70 75 80 Thr Phe Val Ile Arg Arg Val Ile Glu Pro Gln Gly Leu Leu Val Pro 85 90 95 Arg Tyr Ser Asn Thr Pro Gly Met Val Tyr Ile Ile Gln Gly Arg Gly 100 105 110 Ser Met Gly Leu Thr Phe Pro Gly Cys Pro Ala Thr Tyr Gln Gln Gln 115 120 125 Phe Gln Gln Phe Leu Pro Glu Gly Gln Ser Gln Ser Gln Lys Phe Arg 130 135 140 Asp Glu His Gln Lys Ile His Gln Phe Arg Gln Gly Asp Ile Val Ala 145 150 155 160 Leu Pro Ala Gly Val Ala His Trp Phe Tyr Asn Glu Gly Asp Ala Pro 165 170 175 Val Val Ala Leu Tyr Val Phe Asp Leu Asn Asn Asn Ala Asn Gln Leu 180 185 190 Glu Pro Arg Gln Lys Glu Phe Leu Leu Ala Gly Asn Asn Asn Arg Glu 195 200 205 Gln Gln Met Tyr Gly Arg Ser Ile Glu Gln His Ser Gly Gln Asn Ile 210 215 220 Phe Ser Gly Phe Asn Asn Glu Leu Leu Ser Glu Ala Leu Gly Val Asn 225 230 235 240 Ala Leu Val Ala Lys Arg Leu Gln Gly Gln Asn Asp Gln Arg Gly Glu 245 250 255 Ile Ile Arg Val Lys Asn Gly Leu Lys Leu Leu Arg Pro Ala Phe Ala 260 265 270 Gln Gln Gln Glu Gln Ala Gln Gln Gln Glu Gln Ala Gln Ala Gln Tyr 275 280 285 Gln Val Gln Tyr Ser Glu Glu Gln Gln Pro Ser Thr Arg Cys Asn Gly 290 295 300 Leu Asp Glu Asn Phe Cys Thr Ile Lys Ala Arg Leu Asn Ile Glu Asn 305 310 315 320 Pro Ser His Ala Asp Thr Tyr Asn Pro Arg Ala Gly Arg Ile Thr Arg 325 330 335 Leu Asn Ser Gln Lys Phe Pro Ile Leu Asn Leu Val Gln Leu Ser Ala 340 345 350 Thr Arg Val Asn Leu Tyr Gln Asn Ala Ile Leu Ser Pro Phe Trp Asn 355 360 365 Val Asn Ala His Ser Leu Val Tyr Ile Val Gln Gly His Ala Arg Val 370 375 380 Gln Val Val Ser Asn Leu Gly Lys Thr Val Phe Asn Gly Val Leu Arg 385 390 395 400 Pro Gly Gln Leu Leu Ile Ile Pro Gln His Tyr Val Val Leu Lys Lys 405 410 415 Ala Glu His Glu Gly Cys Gln Tyr Ile Ser Phe Lys Thr Asn Ala Asn 420 425 430 Ser Met Val Ser His Leu Ala Gly Lys Asn Ser Ile Phe Arg Ala Met 435 440 445 Pro Val Asp Val Ile Ala Asn Ala Tyr Arg Ile Ser Arg Glu Gln Ala 450 455 460 Arg Ser Leu Lys Asn Asn Arg Gly Glu Glu Leu Gly Ala Phe Thr Pro 465 470 475 480 Arg Tyr Gln Gln Gln Thr Tyr Pro Gly Phe Ser Asn Glu Ser Glu Asn 485 490 495 Glu Ala Leu Glu 500 <210> 15 <211> 609 <212> PRT <213> Rice <400> 15 Met Ser Ala Leu Thr Thr Ser Gln Leu Ala Thr Ser Ala Thr Gly Phe 1 5 10 15 Gly Ile Ala Asp Arg Ser Ala Pro Ser Ser Leu Leu Arg His Gly Phe 20 25 30 Gln Gly Leu Lys Pro Arg Ser Pro Ala Gly Gly Asp Ala Thr Ser Leu 35 40 45 Ser Val Thr Thr Ser Ala Arg Ala Thr Pro Lys Gln Gln Arg Ser Val 50 55 60 Gln Arg Gly Ser Arg Arg Phe Pro Ser Val Val Val Tyr Ala Thr Gly 65 70 75 80 Ala Gly Met Asn Val Val Phe Val Gly Ala Glu Met Ala Pro Trp Ser 85 90 95 Lys Thr Gly Gly Leu Gly Asp Val Leu Gly Gly Leu Pro Pro Ala Met 100 105 110 Ala Ala Asn Gly His Arg Val Met Val Ile Ser Pro Arg Tyr Asp Gln 115 120 125 Tyr Lys Asp Ala Trp Asp Thr Ser Val Val Ala Glu Ile Lys Val Ala 130 135 140 Asp Arg Tyr Glu Arg Val Arg Phe Phe His Cys Tyr Lys Arg Gly Val 145 150 155 160 Asp Arg Val Phe Ile Asp His Pro Ser Phe Leu Glu Lys Val Trp Gly 165 170 175 Lys Thr Gly Glu Lys Ile Tyr Gly Pro Asp Thr Gly Val Asp Tyr Lys 180 185 190 Asp Asn Gln Met Arg Phe Ser Leu Leu Cys Gln Ala Ala Leu Glu Ala 195 200 205 Pro Arg Ile Leu Asn Leu Asn Asn Asn Pro Tyr Phe Lys Gly Thr Tyr 210 215 220 Gly Glu Asp Val Val Phe Val Cys Asn Asp Trp His Thr Gly Pro Leu 225 230 235 240 Ala Ser Tyr Leu Lys Asn Asn Tyr Gln Pro Asn Gly Ile Tyr Arg Asn 245 250 255 Ala Lys Val Ala Phe Cys Ile His Asn Ile Ser Tyr Gln Gly Arg Phe 260 265 270 Ala Phe Glu Asp Tyr Pro Glu Leu Asn Leu Ser Glu Arg Phe Arg Ser 275 280 285 Ser Phe Asp Phe Ile Asp Gly Tyr Asp Thr Pro Val Glu Gly Arg Lys 290 295 300 Ile Asn Trp Met Lys Ala Gly Ile Leu Glu Ala Asp Arg Val Leu Thr 305 310 315 320 Val Ser Pro Tyr Tyr Ala Glu Glu Leu Ile Ser Gly Ile Ala Arg Gly 325 330 335 Cys Glu Leu Asp Asn Ile Met Arg Leu Thr Gly Ile Thr Gly Ile Val 340 345 350 Asn Gly Met Asp Val Ser Glu Trp Asp Pro Ser Lys Asp Lys Tyr Ile 355 360 365 Thr Ala Lys Tyr Asp Ala Thr Thr Ala Ile Glu Ala Lys Ala Leu Asn 370 375 380 Lys Glu Ala Leu Gln Ala Glu Ala Gly Leu Pro Val Asp Arg Lys Ile 385 390 395 400 Pro Leu Ile Ala Phe Ile Gly Arg Leu Glu Glu Gln Lys Gly Pro Asp 405 410 415 Val Met Ala Ala Ala Ile Pro Glu Leu Met Gln Glu Asp Val Gln Ile 420 425 430 Val Leu Leu Gly Thr Gly Lys Lys Lys Phe Glu Lys Leu Leu Lys Ser 435 440 445 Met Glu Glu Lys Tyr Pro Gly Lys Val Arg Ala Val Val Lys Phe Asn 450 455 460 Ala Pro Leu Ala His Leu Ile Met Ala Gly Ala Asp Val Leu Ala Val 465 470 475 480 Pro Ser Arg Phe Glu Pro Cys Gly Leu Ile Gln Leu Gln Gly Met Arg 485 490 495 Tyr Gly Thr Pro Cys Ala Cys Ala Ser Thr Gly Gly Leu Val Asp Thr 500 505 510 Val Ile Glu Gly Lys Thr Gly Phe His Met Gly Arg Leu Ser Val Asp 515 520 525 Cys Lys Val Val Glu Pro Ser Asp Val Lys Lys Val Ala Ala Thr Leu 530 535 540 Lys Arg Ala Ile Lys Val Val Gly Thr Pro Ala Tyr Glu Glu Met Val 545 550 555 560 Arg Asn Cys Met Asn Gln Asp Leu Ser Trp Lys Gly Pro Ala Lys Asn 565 570 575 Trp Glu Asn Val Leu Leu Gly Leu Gly Val Ala Gly Ser Ala Pro Gly 580 585 590 Ile Glu Gly Asp Glu Ile Ala Pro Leu Ala Lys Glu Asn Val Ala Ala 595 600 605 Pro <210> 16 <211> 336 <212> PRT <213> Staphylococcus aureus <400> 16 Met Lys Gly Lys Phe Leu Lys Val Ser Ser Leu Phe Val Ala Thr Leu 1 5 10 15 Thr Thr Ala Thr Leu Val Ser Ser Pro Ala Ala Asn Ala Leu Ser Ser 20 25 30 Lys Ala Met Asp Asn His Pro Gln Gln Thr Gln Ser Ser Lys Gln Gln 35 40 45 Thr Pro Lys Ile Gln Lys Gly Gly Asn Leu Lys Pro Leu Glu Gln Arg 50 55 60 Glu His Ala Asn Val Ile Leu Pro Asn Asn Asp Arg His Gln Ile Thr 65 70 75 80 Asp Thr Thr Asn Gly His Tyr Ala Pro Val Thr Tyr Ile Gln Val Glu 85 90 95 Ala Pro Thr Gly Thr Phe Ile Ala Ser Gly Val Val Val Gly Lys Asp 100 105 110 Thr Leu Leu Thr Asn Lys His Val Val Asp Ala Thr His Gly Asp Pro 115 120 125 His Ala Leu Lys Ala Phe Pro Ser Ala Ile Asn Gln Asp Asn Tyr Pro 130 135 140 Asn Gly Gly Phe Thr Ala Glu Gln Ile Thr Lys Tyr Ser Gly Glu Gly 145 150 155 160 Asp Leu Ala Ile Val Lys Phe Ser Pro Asn Glu Gln Asn Lys His Ile 165 170 175 Gly Glu Val Val Lys Pro Ala Thr Met Ser Asn Asn Ala Glu Thr Gln 180 185 190 Val Asn Gln Asn Ile Thr Val Thr Gly Tyr Pro Gly Asp Lys Pro Val 195 200 205 Ala Thr Met Trp Glu Ser Lys Gly Lys Ile Thr Tyr Leu Lys Gly Glu 210 215 220 Ala Met Gln Tyr Asp Leu Ser Thr Thr Gly Gly Asn Ser Gly Ser Pro 225 230 235 240 Val Phe Asn Glu Lys Asn Glu Val Ile Gly Ile His Trp Gly Gly Val 245 250 255 Pro Asn Glu Phe Asn Gly Ala Val Phe Ile Asn Glu Asn Val Arg Asn 260 265 270 Phe Leu Lys Gln Asn Ile Glu Asp Ile His Phe Ala Asn Asp Asp Gln 275 280 285 Pro Asn Asn Pro Asp Asn Pro Asp Asn Pro Asn Asn Pro Asp Asn Pro 290 295 300 Asn Asn Pro Asp Glu Pro Asn Asn Pro Asp Asn Pro Asn Asn Pro Asp 305 310 315 320 Asn Pro Asp Asn Gly Asp Asn Asn Asn Ser Asp Asn Pro Asp Ala Ala 325 330 335 <210> 17 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 1 <400> 17 Pro Phe Asn Leu Arg Ser Arg Gly Pro Ile Tyr Ser Asn Glu Phe Gly 1 5 10 15 Lys Phe Phe Glu Ile Thr 20 <210> 18 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 1 <400> 18 Lys Pro Asp Asp Arg Asn Ser Phe Asn Leu Glu Arg Gly Asp Thr Ile 1 5 10 15 Lys <210> 19 <211> 27 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 19 Tyr Leu Val Asn Arg Asp Asp Asn Glu Glu Leu Arg Val Leu Asp Leu 1 5 10 15 Ala Ile Pro Val Asn Arg Pro Gly Gln Leu Gln 20 25 <210> 20 <211> 51 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 20 Gln Glu Gln Arg Lys Glu Asp Asp Glu Glu Glu Glu Gln Gly Glu Glu 1 5 10 15 Glu Ile Asn Lys Gln Val Gln Asn Tyr Lys Ala Lys Leu Ser Ser Gly 20 25 30 Asp Val Phe Val Ile Pro Ala Gly His Pro Val Ala Val Lys Ala Ser 35 40 45 Ser Asn Leu 50 <210> 21 <211> 68 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 21 Ser Gly Phe Ser Lys Asn Ile Leu Glu Ala Ser Phe Asn Thr Asp Tyr 1 5 10 15 Glu Glu Ile Glu Lys Val Leu Leu Glu Glu His Glu Lys Glu Thr Gln 20 25 30 His Arg Arg Ser Leu Lys Asp Lys Arg Gln Gln Ser Gln Glu Glu Asn 35 40 45 Val Ile Val Lys Leu Ser Arg Gly Gln Ile Glu Glu Leu Ser Lys Asn 50 55 60 Ala Lys Ser Thr 65 <210> 22 <211> 74 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 1 <400> 22 Pro Phe Ile Phe Lys Ser Asn Lys Phe Gln Thr Leu Phe Glu Asn Glu 1 5 10 15 Asn Gly His Ile Arg Leu Leu Gln Lys Phe Asp Gln Arg Ser Lys Ile 20 25 30 Phe Glu Asn Leu Gln Asn Tyr Arg Leu Leu Glu Tyr Lys Ser Lys Pro 35 40 45 His Thr Ile Phe Leu Pro Gln His Thr Asp Ala Asp Tyr Ile Leu Val 50 55 60 Val Leu Ser Gly Lys Ala Ile Leu Thr Val 65 70 <210> 23 <211> 28 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 23 Gln Glu Val Asp Arg Ile Leu Glu Asn Gln Lys Gln Ser His Phe Ala 1 5 10 15 Asp Ala Gln Pro Gln Gln Arg Glu Arg Gly Ser Arg 20 25 <210> 24 <211> 35 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 2 <400> 24 Asn Asn Ser Gly Lys Phe Phe Glu Leu Thr Pro Glu Lys Asn Gln Gln 1 5 10 15 Leu Gln Asp Leu Asp Leu Phe Val Asn Ser Val Asp Leu Lys Glu Gly 20 25 30 Ser Leu Leu 35 <210> 25 <211> 17 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 2 <400> 25 Lys Val Ser Arg Arg Gln Leu Glu Glu Leu Ser Lys Asn Ala Lys Ser 1 5 10 15 Ser <210> 26 <211> 21 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 3 <400> 26 Gln Arg Gly Ser Arg Gln Glu Glu Asp Glu Asp Glu Asp Glu Glu Arg 1 5 10 15 Gln Pro Arg His Gln 20 <210> 27 <211> 33 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 3 <400> 27 Gln Glu Phe Leu Arg Tyr Gln His Gln Gln Gly Gly Lys Gln Glu Gln 1 5 10 15 Glu Asn Glu Gly Asn Asn Ile Phe Ser Gly Phe Lys Arg Asp Phe Leu 20 25 30 Glu <210> 28 <211> 34 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 4 <400> 28 Tyr Asn Leu Glu Arg Gly Asp Thr Ile Lys Leu Pro Ala Gly Thr Thr 1 5 10 15 Ser Tyr Leu Val Asn Gln Asp Asp Glu Glu Asp Leu Arg Leu Val Asp 20 25 30 Leu Val <210> 29 <211> 80 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 4 <400> 29 Asn Gly Pro Gly Lys Phe Glu Ala Phe Asp Leu Ala Lys Asn Lys Asn 1 5 10 15 Gln Tyr Leu Arg Gly Phe Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asn 20 25 30 Thr Arg Tyr Glu Thr Ile Glu Lys Val Leu Leu Glu Glu Gln Glu Lys 35 40 45 Asp Arg Lys Arg Arg Gln Gln Gly Glu Glu Thr Asp Ala Ile Val Lys 50 55 60 Val Ser Arg Glu Gln Ile Glu Glu Leu Lys Lys Leu Ala Lys Ser Ser 65 70 75 80 <210> 30 <211> 47 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 4 <400> 30 Arg Tyr Glu Ala Arg Leu Ser Pro Gly Asp Val Val Ile Ile Pro Ala 1 5 10 15 Gly His Pro Val Ala Ile Thr Ala Ser Ser Asn Leu Asn Leu Leu Gly 20 25 30 Phe Gly Ile Asn Ala Glu Asn Asn Glu Arg Asn Phe Leu Ser Gly 35 40 45 <210> 31 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 4 <400> 31 His Gly Glu Trp Arg Pro Ser Tyr Glu Lys Gln Glu Asp Glu Glu Glu 1 5 10 15 Lys Gln Lys Tyr Arg Tyr Gln Arg 20 <210> 32 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 4 <400> 32 Pro Ser Tyr Glu Lys Glu Glu Asp Glu Glu Glu Gly Gln Arg Glu Arg 1 5 10 15 Gly Arg Gln <210> 33 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 4 <400> 33 Lys Ser Lys Pro Arg Thr Leu Phe Leu Pro Gln Tyr Thr Asp Ala Asp 1 5 10 15 Phe Ile Leu Val Val Leu Ser Gly Lys Ala Thr Leu Thr Val 20 25 30 <210> 34 <211> 22 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 34 Ser Gln Ser Gln Lys Phe Arg Asp Glu His Gln Lys Ile His Gln Phe 1 5 10 15 Arg Gln Gly Asp Ile Val 20 <210> 35 <211> 23 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 35 Val Asn Ser Gln Lys Phe Pro Ile Leu Asn Leu Ile Gln Met Ser Ala 1 5 10 15 Thr Arg Val Asn Leu Tyr Gln 20 <210> 36 <211> 40 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 36 Tyr Ile Ala Ile Lys Thr Asn Ala Asn Ala Phe Val Ser His Leu Ala 1 5 10 15 Gly Lys Asn Ser Val Phe Arg Ala Leu Pro Val Asp Val Val Ala Asn 20 25 30 Ala Tyr Arg Ile Ser Arg Glu Gln 35 40 <210> 37 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 10 <400> 37 Ala Pro Ile Val Ala Val Tyr Val Tyr Asp Val Asn Asn Asn Ala Asn 1 5 10 15 Gln Leu Glu Pro Arg Gln Lys Glu Phe Leu Leu Ala Gly Asn Asn 20 25 30 <210> 38 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 10 <400> 38 Glu Asn Pro Ser Arg Ala Asp Ser Tyr Asn Pro Arg Ala Gly Arg Ile 1 5 10 15 Thr <210> 39 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 10 <400> 39 Gly Leu Gln Leu Leu Lys Pro Thr Leu Thr Gln Gln Gln Glu Gln Ala 1 5 10 15 Gln Ala Gln Asp Gln Tyr Gln Gln Val Gln Tyr Ser Glu Arg Gln Gln 20 25 30 <210> 40 <211> 18 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 40 Cys Arg Phe Asp Arg Leu Gln Ala Phe Glu Pro Leu Arg Lys Val Arg 1 5 10 15 Ser Glu <210> 41 <211> 48 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 41 Ile Leu Ser Pro Phe Trp Asn Val Asn Ala His Ser Leu Val Tyr Met 1 5 10 15 Ile Gln Gly Arg Ser Arg Val Gln Val Val Ser Asn Phe Gly Lys Thr 20 25 30 Val Phe Asp Gly Val Leu Arg Pro Gly Gln Leu Leu Ile Ile Pro Gln 35 40 45 <210> 42 <211> 24 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 42 Ala Phe Thr Pro Arg Phe Gln Gln Gln Tyr Tyr Pro Gly Leu Ser Asn 1 5 10 15 Glu Ser Glu Ser Glu Thr Ser Glu 20 <210> 43 <211> 31 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 11 <400> 43 Pro Arg Ala Gly Arg Val Thr Asn Leu Asn Thr Gln Asn Phe Pro Ile 1 5 10 15 Leu Ser Leu Val Gln Met Ser Ala Val Lys Val Asn Leu Tyr Gln 20 25 30 <210> 44 <211> 32 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 11 <400> 44 His Ser Val Val Tyr Ile Thr Gln Gly Arg Ala Arg Val Gln Val Val 1 5 10 15 Asn Asn Asn Gly Lys Thr Val Phe Asn Gly Glu Leu Arg Arg Gly Gln 20 25 30 <210> 45 <211> 32 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 11 <400> 45 His Ile Ala Gly Lys Ser Ser Ile Phe Arg Ala Leu Pro Asn Asp Val 1 5 10 15 Leu Ala Asn Ala Tyr Arg Ile Ser Arg Glu Glu Ala Gln Arg Leu Lys 20 25 30 <210> 46 <211> 29 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 11 <400> 46 Val Pro Val Val Ala Ile Tyr Val Thr Asp Leu Asn Asn Gly Ala Asn 1 5 10 15 Gln Leu Asp Pro Arg Gln Arg Asp Phe Leu Leu Ala Gly 20 25 <210> 47 <211> 52 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 47 Thr Phe Cys Thr Met Arg Val Arg Gln Asn Ile Asp Asn Pro Asn Arg 1 5 10 15 Ala Asp Thr Tyr Asn Pro Arg Ala Gly Arg Val Thr Asn Leu Asn Ser 20 25 30 Gln Asn Phe Pro Ile Leu Asn Leu Val Gln Met Ser Ala Val Lys Val 35 40 45 Asn Leu Tyr Gln 50 <210> 48 <211> 73 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 48 Tyr Ile Ala Phe Lys Thr Asn Pro Asn Ser Met Val Ser His Ile Ala 1 5 10 15 Gly Lys Ser Ser Ile Phe Arg Ala Leu Pro Thr Asp Val Leu Ala Asn 20 25 30 Ala Tyr Arg Ile Ser Arg Glu Glu Ala Gln Arg Leu Lys His Asn Arg 35 40 45 Gly Asp Glu Phe Gly Ala Phe Thr Pro Leu Gln Tyr Lys Ser Tyr Gln 50 55 60 Asp Val Tyr Asn Val Ala Glu Ser Ser 65 70 <210> 49 <211> 36 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 49 Ser Gln Ser His Lys Phe Lys Asp Glu His Gln Lys Ile His Arg Phe 1 5 10 15 Arg Gln Gly Asp Val Ile Ala Leu Pro Ala Gly Val Ala His Trp Cys 20 25 30 Tyr Asn Asp Gly 35 <210> 50 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 50 Thr Gln Gly Arg Ala Gln Val Gln Val Val Asn Asn Asn Gly Lys Thr 1 5 10 15 Val Phe Asn Gly Glu Leu Arg Arg Gly Gln Leu Leu Ile 20 25 <210> 51 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 51 Asn Gly Ala Ser Leu Val Tyr Ile Ile Gln Gly Arg Gly Ile Thr Gly 1 5 10 15 Pro Thr Phe Pro Gly Cys Pro Glu 20 <210> 52 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 52 Cys Arg Phe Asp Arg Leu Gln Ala Phe Glu Pro Ile Arg Ser Val Arg 1 5 10 15 Ser Gln Ala Gly Thr 20 <210> 53 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 53 Gln Asn Asp Gln Arg Gly Glu Ile Val Arg Val Glu Arg Gly Leu Ser 1 5 10 15 Leu Leu Gln Pro Tyr Ala Ser Leu Gln Glu Gln Glu Gln Gly Gln Met 20 25 30 Gln Ser Arg Glu His Tyr Gln Glu 35 40 <210> 54 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 54 Pro Arg Gln Arg Asp Phe Leu Leu Ala Gly Asn Lys Arg Asn Pro Gln 1 5 10 15 Ala Tyr Arg Arg Glu Val Glu Glu Trp Ser Gln Asn Ile Phe Ser Gly 20 25 30 Phe Ser Thr 35 <210> 55 <211> 23 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 13 <400> 55 Gly Gly Ile Tyr Arg Glu Leu Gly Ala Pro Asp Val Gly His Pro Met 1 5 10 15 Ser Glu Val Phe Arg Gly Cys 20 <210> 56 <211> 26 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 56 His Ser Leu Val Tyr Ile Val Gln Gly His Ala Arg Val Gln Val Val 1 5 10 15 Ser Asn Leu Gly Lys Thr Val Phe Asn Gly 20 25 <210> 57 <211> 23 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 57 Ala Arg Ser Leu Lys Asn Asn Arg Gly Glu Glu Leu Gly Ala Phe Thr 1 5 10 15 Pro Arg Tyr Gln Gln Gln Thr 20 <210> 58 <211> 23 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 58 Leu Asn Ser Gln Lys Phe Pro Ile Leu Asn Leu Val Gln Leu Ser Ala 1 5 10 15 Thr Arg Val Asn Leu Tyr Gln 20 <210> 59 <211> 84 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 14 <400> 59 Gln Met Tyr Gly Arg Ser Ile Glu