cupin family protein [Arabidopsis thaliana]
vicilin family protein( domain architecture ID 14388890)
vicilin family protein is a cupin domain-containing protein similar to 7S seed storage proteins, such as cupincin, beta-conglycinin, vicilin, provicilin, canavalin, convicilin, and conglutin beta, and Ara h 1, a major peanut allergen
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
cupin_7S_vicilin-like_N | cd02244 | 7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ... |
74-253 | 3.22e-67 | ||||
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal domains of plant 7S seed storage proteins such as vicilin, and includes beta-conglycinin, phaseolin, canavalin, conglutin-beta, a chromatin protein in Pisum sativum called P54, and a sucrose binding protein in soybean called SBP. These 7S globulins also include soybean allergen beta-conglycinin, peanut allergen conarachin (Ara h 1), walnut allergen Jug r 2, and lentil allergen Len c 1. Proteins in this family perform various functions, including a role in sucrose binding, desiccation, defense against microbes and oxidative stress. The vicilin peptides formed by trypsin or chymotrypsin digestion exhibit antihypertensive effects. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). Storage proteins are the cause of well-known allergic reactions to peanuts and cereals. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. : Pssm-ID: 380371 Cd Length: 178 Bit Score: 213.52 E-value: 3.22e-67
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cupin_7S_vicilin-like_C | cd02245 | 7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal ... |
285-457 | 4.92e-62 | ||||
7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal domain of plant 7S seed storage protein such as vicilin and includes beta-conglycinin, phaseolin, canavalin, conglutin-beta, a chromatin protein in Pisum sativum called P54, and a sucrose binding protein in soybean called SBP. These 7S globulins also include soybean allergen beta-conglycinin, peanut allergen conarachin (Ara h 1), walnut allergen Jug r 2 and lentil allergen Len c 1. Proteins in this family perform various functions, including a role in sucrose binding, desiccation, defense against microbes and oxidative stress. The vicilin peptides formed by trypsin or chymotrypsin digestion exhibit antihypertensive effects. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). Storage proteins are the cause of well-known allergic reactions to peanuts and cereals. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. : Pssm-ID: 380372 Cd Length: 166 Bit Score: 199.67 E-value: 4.92e-62
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Name | Accession | Description | Interval | E-value | ||||
cupin_7S_vicilin-like_N | cd02244 | 7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ... |
74-253 | 3.22e-67 | ||||
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal domains of plant 7S seed storage proteins such as vicilin, and includes beta-conglycinin, phaseolin, canavalin, conglutin-beta, a chromatin protein in Pisum sativum called P54, and a sucrose binding protein in soybean called SBP. These 7S globulins also include soybean allergen beta-conglycinin, peanut allergen conarachin (Ara h 1), walnut allergen Jug r 2, and lentil allergen Len c 1. Proteins in this family perform various functions, including a role in sucrose binding, desiccation, defense against microbes and oxidative stress. The vicilin peptides formed by trypsin or chymotrypsin digestion exhibit antihypertensive effects. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). Storage proteins are the cause of well-known allergic reactions to peanuts and cereals. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380371 Cd Length: 178 Bit Score: 213.52 E-value: 3.22e-67
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cupin_7S_vicilin-like_C | cd02245 | 7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal ... |
285-457 | 4.92e-62 | ||||
7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal domain of plant 7S seed storage protein such as vicilin and includes beta-conglycinin, phaseolin, canavalin, conglutin-beta, a chromatin protein in Pisum sativum called P54, and a sucrose binding protein in soybean called SBP. These 7S globulins also include soybean allergen beta-conglycinin, peanut allergen conarachin (Ara h 1), walnut allergen Jug r 2 and lentil allergen Len c 1. Proteins in this family perform various functions, including a role in sucrose binding, desiccation, defense against microbes and oxidative stress. The vicilin peptides formed by trypsin or chymotrypsin digestion exhibit antihypertensive effects. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). Storage proteins are the cause of well-known allergic reactions to peanuts and cereals. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380372 Cd Length: 166 Bit Score: 199.67 E-value: 4.92e-62
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Cupin_1 | smart00835 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
281-448 | 2.07e-35 | ||||
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant. Pssm-ID: 214845 [Multi-domain] Cd Length: 146 Bit Score: 128.94 E-value: 2.07e-35
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Cupin_1 | pfam00190 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
278-448 | 3.00e-22 | ||||
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant. Pssm-ID: 395138 Cd Length: 151 Bit Score: 92.78 E-value: 3.00e-22
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Cupin_1 | smart00835 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
75-222 | 3.42e-15 | ||||
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant. Pssm-ID: 214845 [Multi-domain] Cd Length: 146 Bit Score: 72.70 E-value: 3.42e-15
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ManC | COG0662 | Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism]; |
100-181 | 8.25e-07 | ||||
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 440426 [Multi-domain] Cd Length: 114 Bit Score: 47.83 E-value: 8.25e-07
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Cupin_1 | pfam00190 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
107-217 | 1.46e-06 | ||||
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant. Pssm-ID: 395138 Cd Length: 151 Bit Score: 47.71 E-value: 1.46e-06
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PLN00212 | PLN00212 | glutelin; Provisional |
109-238 | 1.60e-03 | ||||
glutelin; Provisional Pssm-ID: 215106 [Multi-domain] Cd Length: 493 Bit Score: 40.95 E-value: 1.60e-03
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Name | Accession | Description | Interval | E-value | ||||
cupin_7S_vicilin-like_N | cd02244 | 7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ... |
74-253 | 3.22e-67 | ||||
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal domains of plant 7S seed storage proteins such as vicilin, and includes beta-conglycinin, phaseolin, canavalin, conglutin-beta, a chromatin protein in Pisum sativum called P54, and a sucrose binding protein in soybean called SBP. These 7S globulins also include soybean allergen beta-conglycinin, peanut allergen conarachin (Ara h 1), walnut allergen Jug r 2, and lentil allergen Len c 1. Proteins in this family perform various functions, including a role in sucrose binding, desiccation, defense against microbes and oxidative stress. The vicilin peptides formed by trypsin or chymotrypsin digestion exhibit antihypertensive effects. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). Storage proteins are the cause of well-known allergic reactions to peanuts and cereals. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380371 Cd Length: 