Gln His Ser Gly Gln Asn Ile Phe 1 5 10 15 Ser Gly Phe Asn Asn Glu Leu Leu Ser Glu Ala Leu Gly Val Asn Ala 20 25 30 Leu Val Ala Lys Arg Leu Gln Gly Gln Asn Asp Gln Arg Gly Glu Ile 35 40 45 Ile Arg Val Lys Asn Gly Leu Lys Leu Leu Arg Pro Ala Phe Ala Gln 50 55 60 Gln Gln Glu Gln Ala Gln Gln Gln Glu Gln Ala Gln Ala Gln Tyr Gln 65 70 75 80 Val Gln Tyr Ser <210> 60 <211> 24 <212> PRT <213> Artificial Sequence <220> <223>Fragment of SEQ ID 14 <400> 60 Ala Gln Leu Phe Gly Pro Asn Val Asn Pro Trp His Asn Pro Arg Gln 1 5 10 15 Gly Gly Phe Arg Glu Cys Arg Phe 20 <210> 61 <211> 23 <212> PRT <213> Artificial Sequence <220> <223>Fragment of SEQ ID 14 <400> 61 Gly Val Ala His Trp Phe Tyr Asn Glu Gly Asp Ala Pro Val Val Ala 1 5 10 15 Leu Tyr Val Phe Asp Leu Asn 20 <210> 62 <211> 40 <212> PRT <213> Artificial Sequence <220> <223>Fragment of SEQ ID 14 <400> 62 Tyr Ile Ser Phe Lys Thr Asn Ala Asn Ser Met Val Ser His Leu Ala 1 5 10 15 Gly Lys Asn Ser Ile Phe Arg Ala Met Pro Val Asp Val Ile Ala Asn 20 25 30 Ala Tyr Arg Ile Ser Arg Glu Gln 35 40 <210> 63 <211> 38 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 63 Lys Gly Pro Ala Lys Asn Trp Glu Asn Val Leu Leu Gly Leu Gly Val 1 5 10 15 Ala Gly Ser Ala Pro Gly Ile Glu Gly Asp Glu Ile Ala Pro Leu Ala 20 25 30 Lys Glu Asn Val Ala Ala 35 <210> 64 <211> 31 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 64 Arg Ala Val Val Lys Phe Asn Ala Pro Leu Ala His Leu Ile Met Ala 1 5 10 15 Gly Ala Asp Val Leu Ala Val Pro Ser Arg Phe Glu Pro Cys Gly 20 25 30 <210> 65 <211> 22 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 65 Lys Arg Ala Ile Lys Val Val Gly Thr Pro Ala Tyr Glu Glu Met Val 1 5 10 15 Arg Asn Cys Met Asn Gln 20 <210> 66 <211> 55 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 66 Ala Pro Trp Ser Lys Thr Gly Gly Leu Gly Asp Val Leu Gly Gly Leu 1 5 10 15 Pro Pro Ala Met Ala Ala Asn Gly His Arg Val Met Val Ile Ser Pro 20 25 30 Arg Tyr Asp Gln Tyr Lys Asp Ala Trp Asp Thr Ser Val Val Ala Glu 35 40 45 Ile Lys Val Ala Asp Arg Tyr 50 55 <210> 67 <211> 109 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 67 Ile Asn Trp Met Lys Ala Gly Ile Leu Glu Ala Asp Arg Val Leu Thr 1 5 10 15 Val Ser Pro Tyr Tyr Ala Glu Glu Leu Ile Ser Gly Ile Ala Arg Gly 20 25 30 Cys Glu Leu Asp Asn Ile Met Arg Leu Thr Gly Ile Thr Gly Ile Val 35 40 45 Asn Gly Met Asp Val Ser Glu Trp Asp Pro Ser Lys Asp Lys Tyr Ile 50 55 60 Thr Ala Lys Tyr Asp Ala Thr Thr Ala Ile Glu Ala Lys Ala Leu Asn 65 70 75 80 Lys Glu Ala Leu Gln Ala Glu Ala Gly Leu Pro Val Asp Arg Lys Ile 85 90 95 Pro Leu Ile Ala Phe Ile Gly Arg Leu Glu Glu Gln Lys 100 105 <210> 68 <211> 45 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 15 <400> 68 Arg Gly Val Asp Arg Val Phe Ile Asp His Pro Ser Phe Leu Glu Lys 1 5 10 15 Val Trp Gly Lys Thr Gly Glu Lys Ile Tyr Gly Pro Asp Thr Gly Val 20 25 30 Asp Tyr Lys Asp Asn Gln Met Arg Phe Ser Leu Leu Cys 35 40 45 <210> 69 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 15 <400> 69 Leu Glu Ala Pro Arg Ile Leu Asn Leu Asn Asn Asn Pro Tyr Phe Lys 1 5 10 15 Gly Thr Tyr Gly Glu 20 <210> 70 <211> 26 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 16 <400> 70 Tyr Ile Gln Val Glu Ala Pro Thr Gly Thr Phe Ile Ala Ser Gly Val 1 5 10 15 Val Val Gly Lys Asp Thr Leu Leu Thr Asn 20 25 <210> 71 <211> 12 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 71 Ser Arg Gly Pro Ile Tyr Ser Asn Glu Phe Gly Lys 1 5 10 <210> 72 <211> 7 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 72 Asn Ser Phe Asn Leu Glu Arg 1 5 <210> 73 <211> 10 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 73 Val Leu Asp Leu Ala Ile Pro Val Asn Arg 1 5 10 <210> 74 <211> 7 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 74 Asp Asp Asn Glu Glu Leu Arg 1 5 <210> 75 <211> 18 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 75 Leu Ser Ser Gly Asp Val Phe Val Ile Pro Ala Gly His Pro Val Ala 1 5 10 15 Val Lys <210> 76 <211> 15 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 76 Glu Asp Asp Glu Glu Glu Glu Gln Gly Glu Glu Glu Ile Asn Lys 1 5 10 15 <210> 77 <211> 29 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 77 Asn Ile Leu Glu Ala Ser Phe Asn Thr Asp Tyr Glu Glu Ile Glu Lys 1 5 10 15 Val Leu Leu Glu Glu His Glu Lys Glu Thr Gln His Arg 20 25 <210> 78 <211> 24 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 78 Asn Ile Leu Glu Ala Ser Phe Asn Thr Asp Tyr Glu Glu Ile Glu Lys 1 5 10 15 Val Leu Leu Glu Glu His Glu Lys 20 <210> 79 <211> 16 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 79 Asn Ile Leu Glu Ala Ser Phe Asn Thr Asp Tyr Glu Glu Ile Glu Lys 1 5 10 15 <210> 80 <211> 12 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 80 Arg Gln Gln Ser Gln Glu Glu Asn Val Ile Val Lys 1 5 10 <210> 81 <211> 11 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 81 Gln Gln Ser Gln Glu Glu Asn Val Ile Val Lys 1 5 10 <210> 82 <211> 11 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 82 Leu Ser Arg Gly Gln Ile Glu Glu Leu Ser Lys 1 5 10 <210> 83 <211> 8 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 83 Gly Gln Ile Glu Glu Leu Ser Lys 1 5 <210> 84 <211> 8 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 84 Val Leu Leu Glu Glu His Glu Lys 1 5 <210> 85 <211> 24 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 85 Ser Lys Pro His Thr Ile Phe Leu Pro Gln His Thr Asp Ala Asp Tyr 1 5 10 15 Ile Leu Val Val Leu Ser Gly Lys 20 <210> 86 <211> 22 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 86 Pro His Thr Ile Phe Leu Pro Gln His Thr Asp Ala Asp Tyr Ile Leu 1 5 10 15 Val Val Leu Ser Gly Lys 20 <210> 87 <211> 16 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 87 Ser Asn Lys Phe Gln Thr Leu Phe Glu Asn Glu Asn Gly His Ile Arg 1 5 10 15 <210> 88 <211> 11 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 88 Ser Lys Ile Phe Glu Asn Leu Gln Asn Tyr Arg 1 5 10 <210> 89 <211> 9 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 89 Ile Phe Glu Asn Leu Gln Asn Tyr Arg 1 5 <210> 90 <211> 18 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 90 Ile Leu Glu Asn Gln Lys Gln Ser His Phe Ala Asp Ala Gln Pro Gln 1 5 10 15 Gln Arg <210> 91 <211> 24 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 1 <400> 91 Pro Gly Gln Leu Gln Ser Phe Leu Leu Ser Gly Asn Gln Asn Gln Gln 1 5 10 15 Asn Tyr Leu Ser Gly Phe Ser Lys 20 <210> 92 <211> 25 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 2 <400> 92 Phe Phe Glu Leu Thr Pro Glu Lys Asn Gln Gln Leu Gln Asp Leu Asp 1 5 10 15 Leu Phe Val Asn Ser Val Asp Leu Lys 20 25 <210> 93 <211> 7 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 2 <400> 93 Gln Leu Glu Glu Leu Ser Lys 1 5 <210> 94 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SE QID 3 <400> 94 Gln Glu Glu Asp Glu Asp Glu Asp Glu Glu Arg 1 5 10 <210> 95 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ 3 <400> 95 Tyr Gln His Gln Gln Gly Gly Lys Gln Glu Gln Glu Asn Glu Gly Asn 1 5 10 15 Asn Ile Phe Ser Gly Phe Lys 20 <210> 96 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 4 <400> 96 Gly Asp Thr Ile Lys Leu Pro Ala Gly Thr Thr Ser Tyr Leu Val Asn 1 5 10 15 Gln Asp Asp Glu Glu Asp Leu Arg 20 <210> 97 <211> 12 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 4 <400> 97 Arg Gln Gln Gly Glu Glu Thr Asp Ala Ile Val Lys 1 5 10 <210> 98 <211> 11 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 4 <400> 98 Val Leu Leu Glu Glu Gln Glu Lys Asp Arg Lys 1 5 10 <210> 99 <211> 10 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 4 <400> 99 Asn Ile Leu Glu Ala Ser Tyr Asn Thr Arg 1 5 10 <210> 100 <211> 8 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 4 <400> 100 Phe Glu Ala Phe Asp Leu Ala Lys 1 5 <210> 101 <211> 8 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 4 <400> 101 Glu Gln Ile Glu Glu Leu Lys Lys 1 5 <210> 102 <211> 7 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 4 <400> 102 Glu Gln Ile Glu Glu Leu Lys 1 5 <210> 103 <211> 7 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 4 <400> 103 Asn Lys Asn Gln Tyr Leu Arg 1 5 <210> 104 <211> 37 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 4 <400> 104 Leu Ser Pro Gly Asp Val Val Ile Ile Pro Ala Gly His Pro Val Ala 1 5 10 15 Ile Thr Ala Ser Ser Asn Leu Asn Leu Leu Gly Phe Gly Ile Asn Ala 20 25 30 Glu Asn Asn Glu Arg 35 <210> 105 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 4 <400> 105 Pro Ser Tyr Glu Lys Gln Glu Asp Glu Glu Glu Lys Gln Lys 1 5 10 <210> 106 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 4 <400> 106 Glu Glu Asp Glu Glu Glu Gly Gln Arg 1 5 <210> 107 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 5 <400> 107 Thr Leu Phe Leu Pro Gln Tyr Thr Asp Ala Asp Phe Ile Leu Val Val 1 5 10 15 Leu Ser Gly Lys 20 <210> 108 <211> 24 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 6 <400> 108 Gly Tyr Val Gly Leu Thr Phe Pro Gly Cys Pro Ala Thr His Gln Gln 1 5 10 15 Gln Phe Gln Leu Phe Glu Gln Arg 20 <210> 109 <211> 14 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 7 <400> 109 Arg Gly Pro Gln Gln Tyr Ala Glu Trp Gln Ile Asn Glu Lys 1 5 10 <210> 110 <211> 21 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 8 <400> 110 Leu Val Asp Leu Val Ile Pro Val Asn Gly Pro Gly Lys Phe Glu Ala 1 5 10 15 Phe Asp Leu Ala Lys 20 <210> 111 <211> 18 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 9 <400> 111 Lys Asn Pro Gln Leu Gln Asp Leu Asp Ile Phe Val Asn Tyr Val Glu 1 5 10 15 Ile Lys <210> 112 <211> 10 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 112 Asp Glu His Gln Lys Ile His Gln Phe Arg 1 5 10 <210> 113 <211> 7 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 113 Phe Arg Asp Glu His Gln Lys 1 5 <210> 114 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 114 Phe Pro Ile Leu Asn Leu Ile Gln Met Ser Ala Thr Arg 1 5 10 <210> 115 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 115 Thr Asn Ala Asn Ala Phe Val Ser His Leu Ala Gly Lys 1 5 10 <210> 116 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 10 <400> 116 Ala Leu Pro Val Asp Val Val Ala Asn Ala Tyr Arg 1 5 10 <210> 117 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 10 <400> 117 Tyr Val Tyr Asp Val Asn Asn Asn Ala Asn Gln Leu Glu Pro Arg Gln 1 5 10 15 Lys Glu Phe Leu 20 <210> 118 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 10 <400> 118 Val Tyr Val Tyr Asp Val Asn Asn Asn Ala Asn Gln Leu Glu Pro Arg 1 5 10 15 Gln Lys Glu Phe Leu 20 <210> 119 <211> 7 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 10 <400> 119 Ala Asp Ser Tyr Asn Pro Arg 1 5 <210> 120 <211> 16 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 120 Lys Pro Thr Leu Thr Gln Gln Gln Glu Gln Ala Gln Ala Gln Asp Gln 1 5 10 15 <210> 121 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 121 Gln Ala Gln Ala Gln Asp Gln Tyr Gln Gln Val Gln Tyr 1 5 10 <210> 122 <211> 11 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 122 Gln Ala Gln Asp Gln Tyr Gln Gln Val Gln Tyr 1 5 10 <210> 123 <211> 8 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 123 Leu Gln Ala Phe Glu Pro Leu Arg 1 5 <210> 124 <211> 11 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 124 Ser Arg Val Gln Val Val Ser Asn Phe Gly Lys 1 5 10 <210> 125 <211> 10 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 125 Trp Asn Val Asn Ala His Ser Leu Val Tyr 1 5 10 <210> 126 <211> 9 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 126 Asn Val Asn Ala His Ser Leu Val Tyr 1 5 <210> 127 <211> 15 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 127 Ile Gln Gly Arg Ser Arg Val Gln Val Val Ser Asn Phe Gly Lys 1 5 10 15 <210> 128 <211> 14 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 128 Gly Lys Thr Val Phe Asp Gly Val Leu Arg Pro Gly Gln Leu 1 5 10 <210> 129 <211> 15 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 129 Phe Gly Lys Thr Val Phe Asp Gly Val Leu Arg Pro Gly Gln Leu 1 5 10 15 <210> 130 <211> 19 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 130 Phe Gln Gln Gln Tyr Tyr Pro Gly Leu Ser Asn Glu Ser Glu Ser Glu 1 5 10 15 Thr Ser Glu <210> 131 <211> 9 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 131 Gln Gln Tyr Tyr Pro Gly Leu Ser Asn 1 5 <210> 132 <211> 10 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 10 <400> 132 Gln Gln Gln Tyr Tyr Pro Gly Leu Ser Asn 1 5 10 <210> 133 <211> 21 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 11 <400> 133 Val Thr Asn Leu Asn Thr Gln Asn Phe Pro Ile Leu Ser Leu Val Gln 1 5 10 15 Met Ser Ala Val Lys 20 <210> 134 <211> 19 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 11 <400> 134 Ile Thr Gln Gly Arg Ala Arg Val Gln Val Val Asn Asn Asn Gly Lys 1 5 10 15 Thr Val Phe <210> 135 <211> 22 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 11 <400> 135 Ile Thr Gln Gly Arg Ala Arg Val Gln Val Val Asn Asn Asn Gly Lys 1 5 10 15 Thr Val Phe Asn Gly Glu 20 <210> 136 <211> 21 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 11 <400> 136 Ile Thr Gln Gly Arg Ala Arg Val Gln Val Val Asn Asn Asn Gly Lys 1 5 10 15 Thr Val Phe Asn Gly 20 <210> 137 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 11 <400> 137 Arg Val Gln Val Val Asn Asn Asn Gly Lys Thr Val Phe 1 5 10 <210> 138 <211> 18 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 11 <400> 138 Arg Ala Leu Pro Asn Asp Val Leu Ala Asn Ala Tyr Arg Ile Ser Arg 1 5 10 15 Glu Glu <210> 139 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 11 <400> 139 Ser Ile Phe Arg Ala Leu Pro Asn Asp Val Leu Ala Asn Ala Tyr Arg 1 5 10 15 <210> 140 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 11 <400> 140 Ser Ile Phe Arg Ala Leu Pro Asn Asp Val Leu Ala Asn Ala Tyr 1 5 10 15 <210> 141 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 11 <400> 141 Ser Ile Phe Arg Ala Leu Pro Asn Asp Val Leu Ala Asn 1 5 10 <210> 142 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 11 <400> 142 Ser Ser Ile Phe Arg Ala Leu Pro Asn Asp Val Leu Ala Asn Ala Tyr 1 5 10 15 Arg <210> 143 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 11 <400> 143 Ser Ile Phe Arg Ala Leu Pro Asn Asp Val Leu Ala Asn Ala Tyr Arg 1 5 10 15 Ile Ser Arg Glu Glu 20 <210> 144 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 11 <400> 144 Ser Ile Phe Arg Ala Leu Pro Asn Asp 1 5 <210> 145 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 11 <400> 145 Ile Tyr Val Thr Asp Leu Asn Asn Gly Ala Asn Gln Leu Asp Pro Arg 1 5 10 15 Gln Arg Asp <210> 146 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 146 Val Thr Asn Leu Asn Ser Gln Asn Phe Pro Ile Leu Asn Leu Val Gln 1 5 10 15 Met Ser Ala Val Lys 20 <210> 147 <211> 8 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 147 Gln Asn Ile Asp Asn Pro Asn Arg 1 5 <210> 148 <211> 7 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 148 Ala Asp Thr Tyr Asn Pro Arg 1 5 <210> 149 <211> 21 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 149 Asn Ile Asp Asn Pro Asn Arg Ala Asp Thr Tyr Asn Pro Arg Ala Gly 1 5 10 15 Arg Val Thr Asn Leu 20 <210> 150 <211> 25 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 150 Arg Val Arg Gln Asn Ile Asp Asn Pro Asn Arg Ala Asp Thr Tyr Asn 1 5 10 15 Pro Arg Ala Gly Arg Val Thr Asn Leu 20 25 <210> 151 <211> 18 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 151 Thr Asn Pro Asn Ser Met Val Ser His Ile Ala Gly Lys Ser Ser Ile 1 5 10 15 Phe Arg <210> 152 <211> 16 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 152 His Asn Arg Gly Asp Glu Phe Gly Ala Phe Thr Pro Leu Gln Tyr Lys 1 5 10 15 <210> 153 <211> 12 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 153 Ser Tyr Gln Asp Val Tyr Asn Val Ala Glu Ser Ser 1 5 10 <210> 154 <211> 8 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 12 <400> 154 Ile Ser Arg Glu Glu Ala Gln Arg 1 5 <210> 155 <211> 21 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 12 <400> 155 Ser Ile Phe Arg Ala Leu Pro Thr Asp Val Leu Ala Asn Ala Tyr Arg 1 5 10 15 Ile Ser Arg Glu Glu 20 <210> 156 <211> 19 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 12 <400> 156 Tyr Arg Ile Ser Arg Glu Glu Ala Gln Arg Leu Lys His Asn Arg Gly 1 5 10 15 Asp Glu Phe <210> 157 <211> 18 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 12 <400> 157 Tyr Arg Ile Ser Arg Glu Glu Ala Gln Arg Leu Lys His Asn Arg Gly 1 5 10 15 Asp Glu <210> 158 <211> 10 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 158 Phe Lys Asp Glu His Gln Lys Ile His Arg 1 5 10 <210> 159 <211> 14 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 159 Gln Gly Asp Val Ile Ala Leu Pro Ala Gly Val Ala His Trp 1 5 10 <210> 160 <211> 9 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 160 Thr Val Phe Asn Gly Glu Leu Arg Arg 1 5 <210> 161 <211> 8 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 161 Thr Val Phe Asn Gly Glu Leu Arg 1 5 <210> 162 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 162 Gln Val Gln Val Val Asn Asn Asn Gly Lys Thr Val Phe 1 5 10 <210> 163 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 163 Tyr Ile Ile Gln Gly Arg Gly Ile Thr Gly Pro Thr Phe 1 5 10 <210> 164 <211> 14 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 164 Val Tyr Ile Ile Gln Gly Arg Gly Ile Thr Gly Pro Thr Phe 1 5 10 <210> 165 <211> 11 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 12 <400> 165 Leu Gln Ala Phe Glu Pro Ile Arg Ser Val Arg 1 5 10 <210> 166 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 166 Gly Leu Ser Leu Leu Gln Pro Tyr Ala Ser Leu Gln Glu Gln Glu Gln 1 5 10 15 Gly Gln Met Gln Ser Arg 20 <210> 167 <211> 8 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 167 Gly Glu Ile Val Arg Val Glu Arg 1 5 <210> 168 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 168 Arg Gly Leu Ser Leu Leu Gln Pro Tyr Ala Ser Leu Gln 1 5 10 <210> 169 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 169 Arg Gly Leu Ser Leu Leu Gln Pro Tyr Ala Ser Leu Gln Glu Gln 1 5 10 15 <210> 170 <211> 16 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 12 <400> 170 Arg Gly Leu Ser Leu Leu Gln Pro Tyr Ala Ser Leu Gln Glu Gln Glu 1 5 10 15 <210> 171 <211> 14 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 12 <400> 171 Arg Gly Leu Ser Leu Leu Gln Pro Tyr Ala Ser Leu Gln Glu 1 5 10 <210> 172 <211> 7 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 12 <400> 172 Arg Asn Pro Gln Ala Tyr Arg 1 5 <210> 173 <211> 13 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 12 <400> 173 Phe Leu Leu Ala Gly Asn Lys Arg Asn Pro Gln Ala Tyr 1 5 10 <210> 174 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 174 Glu Val Glu Glu Trp Ser Gln Asn Ile Phe 1 5 10 <210> 175 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 175 Leu Ala Gly Asn Lys Arg Asn Pro Gln Ala Tyr Arg 1 5 10 <210> 176 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 12 <400> 176 Phe Leu Leu Ala Gly Asn Lys Arg Asn Pro Gln Ala 1 5 10 <210> 177 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 13 <400> 177 Glu Leu Gly Ala Pro Asp Val Gly His Pro Met Ser Glu 1 5 10 <210> 178 <211> 16 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 178 Ile Val Gln Gly His Ala Arg Val Gln Val Val Ser Asn Leu Gly Lys 1 5 10 15 <210> 179 <211> 14 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 179 Ile Val Gln Gly His Ala Arg Val Gln Val Val Ser Asn Leu 1 5 10 <210> 180 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 180 Ile Val Gln Gly His Ala Arg Val Gln Val Val Ser Asn 1 5 10 <210> 181 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 181 Asn Asn Arg Gly Glu Glu Leu Gly Ala Phe Thr Pro Arg 1 5 10 <210> 182 <211> 10 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 182 Gly Glu Glu Leu Gly Ala Phe Thr Pro Arg 1 5 10 <210> 183 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 183 Phe Pro Ile Leu Asn Leu Val Gln Leu Ser Ala Thr Arg 1 5 10 <210> 184 <211> 31 <212> PRT <213> Artificial sequence <220> <223> Fragment of SE QID 14 <400> 184 Ser Ile Glu Gln His Ser Gly Gln Asn Ile Phe Ser Gly Phe Asn Asn 1 5 10 15 Glu Leu Leu Ser Glu Ala Leu Gly Val Asn Ala Leu Val Ala Lys 20 25 30 <210> 185 <211> 8 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 185 Leu Gln Gly Gln Asn Asp Gln Arg 1 5 <210> 186 <211> 20 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 186 Ser Gly Phe Asn Asn Glu Leu Leu Ser Glu Ala Leu Gly Val Asn Ala 1 5 10 15 Leu Val Ala Lys 20 <210> 187 <211> 20 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 187 Pro Ala Phe Ala Gln Gln Gln Glu Gln Ala Gln Gln Gln Glu Gln Ala 1 5 10 15 Gln Ala Gln Tyr 20 <210> 188 <211> 15 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 188 Val Ala Lys Arg Leu Gln Gly Gln Asn Asp Gln Arg Gly Glu Ile 1 5 10 15 <210> 189 <211> 17 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 189 Ala Leu Val Ala Lys Arg Leu Gln Gly Gln Asn Asp Gln Arg Gly Glu 1 5 10 15 Ile <210> 190 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 190 Leu Gln Gly Gln Asn Asp Gln Arg Gly Glu Ile Ile Arg 1 5 10 <210> 191 <211> 14 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 191 Pro Asn Val Asn Pro Trp His Asn Pro Arg Gln Gly Gly Phe 1 5 10 <210> 192 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 192 Phe Tyr Asn Glu Gly Asp Ala Pro Val Val Ala Leu Tyr 1 5 10 <210> 193 <211> 10 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 193 Phe Tyr Asn Glu Gly Asp Ala Pro Val Val 1 5 10 <210> 194 <211> 12 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 194 Phe Tyr Asn Glu Gly Asp Ala Pro Val Val Ala Leu 1 5 10 <210> 195 <211> 11 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 195 Phe Tyr Asn Glu Gly Asp Ala Pro Val Val Ala 1 5 10 <210> 196 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 196 Thr Asn Ala Asn Ser Met Val Ser His Leu Ala Gly Lys 1 5 10 <210> 197 <211> 12 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 14 <400> 197 Ala Met Pro Val Asp Val Ile Ala Asn Ala Tyr Arg 1 5 10 <210> 198 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 15 <400> 198 Asn Trp Glu Asn Val Leu Leu Gly Leu Gly Val Ala Gly Ser Ala Pro 1 5 10 15 Gly Ile Glu Gly Asp Glu Ile Ala Pro Leu Ala Lys 20 25 <210> 199 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 15 <400> 199 Asn Val Leu Leu Gly Leu Gly Val Ala Gly Ser Ala Pro Gly Ile Glu 1 5 10 15 Gly Asp Glu <210> 200 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Fragment of SEQ ID 15 <400> 200 Asn Trp Glu Asn Val Leu Leu Gly Leu Gly Val Ala Gly Ser Ala Pro 1 5 10 15 Gly Ile Glu Gly Asp Glu Ile Ala Pro Leu Ala Lys 20 25 <210> 201 <211> 21 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 15 <400> 201 Phe Asn Ala Pro Leu Ala His Leu Ile Met Ala Gly Ala Asp Val Leu 1 5 10 15 Ala Val Pro Ser Arg 20 <210> 202 <211> 10 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 15 <400> 202 Phe Asn Ala Pro Leu Ala His Leu Ile Met 1 5 10 <210> 203 <211> 21 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 15 <400> 203 Phe Asn Ala Pro Leu Ala His Leu Ile Met Ala Gly Ala Asp Val Leu 1 5 10 15 Ala Val Pro Ser Arg 20 <210> 204 <211> 12 <212> PRT <213> Synthetic sequence <220> <223> Fragment of SEQ ID 15 <400> 204 Val Val Gly Thr Pro Ala Tyr Glu Glu Met Val Arg 1 5 10 <210> 205 <211> 21 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 205 Thr Gly Gly Leu Gly Asp Val Leu Gly Gly Leu Pro Pro Ala Met Ala 1 5 10 15 Ala Asn Gly His Arg 20 <210> 206 <211> 17 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 206 Tyr Asp Gln Tyr Lys Asp Ala Trp Asp Thr Ser Val Val Ala Glu Ile 1 5 10 15 Lys <210> 207 <211> 12 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 207 Asp Ala Trp Asp Thr Ser Val Val Ala Glu Ile Lys 1 5 10 <210> 208 <211> 7 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 208 Val Met Val Ile Ser Pro Arg 1 5 <210> 209 <211> 22 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 209 Leu Thr Gly Ile Thr Gly Ile Val Asn Gly Met Asp Val Ser Glu Trp 1 5 10 15 Asp Pro Ser Lys Asp Lys 20 <210> 210 <211> 18 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 210 Val Leu Thr Val Ser Pro Tyr Tyr Ala Glu Glu Leu Ile Ser Gly Ile 1 5 10 15 Ala Arg <210> 211 <211> 14 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 211 Glu Ala Leu Gln Ala Glu Ala Gly Leu Pro Val Asp Arg Lys 1 5 10 <210> 212 <211> 10 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 212 Tyr Asp Ala Thr Thr Ala Ile Glu Ala Lys 1 5 10 <210> 213 <211> 9 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 213 Ile Pro Leu Ile Ala Phe Ile Gly Arg 1 5 <210> 214 <211> 8 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 214 Ala Gly Ile Leu Glu Ala Asp Arg 1 5 <210> 215 <211> 9 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 215 Ile Pro Leu Ile Ala Phe Ile Gly Arg 1 5 <210> 216 <211> 11 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 216 Val Phe Ile Asp His Pro Ser Phe Leu Glu Lys 1 5 10 <210> 217 <211> 13 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 217 Gly Pro Asp Thr Gly Val Asp Tyr Lys Asp Asn Gln Met 1 5 10 <210> 218 <211> 16 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 218 Ile Tyr Gly Pro Asp Thr Gly Val Asp Tyr Lys Asp Asn Gln Met Arg 1 5 10 15 <210> 219 <211> 11 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 219 Ile Tyr Gly Pro Asp Thr Gly Val Asp Tyr Lys 1 5 10 <210> 220 <211> 11 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 15 <400> 220 Ile Leu Asn Leu Asn Asn Asn Pro Tyr Phe Lys 1 5 10 <210> 221 <211> 16 <212> PRT <213> Artificial sequence <220> <223> Fragment of SEQ ID 16 <400> 221 Ala Pro Thr Gly Thr Phe Ile Ala Ser Gly Val Val Val Gly Lys Asp 1 5 10 15 <210> 222 <211> 463 <212> PRT <213> Vicia faba <400> 222 Met Ala Ala Thr Thr Leu Lys Asp Ser Phe Pro Leu Leu Thr Leu Leu 1 5 10 15 Gly Ile Ala Phe Leu Ala Ser Val Cys Leu Ser Ser Arg Ser Asp Gln 20 25 30 Asp Asn Pro Phe Val Phe Glu Ser Asn Arg Phe Gln Thr Leu Phe Glu 35 40 45 Asn Glu Asn Gly His Ile Arg Leu Leu Gln Lys Phe Asp Gln His Ser 50 55 60 Lys Leu Leu Glu Asn Leu Gln Asn Tyr Arg Leu Leu Glu Tyr Lys Ser 65 70 75 80 Lys Pro His Thr Ile Phe Leu Pro Gln Gln Thr Asp Ala Asp Phe Ile 85 90 95 Leu Val Val Leu Ser Gly Lys Ala Ile Leu Thr Val Leu Leu Pro Asn 100 105 110 Asp Arg Asn Ser Phe Ser Leu Glu Arg Gly Asp Thr Ile Lys Leu Pro 115 120 125 Ala Gly Thr Ile Gly Tyr Leu Val Asn Arg Asp Asp Glu Glu Asp Leu 130 135 140 Arg Val Leu Asp Leu Val Ile Pro Val Asn Arg Pro Gly Glu Pro Gln 145 150 155 160 Ser Phe Leu Leu Ser Gly Asn Gln Asn Gln Pro Ser Ile Leu Ser Gly 165 170 175 Phe Ser Lys Asn Ile Leu Glu Ala Ser Phe Asn Thr Asp Tyr Lys Glu 180 185 190 Ile Glu Lys Val Leu Leu Glu Glu His Gly Lys Glu Lys Tyr His Arg 195 200 205 Arg Gly Leu Lys Asp Arg Arg Gln Arg Gly Gln Glu Glu Asn Val Ile 210 215 220 Val Lys Ile Ser Arg Lys Gln Ile Glu Glu Leu Asn Lys Asn Ala Lys 225 230 235 240 Ser Ser Ser Lys Lys Ser Thr Ser Ser Glu Ser Glu Pro Phe Asn Leu 245 250 255 Arg Ser Arg Glu Pro Ile Tyr Ser Asn Lys Phe Gly Lys Phe Phe Glu 260 265 270 Ile Thr Pro Lys Arg Asn Pro Gln Leu Gln Asp Leu Asn Ile Phe Val 275 280 285 Asn Tyr Val Glu Ile Asn Glu Gly Ser Leu Leu Leu Pro His Tyr Asn 290 295 300 Ser Arg Ala Ile Val Ile Val Thr Val Asn Glu Gly Lys Gly Asp Phe 305 310 315 320 Glu Leu Val Gly Gln Arg Asn Glu Asn Gln Gln Gly Leu Arg Glu Glu 325 330 335 Tyr Asp Glu Glu Lys Glu Gln Gly Glu Glu Glu Ile Arg Lys Gln Val 340 345 350 Gln Asn Tyr Lys Ala Lys Leu Ser Pro Gly Asp Val Leu Val Ile Pro 355 360 365 Ala Gly Tyr Pro Val Ala Ile Lys Ala Ser Ser Asn Leu Asn Leu Val 370 375 380 Gly Phe Gly Ile Asn Ala Glu Asn Asn Gln Arg Tyr Phe Leu Ala Gly 385 390 395 400 Glu Glu Asp Asn Val Ile Ser Gln Ile His Lys Pro Val Lys Glu Leu 405 410 415 Ala Phe Pro Gly Ser Ala Gln Glu Val Asp Thr Leu Leu Glu Asn Gln 420 425 430 Lys Gln Ser His Phe Ala Asn Ala Gln Pro Arg Glu Arg Glu Arg Gly 435 440 445 Ser Gln Glu Ile Lys Asp His Leu Tyr Ser Ile Leu Gly Ser Phe 450 455 460 <210> 223 <211> 446 <212> PRT <213> Chickpea <400> 223 Met Ala Ile Lys Ala Arg Phe Pro Leu Leu Val Leu Leu Gly Ile Val 1 5 10 15 Phe Leu Ala Ser Val Cys Ala Lys Ser Asp Lys Glu Asn Pro Phe Phe 20 25 30 Phe Lys Ser Asn Asn Cys Gln Thr Leu Phe Glu Asn Glu Asn Gly His 35 40 45 Val Arg Leu Leu Gln Arg Phe Asp Lys Arg Ser Gln Leu Phe Glu Asn 50 55 60 Leu Gln Asn Tyr Arg Leu Met Glu Tyr Asn Ser Lys Pro His Thr Leu 65 70 75 80 Phe Leu Pro Gln His Asn Asp Ala Asp Phe Ile Leu Val Val Leu Arg 85 90 95 Gly Arg Ala Ile Leu Thr Val Leu Asn Pro Asn Asp Arg Asn Thr Phe 100 105 110 Lys Leu Glu Arg Gly Asp Thr Ile Lys Leu Pro Ala Gly Thr Ile Ala 115 120 125 Tyr Leu Ala Asn Arg Asp Asp Asn Glu Asp Leu Arg Val Leu Asp Leu 130 135 140 Ala Ile Pro Val Asn Arg Pro Gly Gln Phe Gln Ser Phe Ser Leu Ser 145 150 155 160 Gly Asn Glu Asn Gln Gln Ser Tyr Phe Gln Gly Phe Ser Lys Lys Ile 165 170 175 Leu Glu Ala Ser Phe Asn Ser Asp Tyr Glu Glu Ile Glu Arg Val Leu 180 185 190 Leu Glu Glu Gln Glu Gln Lys Pro Glu Gln Arg Arg Gly His Lys Gly 195 200 205 Arg Gln Gln Ser Gln Glu Thr Asp Val Ile Val Lys Ile Ser Arg Glu 210 215 220 Gln Ile Glu Glu Leu Ser Lys Asn Ala Lys Ser Asn Cys Lys Lys Ser 225 230 235 240 Val Ser Ser Glu Ser Glu Pro Phe Asn Leu Arg Ser Arg Ser Pro Ile 245 250 255 Tyr Ser Asn Arg Phe Gly Asn Phe Phe Glu Ile Thr Pro Glu Lys Asn 260 265 270 Pro Gln Leu Lys Asp Leu Asp Ile Phe Val Asn Ser Val Glu Ile Lys 275 280 285 Glu Gly Ser Leu Leu Leu Pro His Phe Asn Ser Arg Ala Thr Val Ile 290 295 300 Leu Val Val Asn Glu Gly Lys Gly Glu Val Glu Leu Val Gly Leu Arg 305 310 315 320 Asn Glu Asn Glu Gln Glu Asn Lys Lys Glu Asp Glu Glu Glu Glu Glu 325 330 335 Asp Arg Asn Val Gln Val Gln Arg Phe Gln Ser Lys Leu Ser Ser Gly 340 345 350 Asp Val Val Val Ile Pro Ala Ser His Pro Phe Ser Ile Asn Ala Ser 355 360 365 Ser Asp Leu Phe Leu Leu Gly Phe Gly Ile Asn Ala Gln Asn Asn Gln 370 375 380 Arg Asn Phe Leu Ala Gly Glu Glu Asp Asn Val Ile Ser Gln Ile Gln 385 390 395 400 Arg Pro Val Lys Glu Val Ala Phe Pro Gly Ser Ala Glu Glu Val Asp 405 410 415 Arg Leu Leu Lys Asn Gln Arg Gln Ser His Phe Ala Asn Ala Gln Pro 420 425 430 Gln Gln Lys Arg Lys Gly Ser Gln Arg Ile Arg Ser Pro Phe 435 440 445 <210> 224 <211> 418 <212> PRT <213> Lens culinaris <400> 224 Ser Arg Ser Asp Gln Glu Asn Pro Phe Ile Phe Lys Ser Asn Arg Phe 1 5 10 15 Gln Thr Ile Tyr Glu Asn Glu Asn Gly His Ile Arg Leu Leu Gln Arg 20 25 30 Phe Asp Lys Arg Ser Lys Ile Phe Glu Asn Leu Gln Asn Tyr Arg Leu 35 40 45 Leu Glu Tyr Lys Ser Lys Pro His Thr Ile Phe Leu Pro Gln Phe Thr 50 55 60 Asp Ala Asp Phe Ile Leu Val Val Leu Ser Gly Lys Ala Ile Leu Thr 65 70 75 80 Val Leu Asn Ser Asn Asp Arg Asn Ser Phe Asn Leu Glu Arg Gly Asp 85 90 95 Thr Ile Lys Leu Pro Ala Gly Thr Ile Ala Tyr Leu Ala Asn Arg Asp 100 105 110 Asp Asn Glu Asp Leu Arg Val Leu Asp Leu Ala Ile Pro Val Asn Arg 115 120 125 Pro Gly Gln Leu Gln Ser Phe Leu Leu Ser Gly Thr Gln Asn Gln Pro 130 135 140 Ser Phe Leu Ser Gly Phe Ser Lys Asn Ile Leu Glu Ala Ala Phe Asn 145 150 155 160 Thr Glu Tyr Glu Glu Ile Glu Lys Val Leu Leu Glu Glu Gln Glu Gln 165 170 175 Lys Ser Gln His Arg Arg Ser Leu Arg Asp Lys Arg Gln Glu Ile Thr 180 185 190 Asn Glu Asp Val Ile Val Lys Val Ser Arg Glu Gln Ile Glu Glu Leu 195 200 205 Ser Lys Asn Ala Lys Ser Ser Ser Lys Lys Ser Val Ser Ser Glu Ser 210 215 220 Glu Pro Phe Asn Leu Arg Ser Arg Asn Pro Ile Tyr Ser Asn Lys Phe 225 230 235 240 Gly Lys Phe Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln Leu Gln Asp 245 250 255 Leu Asp Ile Phe Val Asn Ser Val Glu Ile Lys Glu Gly Ser Leu Leu 260 265 270 Leu Pro Asn Tyr Asn Ser Arg Ala Ile Val Ile Val Thr Val Asn Glu 275 280 285 Gly Lys Gly Asp Phe Glu Leu Val Gly Gln Arg Asn Glu Asn Gln Gln 290 295 300 Glu Gln Arg Glu Glu Asn Asp Glu Glu Glu Gly Gln Glu Glu Glu Thr 305 310 315 320 Thr Lys Gln Val Gln Arg Tyr Arg Ala Arg Leu Ser Pro Gly Asp Val 325 330 335 Leu Val Ile Pro Ala Gly His Pro Val Ala Ile Asn Ala Ser Ser Asp 340 345 350 Leu Asn Leu Ile Gly Phe Gly Ile Asn Ala Lys Asn Asn Gln Arg Asn 355 360 365 Phe Leu Ala Gly Glu Glu Asp Asn Val Ile Ser Gln Ile Gln Arg Pro 370 375 380 Val Lys Glu Leu Ala Phe Pro Gly Ser Ser Arg Glu Val Asp Arg Leu 385 390 395 400 Leu Thr Asn Gln Lys Gln Ser His Phe Ala Asn Ala Gln Pro Leu Gln 405 410 415 Ile Glu <210> 225 <211> 415 <212> PRT <213> Lentil <400> 225 Ser Arg Ser Asp Gln Glu Asn Pro Phe Ile Phe Lys Ser Asn Arg Phe 1 5 10 15 Gln Thr Ile Tyr Glu Asn Glu Asn Gly His Ile Arg Leu Leu Gln Lys 20 25 30 Phe Asp Lys Arg Ser Lys Ile Phe Glu Asn Leu Gln Asn Tyr Arg Leu 35 40 45 Leu Glu Tyr Lys Ser Lys Pro His Thr Leu Phe Leu Pro Gln Tyr Thr 50 55 60 Asp Ala Asp Phe Ile Leu Val Val Leu Ser Gly Lys Ala Val Leu Thr 65 70 75 80 Val Leu Asn Ser Asn Asp Arg Asn Ser Phe Asn Leu Glu Arg Gly Asp 85 90 95 Thr Ile Lys Leu Pro Ala Gly Thr Ile Ala Tyr Leu Ala Asn Arg Asp 100 105 110 Asp Asn Glu Asp Leu Arg Val Leu Asp Leu Ala Ile Pro Val Asn Asn 115 120 125 Pro Gly Gln Leu Glu Ser Phe Leu Leu Ser Gly Thr Gln Asn Gln Pro 130 135 140 Ser Phe Leu Ser Gly Phe Asn Lys Ser Ile Leu Glu Ala Ala Phe Asn 145 150 155 160 Thr Asp Tyr Glu Glu Ile Glu Lys Val Leu Leu Glu Asp Gln Glu Gln 165 170 175 Glu Pro Gln His Arg Arg Ser Leu Arg Asp Arg Arg Gln Glu Ile Asn 180 185 190 Lys Glu Asn Val Ile Val Lys Val Ser Arg Glu Gln Ile Lys Glu Leu 195 200 205 Ser Lys Asn Ala Lys Ser Ser Ser Lys Lys Ser Val Ser Ser Glu Ser 210 215 220 Glu Pro Phe Asn Leu Arg Ser Arg Asn Pro Ile Tyr Ser Asn Lys Phe 225 230 235 240 Gly Lys Phe Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln Leu Gln Asp 245 250 255 Leu Asp Ile Phe Val Asn Ser Val Glu Ile Lys Glu Gly Ser Leu Leu 260 265 270 Leu Pro Asn Tyr Asn Ser Arg Ala Ile Val Ile Val Thr Val Asn Glu 275 280 285 Gly Lys Gly Tyr Phe Glu Leu Val Gly Gln Arg Asn Glu Asn Gln Arg 290 295 300 Glu Glu Asn Asp Asp Glu Glu Glu Gln Glu Glu Glu Thr Ser Thr Gln 305 310 315 320 Val Gln Arg Tyr Arg Ala Lys Leu Ser Pro Gly Asp Val Phe Val Val 325 330 335 Pro Ala Gly His Pro Val Ala Ile Asn Ala Ser Ser Asp Leu Asn Leu 340 345 350 Ile Gly Phe Gly Ile Asn Ala Lys Asn Asn Gln Arg Asn Phe Leu Ala 355 360 365 Gly Glu Glu Asp Asn Val Ile Ser Gln Ile Gln Arg Pro Val Lys Glu 370 375 380 Leu Ala Phe Pro Gly Ser Ser Arg Glu Val Asp Arg Leu Leu Thr Asn 385 390 395 400 Gln Lys Gln Ser His Phe Ala Asn Ala Gln Pro Leu Gln Ile Glu 405 410 415 <210> 226 <211> 463 <212> PRT <213> Vicia villosa Roth <400> 226 Met Ala Ala Ile Thr Met Lys Val Ser Phe Pro Leu Leu Met Leu Leu 1 5 10 15 Gly Ile Ser Phe Leu Ala Ser Val Cys Val Ser Ser Arg Ser Asp Gln 20 25 30 Glu Asn Pro Phe Ile Phe Lys Ser Asn Lys Phe Gln Thr Leu Phe Glu 35 40 45 Asn Asp Asn Gly His Ile Arg Leu Leu Gln Lys Phe Asp Glu Arg Ser 50 55 60 Lys Ile Leu Glu Asn Leu Gln Asn Tyr Arg Leu Leu Glu Tyr Lys Ser 65 70 75 80 Lys Pro Arg Thr Ile Phe Leu Pro Gln Gln Thr Asn Ala Asp Phe Ile 85 90 95 Leu Val Val Leu Ser Gly Lys Ala Ile Leu Thr Val Leu Lys Pro Asp 100 105 110 Asp Arg Asn Ser Phe Asn Leu Glu Arg Gly Asp Thr Ile Lys Leu Pro 115 120 125 Ala Gly Thr Ile Ala Tyr Leu Val Asn Lys Asp Asp Asn Glu Asp Leu 130 135 140 Arg Val Leu Asp Leu Ala Ile Pro Val Asn Gly Pro Asp Gln Leu Gln 145 150 155 160 Ser Phe Leu Leu Ser Gly Ser Glu Asn Gln Gln Ser Ile Leu Ser Gly 165 170 175 Phe Ser Lys Ser Val Leu Glu Ala Ser Phe Asn Thr Gly Tyr Glu Glu 180 185 190 Ile Glu Lys Val Leu Leu Glu Glu Arg Glu Lys Glu Thr Gln His Arg 195 200 205 Arg Ser Leu Arg Asp Lys Arg Gln His Ser Gln Asp Glu Asp Val Ile 210 215 220 Val Lys Leu Ser Arg Gly Gln Ile Glu Glu Leu Ser Arg Asn Ala Lys 225 230 235 240 Ser Ser Ser Lys Lys Ser Val Ser Ser Glu Ser Glu Pro Phe Asn Leu 245 250 255 Arg Ser Arg Asn Pro Ile Tyr Ser Asn Lys Phe Gly Lys Phe Phe Glu 260 265 270 Ile Thr Pro Glu Lys Asn Pro Gln Leu Gln Asp Leu Asp Val Leu Val 275 280 285 Asn Ser Val Glu Ile Lys Glu Gly Ser Leu Leu Leu Pro His Tyr Asn 290 295 300 Ser Arg Ala Ile Val Ile Val Thr Val Asn Asp Gly Lys Gly Asp Phe 305 310 315 320 Glu Ile Val Gly Gln Arg Asn Glu Asn Arg Gln Gly Gln Arg Lys Glu 325 330 335 Asp Asp Glu Glu Glu Glu Gln Gly Asp Glu Asn Thr Asn Thr Gln Val 340 345 350 Gln Asn Tyr Lys Ala Lys Leu Ser Arg Gly Asp Val Phe Val Ile Pro 355 360 365 Ala Gly His Pro Val Ser Ile Lys Ala Ser Ser Asn Leu Asp Leu Leu 370 375 380 Gly Phe Gly Ile Asn Ala Lys Asn Asn Gln Arg Asn Phe Leu Ala Gly 385 390 395 400 Glu Glu Asp Asn Val Ile Ser Gln Ile Asp Arg Pro Val Lys Glu Leu 405 410 415 Ala Phe Pro Gly Ser Ala Gln Glu Val Asp Arg Leu Leu Glu Asn Gln 420 425 430 Lys Gln Ser His Phe Ala Asn Ala Gln Pro Gln Gln Arg Glu Arg Gly 435 440 445 Ser His Glu Thr Arg Asp His Leu Ser Ser Ile Leu Asp Ala Phe 450 455 460 <210> 227 <211> 396 <212> PRT <213> Soybean <400> 227 Gln Tyr Gly His Val Arg Val Leu Gln Arg Phe Asn Lys Arg Ser Gln 1 5 10 15 Gln Leu Gln Asn Leu Arg Asp Tyr Arg Ile Leu Glu Phe Asn Ser Lys 20 25 30 Pro Asn Thr Leu Leu Leu Pro His His Ala Asp Ala Asp Tyr Leu Ile 35 40 45 Val Ile Leu Asn Gly Thr Ala Ile Leu Thr Leu Val Asn Asn Asp Asp 50 55 60 Arg Asp Ser Tyr Asn Leu Gln Ser Gly Asp Ala Leu Arg Val Pro Ala 65 70 75 80 Gly Thr Thr Tyr Tyr Val Val Asn Pro Asp Asn Asp Glu Asn Leu Arg 85 90 95 Met Ile Thr Leu Ala Ile Pro Val Asn Lys Pro Gly Arg Phe Glu Ser 100 105 110 Phe Phe Leu Ser Ser Thr Gln Ala Gln Gln Ser Tyr Leu Gln Gly Phe 115 120 125 Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys Phe Glu Glu Ile 130 135 140 Asn Lys Val Leu Phe Gly Arg Glu Glu Gly Gln Gln Gln Gly Glu Glu 145 150 155 160 Arg Leu Gln Glu Ser Val Ile Val Glu Ile Ser Lys Lys Gln Ile Arg 165 170 175 Glu Leu Ser Lys His Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser Ser 180 185 190 Glu Asp Lys Pro Phe Asn Leu Arg Ser Arg Asp Pro Ile Tyr Ser Asn 195 200 205 Lys Leu Gly Lys Leu Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln Leu 210 215 220 Arg Asp Leu Asp Val Phe Leu Ser Val Val Asp Met Asn Glu Gly Ala 225 230 235 240 Leu Phe Leu Pro His Phe Asn Ser Lys Ala Ile Val Val Leu Val Ile 245 250 255 Asn Glu Gly Glu Ala Asn Ile Glu Leu Val Gly Ile Lys Glu Gln Gln 260 265 270 Gln Arg Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg Lys Tyr Arg 275 280 285 Ala Glu Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala Gly Tyr Pro 290 295 300 Val Val Val Asn Ala Thr Ser Asp Leu Asn Phe Phe Ala Phe Gly Ile 305 310 315 320 Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser Lys Asp Asn 325 330 335 Val Ile Ser Gln Ile Pro Ser Gln Val Gln Glu Leu Ala Phe Pro Gly 340 345 350 Ser Ala Lys Asp Ile Glu Asn Leu Ile Lys Ser Gln Ser Glu Ser Tyr 355 360 365 Phe Val Asp Ala Gln Pro Gln Gln Lys Glu Glu Gly Asn Lys Gly Arg 370 375 380 Lys Gly Pro Leu Ser Ser Ile Leu Arg Ala Phe Tyr 385 390 395 <210> 228 <211> 498 <212> PRT <213> Vicia sativa <400> 228 Met Ala Lys Leu Leu Ala Leu Ser Leu Ser Phe Cys Phe Leu Leu Phe 1 5 10 15 Ser Ser Cys Phe Ala Leu Arg Glu Gln Ser Gln Gln Asn Glu Cys Gln 20 25 30 Leu Glu Arg Ile Asn Ala Leu Glu Pro Asp Asn Arg Ile Glu Ser Glu 35 40 45 Gly Gly Leu Ile Glu Thr Trp Asn Pro Asn Asn Arg Gln Phe Arg Cys 50 55 60 Ala Arg Val Ala Leu Ser Arg Ala Thr Leu Gln Arg Asn Ala Leu Arg 65 70 75 80 Arg Pro Tyr Tyr Ser Asn Ala Pro Gln Glu Ile Tyr Ile Gln Gln Gly 85 90 95 Asn Gly Tyr Phe Gly Met Val Phe Pro Gly Cys Pro Glu Thr His Glu 100 105 110 Glu Pro Gln Gln Ser Glu Gln Gly Glu Gly Arg Arg Tyr Arg Asp Ser 115 120 125 His Gln Lys Val Asn Arg Phe Arg Glu Gly Asp Ile Ile Ala Val Pro 130 135 140 Thr Gly Ile Ala Phe Trp Met Tyr Asn Asp Gln Asp Thr Pro Val Ile 145 150 155 160 Ala Ile Ser Leu Thr Asp Thr Gly Ser Ser Asn Asn Gln Leu Asp Gln 165 170 175 Met Pro Arg Arg Phe Tyr Leu Ala Gly Asn Gln Glu Gln Glu Phe Leu 180 185 190 Arg Tyr Gln His Gln Gln Gly Gly Lys Gln Glu Gln Asp Asn Asp Gly 195 200 205 Asn Asn Ile Phe Ser Gly Phe Lys Arg Asp Phe Leu Glu Asp Ala Phe 210 215 220 Asn Val Asn Arg His Ile Val Asp Arg Leu Gln Gly Arg Asn Glu Asp 225 230 235 240 Glu Glu Lys Gly Ala Ile Val Lys Val Lys Gly Gly Leu Ser Ile Ile 245 250 255 Ala Pro Pro Glu Arg Gln Ala Arg His Glu Arg Gly Ser Arg Gln Glu 260 265 270 Glu Asp Glu Asp Glu Lys Glu Glu Arg Gln Pro Ser His His Lys Ser 275 280 285 Arg Arg Asp Glu Asp Glu Asp Asp Lys Glu Lys Arg His Ser Gln Lys 290 295 300 Gly Gln Ser Arg Arg Gln Gly Asp Asn Gly Leu Glu Glu Thr Val Cys 305 310 315 320 Thr Ala Lys Leu Arg Ala Asn Ile Gly Ser Ser Pro Ser Pro Asp Ile 325 330 335 Tyr Asn Pro Gln Ala Gly Arg Ile Lys Thr Val Thr Ser Leu Asp Leu 340 345 350 Pro Val Leu Arg Trp Leu Lys Leu Ser Ala Glu His Gly Ser Leu His 355 360 365 Lys Asn Ala Met Phe Val Pro His Tyr Asn Leu Asn Ala Asn Ser Val 370 375 380 Ile Tyr Ala Leu Lys Gly Arg Ala Arg Leu Gln Val Val Asn Cys Asn 385 390 395 400 Gly Asn Thr Val Phe Asp Gly Glu Leu Glu Ala Gly Arg Ala Leu Thr 405 410 415 Val Pro Gln Asn Tyr Ala Val Ala Ala Lys Ser Leu Ser Glu Arg Phe 420 425 430 Thr Tyr Val Ala Phe Lys Thr Asp Asp Arg Ala Ser Ile Ala Arg Leu 435 440 445 Ala Gly Thr Ser Ser Val Ile Asp Asp Leu Pro Leu Asp Val Val Ala 450 455 460 Ala Thr Phe Asn Met Gln Arg Asn Glu Ala Arg Gln Leu Lys Ser Asn 465 470 475 480 Asn Pro Phe Lys Phe Leu Val Pro Pro Arg Gln Ser Glu Met Arg Ala 485 490 495 Ser Ala <210> 229 <211> 531 <212> PRT <213> Medicago truncatula <400> 229 Met Ala Lys Leu Leu Ala Leu Ser Leu Ser Leu Cys Phe Leu Leu Phe 1 5 10 15 Ser Gly Cys Phe Ala Ile Arg Glu His Gln Pro His Gln Lys Gln Gln 20 25 30 Pro Gln Gln Asn Glu Cys Gln Leu Glu Gln Leu Asn Ala Leu Glu Pro 35 40 45 Asp Asn Arg Ile Glu Ser Glu Gly Gly Ile Ile Glu Thr Trp Asn Pro 50 55 60 Asn Asn Arg Gln Phe Arg Cys Ala Gly Val Ala Leu Ser Arg Cys Thr 65 70 75 80 Leu Gln Arg Asn Ser Leu Arg Arg Pro Phe Tyr Ser Asn Ala Pro Gln 85 90 95 Glu Ile Phe Ile Gln Gln Gly Ser Gly Tyr Phe Gly Met Val Phe Pro 100 105 110 Gly Cys Pro Glu Thr Phe Glu Glu Pro Gln Glu Ser Glu Gln Arg Glu 115 120 125 Ser Arg Arg Ile Arg Glu Ser Glu Gln Gly Glu Ser Arg Arg Ile Arg 130 135 140 Glu Ser Glu Gln Gly Glu Gly Arg Arg Phe Arg Asp Ser His Gln Lys 145 150 155 160 Val Asn Arg Phe Arg Glu Gly Asp Leu Ile Ala Val Pro Thr Gly Thr 165 170 175 Val Phe Trp Met Tyr Asn Asp Gln Asp Thr Pro Val Ile Ala Val Ser 180 185 190 Leu Ile Asp Thr Gly Ser Phe Gln Asn Gln Leu Asp Glu Met Pro Arg 195 200 205 Arg Phe Tyr Leu Ala Gly Asn Gln Glu Gln Glu Phe Leu Gln Tyr Gln 210 215 220 Gln Gln Gln Val Arg Gly Arg Gly Glu Gln Arg Arg Gly Arg Glu Gln 225 230 235 240 Gln Glu Asn Glu Gly Gly Asn Ile Phe Ser Gly Phe Lys Arg Asp Phe 245 250 255 Leu Glu Asp Ala Leu Asn Val Asn Arg His Ile Val Asp Arg Leu Gln 260 265 270 Gly Arg Asn Glu Asp Glu Glu Lys Gly Ala Ile Val Lys Val Arg Gly 275 280 285 Gly Leu Ser Phe Val Thr Pro Pro Glu Arg Gln Ser Arg His Gln Gly 290 295 300 Gly Ser Ile Ile Glu Glu Asp Glu Asp Glu Glu Asp Glu Trp Arg Arg 305 310 315 320 Pro His His Gln Lys Ser Arg Arg Gly Glu Glu Glu Glu Arg Pro Cys 325 330 335 Arg Arg Gly Gln Lys Cys Glu Arg Ser Asn Gly Leu Glu Glu Thr Ile 340 345 350 Cys Thr Ala Arg Leu Arg Gln Asn Ile Gly Ser Ser Ser Ser Pro Asp 355 360 365 Ile Tyr Asn Pro Glu Ala Gly Arg Ile Lys Thr Val Thr Ser Phe Asp 370 375 380 Leu Pro Ala Leu Arg Trp Leu Arg Leu Ser Ala Glu His Gly Thr Leu 385 390 395 400 His Arg Asn Ala Met Phe Val Pro His Tyr Asn Leu Asn Ala Asn Ser 405 410 415 Ala Ile Tyr Ala Leu Arg Gly Arg Ala Arg Leu Gln Val Val Asn Cys 420 425 430 Asn Gly Asn Thr Val Phe Asp Gly Glu Leu Glu Ala Gly Arg Val Leu 435 440 445 Ile Val Pro Gln Asn Phe Ala Val Ala Ala Lys Ser Met Ser Asp Arg 450 455 460 Phe Gln Tyr Val Ser Phe Lys Thr Asn Asp Asn Ala Ala Ile Ala Arg 465 470 475 480 Leu Ala Gly Thr Gln Ser Thr Leu Ser Gly Val Pro Met Asp Val Leu 485 490 495 Ala Ala Thr Tyr Asn Met Asp Arg Asn Glu Ala Arg Gln Leu Lys Asn 500 505 510 Asn Asn Leu Tyr Lys Phe Leu Val Pro Pro Arg Glu Ser Glu Arg Arg 515 520 525 Ala Ala Ala 530 <210> 230 <211> 476 <212> PRT <213> Lotus japonicus <400> 230 Met Ala Tyr Lys Leu Phe Ala Leu Ser Leu Ser Phe Cys Phe Leu Leu 1 5 10 15 Phe Gly Gly Cys Phe Ala Ile Arg Gln Gln Ser Gln Gln Gln Asn Glu 20 25 30 Cys Gln Leu Glu Arg Leu Asn Ala Leu Lys Pro Asp Asn Arg Ile Glu 35 40 45 Ser Glu Ala Gly Tyr Ile Glu Thr Trp Asn Pro Thr Asn Asn Gln Phe 50 55 60 Arg Cys Ala Gly Val Ala Leu Ser Arg Cys Thr Leu Arg Arg Asn Gly 65 70 75 80 Leu Lys Arg Pro Ser Tyr Ser Asn Ala Pro Gln Glu Ile Phe Ile Gln 85 90 95 Gln Gly Ser Gly Ile Phe Gly Met Ile Phe Pro Gly Cys Pro Glu Thr 100 105 110 Val Glu Glu Pro Phe Glu Ser Asp Gln Gln Gly Arg Arg Asp Arg His 115 120 125 Gln Lys Val Asn Arg Phe Arg Glu Gly Asp Val Ile Ala Val Pro Pro 130 135 140 Gly Val Val Phe Trp Met Tyr Asn Glu Glu Glu Thr Pro Val Ile Ala 145 150 155 160 Val Ser Leu Ile Asp Thr Gly Ser Tyr Leu Asn Gln Leu Asp Gln Met 165 170 175 Pro Arg Arg Phe Tyr Leu Ser Gly Asn Gln Glu Gln Glu Phe Leu Gln 180 185 190 Tyr Gln Arg Gln Glu Val Arg Gly Arg Glu Glu Glu Asn Gln Gly Gly 195 200 205 Asn Ile Phe Ser Gly Phe Gly Gly Glu Phe Leu Glu Asp Ala Leu Asn 210 215 220 Ile Asp Arg Asn Ile Val His Lys Leu Gln Gly Arg Asp Glu Glu Gln 225 230 235 240 Asp Lys Gly Ala Ile Val Arg Val Lys Gly Gly Leu Ser Val Ile Thr 245 250 255 Pro Pro Glu Arg Gln Ser His Arg Arg Gly Ser Glu Glu Glu Glu Asp 260 265 270 Glu Glu Glu Asp Arg Pro Ser Arg His Gln Ser Arg Gly Gly Ser Arg 275 280 285 Arg Asn Gly Leu Glu Glu Thr Ile Cys Thr Val Arg Leu Arg Met Asn 290 295 300 Ile Gly Lys Ser Ser Ser Pro Asp Ile Phe Asn Pro Gln Ala Gly Arg 305 310 315 320 Ile Lys Thr Ala Thr Gly Phe Asp Phe Pro Ala Leu Arg Phe Leu Lys 325 330 335 Leu Ser Ala Glu His Gly Ser Leu Asn Arg Asn Ala Met Val Val Pro 340 345 350 His Tyr Asn Leu Asn Ala Asn Ser Ile Ile Tyr Ala Leu Arg Gly Arg 355 360 365 Ala Trp Ile Gln Val Val Asn Cys Lys Gly Asn Arg Ile Phe Asp Gly 370 375 380 Glu Leu Glu Glu Gly Gln Val Leu Ile Val Pro Gln Asn Phe Val Val 385 390 395 400 Ala Ala Arg Ser Met Ser Asp Lys Phe Asn Tyr Val Ala Phe Lys Thr 405 410 415 Asn Asp Met Pro Thr Met Ala Lys Leu Ala Gly Ala Thr Ser Glu Ile 420 425 430 Gln Ala Met Pro Leu Glu Val Ile Gln Asn Ala Phe Asn Leu Glu Arg 435 440 445 Glu Gln Ala Lys Gln Val Lys Phe Asn Asn Arg Phe Asn Phe Leu Val 450 455 460 Pro Pro Arg Glu Gln Ser Gln Arg Arg Ala Ser Ala 465 470 475 <210> 231 <211> 526 <212> PRT <213> Ethiopian pea <400> 231 Met Ala Thr Thr Val Glu Ser Arg Phe Pro Leu Leu Leu Phe Pro Gly 1 5 10 15 Ile Ile Phe Leu Ala Ser Val Cys Val Thr Tyr Ala Asn Tyr Asp Glu 20 25 30 Gly Ser Glu Thr Arg Val Pro Gly Gln Arg Glu Arg Gly Arg Gln Glu 35 40 45 Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Arg Pro Ser Tyr Glu 50 55 60 Lys Glu Glu Asp Glu Glu Glu Lys Gln Lys Tyr Arg Tyr Gln Arg Glu 65 70 75 80 Lys Glu Asp Glu Glu Glu Lys Gln Lys Tyr Arg Tyr Gln Arg Glu Lys 85 90 95 Lys Glu Glu Lys Glu Val Gln Pro Gly Arg Glu Arg Trp Glu Arg Glu 100 105 110 Glu Asp Glu Glu Gln Val Asp Glu Glu Trp Arg Gly Ser Gln Arg Arg 115 120 125 Gln Asp Pro Glu Glu Arg Ala Arg Leu Arg His Arg Glu Glu Arg Thr 130 135 140 Lys Arg Asp Arg Arg His Lys Arg Glu Gly Glu Glu Glu Glu Arg Ser 145 150 155 160 Ser Glu Ser Gln Glu Gln Arg Asn Pro Phe Leu Phe Lys Ser Asn Lys 165 170 175 Phe Leu Thr Leu Phe Glu Asn Glu Asn Gly His Ile Arg Arg Leu Gln 180 185 190 Arg Phe Asp Lys Arg Ser Asp Leu Phe Glu Asn Leu Gln Asn Tyr Arg 195 200 205 Leu Val Glu Tyr Arg Ala Lys Pro His Thr Ile Phe Leu Pro Gln His 210 215 220 Ile Asp Ala Asp Leu Ile Leu Val Val Leu Asn Gly Lys Ala Ile Leu 225 230 235 240 Thr Val Leu Ser Pro Asn Asp Arg Asn Ser Tyr Asn Leu Glu Arg Gly 245 250 255 Asp Thr Ile Lys Ile Pro Ala Gly Thr Thr Ser Tyr Leu Val Asn Gln 260 265 270 Asp Asp Glu Glu Asp Leu Arg Val Val Asp Phe Val Ile Pro Val Asn 275 280 285 Arg Pro Gly Lys Phe Glu Ala Phe Gly Leu Ser Glu Asn Lys Asn Gln 290 295 300 Tyr Leu Arg Gly Phe Ser Lys Asn Ile Leu Glu Ala Ser Leu Asn Thr 305 310 315 320 Lys Tyr Glu Thr Ile Glu Lys Val Leu Leu Glu Glu Gln Glu Lys Lys 325 330 335 Pro Gln Gln Leu Arg Asp Arg Lys Arg Arg Gln Gln Gly Gly Glu Arg 340 345 350 Asp Ala Ile Ile Lys Val Ser Arg Glu Gln Ile Glu Glu Leu Arg Lys 355 360 365 Leu Ala Lys Ser Ser Ser Lys Lys Ser Leu Pro Ser Glu Phe Glu Pro 370 375 380 Phe Asn Leu Arg Ser His Lys Pro Glu Tyr Ser Asn Lys Phe Gly Lys 385 390 395 400 Leu Phe Glu Ile Thr Pro Glu Lys Lys Tyr Pro Gln Leu Gln Asp Leu 405 410 415 Asp Ile Leu Val Ser Cys Val Glu Ile Asn Lys Gly Ala Leu Met Leu 420 425 430 Pro His Tyr Asn Ser Arg Ala Ile Val Val Leu Leu Val Asn Glu Gly 435 440 445 Lys Gly Asn Leu Glu Leu Leu Gly Leu Lys Asn Glu Gln Gln Glu Arg 450 455 460 Glu Asp Arg Lys Glu Arg Asn Asn Glu Val Gln Arg Tyr Glu Ala Arg 465 470 475 480 Leu Ser Pro Gly Asp Val Val Ile Ile Pro Ala Gly His Pro Val Ala 485 490 495 Ile Ser Ala Ser Ser Asn Leu Asn Leu Leu Gly Phe Gly Thr Asn Ala 500 505 510 Glu Asn Asn Gln Arg Asn Phe Leu Ser Gly Ser Asp Asp Asn 515 520 525 <210> 232 <211> 541 <212> PRT <213> Lathyrus sativus <400> 232 Met Ala Thr Thr Ile Lys Ser Arg Phe Pro Leu Leu Leu Leu Leu Gly 1 5 10 15 Ile Ile Phe Leu Ala Ser Val Cys Val Thr Trp Ala Asn Tyr Asp Glu 20 25 30 Gly Ser Glu Pro Arg Val Pro Gly Gln Arg Glu Arg Gly Arg Gln Glu 35 40 45 Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Arg Pro Ser Tyr Glu 50 55 60 Glu Glu Tyr Asp Glu Gly Leu Glu Pro Lys Val Pro Gly Lys Arg Glu 65 70 75 80 Arg Gly Arg Gln Glu Gly Glu Lys Glu Glu Lys Arg His Glu Glu Trp 85 90 95 Arg Pro Ser Tyr Glu Lys Glu Glu Asp Glu Glu Glu Lys Gln Lys Tyr 100 105 110 Asn Tyr Gln Arg Glu Lys Lys Glu His Lys Glu Val Gln Pro Gly Arg 115 120 125 Glu Arg Trp Glu Arg Lys Gln Asp Glu Lys Gln Val Glu Glu Asp Glu 130 135 140 Glu Pro Gly Glu Glu Gln Trp Arg Gly Ser Lys Arg His Glu Asp Pro 145 150 155 160 Glu Glu Arg Ala Arg Leu Arg His Arg Glu Glu Lys Thr Lys Ser Tyr 165 170 175 Val Glu Asp Asn Glu Glu Thr Ser Ser Lys Glu Gly Arg Asn Pro Phe 180 185 190 Leu Phe Lys Ser Asn Lys Phe Leu Thr Leu Phe Glu Asn Glu Asn Gly 195 200 205 His Ile Arg Arg Leu Gln Arg Phe Asp Glu Arg Ser Asp Ile Phe Glu 210 215 220 Asn Leu Gln Asn Tyr Arg Leu Val Glu Tyr Arg Ala Lys Pro His Thr 225 230 235 240 Met Phe Leu Pro Gln His Ile Asp Ala Asp Leu Ile Leu Val Val Leu 245 250 255 Asn Gly Lys Ala Ile Leu Thr Val Leu Ser Pro Asn Asp Arg Asn Ser 260 265 270 Tyr Asn Leu Glu Arg Gly Asp Thr Val Lys Leu Pro Ala Gly Thr Thr 275 280 285 Ser Tyr Leu Val Asn Gln Asp Asp Glu Glu Asp Leu Arg Val Val Asp 290 295 300 Leu Ala Ile Pro Val Asn Arg Pro Gly Lys Phe Glu Ala Phe Gly Leu 305 310 315 320 Ser Ala Asn Lys Asn Gln Tyr Leu Arg Gly Phe Ser Lys Asn Ile Leu 325 330 335 Glu Ala Ser Leu Asn Thr Lys Tyr Glu Thr Ile Glu Lys Val Leu Leu 340 345 350 Glu Glu Arg Arg Asp Gln Lys Gly Arg Gln Gln Gly Gln Glu Thr Asn 355 360 365 Ala Ile Val Lys Val Ser Arg Glu Gln Ile Glu Glu Leu Arg Lys Leu 370 375 380 Ala Lys Ser Ser Ser Lys Lys Ser Leu Leu Ser Glu Ser Glu Pro Leu 385 390 395 400 Asn Leu Arg Ser Gln Asn Pro Lys Tyr Ser Asn Lys Phe Gly Lys Phe 405 410 415 Phe Glu Ile Thr Pro Gln Lys Lys Tyr Pro Gln Leu Gln Asp Leu Asp 420 425 430 Val Ser Ile Ser Cys Val Glu Ile Asn Lys Gly Ala Leu Leu Leu Pro 435 440 445 His Tyr Asn Ser Arg Ser Ile Gly Ile Leu Leu Val Asn Glu Gly Lys 450 455 460 Gly Asn Leu Glu Leu Val Gly Phe Lys Asn Glu Gln Gln Arg Gln Arg 465 470 475 480 Glu Asn Glu Glu Thr Asn Lys Lys Leu Gln Arg Tyr Glu Ala Arg Leu 485 490 495 Ser Ser Gly Asp Val Val Val Ile Pro Glu Gly His Pro Val Ala Ile 500 505 510 Ser Ala Ser Ser Asn Leu Asn Leu Leu Gly Phe Gly Ile Asn Ala Ala 515 520 525 Asn Asn Gln Arg Asn Phe Leu Thr Gly Ser Asp Asp Asn 530 535 540 <210> 233 <211> 589 <212> PRT <213> Vicia villosa Roth <400> 233 Met Ala Thr Thr Ile Lys Ser Arg Phe Pro Val Leu Leu Leu Leu Gly 1 5 10 15 Ile Ile Phe Leu Thr Ser Val Cys Val Thr Tyr Ala Asn Tyr Asp Glu 20 25 30 Gly Arg Glu Pro Ser Val Pro Gly Gln Arg Glu Arg Gly Arg Gln Glu 35 40 45 Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Arg Pro Ser Glu Glu 50 55 60 Asp Glu Glu Glu Lys Tyr Lys Tyr Glu Glu Gly Arg Val Pro Gly Gln 65 70 75 80 Arg Glu Arg Gly Arg Gln Glu Gly Glu Lys Glu Glu Lys Arg His Gly 85 90 95 Lys Trp Arg Pro Ser Glu Glu Glu Asp Glu Glu Glu Lys Tyr Arg Tyr 100 105 110 Glu Glu Gly Ser Glu Pro Arg Gly Pro Gly Gln Arg Glu Thr Gly Arg 115 120 125 Gln Glu Gly Glu Lys Glu Lys Gln Arg Pro Glu Arg Glu Pro Ser Tyr 130 135 140 Glu Lys Glu Glu Asp Glu Glu Glu Lys Gln Lys Tyr Gln Tyr His Arg 145 150 155 160 Glu Lys Lys Glu Gln Arg Glu Val Arg Pro Gly Arg Glu Arg Phe Glu 165 170 175 Arg His Glu Asp Glu Glu Gln Trp Arg Gly Ile Gln Arg His Glu Asp 180 185 190 Pro Glu Glu Arg Ala Arg Glu Arg Tyr Arg Ala Glu Ile Ala Lys Arg 195 200 205 Gln Val Glu Glu Glu Arg Glu Glu Arg Asp Ile Pro His Glu Arg Glu 210 215 220 Gln Arg Asn Pro Phe Leu Phe Lys Ser Asn Lys Phe Gln Thr Leu Phe 225 230 235 240 Gln Asn Glu Asn Gly Tyr Ile Arg Arg Leu Gln Arg Phe Asp Lys Arg 245 250 255 Ser Asp Leu Phe Glu Asn Leu Gln Asn Tyr Arg Leu Val Glu Tyr Arg 260 265 270 Ala Lys Pro His Thr Ile Phe Leu Pro Gln His Ile Asp Ala Asp Leu 275 280 285 Ile Ile Val Val Leu Ser Gly Arg Ala Ile Leu Thr Val Leu Ser Pro 290 295 300 Asp Asp Arg Asn Ser Tyr Asn Leu Glu Arg Gly Asp Thr Ile Lys Leu 305 310 315 320 Pro Ala Gly Thr Thr Ser Tyr Leu Val Asn Gln Asp Asp Glu Glu Asp 325 330 335 Leu Arg Val Val Asp Leu Ala Ile Pro Val Asn Arg Pro Gly Lys Val 340 345 350 Glu Ser Phe Leu Leu Ser Gly Asn Lys Asn Gln Tyr Leu Arg Gly Phe 355 360 365 Ser Lys Asn Ile Leu Glu Ala Ser Phe Asn Thr Asn Tyr Glu Thr Ile 370 375 380 Glu Arg Val Leu Leu Glu Glu Gln Asp Lys Glu Ser Gln Gln Ser Ile 385 390 395 400 Gly Gln Lys Arg Arg Ser Gln Arg Gln Glu Thr Asn Ala Leu Val Lys 405 410 415 Val Ser Arg Glu Gln Leu Glu Asp Leu Lys Arg Leu Ala Lys Ser Ser 420 425 430 Ser Gln Glu Gly Leu Ser Ser Gln Phe Glu Pro Ile Asn Leu Arg Ser 435 440 445 Gln Asn Pro Lys Tyr Ser Asn Lys Phe Gly Lys Val Phe Glu Ile Thr 450 455 460 Pro Glu Lys Lys Tyr Pro Gln Leu Gln Asp Leu Asp Leu Phe Val Ser 465 470 475 480 Ser Val Asp Ile Lys Glu Gly Ala Leu Met Leu Pro His Tyr Asn Ser 485 490 495 Arg Ala Ile Val Val Leu Leu Val Asn Glu Gly Arg Gly Asn Leu Glu 500 505 510 Leu Val Gly Leu Lys Asn Glu Gln Gln Glu Gln Arg Glu Lys Glu Asp 515 520 525 Glu Gln Gln Glu Arg Asn Asn Gln Val Gln Arg Tyr Glu Ala Arg Leu 530 535 540 Ser Pro Gly Asp Val Val Ile Ile Pro Ala Gly His Pro Val Ala Val 545 550 555 560 Arg Ala Ser Ser Asp Leu Asn Leu Leu Ala Phe Gly Ile Asn Ala Glu 565 570 575 Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser Asp Asp Asn 580 585 <210> 234 <211> 463 <212> PRT <213> Medicago truncatula <400> 234 Met Ala Ile Lys Ala Pro Phe Gln Leu Leu Met Leu Leu Gly Ile Phe 1 5 10 15 Phe Leu Ala Ser Val Cys Val Ser Ser Arg Asp Asp Arg His Asp Gln 20 25 30 Glu Asn Pro Phe Phe Phe Asn Ala Asn His Phe Gln Thr Leu Phe Glu 35 40 45 Asn Glu Asn Gly His Ile Arg Leu Leu Gln Arg Phe Asp Lys Arg Ser 50 55 60 Lys Ile Phe Glu Asn Leu Gln Asn Tyr Arg Leu Leu Glu Tyr His Ser 65 70 75 80 Lys Pro His Thr Leu Phe Leu Pro Gln His Asn Asp Ala Asp Phe Ile 85 90 95 Leu Ala Val Leu Ser Gly Lys Ala Ile Leu Thr Val Leu Asn Pro Asp 100 105 110 Asn Arg Asn Ser Phe Asn Leu Glu Arg Gly Asp Thr Ile Lys Leu Pro 115 120 125 Ala Gly Ser Ile Ala Tyr Leu Ala Asn Arg Asp Asp Asn Glu Asp Leu 130 135 140 Arg Val Leu Asp Leu Ala Ile Pro Val Asn Arg Pro Gly Lys Phe Gln 145 150 155 160 Ser Phe Ser Leu Ser Gly Ser Gln Asn Gln Gln Ser Phe Phe Ser Gly 165 170 175 Phe Ser Lys Asn Ile Leu Glu Ala Ala Phe Asn Ala Asn Tyr Glu Glu 180 185 190 Ile Glu Arg Val Leu Ile Glu Glu His Glu Gln Glu Pro Gln His Arg 195 200 205 Arg Gly Leu Arg Lys Asp Arg Arg Gln Gln Ser Gln Asp Ser Asn Val 210 215 220 Ile Val Lys Val Ser Arg Glu Gln Ile Glu Glu Leu Ser Arg His Ala 225 230 235 240 Lys Ser Ser Ser Arg Arg Ser Gly Ser Ser Glu Ser Ala Pro Phe Asn 245 250 255 Leucine Arginine Serine Arginine Glutamic acid Proline Isoleucine Tyrosine Serine Asparagine Glutamic acid Phenylalanine Glycine Asparagine Phenylalanine Phenylalanine 260 265 270 Glutamic acid Isoleucine Threonine Proline Glutamic acid Lysine Asparagine Proline Glutamine Leucine Lysine Aspartic acid Leucine Aspartic acid Isoleucine Leucine 275 280 285 Valine Asparagine Tyrosine Alanine Glutamic acid Isoleucine Arginine Glutamic acid Glycine Serine Leucine Leucine Leucine Proline Histidine Phenylalanine 290 295 300 Asparagine Serine Arginine Alanine Threonine Valine Isoleucine Valine Valine Valine Aspartic acid Glutamic acid Glycine Lysine Glycine Glutamic acid 305 310 315 320 Phenylalanine Glutamic acid Leucine Valine Glycine Glutamine Arginine Asparagine Glutamic acid Asparagine Glutamine Glutamine Glutamic acid Glutamine Arginine Glutamic acid 325 330 335 Glutamic acid Aspartic acid Glutamic acid Glutamine Glutamine Glutamic acid Glutamic acid Glutamic acid Arginine Serine Glutamine Glutamine Valine Glutamine Arginine Tyrosine 340 345 350 Arginine Alanine Arginine Leucine Serine Proline Glycine Aspartic acid Valine Tyrosine Valine Isoleucine Proline Alanine Glycine Histidine 355 360 365 Proline Threonine Valine Valine Serine Alanine Serine Serine Aspartic acid Leucine Serine Leucine Leucine Glycine Phenylalanine Glycine 370 375 380 Isoleucine Asparagine Alanine Glutamic acid Asparagine Asparagine Glutamic acid Arginine Asparagine Phenylalanine Leucine Alanine Glycine Glutamic acid Glutamic acid Aspartic acid 385 390 395 400 Asparagine Valine Isoleucine Serine Glutamine Isoleucine Glutamic acid Arginine Proline Valine Lysine Glutamic acid Valine Alanine Phenylalanine Proline 405 410 415 Gly Ser Ala Gln Asp Val Glu Ser Leu Leu Lys Asn Gln Arg Gln Ser 420 425 430 Tyr Phe Ala Asn Ala Gln Pro Gln Gln Arg Glu Arg Glu Glu Gly Arg 435 440 445 Ser Gln Arg Gln Arg Glu Leu Ile Ser Ser Ile Leu Gly Val Phe 450 455 460 <210> 235 <211> 499 <212> PRT <213> Vicia peregrina <400> 235 Met Ala Thr Thr Phe Lys Ser Arg Phe Ser Leu Leu Leu Leu Leu Gly 1 5 10 15 Ile Ile Phe Leu Ala Phe Val Cys Val Thr Cys Ala Asn Tyr Asp Glu 20 25 30 Gly Ser Glu Pro Arg Val Pro Gly Gln Arg Glu Arg Gly Arg Gln Glu 35 40 45 Gly Glu Lys Glu Glu Gln Ser Arg Glu Arg His Pro Gln Arg Glu Pro 50 55 60 Ser Arg Glu Lys Glu Glu Asp Glu Glu Glu Lys Gln Lys Tyr Asp Glu 65 70 75 80 Gly Thr Glu Pro Arg Val Pro Gly Gln Arg Glu Arg Gly Arg Gln Glu 85 90 95 Gly Glu Lys Glu Glu Gln Arg Arg Glu Arg His Pro Gly Gln Arg Glu 100 105 110 Pro Ser Gln Glu Glu Asp Glu Glu Arg Glu Glu Ser Asp Arg Arg Gln 115 120 125 Glu Gly Ser Ser Lys Ser Glu Glu Gln Arg Asn Pro Phe Leu Phe Lys 130 135 140 Ser Asn Lys Phe Leu Thr Leu Phe Gln Asn Gly Asn Gly His Ile Arg 145 150 155 160 Leu Leu Gln Arg Phe Asp Lys Arg Ser Asp Leu Phe Glu Asn Leu Gln 165 170 175 Asn Tyr Arg Leu Leu Glu Tyr Arg Ala Lys Pro His Thr Ile Phe Leu 180 185 190 Pro Gln His Ile Asp Ala Asp Leu Ile Leu Val Val Leu Ser Gly Arg 195 200 205 Ala Ile Leu Thr Val Leu Ser Pro Asp Asp Arg Asn Ser Tyr Asn Leu 210 215 220 Glu Arg Gly Asp Thr Ile Lys Leu Pro Ala Gly Thr Thr Ser Tyr Pro 225 230 235 240 Leu Asn Gln Asp Asp Glu Glu Asp Leu Arg Val Val Asp Leu Ala Ile 245 250 255 Ser Val Asn Arg Pro Gly Lys Val Glu Ser Phe Asn Leu Ser Gly Asn 260 265 270 Lys Asn Gln Tyr Leu Arg Gly Phe Ser Glu Asn Ile Leu Glu Ala Ser 275 280 285 Phe Asn Thr Lys Tyr Glu Thr Ile Glu Lys Val Leu Leu Glu Glu Gln 290 295 300 Asp Lys Glu Ser Gln Gln Pro Arg Gly Gln Arg Leu Gln Arg Gln Glu 305 310 315 320 Thr Asn Ala Leu Val Lys Val Ser Arg Glu Gln Val Glu Glu Leu Lys 325 330 335 Arg Leu Ala Arg Thr Ser Ser Lys Lys Gly Val Ser Ser Glu Phe Glu 340 345 350 Pro Phe Asn Leu Arg Ser His Gly Pro Lys Tyr Ser Asn Lys Phe Gly 355 360 365 Lys Phe Phe Glu Ile Thr Pro Glu Lys Lys Tyr Pro Gln Leu Gln Asp 370 375 380 Leu Asp Ile Ser Val Ser Ser Val Glu Ile Asn Glu Gly Ala Leu Phe 385 390 395 400 Leu Pro His Tyr Asn Ser Arg Ala Ile Val Val Val Leu Val Asp Glu 405 410 415 Gly Lys Gly Asn Leu Glu Leu Val Gly Phe Lys Asn Glu Gln Gln Glu 420 425 430 Gln Arg Glu Lys Glu Asp Glu Gln Glu Glu Arg Asn Lys Gln Val Gln 435 440 445 Arg Tyr Glu Ala Lys Leu Ser Pro Gly Asp Val Val Ile Ile Pro Ala 450 455 460 Gly His Pro Val Ala Val Ser Ala Ser Ser Asn Leu Asn Leu Leu Gly 465 470 475 480 Phe Gly Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Thr Gly Ser 485 490 495 Asp Asp Asn <210> 236 <211> 515 <212> PRT <213> Yellow pea <400> 236 Met Ala Thr Thr Ile Lys Leu Arg Phe Pro Leu Leu Leu Leu Leu Gly 1 5 10 15 Val Ile Leu Leu Ala Ser Val Cys Val Thr Cys Ala Asn Tyr Asp Glu 20 25 30 Gly Ser Glu Pro Arg Val Pro Gly Arg Pro Glu Gly Glu Lys Glu Glu 35 40 45 Lys His Arg Gly Lys Leu Arg Pro Ser Tyr Glu Lys Glu Glu Asp Glu 50 55 60 Gly Glu Lys Gln Arg Tyr His Tyr Glu Lys Lys Glu Gln Lys Glu Ala 65 70 75 80 Gln Pro Arg Arg Glu Lys Lys Glu Gln Lys Glu Glu Glu Lys Gln Val 85 90 95 Glu Glu Glu Ser Arg Glu Ser Gln Arg Tyr Glu Asp Pro Gly Glu Arg 100 105 110 Ala Arg Glu Arg Tyr Arg Ala Glu Ile Ile Lys Arg Gln Val Glu Lys 115 120 125 Glu Arg Glu Glu Arg Asp Arg Arg His Gln Arg Glu Gly Glu Glu Glu 130 135 140 Glu Gly Ser Ser Lys Ser Arg Asn Pro Phe Leu Phe Lys Ser Asn Asn 145 150 155 160 Phe Leu Thr Leu Phe Glu Asn Glu Asn Gly His Ile Arg Leu Leu Gln 165 170 175 Arg Phe Asp Lys Arg Ser Asp Leu Phe Glu Asn Leu Gln Asn Tyr Arg 180 185 190 Leu Val Glu Tyr Arg Ala Lys Pro His Thr Ile Phe Leu Pro Gln His 195 200 205 Ile Asp Ala Asp Leu Ile Leu Val Val Leu Ser Gly Lys Ala Ile Leu 210 215 220 Thr Val Leu Ser Pro Asn Asn Arg Asn Ser Tyr Asn Leu Lys Arg Gly 225 230 235 240 Asp Thr Ile Lys Leu Pro Ala Gly Thr Thr Ser Tyr Leu Leu Asn Ser 245 250 255 Asp Asp Glu Glu Asp Leu Arg Met Val Asp Leu Ala Ile Ser Val Asn 260 265 270 Arg Pro Gly Lys Val Glu Ser Phe Asn Leu Ser Gly Asn Lys Asn Gln 275 280 285 Tyr Leu Arg Gly Phe Ser Lys Asn Ile Leu Glu Ala Ser Phe Asn Thr 290 295 300 Lys Tyr Glu Thr Ile Glu Lys Val Leu Leu Glu Glu Gln Asp Lys Glu 305 310 315 320 Ser Gln Gln Ser Ile Gly Gln Lys Arg Ile Ser Gln Arg Gln Glu Thr 325 330 335 Asn Ala Leu Val Lys Val Ser Arg Glu Gln Ile Glu Glu Pro Lys Arg 340 345 350 Leu Ala Arg Ser Ser Ser Arg Lys Gly Val Ser Ser Glu Phe Glu Pro 355 360 365 Ile Asn Leu Arg Ser Gln Arg Pro Lys Tyr Ser Asn Lys Phe Gly Lys 370 375 380 Phe Tyr Glu Ile Ser Pro Glu Lys Lys Tyr Pro Gln Leu Gln Asp Leu 385 390 395 400 Asp Val Ser Val Ser Ser Val Glu Ile Asn Glu Gly Ala Leu Leu Leu 405 410 415 Pro His Tyr Asn Ser Arg Ala Ile Val Thr Val Leu Val Asn Glu Gly 420 425 430 Lys Gly Asn Leu Glu Leu Ile Gly Phe Gln Asn Glu Gln Gln Gly Gln 435 440 445 Arg Glu Lys Glu Asp Glu Gln Gln His Glu Arg Asn Lys Gln Val Gln 450 455 460 Arg Tyr Asp Ala Arg Leu Ser Ser Gly Asp Val Val Ile Ile Pro Ala 465 470 475 480 Gly His Pro Val Ala Val Ser Ala Ser Ser Asn Leu Asp Leu Leu Gly 485 490 495 Phe Gly Ile Asn Ala Glu Asn Ser Gln Arg Asn Phe Leu Thr Gly Ser 500 505 510 Asp Asp Asn 515 <210> 237 <211> 494 <212> PRT <213> Oryza brachyantha <400> 237 Met Ala Thr Thr Thr Phe Ser Arg Phe Ser Ile Tyr Phe Cys Val Leu 1 5 10 15 Leu Leu Cys His Gly Ser Met Ala Gln Leu Phe Ser Pro Thr Leu Asn 20 25 30 Pro Trp His Ser Ser Arg Arg Gly Gly Ser Arg Asp Cys Arg Phe Asp 35 40 45 Arg Leu Gln Ala Phe Glu Pro Leu Arg Arg Val Arg Ser Glu Ala Gly 50 55 60 Val Thr Glu Tyr Phe Asp Glu Arg Asn Glu Gln Phe Gln Cys Thr Gly 65 70 75 80 Thr Phe Val Ile Arg Arg Val Ile Glu Pro Gln Gly Leu Leu Val Pro 85 90 95 Arg Tyr Thr Asn Thr Pro Gly Val Val Tyr Ile Met Gln Gly Arg Gly 100 105 110 Ser Met Gly Leu Thr Phe Pro Gly Cys Pro Ala Thr Tyr Gln Gln Gln 115 120 125 Phe Gln Gln Phe Leu Pro Glu Gly Gln Ser Gln Ser Gln Lys Phe Arg 130 135 140 Asp Glu His Gln Lys Ile His Gln Phe Arg Gln Gly Asp Ile Val Ala 145 150 155 160 Leu Pro Ala Gly Val Ala His Trp Phe Tyr Asn Glu Gly Asp Thr Pro 165 170 175 Val Val Ala Leu Tyr Val Phe Asp Ile Asn Asn Ser Ala Asn Gln Leu 180 185 190 Glu Pro Arg Gln Lys Asp Phe Leu Leu Ala Gly Asn Asn Asn Arg Glu 195 200 205 Gln Gln Val Tyr Gly Arg Ser Ile Glu Lys His Ser Gly Gln Asn Ile 210 215 220 Phe Ser Gly Phe Asn His Glu Leu Leu Ser Glu Ala Leu Gly Ile Ser 225 230 235 240 Thr Leu Ala Ala Lys Arg Leu Gln Gly Gln Asn Asp His Arg Gly Glu 245 250 255 Ile Ile Arg Val Arg Asn Gly Leu Gln Leu Leu Lys Pro Thr Phe Thr 260 265 270 Gln Gln Gln Glu Gln Ala Gln Ser Gln Tyr Gln Val Gln Tyr Ser Glu 275 280 285 Lys Gln Gln Glu Ser Thr Arg Cys Asn Gly Leu Asp Glu Asn Phe Cys 290 295 300 Thr Ile Asn Ala Arg Leu Asn Ile Glu Asn Pro Ser Arg Ala Asp Thr 305 310 315 320 Tyr Asn Pro Arg Ala Gly Arg Ile Thr His Leu Asn Asn Gln Lys Phe 325 330 335 Pro Ile Leu Asn Leu Val Gln Met Ser Ala Thr Arg Val Asn Leu Tyr 340 345 350 Gln Asn Ala Ile Leu Ser Pro Tyr Trp Asn Val Asn Ala His Ser Leu 355 360 365 Val Tyr Met Val Gln Gly His Ala Arg Val Gln Val Val Ser Asn Leu 370 375 380 Gly Lys Thr Val Phe Asn Ser Val Leu Arg Pro Gly Gln Leu Leu Ile 385 390 395 400 Ile Pro Gln His Tyr Val Val Leu Lys Lys Ala Glu Arg Glu Gly Cys 405 410 415 Gln Tyr Ile Ala Phe Lys Thr Asn Ala Asn Ser Ile Val Ser Gln Leu 420 425 430 Ala Gly Lys Asn Ser Ile Leu Arg Ala Met Pro Val Asp Val Val Ala 435 440 445 Asn Ala Tyr Arg Ile Ser Arg Glu Gln Ala Arg Asp Leu Lys Asn Asn 450 455 460 Arg Gly Glu Glu Leu Gly Ala Phe Thr Pro Lys Phe Glu Gln Gln Ser 465 470 475 480 Tyr Pro Gly Leu Ser Asn Glu Ser Glu Ser Glu Ala Ser Glu 485 490 <210> 238 <211> 515 <212> PRT <213> Oat <400> 238 Met Ala Thr Thr Ser Phe Pro Ser Val Leu Phe Tyr Ser Cys Ile Phe 1 5 10 15 Leu Leu Tyr Asn Gly Ser Met Ala Gln Leu Phe Gly Gln Ser Phe Thr 20 25 30 Pro Trp Gln Ser Ser Arg Gln Gly Gly Leu Lys Gly Cys Lys Phe Asp 35 40 45 Arg Leu Gln Ala Phe Glu Pro Leu Arg Gln Val Arg Ser Gln Ala Gly 50 55 60 Val Thr Glu Tyr Phe Asp Glu Gln Asn Glu Gln Phe Arg Cys Thr Gly 65 70 75 80 Val Phe Val Ile Arg Arg Val Ile Glu Pro Gln Gly Leu Leu Leu Pro 85 90 95 Gln Tyr His Asn Ala Pro Gly Leu Val Tyr Ile Leu Gln Gly Arg Gly 100 105 110 Tyr Thr Gly Leu Thr Phe Pro Gly Cys Pro Ala Thr Phe Gln Gln Gln 115 120 125 Phe Gln Pro Phe Asp Gln Ala Gln Asp Gln Ser Gln Ser His Leu Lys 130 135 140 Asp Glu His Gln Arg Val His Arg Phe Lys Gln Gly Asp Val Ile Ala 145 150 155 160 Leu Pro Ala Gly Ile Val His Trp Gly Tyr Asn Asp Gly Asp Ala Pro 165 170 175 Val Val Ala Ile Tyr Val Phe Asp Val Asn Asn Asn Ala Asn Gln Leu 180 185 190 Glu Pro Arg Gln Lys Glu Phe Leu Leu Ala Gly Asn Asn Lys Glu Asp 195 200 205 Gln Gln Phe Gly Gln Asn Ile Phe Ser Gly Phe Asn Ile Gln Leu Leu 210 215 220 Ser Glu Ala Leu Gly Ile Ser Gln Gln Ala Ala Gln Arg Ile Gln Ser 225 230 235 240 Gln Lys Glu Gln Arg Gly Glu Ile Ile Arg Val Thr Gln Ala Leu Gln 245 250 255 Phe Leu Lys Pro Thr Met Ser Gln Gln Glu Leu Val Glu His Gln Ala 260 265 270 Tyr Gln Pro Ile Gln Ser Gln Glu Gly Gln Ser Thr Gln Tyr Gln Val 275 280 285 Gly Gln Ser Thr Gln Tyr Gln Glu Gly Gln Ser Thr Gln Tyr Gln Ala 290 295 300 Gly Gln Ser Gln Asp Arg Ser Phe Asn Gly Leu Glu Glu Asn Phe Cys 305 310 315 320 Ser Leu Glu Ala Arg Gln Asn Ile Gly Asn Pro Lys Arg Ala Asp Thr 325 330 335 His Asn Pro Arg Ala Gly Arg Ile Thr Arg Leu His Gly Gln Asn Phe 340 345 350 Pro Ile Leu Asn Leu Val Gln Met Ser Ala Thr Arg Val Asn Leu Tyr 355 360 365 Gln Asn Ala Ile Leu Ser Pro Phe Trp Asn Ile Asn Ala His Ser Val 370 375 380 Val Tyr Met Ile Gln Gly His Ala Gln Val Gln Val Val Asn Asn Asn 385 390 395 400 Gly Gln Thr Val Phe Asn Asp Arg Leu Arg Gln Gly Gln Leu Leu Ile 405 410 415 Val Pro Gln His Tyr Val Val Leu Lys Lys Ala Glu Arg Glu Gly Cys 420 425 430 Gln Tyr Ile Ser Phe Lys Thr Asn Pro Asn Ser Met Val Ser His Ile 435 440 445 Ala Gly Lys Ser Ser Ile Leu Arg Ala Leu Pro Val Asp Val Leu Ala 450 455 460 Asn Ala Tyr Arg Ile Ser Arg Gln Glu Ala Arg Asn Leu Lys Asn Asn 465 470 475 480 Arg Gly Gln Glu Ser Gly Val Phe Thr Pro Lys Phe Thr Gln Thr Ser 485 490 495 Phe Gln Pro Tyr Pro Glu Gly Glu Asp Glu Ser Ser Leu Thr Asn Lys 500 505 510 Ala Ser Glu 515 <210> 239 <211> 493 <212> PRT <213> Brachypodium distachyon <400> 239 Met Ala His Thr Ser Phe Ser Ser Val Leu Ser Tyr Phe Cys Ile Phe 1 5 10 15 Leu Leu Phe His Gly Ser Met Ala Gln Val Pro Gly Gln Gly Ser Thr 20 25 30 Trp Gln Ser Pro Arg Gln Gly Gly Ser Arg Glu Cys Ser Phe Asp Arg 35 40 45 Leu Gln Thr Ile Glu Pro Leu Thr Gln Val Arg Ser Gln Ala Gly Leu 50 55 60 Thr Glu Tyr Phe Asp Glu Gln Asn Glu Gln Phe Arg Cys Ala Gly Val 65 70 75 80 Ser Val Ile Arg Arg Val Ile Glu Pro Arg Gly Leu Leu Leu Pro Arg 85 90 95 Tyr His Asn Thr Pro Gly Leu Val Tyr Ile Leu Glu Gly Ser Gly Phe 100 105 110 Val Gly Leu Ala Phe Pro Gly Cys Pro Glu Thr Phe Leu Glu Gln Phe 115 120 125 Gln Gln Ser Arg Gln Thr Gln Ser Thr Leu Gly Gln Ser Gln Cys Gln 130 135 140 Ser Gln Ser Gln Lys Leu Gly Asp Val His Gln Arg Val His Gln Phe 145 150 155 160 Thr Gln Gly Asp Val Val Ala Leu Pro Ala Gly Val Ala His Trp Phe 165 170 175 Tyr Asn Gly Gly Asp Ala Pro Val Val Ala Val Tyr Val Phe Asp Val 180 185 190 Asn Asn Asn Ala Asn Gln Leu Glu Pro Arg Gln Lys Glu Phe Leu Leu 195 200 205 Ala Gly Asn Tyr Asn Gly Val Leu Gln Ser Gly Arg Asn Ile Leu Asn 210 215 220 Gly Leu Asn Ala Gln Leu Leu Ser Gln Ala Phe Gly Ile Asn Glu Gln 225 230 235 240 Thr Ser Arg Ile Ile Gln Asn Gln Asn Asp Gly Arg Gly Glu Ile Val 245 250 255 Arg Val Glu Tyr Gly Leu Gln Phe Leu Thr Pro Val Val Thr Gln Gln 260 265 270 Gln Gln Lys Gln Pro Phe Leu Pro Ile Glu Pro Gln Glu Gly Gln Ser 275 280 285 Ser Arg Asn Gly Leu Glu Glu Asn Phe Cys Ser Leu Glu Pro Arg Gln 290 295 300 Asn Ile Glu Asp Pro Asn Arg Ala Asp Thr Tyr Asn Pro Arg Ala Gly 305 310 315 320 Ser Ile Ala Arg Leu Asn Gly Gln Asn Phe Pro Ile Leu Asn Leu Val 325 330 335 Gln Met Ser Ala Thr Arg Val Asn Leu Gln Lys Asn Ala Ile Val Ser 340 345 350 Pro Phe Trp Asn Ile Asn Ala His Ser Val Val Tyr Val Ile Gln Gly 355 360 365 Gln Ala Ser Val Gln Val Val Asn Asn Gln Gly Arg Asn Val Phe Asn 370 375 380 Gly Leu Leu Arg Arg Gly Gln Leu Leu Ile Ile Pro Gln Asn Tyr Val 385 390 395 400 Val Leu Lys Lys Ala Glu Ser Glu Gly Tyr Gln Tyr Ile Ala Phe Lys 405 410 415 Thr Asn Ala Asn Ser Met Val Ser His Ile Ala Gly Lys Asn Ser Ile 420 425 430 Leu Arg Ala Leu Pro Val Asp Val Ile Ala Asn Ala Tyr Arg Ile Ser 435 440 445 Arg Gln Glu Ala Gln Asn Leu Lys Asn Asn Arg Gly Glu Glu Ile Gly 450 455 460 Val Leu Thr Pro Asn Phe Pro Gln Ser Ser Cys Gln Ser Tyr Pro Ile 465 470 475 480 Gly Asp Val Asp Ser Ser Ser Thr Pro Lys Ala Gln Glu 485 490 <210> 240 <211> 489 <212> PRT <213> Rice <400> 240 Methionine Alanine Glutamine Phenylalanine Serine Phenylalanine Glycine Glycine Serine Proline Leucine Glutamine Serine Proline Arginine Glycine 1 5 10 15 Phenylalanine Arginine Glycine Aspartic Acid Glutamine Aspartic Acid Serine Arginine Histidine Glutamine Cysteine Arginine Phenylalanine Glutamic Acid Histidine Leucine 20 25 30 Threonine Alanine Leucine Glutamic Acid Alanine Threonine Histidine Glutamine Glutamine Arginine Serine Glutamic Acid Alanine Glycine Phenylalanine Threonine 35 40 45 Glutamic Acid Tyrosine Tyrosine Asparagine Isoleucine Glutamic Acid Alanine Arginine Asparagine Glutamic Acid Phenylalanine Arginine Cysteine Alanine Glycine Valine 50 55 60 Serine Valine Arginine Arginine Leucine Valine Valine Glutamic Acid Serine Lysine Glycine Leucine Valine Leucine Proline Methionine 65 70 75 80 Tyrosine Alanine Asparagine Alanine Histidine Lysine Leucine Valine Tyrosine Isoleucine Valine Glutamine Glycine Arginine Glycine Valine 85 90 95 Phenylalanine Glycine Methionine Alanine Leucine Proline Glycine Cysteine Proline Glutamic Acid Threonine Phenylalanine Glutamine Serine Valine Arginine 100 105 110 Serine Proline Phenylalanine Glutamic Acid Glutamine Glutamic Acid Valine Alanine Threonine Alanine Glycine Glutamic Acid Alanine Glutamine Serine Serine 115 120 125 Isoleucine Glutamine Lysine Methionine Arginine Aspartic Acid Glutamic Acid Histidine Glutamine Glutamine Leucine Histidine Glutamine Phenylalanine Histidine Glutamine 130 135 140 Glycine Aspartic Acid Valine Isoleucine Alanine Valine Proline Alanine Glycine Valine Alanine Histidine Tryptophan Leucine Tyrosine Asparagine 145 150 155 160 Asn Gly Asp Ser Pro Val Val Ala Phe Thr Val Ile Asp Thr Ser Asn 165 170 175 Asn Ala Asn Gln Leu Asp Pro Lys Arg Arg Glu Phe Phe Leu Ala Gly 180 185 190 Lys Pro Arg Ser Ser Trp Gln Gln Gln Ser Tyr Ser Tyr Gln Thr Glu 195 200 205 Gln Leu Ser Arg Asn Gln Asn Ile Phe Ala Gly Phe Ser Pro Asp Leu 210 215 220 Leu Ser Glu Ala Leu Ser Val Ser Lys Gln Thr Val Leu Arg Leu Gln 225 230 235 240 Gly Leu Ser Asp Pro Arg Gly Ala Ile Ile Arg Val Glu Asn Gly Leu 245 250 255 Gln Ala Leu Gln Pro Ser Leu Gln Val Glu Pro Val Lys Glu Glu Gln 260 265 270 Thr Gln Ala Tyr Leu Pro Thr Lys Gln Leu Gln Pro Thr Trp Leu Arg 275 280 285 Ser Gly Gly Ala Cys Gly Gln Gln Asn Val Leu Asp Glu Ile Met Cys 290 295 300 Ala Phe Lys Leu Arg Lys Asn Ile Asp Asn Pro Gln Ser Ser Asp Ile 305 310 315 320 Phe Asn Pro His Gly Gly Arg Ile Thr Arg Ala Asn Ser Gln Asn Phe 325 330 335 Pro Ile Leu Asn Ile Ile Gln Met Ser Ala Thr Arg Ile Val Leu Gln 340 345 350 Asn Asn Ala Leu Leu Thr Pro His Trp Thr Val Asn Ala His Thr Val 355 360 365 Met Tyr Val Thr Ala Gly Gln Gly His Ile Gln Val Val Asp His Arg 370 375 380 Gly Arg Ser Val Phe Asp Gly Glu Leu His Gln Gln Gln Ile Leu Leu 385 390 395 400 Ile Pro Gln Asn Phe Ala Val Val Val Lys Ala Arg Arg Glu Gly Phe 405 410 415 Ala Trp Val Ser Phe Lys Thr Asn His Asn Ala Val Asp Ser Gln Ile 420 425 430 Ala Gly Lys Ala Ser Ile Leu Arg Ala Leu Pro Val Asp Val Val Ala 435 440 445 Asn Ala Tyr Arg Leu Ser Arg Glu Asp Ser Arg His Val Lys Phe Asn 450 455 460 Arg Gly Asp Glu Met Ala Val Phe Ala Pro Arg Arg Gly Pro Gln Gln 465 470 475 480 Tyr Ala Glu Trp Gln Ile Asn Glu Lys 485 <210> 241 <211> 489 <212> PRT <213> Rice <400> 241 Met Ala Gln Phe Ser Phe Gly Gly Ser Pro Leu Gln Ser Pro Arg Gly 1 5 10 15 Phe Arg Gly Asp Gln Asp Ser Arg His Gln Cys Arg Phe Glu His Leu 20 25 30 Thr Ala Leu Glu Ala Thr His Gln Gln Arg Ser Glu Ala Gly Phe Thr 35 40 45 Glu Tyr Tyr Asn Ile Glu Ala Arg Asn Glu Phe Arg Cys Ala Gly Val 50 55 60 Ser Val Arg Arg Leu Val Val Glu Ser Lys Gly Leu Val Leu Pro Met 65 70 75 80 Tyr Ala Asn Ala His Lys Leu Val Tyr Ile Val Gln Gly Arg Gly Val 85 90 95 Phe Gly Met Ala Leu Pro Gly Cys Pro Glu Thr Phe Gln Ser Val Arg 100 105 110 Ser Pro Phe Glu Gln Glu Val Ala Thr Ala Gly Glu Ala Gln Ser Ser 115 120 125 Met Gln Lys Met Arg Asp Glu His Gln Gln Leu His Gln Phe His Gln 130 135 140 Gly Asp Val Ile Ala Val Pro Ala Gly Val Ala His Trp Leu Tyr Asn 145 150 155 160 Asn Gly Asp Ser Pro Val Val Ala Phe Thr Val Ile Asp Thr Ser Asn 165 170 175 Asn Ala Asn Gln Leu Asp Pro Lys Arg Arg Glu Phe Phe Leu Ala Gly 180 185 190 Lys Pro Arg Ser Ser Trp Gln Gln Gln Ser Tyr Ser Tyr Gln Thr Glu 195 200 205 Gln Leu Ser Arg Asn Gln Asn Ile Phe Ala Gly Phe Asn Pro Asp Leu 210 215 220 Leu Ser Glu Ala Leu Ser Val Ser Lys Gln Thr Val Leu Arg Leu Gln 225 230 235 240 Gly Leu Ser Asp Pro Arg Gly Ala Ile Ile Arg Val Glu Asn Gly Leu 245 250 255 Gln Ala Leu Gln Pro Ser Leu Gln Val Glu Pro Val Lys Glu Glu Gln 260 265 270 Thr Gln Ala Tyr Leu Pro Thr Lys Gln Leu Gln Pro Thr Trp Ser Arg 275 280 285 Ser Gly Gly Ala Cys Gly Gln Gln Asn Gly Leu Asp Glu Ile Met Cys 290 295 300 Ala Phe Lys Leu Arg Lys Asn Ile Asp Asn Pro Gln Ser Ser Asp Ile 305 310 315 320 Phe Asn Pro His Gly Gly Arg Ile Thr Arg Ala Asn Ser Gln Asn Phe 325 330 335 Pro Ile Leu Asn Ile Ile Gln Met Ser Ala Thr Arg Ile Val Leu Gln 340 345 350 Asn Asn Ala Leu Leu Thr Pro His Trp Thr Val Asn Ala His Thr Val 355 360 365 Met Tyr Val Thr Ala Gly Gln Gly Arg Ile Gln Val Val Asp His Arg 370 375 380 Gly Arg Ser Val Phe Asp Gly Glu Leu His Gln Gln Gln Ile Leu Leu 385 390 395 400 Ile Pro Gln Asn Phe Ala Val Val Val Lys Ala Arg Arg Glu Gly Phe 405 410 415 Ala Trp Val Ser Phe Lys Thr Asn His Asn Ala Val Asp Ser Gln Ile 420 425 430 Ala Gly Lys Ala Ser Ile Leu Arg Ala Leu Pro Val Asp Val Val Ala 435 440 445 Asn Ala Tyr Arg Leu Ser Arg Glu Asp Ser Arg Arg Val Lys Phe Asn 450 455 460 Arg Gly Asp Glu Met Ala Val Phe Ala Pro Arg Arg Gly Pro Gln Gln 465 470 475 480 Tyr Ala Glu Trp Gln Ile Asn Glu Lys 485 <210> 242 <211> 504 <212> PRT <213> Oryza brachyantha <400> 242 Met Val Asp Met Ser Ile Val Val Pro Val Cys Leu Thr Ile Phe Leu 1 5 10 15 Leu Ser Gln Val Cys Ile Ala Gln Val Ser Phe Asp Gly Ser Pro Leu 20 25 30 Tyr Ser Ser Arg Gly Phe Arg Gly Gly Ser Ala Ser Gln Gln Gln Cys 35 40 45 Arg Phe Glu His Leu Ala Ala Leu Glu Val Thr His Gln Glu Lys Ser 50 55 60 Glu Ala Gly Ser Ile Glu Tyr Tyr Asn Thr Glu Ala Arg Asp Glu Phe 65 70 75 80 Arg Cys Ala Arg Val Ser Ala Arg Arg Leu Val Ile Glu Ser Arg Gly 85 90 95 Leu Val Leu Pro Val Tyr Ala Asn Ala His Lys Leu Leu Tyr Ile Val 100 105 110 Gln Gly Arg Gly Val Phe Gly Met Ala Leu Pro Gly Cys Pro Glu Thr 115 120 125 Phe Gln Ser Val Arg Ser Ala Phe Glu Met Ala Thr Gly Asp Ala Glu 130 135 140 Ser Ser Thr Arg Lys Leu Arg Asp Glu His Gln Lys Ile His Gln Phe 145 150 155 160 Arg Gln Gly Asp Val Ile Ala Val Pro Pro Gly Val Ala His Trp Leu 165 170 175 Tyr Asn Asn Gly Asp Ser Pro Val Val Ala Phe Ser Val Ile Asp Phe 180 185 190 Gly Asn Asn Ala Asn Gln Leu Asp Pro Lys Pro Arg Glu Phe Phe Leu 195 200 205 Ala Gly Lys Pro Trp Gly Trp Gln Gln Val Gln Tyr Ser Tyr Gln Ser 210 215 220 Glu Gln Gln Ser Lys His Gln Asn Ile Phe Ala Gly Phe Asn Pro Asp 225 230 235 240 Leu Leu Ala Glu Ala Leu Ser Val Ser Arg Gln Thr Ala Met Arg Leu 245 250 255 Gln Glu Leu Asn Asp Gln Arg Gly Ala Ile Ile Arg Val Glu Gln Gly 260 265 270 Leu Gln Leu Ala Leu Asp Pro Ser Phe Gln Ala Glu Gln Glu Gln Glu 275 280 285 Glu Gln Pro Gln Glu Tyr Leu Ser Ser Gln Gln Gln Gln Pro Thr Trp 290 295 300 Ser Gln Arg Ser Gly Ala Cys Val Gln Asn Asn Gly Leu Asp Glu Ile 305 310 315 320 Met Cys Ala Phe Lys Val Ser Lys Asn Ile Asn Ser Ala Gln Ser Thr 325 330 335 Asp Ile Phe Asn Pro Arg Gly Gly Arg Ile Thr Arg Ala Asn Ser Gln 340 345 350 Asn Phe Pro Val Leu Asn Ile Ile Gln Met Ser Ala Thr Arg Thr Val 355 360 365 Leu Gln Asn Asn Ala Leu Leu Thr Pro His Trp Thr Val Asn Ala His 370 375 380 Thr Val Met Tyr Val Thr Ala Gly Gln Gly Arg Ile Gln Val Val Asp 385 390 395 400 His Arg Gly Arg Thr Val Phe Asp Gly Glu Leu Arg Gln Gln Gln Ile 405 410 415 Leu Leu Ile Pro Gln Asn Phe Ala Val Ala Val Lys Ala Arg His Glu 420 425 430 Gly Phe Ser Trp Val Ser Phe Lys Thr Ser His Asn Ala Ile Asp Ser 435 440 445 Gln Ile Ala Gly Lys Gly Ser Ile Leu Arg Ala Leu Pro Val Asp Val 450 455 460 Leu Ala Lys Ala Tyr Met Leu Ser Arg Glu Glu Ser Arg Thr Leu Lys 465 470 475 480 Tyr Asn Arg Ala Asp Glu Thr Leu Val Phe Ala Pro Arg Pro Glu Ile 485 490 495 Gln Leu Tyr Ala Glu Ser Glu Lys 500 <210> 243 <211> 543 <212> PRT <213> Wild pea <400> 243 Met Ala Thr Thr Thr Lys Ser Arg Phe Pro Leu Leu Leu Leu Leu Gly 1 5 10 15 Ile Ile Phe Leu Ala Ser Val Val Cys Val Thr Tyr Ala Asn Tyr Asp 20 25 30 Glu Gly Ser Glu Pro Arg Val Pro Gly Arg Arg Glu Arg Gly Arg Gln 35 40 45 Glu Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Arg Pro Ser Tyr 50 55 60 Glu Lys Glu Glu Asp Glu Glu Glu Gly Gln Arg Glu Arg Gly Arg Gln 65 70 75 80 Glu Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Gly Pro Ser Tyr 85 90 95 Glu Lys Gln Glu Asp Glu Glu Glu Lys Gln Lys Tyr Arg Tyr Gln Arg 100 105 110 Glu Lys Glu Asp Glu Glu Glu Lys Gln Lys Tyr Arg Tyr Gln Arg Glu 115 120 125 Lys Lys Glu Gln Lys Glu Val Gln Pro Gly Arg Glu Arg Trp Glu Arg 130 135 140 Glu Glu Asp Glu Glu His Val Asp Glu Glu Trp Arg Gly Ser Gln Arg 145 150 155 160 His Glu Asp Pro Glu Glu Arg Ala Arg Leu Arg Tyr Arg Glu Glu Arg 165 170 175 Thr Lys Arg Asp Arg Arg His Gln Arg Glu Gly Glu Glu Glu Glu Arg 180 185 190 Ser Ser Glu Ser Gln Glu Arg Arg Asn Pro Phe Leu Phe Lys Ser Asn 195 200 205 Lys Phe Gln Thr Leu Phe Glu Asn Glu Asn Gly His Ile Arg Leu Leu 210 215 220 Gln Arg Phe Asp Lys Arg Ser Asp Leu Phe Glu Asn Leu Gln Asn Tyr 225 230 235 240 Arg Leu Val Glu Tyr Arg Ala Lys Pro His Thr Ile Phe Leu Pro Gln 245 250 255 His Ile Asp Ala Asp Leu Ile Leu Val Val Leu Ser Gly Lys Ala Ile 260 265 270 Leu Thr Val Leu Ser Pro Asn Ala Arg Asn Ser Tyr Asn Leu Glu Arg 275 280 285 Gly Asp Thr Ile Lys Leu Pro Ala Gly Thr Thr Ser Tyr Leu Val Asn 290 295 300 Gln Asp Asp Glu Glu Asp Leu Arg Leu Val Asp Leu Val Ile Pro Val 305 310 315 320 Asn Gly Pro Gly Lys Phe Glu Ala Phe Asp Leu Ser Lys Asn Lys Asn 325 330 335 Gln Tyr Leu Arg Gly Phe Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asn 340 345 350 Thr Lys Tyr Glu Thr Ile Glu Lys Val Leu Leu Glu Glu Gln Glu Lys 355 360 365 Thr Asp Ala Ile Val Lys Val Ser Arg Glu Gln Ile Glu Glu Leu Arg 370 375 380 Lys His Ala Lys Ser Ser Ser Lys Lys Ile Phe Pro Ser Glu Phe Glu 385 390 395 400 Pro Ile Asn Leu Arg Asn His Lys Pro Glu Tyr Ser Asn Lys Phe Gly 405 410 415 Lys Leu Phe Glu Ile Thr Pro Glu Lys Lys Tyr Pro Gln Leu Gln Asp 420 425 430 Leu Asp Ile Phe Val Ser Cys Val Glu Ile Asn Glu Gly Ala Leu Met 435 440 445 Leu Pro His Tyr Asn Ser Arg Ala Ile Val Val Leu Leu Val Asn Glu 450 455 460 Gly Lys Gly Asn Leu Glu Leu Leu Gly Leu Glu Asn Glu Gln Gln Glu 465 470 475 480 Arg Glu Asp Arg Lys Glu Arg Asn Asn Glu Val Gln Arg Tyr Glu Ala 485 490 495 Arg Leu Ser Pro Gly Asp Val Val Ile Ile Pro Ala Gly His Pro Val 500 505 510 Ala Ile Thr Ala Ser Ser Asn Leu Asn Leu Leu Ala Phe Gly Ile Asn 515 520 525 Ala Glu Asn Asn Gln Arg Asn Phe Leu Ser Gly Ser Asp Asp Asn 530 535 540 <210> 244 <211> 526 <212> PRT <213> Ethiopian pea <400> 244 Met Ala Thr Thr Val Glu Ser Arg Phe Pro Leu Leu Leu Phe Pro Gly 1 5 10 15 Ile Ile Phe Leu Ala Ser Val Cys Val Thr Tyr Ala Asn Tyr Asp Glu 20 25 30 Gly Ser Glu Thr Arg Val Pro Gly Gln Arg Glu Arg Gly Arg Gln Glu 35 40 45 Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Arg Pro Ser Tyr Glu 50 55 60 Lys Glu Glu Asp Glu Glu Glu Lys Gln Lys Tyr Arg Tyr Gln Arg Glu 65 70 75 80 Lys Glu Asp Glu Glu Glu Lys Gln Lys Tyr Arg Tyr Gln Arg Glu Lys 85 90 95 Lys Glu Glu Lys Glu Val Gln Pro Gly Arg Glu Arg Trp Glu Arg Glu 100 105 110 Glu Asp Glu Glu Gln Val Asp Glu Glu Trp Arg Gly Ser Gln Arg Arg 115 120 125 Gln Asp Pro Glu Glu Arg Ala Arg Leu Arg His Arg Glu Glu Arg Thr 130 135 140 Lys Arg Asp Arg Arg His Lys Arg Glu Gly Glu Glu Glu Glu Arg Ser 145 150 155 160 Ser Glu Ser Gln Glu Gln Arg Asn Pro Phe Leu Phe Lys Ser Asn Lys 165 170 175 Phe Leu Thr Leu Phe Glu Asn Glu Asn Gly His Ile Arg Arg Leu Gln 180 185 190 Arg Phe Asp Lys Arg Ser Asp Leu Phe Glu Asn Leu Gln Asn Tyr Arg 195 200 205 Leu Val Glu Tyr Arg Ala Lys Pro His Thr Ile Phe Leu Pro Gln His 210 215 220 Ile Asp Ala Asp Leu Ile Leu Val Val Leu Asn Gly Lys Ala Ile Leu 225 230 235 240 Thr Val Leu Ser Pro Asn Asp Arg Asn Ser Tyr Asn Leu Glu Arg Gly 245 250 255 Asp Thr Ile Lys Ile Pro Ala Gly Thr Thr Ser Tyr Leu Val Asn Gln 260 265 270 Asp Asp Glu Glu Asp Leu Arg Val Val Asp Phe Val Ile Pro Val Asn 275 280 285 Arg Pro Gly Lys Phe Glu Ala Phe Gly Leu Ser Glu Asn Lys Asn Gln 290 295 300 Tyr Leu Arg Gly Phe Ser Lys Asn Ile Leu Glu Ala Ser Leu Asn Thr 305 310 315 320 Lys Tyr Glu Thr Ile Glu Lys Val Leu Leu Glu Glu Gln Glu Lys Lys 325 330 335 Pro Gln Gln Leu Arg Asp Arg Lys Arg Arg Gln Gln Gly Gly Glu Arg 340 345 350 Asp Ala Ile Ile Lys Val Ser Arg Glu Gln Ile Glu Glu Leu Arg Lys 355 360 365 Leu Ala Lys Ser Ser Ser Lys Lys Ser Leu Pro Ser Glu Phe Glu Pro 370 375 380 Phe Asn Leu Arg Ser His Lys Pro Glu Tyr Ser Asn Lys Phe Gly Lys 385 390 395 400 Leu Phe Glu Ile Thr Pro Glu Lys Lys Tyr Pro Gln Leu Gln Asp Leu 405 410 415 Asp Ile Leu Val Ser Cys Val Glu Ile Asn Lys Gly Ala Leu Met Leu 420 425 430 Pro His Tyr Asn Ser Arg Ala Ile Val Val Leu Leu Val Asn Glu Gly 435 440 445 Lys Gly Asn Leu Glu Leu Leu Gly Leu Lys Asn Glu Gln Gln Glu Arg 450 455 460 Glu Asp Arg Lys Glu Arg Asn Asn Glu Val Gln Arg Tyr Glu Ala Arg 465 470 475 480 Leu Ser Pro Gly Asp Val Val Ile Ile Pro Ala Gly His Pro Val Ala 485 490 495 Ile Ser Ala Ser Ser Asn Leu Asn Leu Leu Gly Phe Gly Thr Asn Ala 500 505 510 Glu Asn Asn Gln Arg Asn Phe Leu Ser Gly Ser Asp Asp Asn 515 520 525 <210> 245 <211> 589 <212> PRT <213> Vicia villosa <400> 245 Met Ala Thr Thr Ile Lys Ser Arg Phe Pro Val Leu Leu Leu Leu Gly 1 5 10 15 Ile Ile Phe Leu Thr Ser Val Cys Val Thr Tyr Ala Asn Tyr Asp Glu 20 25 30 Gly Arg Glu Pro Ser Val Pro Gly Gln Arg Glu Arg Gly Arg Gln Glu 35 40 45 Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Arg Pro Ser Glu Glu 50 55 60 Asp Glu Glu Glu Lys Tyr Lys Tyr Glu Glu Gly Arg Val Pro Gly Gln 65 70 75 80 Arg Glu Arg Gly Arg Gln Glu Gly Glu Lys Glu Glu Lys Arg His Gly 85 90 95 Lys Trp Arg Pro Ser Glu Glu Glu Asp Glu Glu Glu Lys Tyr Arg Tyr 100 105 110 Glu Glu Gly Ser Glu Pro Arg Gly Pro Gly Gln Arg Glu Thr Gly Arg 115 120 125 Gln Glu Gly Glu Lys Glu Lys Gln Arg Pro Glu Arg Glu Pro Ser Tyr 130 135 140 Glu Lys Glu Glu Asp Glu Glu Glu Lys Gln Lys Tyr Gln Tyr His Arg 145 150 155 160 Glu Lys Lys Glu Gln Arg Glu Val Arg Pro Gly Arg Glu Arg Phe Glu 165 170 175 Arg His Glu Asp Glu Glu Gln Trp Arg Gly Ile Gln Arg His Glu Asp 180 185 190 Pro Glu Glu Arg Ala Arg Glu Arg Tyr Arg Ala Glu Ile Ala Lys Arg 195 200 205 Gln Val Glu Glu Glu Arg Glu Glu Arg Asp Ile Pro His Glu Arg Glu 210 215 220 Gln Arg Asn Pro Phe Leu Phe Lys Ser Asn Lys Phe Gln Thr Leu Phe 225 230 235 240 Gln Asn Glu Asn Gly Tyr Ile Arg Arg Leu Gln Arg Phe Asp Lys Arg 245 250 255 Ser Asp Leu Phe Glu Asn Leu Gln Asn Tyr Arg Leu Val Glu Tyr Arg 260 265 270 Ala Lys Pro His Thr Ile Phe Leu Pro Gln His Ile Asp Ala Asp Leu 275 280 285 Ile Ile Val Val Leu Ser Gly Arg Ala Ile Leu Thr Val Leu Ser Pro 290 295 300 Asp Asp Arg Asn Ser Tyr Asn Leu Glu Arg Gly Asp Thr Ile Lys Leu 305 310 315 320 Pro Ala Gly Thr Thr Ser Tyr Leu Val Asn Gln Asp Asp Glu Glu Asp 325 330 335 Leu Arg Val Val Asp Leu Ala Ile Pro Val Asn Arg Pro Gly Lys Val 340 345 350 Glu Ser Phe Leu Leu Ser Gly Asn Lys Asn Gln Tyr Leu Arg Gly Phe 355 360 365 Ser Lys Asn Ile Leu Glu Ala Ser Phe Asn Thr Asn Tyr Glu Thr Ile 370 375 380 Glu Arg Val Leu Leu Glu Glu Gln Asp Lys Glu Ser Gln Gln Ser Ile 385 390 395 400 Gly Gln Lys Arg Arg Ser Gln Arg Gln Glu Thr Asn Ala Leu Val Lys 405 410 415 Val Ser Arg Glu Gln Leu Glu Asp Leu Lys Arg Leu Ala Lys Ser Ser 420 425 430 Ser Gln Glu Gly Leu Ser Ser Gln Phe Glu Pro Ile Asn Leu Arg Ser 435 440 445 Gln Asn Pro Lys Tyr Ser Asn Lys Phe Gly Lys Val Phe Glu Ile Thr 450 455 460 Pro Glu Lys Lys Tyr Pro Gln Leu Gln Asp Leu Asp Leu Phe Val Ser 465 470 475 480 Ser Val Asp Ile Lys Glu Gly Ala Leu Met Leu Pro His Tyr Asn Ser 485 490 495 Arg Ala Ile Val Val Leu Leu Val Asn Glu Gly Arg Gly Asn Leu Glu 500 505 510 Leu Val Gly Leu Lys Asn Glu Gln Gln Glu Gln Arg Glu Lys Glu Asp 515 520 525 Glu Gln Gln Glu Arg Asn Asn Gln Val Gln Arg Tyr Glu Ala Arg Leu 530 535 540 Ser Pro Gly Asp Val Val Ile Ile Pro Ala Gly His Pro Val Ala Val 545 550 555 560 Arg Ala Ser Ser Asp Leu Asn Leu Leu Ala Phe Gly Ile Asn Ala Glu 565 570 575 Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser Asp Asp Asn 580 585 <210> 246 <211> 576 <212> PRT <213> Lathyrus hirsutus <400> 246 Met Ala Ile Ile Ile Lys Ser Arg Phe Pro Leu Leu Leu Leu Leu Gly 1 5 10 15 Ile Ile Phe Leu Ala Ser Val Cys Ala Thr Trp Ala Asn Tyr Asp Glu 20 25 30 Gly Ser Glu Pro Arg Val Pro Gly Gln Arg Glu Arg Gly Arg Gln Glu 35 40 45 Gly Glu Lys Ala Glu Lys Ser His Glu Lys Trp Arg Pro Ser Tyr Glu 50 55 60 Glu Glu Tyr Asp Glu Gly Ser Glu Pro Arg Val Pro Gly Lys Arg Glu 65 70 75 80 Arg Gly Arg Gln Glu Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp 85 90 95 Arg Pro Ser His Glu Glu Glu Tyr Asp Glu Gly Ser Glu Pro Arg Val 100 105 110 Pro Thr His Gly Glu Arg Gly Arg Gln Glu Gly Glu Lys Glu Glu Lys 115 120 125 Arg His Glu Glu Trp Arg Pro Ser Tyr Glu Lys Glu Glu Asp Glu Glu 130 135 140 Glu Lys Glu Lys Tyr Lys Tyr Gln Arg Glu Lys Lys Glu Gln Lys Glu 145 150 155 160 Val Gln Pro Gly Arg Glu Lys Trp Glu Arg Lys Gln Asp Glu Lys His 165 170 175 Val Glu Glu Asp Glu Asp Gln Glu Glu Glu Gln Trp Arg Gly Ser Lys 180 185 190 Arg Arg Glu Asp Pro Glu Glu Arg Ala Arg Leu Arg Tyr Arg Glu Glu 195 200 205 Arg Thr Lys Ser Asn Val Glu Glu Glu Thr Glu Glu Arg Arg Asn Pro 210 215 220 Phe Leu Phe Lys Ser Asn Lys Phe Leu Thr Leu Phe Glu Asn Glu Asn 225 230 235 240 Gly His Ile Arg Arg Leu Gln Arg Phe Asp Glu Arg Ser Asp Ile Phe 245 250 255 Glu Asn Leu Gln Asn Tyr Arg Leu Val Glu Tyr Lys Ala Lys Pro His 260 265 270 Thr Met Phe Leu Pro Gln His Ile Asp Ala Asp Leu Ile Ile Val Val 275 280 285 Leu Asn Gly Lys Ala Ile Leu Thr Val Leu Ser Pro Asn Asp Arg Asn 290 295 300 Ser Tyr Asn Leu Glu Arg Gly Asp Thr Ile Lys Leu Pro Ala Gly Thr 305 310 315 320 Thr Ser Tyr Leu Val Asn Gln Asp Asp Glu Glu Asp Leu Arg Val Val 325 330 335 Asp Leu Ala Ile Pro Val Asn Arg Pro Gly Lys Phe Glu Ala Phe Gly 340 345 350 Leu Ser Ala Asn Lys Asn Gln Tyr Leu Arg Gly Phe Ser Lys Asn Ile 355 360 365 Leu Glu Ala Phe Leu Asn Thr Lys Tyr Glu Thr Ile Glu Lys Val Leu 370 375 380 Leu Glu Glu Gln Glu Arg Arg Asp Arg Lys Gly Arg Gln Gln Gly Gln 385 390 395 400 Glu Thr Asn Ala Ile Val Lys Val Ser Arg Glu Gln Ile Glu Glu Leu 405 410 415 Arg Lys Leu Ala Lys Ser Ser Ser Lys Lys Ser Leu Leu Ser Glu Ser 420 425 430 Glu Pro Ile Asn Leu Arg Ser Gln Asn Pro Lys Tyr Ser Asn Lys Phe 435 440 445 Gly Lys Leu Phe Glu Ile Thr Pro Glu Lys Lys Tyr Pro Gln Leu Gln 450 455 460 Asp Leu Asp Val Ser Ile Ser Cys Val Glu Ile Asn Glu Gly Ala Pro 465 470 475 480 Leu Leu Pro His Tyr Asn Ser Arg Ala Ile Val Leu Leu Leu Val Asn 485 490 495 Glu Gly Lys Gly Asn Leu Glu Leu Val Gly Phe Lys Asn Glu Gln Gln 500 505 510 Arg Gln Arg Glu Asn Glu Glu Arg Asn Lys Lys Val Gln Arg Tyr Glu 515 520 525 Ala Arg Leu Ser Pro Gly Asp Val Val Val Ile Pro Ala Gly His Pro 530 535 540 Val Ala Ile Ser Ala Ser Leu Asn Leu Asn Leu Val Gly Phe Gly Val 545 550 555 560 Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Thr Gly Ser Asp Asp Asn 565 570 575 <210> 247 <211> 564 <212> PRT <213> Lathyrus cicera <400> 247 Met Ala Thr Ile Ile Lys Ser Arg Phe Pro Leu Leu Leu Leu Leu Gly 1 5 10 15 Ile Ile Phe Leu Ala Ser Val Cys Val Thr Leu Ala Asn Tyr Asp Glu 20 25 30 Gly Ser Glu Pro Arg Val Pro Ala Gln Arg Glu Arg Gly Arg Gln Glu 35 40 45 Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Arg Pro Ser His Glu 50 55 60 Lys Glu Tyr Asp Glu Gly Ser Glu Pro Arg Val Pro Gly Arg Arg Glu 65 70 75 80 Arg Gly Arg Gln Glu Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp 85 90 95 Arg Pro Ser Tyr Glu Lys Glu Tyr Asp Glu Gly Ser Glu Pro Arg Val 100 105 110 Pro Gly Arg Arg Glu Arg Gly Arg Gln Glu Gly Glu Lys Glu Glu Lys 115 120 125 Arg His Gly Glu Trp Arg Pro Ser Tyr Glu Lys Glu Tyr Asp Glu Glu 130 135 140 Glu Lys Gln Lys Tyr Gln Tyr Glu Arg Glu Lys Glu Glu Gln Lys Glu 145 150 155 160 Val Gln Pro Gly Arg Glu Arg Trp Glu Arg Lys Glu Asp Glu Glu Lys 165 170 175 Glu Glu Asp Gln Trp Arg Gly Ser Gln Arg His Glu Asp Pro Glu Glu 180 185 190 Arg Ala Arg Leu Arg Tyr Arg Lys Glu Arg Thr Lys Lys Tyr Val Glu 195 200 205 Glu Asp Thr Glu Glu Thr Ser Ser Glu Ser Gln Gly Arg Arg Asn Pro 210 215 220 Phe Leu Phe Lys Ser Asn Lys Phe Leu Thr Leu Phe Glu Asn Glu Asn 225 230 235 240 Gly Tyr Ile Arg Arg Leu Gln Arg Phe Asp Glu Arg Ser Asp Ile Phe 245 250 255 Glu Asn Leu Gln Asn Tyr Arg Leu Val Glu Tyr Arg Ala Lys Pro His 260 265 270 Thr Ile Phe Leu Pro Gln His Ile Asp Ala Asp Leu Ile Leu Val Ile 275 280 285 Leu Asn Gly Lys Ala Ile Leu Thr Val Leu Ser Pro Asn Asp Arg Asn 290 295 300 Ser Tyr Asn Leu Glu Arg Gly Asp Thr Ile Lys Leu Pro Ala Gly Thr 305 310 315 320 Thr Ser Tyr Leu Val Asn Glu Asp Asp Glu Glu Asp Leu Arg Val Val 325 330 335 Asp Leu Val Ile Pro Val Asn Arg Pro Gly Lys Phe Glu Ala Phe Asp 340 345 350 Leu Asn Gln Tyr Leu Gly Gly Phe Ser Lys Ser Val Leu Glu Ala Ser 355 360 365 Leu Asn Thr Lys Tyr Glu Thr Ile Glu Lys Val Leu Leu Glu Glu Gln 370 375 380 Gln Lys Gln Gly Gln Glu Thr Asn Ala Ile Val Lys Val Ser Arg Glu 385 390 395 400 Gln Ile Glu Glu Leu Arg Lys Leu Ala Lys Ser Ser Ser Lys Lys Ser 405 410 415 Leu Leu Ser Glu Leu Glu Pro Val Asn Leu Arg Ser His Ser Pro Lys 420 425 430 Tyr Ser Asn Lys Phe Gly Lys Phe Phe Glu Ile Thr Pro Glu Lys Lys 435 440 445 Tyr Pro Gln Leu Gln Asp Leu Asp Val Ser Ile Ser Cys Val Glu Ile 450 455 460 Asn Glu Gly Ala Leu Leu Leu Pro His Tyr Asn Ser Arg Ala Ile Val 465 470 475 480 Val Val Leu Val Asn Glu Gly Lys Gly Asn Leu Glu Leu Leu Gly Val 485 490 495 Gln Asn Glu Asp Glu Gln Gln Glu Arg Lys Glu Arg Asn Lys Glu Val 500 505 510 Gln Arg Tyr Glu Ala Arg Leu Ser Pro Gly Asp Val Val Ile Ile Pro 515 520 525 Ser Gly His Pro Val Ala Val Ser Ala Ser Ser Asn Leu Asn Leu Leu 530 535 540 Gly Phe Gly Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ser Gly 545 550 555 560 Ser Asp Asp Asn <210> 248 <211> 527 <212> PRT <213> Lathyrus palustris <400> 248 Met Ala Thr Ile Ile Lys Ser Arg Phe Pro Leu Leu Leu Leu Leu Gly 1 5 10 15 Ile Ile Phe Leu Ala Ser Val Cys Val Thr Tyr Ala Asn Tyr Asp Glu 20 25 30 Gly Ser Glu Pro Arg Val Pro Ala Gln Arg Glu Arg Gly Arg Gln Glu 35 40 45 Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp Arg Pro Ser Ser Glu 50 55 60 Lys Glu Tyr Asp Glu Gly Ser Glu Pro Arg Val Pro Gly Arg Arg Glu 65 70 75 80 Arg Gly Arg Gln Glu Gly Glu Lys Glu Glu Lys Arg His Gly Glu Trp 85 90 95 Arg Pro Ser Tyr Glu Lys Glu Tyr Asp Glu Glu Glu Lys Gln Lys Tyr 100 105 110 Gln Tyr Glu Arg Glu Lys Lys Glu Gln Lys Glu Val Glu Pro Gly Arg 115 120 125 Glu Arg Trp Glu Arg Lys Glu Asp Glu Glu Lys Glu Glu Asp Gln Trp 130 135 140 Arg Gly Ser Gln Arg His Glu Asp Pro Glu Glu Arg Ala Arg Leu Arg 145 150 155 160 Tyr Arg Lys Glu Arg Thr Lys Lys Tyr Val Glu Glu Asp Thr Glu Glu 165 170 175 Thr Ser Ser Glu Ser Gln Gly Arg Arg Asn Pro Phe Leu Phe Lys Ser 180 185 190 Asn Lys Phe Leu Thr Leu Phe Glu Asn Glu Asn Gly Tyr Ile Arg Arg 195 200 205 Leu Gln Arg Phe Asp Glu Arg Ser Asp Leu Phe Glu Asn Leu Gln Asn 210 215 220 Tyr Arg Leu Val Glu Tyr Arg Ala Lys Pro His Thr Ile Phe Leu Pro 225 230 235 240 Gln His Ile Asp Ala Asp Leu Ile Leu Val Ile Leu Asn Gly Lys Ala 245 250 255 Ile Leu Thr Val Leu Ser Pro Asn Asp Arg Asn Ser Tyr Asn Leu Glu 260 265 270 Arg Gly Asp Thr Ile Lys Leu Pro Ala Gly Thr Thr Ser Tyr Leu Val 275 280 285 Asn Glu Asp Asp Glu Glu Asp Leu Arg Val Val Asp Leu Val Ile Pro 290 295 300 Val Asn Arg Pro Gly Lys Phe Glu Ala Phe Asp Leu Asn Gln Tyr Leu 305 310 315 320 Gly Gly Phe Ser Lys Ser Val Leu Lys Ala Ser Leu Asn Thr Lys Tyr 325 330 335 Glu Thr Ile Glu Lys Val Leu Leu Glu Glu Gln Gln Lys Gln Gly Gln 340 345 350 Glu Thr Asn Ala Ile Val Lys Val Ser Arg Glu Gln Ile Glu Glu Leu 355 360 365 Arg Lys Leu Ala Lys Ser Ser Ser Lys Lys Ser Leu Leu Ser Glu Leu 370 375 380 Glu Pro Val Asn Leu Arg Ser His Ser Pro Lys Tyr Ser Asn Lys Phe 385 390 395 400 Gly Lys Phe Phe Glu Ile Thr Pro Glu Lys Lys Tyr Pro Gln Leu Gln 405 410 415 Asp Leu Asp Val Ser Ile Ser Cys Val Glu Ile Asn Glu Gly Ala Leu 420 425 430 Leu Leu Pro His Tyr Asn Ser Arg Ala Ile Val Val Leu Leu Val Asn 435 440 445 Glu Gly Lys Gly Asn Leu Glu Leu Leu Gly Val Gln Asp Glu Asp Glu 450 455 460 Gln Gln Glu Arg Lys Lys Arg Asn Lys Glu Val Gln Arg Tyr Glu Ala 465 470 475 480 Arg Leu Ser Pro Ser Asp Val Val Ile Ile Pro Ala Gly His Pro Val 485 490 495 Ala Val Ser Ala Ser Ser Asn Leu Asn Leu Leu Gly Phe Gly Ile Asn 500 505 510 Ala Glu Asn Asn Glu Arg Asn Phe Leu Ser Gly Ser Asp Asp Asn 515 520 525 <210> 249 <211> 495 <212> PRT <213> Oryza brachyantha <400> 249 Met Ala Thr Thr Val Phe Ser Arg Phe Ser Thr Tyr Phe Cys Val Leu 1 5 10 15 Leu Leu Cys His Gly Ser Met Ala Gln Leu Phe Asn Pro Ser Thr Asn 20 25 30 Pro Trp His Asn Pro Arg Gln Gly Ser Ser Arg Glu Cys Arg Phe Asp 35 40 45 Arg Leu Gln Pro Phe Glu Pro Leu Arg Lys Val Arg Ser Glu Ala Gly 50 55 60 Val Thr Glu Tyr Phe Asp Glu Lys Asn Glu Leu Phe Gln Cys Thr Gly 65 70 75 80 Thr Phe Val Ile Arg Arg Val Ile Gln Pro Gln Gly Leu Leu Val Pro 85 90 95 Arg Tyr Thr Asn Ala Pro Gly Leu Val Tyr Ile Ile Gln Gly Arg Gly 100 105 110 Ser Ile Gly Leu Thr Phe Pro Gly Cys Pro Ala Thr Tyr Gln Gln Gln 115 120 125 Phe Gln Gln Phe Leu Pro Gln Glu Gln Ser Gln Ser Gln Lys Phe Arg 130 135 140 Asp Glu His Gln Lys Ile His Gln Phe Arg Gln Gly Asp Ile Val Ala 145 150 155 160 Leu Pro Ala Gly Val Ala His Trp Phe Tyr Asn Asp Gly Asp Ala Pro 165 170 175 Val Val Ala Val Tyr Val Tyr Asp Val Lys Asn Ser Ala Asn Gln Leu 180 185 190 Glu Pro Arg Gln Arg Glu Phe Leu Leu Gly Gly Asn Asn Met Arg Ala 195 200 205 Gln Gln Val Tyr Gly Ser Ser Ala Glu Gln His Ser Arg Gln Asn Ile 210 215 220 Phe Ser Gly Phe Gly Val Glu Ile Leu Ser Glu Ala Leu Gly Ile Ser 225 230 235 240 Thr Val Thr Thr Lys Arg Leu Gln Ser Gln Asn Asp Gln Arg Gly Glu 245 250 255 Ile Ile His Val Lys Asn Gly Leu Gln Phe Leu Lys Pro Thr Leu Thr 260 265 270 Gln Gln Gln Glu Gln Ala Gln Ala Gln Tyr Gln Glu Val Gln Tyr Ser 275 280 285 Glu Gln Gln Gln Thr Ser Ser Arg Trp Asn Gly Leu Asp Glu Asn Phe 290 295 300 Cys Thr Ile Lys Ala Arg Met Asn Ile Glu Asn Thr Ser Arg Ala Asp 305 310 315 320 Thr Tyr Asn Pro Arg Ala Gly Arg Thr Thr Ser Leu Asn Ser Gln Lys 325 330 335 Phe Pro Ile Leu Asn Leu Val Gln Met Ser Ala Thr Arg Val Asn Leu 340 345 350 Tyr Gln Asn Ala Ile Leu Ser Thr Phe Trp Asn Val Asn Ala His Ser 355 360 365 Leu Val Tyr Thr Ile Gln Gly Arg Ala Arg Val Gln Val Val Ser Asn 370 375 380 Phe Gly Lys Thr Val Phe Asp Gly Glu Leu Arg Pro Gly Gln Leu Leu 385 390 395 400 Ile Ile Pro Gln His Tyr Val Val Leu Lys Lys Ala Gln Arg Glu Gly 405 410 415 Phe Arg Tyr Ile Ala Ile Lys Thr Asn Ala Asn Ala Phe Val Ser Gln 420 425 430 Leu Val Gly Lys Asn Ser Val Phe Arg Ser Leu Pro Val Asp Val Ile 435 440 445 Ala Asn Val Tyr Arg Ile Ser Arg Glu Gln Ala Arg Ser Leu Lys Asn 450 455 460 Asn Arg Gly Glu Glu His Gly Ala Phe Ala Pro Arg Ser Gln Gln Gln 465 470 475 480 Ser Tyr Pro Gly Phe Ser Asn Gln Ser Glu Ser Glu Thr Ser Glu 485 490 495 <210> 250 <211> 494 <212> PRT <213> Oryza brachyantha <400> 250 Met Ala Thr Thr Thr Phe Ser Arg Phe Ser Ile Tyr Phe Cys Val Leu 1 5 10 15 Leu Leu Cys His Gly Ser Met Ala Gln Leu Phe Ser Pro Thr Leu Asn 20 25 30 Pro Trp His Ser Ser Arg Arg Gly Gly Ser Arg Asp Cys Arg Phe Asp 35 40 45 Arg Leu Gln Ala Phe Glu Pro Leu Arg Arg Val Arg Ser Glu Ala Gly 50 55 60 Val Thr Glu Tyr Phe Asp Glu Arg Asn Glu Gln Phe Gln Cys Thr Gly 65 70 75 80 Thr Phe Val Ile Arg Arg Val Ile Glu Pro Gln Gly Leu Leu Val Pro 85 90 95 Arg Tyr Thr Asn Thr Pro Gly Val Val Tyr Ile Met Gln Gly Arg Gly 100 105 110 Ser Met Gly Leu Thr Phe Pro Gly Cys Pro Ala Thr Tyr Gln Gln Gln 115 120 125 Phe Gln Gln Phe Leu Pro Glu Gly Gln Ser Gln Ser Gln Lys Phe Arg 130 135 140 Asp Glu His Gln Lys Ile His Gln Phe Arg Gln Gly Asp Ile Val Ala 145 150 155 160 Leu Pro Ala Gly Val Ala His Trp Phe Tyr Asn Glu Gly Asp Thr Pro 165 170 175 Val Val Ala Leu Tyr Val Phe Asp Ile Asn Asn Ser Ala Asn Gln Leu 180 185 190 Glu Pro Arg Gln Lys Asp Phe Leu Leu Ala Gly Asn Asn Asn Arg Glu 195 200 205 Gln Gln Val Tyr Gly Arg Ser Ile Glu Lys His Ser Gly Gln Asn Ile 210 215 220 Phe Ser Gly Phe Asn His Glu Leu Leu Ser Glu Ala Leu Gly Ile Ser 225 230 235 240 Thr Leu Ala Ala Lys Arg Leu Gln Gly Gln Asn Asp His Arg Gly Glu 245 250 255 Ile Ile Arg Val Arg Asn Gly Leu Gln Leu Leu Lys Pro Thr Phe Thr 260 265 270 Gln Gln Gln Glu Gln Ala Gln Ser Gln Tyr Gln Val Gln Tyr Ser Glu 275 280 285 Lys Gln Gln Glu Ser Thr Arg Cys Asn Gly Leu Asp Glu Asn Phe Cys 290 295 300 Thr Ile Asn Ala Arg Leu Asn Ile Glu Asn Pro Ser Arg Ala Asp Thr 305 310 315 320 Tyr Asn Pro Arg Ala Gly Arg Ile Thr His Leu Asn Asn Gln Lys Phe 325 330 335 Pro Ile Leu Asn Leu Val Gln Met Ser Ala Thr Arg Val Asn Leu Tyr 340 345 350 Gln Asn Ala Ile Leu Ser Pro Tyr Trp Asn Val Asn Ala His Ser Leu 355 360 365 Val Tyr Met Val Gln Gly His Ala Arg Val Gln Val Val Ser Asn Leu 370 375 380 Gly Lys Thr Val Phe Asn Ser Val Leu Arg Pro Gly Gln Leu Leu Ile 385 390 395 400 Ile Pro Gln His Tyr Val Val Leu Lys Lys Ala Glu Arg Glu Gly Cys 405 410 415 Gln Tyr Ile Ala Phe Lys Thr Asn Ala Asn Ser Ile Val Ser Gln Leu 420 425 430 Ala Gly Lys Asn Ser Ile Leu Arg Ala Met Pro Val Asp Val Val Ala 435 440 445 Asn Ala Tyr Arg Ile Ser Arg Glu Gln Ala Arg Asp Leu Lys Asn Asn 450 455 460 Arg Gly Glu Glu Leu Gly Ala Phe Thr Pro Lys Phe Glu Gln Gln Ser 465 470 475 480 Tyr Pro Gly Leu Ser Asn Glu Ser Glu Ser Glu Ala Ser Glu 485 490 <210> 251 <211> 500 <212> PRT <213> Wild rice <400> 251 Met Asn Met Ala Thr Ile Asn Gly Pro Thr Ile Phe Phe Thr Val Cys 1 5 10 15 Leu Phe Leu Leu Cys His Gly Ser Leu Ala Gln Leu Leu Gly Gln Ser 20 25 30 Thr Ser Gln Trp Gln Ser Ser His Arg Gly Ser Ser Arg Gln Cys Arg 35 40 45 Phe Asp Arg Leu Gln Ala Phe Glu Pro Val Arg Ser Val Arg Ser Gln 50 55 60 Ala Gly Thr Thr Glu Phe Phe Asp Ala Ser Asn Glu Leu Phe Gln Cys 65 70 75 80 Ala Gly Val Ser Ile Val Arg Arg Ile Ile Glu Pro Arg Gly Leu Leu 85 90 95 Leu Pro Gln Tyr Thr As...

Claims

1. A peptide consisting of SEQUENCE ID NO:

349.

2. The peptide according to claim 1, which is a modified peptide.

3. The peptide according to claim 2, which is chemically modified by side chain modification, incorporation of protecting groups, incorporation of unnatural amino acids and / or their derivatives during peptide synthesis, and use of crosslinking agents, and other methods of imposing conformational constraints on the peptide.

4. A conjugate comprising the peptide according to claim 1 conjugated, linked or fused to a binding partner.

5. The conjugate according to claim 4, wherein the binding partner is selected from polyethylene glycol polymers, molecular weight increasing compounds, lipophilic groups or antibody molecules.

6. A conjugate comprising the peptide according to claim 2 conjugated, linked or fused to a binding partner.

7. The conjugate according to claim 6, wherein the binding partner is selected from polyethylene glycol polymers, molecular weight increasing compounds, lipophilic groups or antibody molecules.

8. A composition comprising a peptide according to any one of claims 1 - 3, or a conjugate according to any one of claims 4 - 7.

9. The composition according to claim 8, wherein the composition is a powder.

10. The composition according to claim 8 or 9, which is a topical composition.

11. The topical composition according to claim 10, which is present in a formulation selected from anhydrous compositions, aqueous dispersions, oils, milks, lotions, cosmetics, liniments, soaps, powders, semi - solid formulations, serums, shampoos, conditioners, any rinses, talc, mousses, powder formulations, sprays, aerosols, solutions, suspensions, emulsions, syrups, elixirs, polysaccharide films, patches, bandages and adhesive systems.

12. The topical composition according to claim 11, wherein the semi - solid formulation is a paste.

13. The topical composition according to claim 11, which is present in the form of a personal care product formulation.

14. The topical composition according to claim 11, which is present in the form of a gel formulation.

15. The topical composition according to claim 11, which is present in the form of a formulation selected from creams, gel - creams, hydrogels, ointments, balms, foams and gel patches.

16. The topical composition according to claim 11, which is present in the form of a formulation selected from water - in - oil emulsions, oil - in - water emulsions, multiple emulsions, hydroalcoholic solutions and hydroglycolic solutions.

17. The topical composition according to claim 10, which comprises at least one cosmetically acceptable excipient.

18. The topical composition according to claim 17, wherein at least one cosmetically acceptable excipient is a diluent, carrier, binder, lubricant, suspending agent, coating agent, preservative, stabilizer, dye, carrier, solubilizer, base, emollient, emulsifier, fragrance, humectant and / or surfactant.

19. A personal care composition or a cosmetic composition comprising the composition according to any one of claims 8 - 18.

20. The personal care composition or cosmetic composition according to claim 19, which is a shampoo.

21. Use of a peptide according to any one of claims 1-3, a conjugate according to any one of claims 4-7, or a composition according to any one of claims 8-9 in the manufacture of a medicament for treating or preventing inflammation or an inflammatory disorder in a mammal.

22. Use according to claim 21, wherein the inflammatory disorder is selected from skin inflammatory disorders, arthritis inflammatory disorders, cardiovascular system inflammatory disorders, lung or airway inflammatory disorders, and intestinal inflammatory disorders.

23. Use of a peptide according to any one of claims 1-3, a conjugate according to any one of claims 4-7, or a composition according to any one of claims 8-9 in the manufacture of a medicament for maintaining intestinal health in a mammal.

Images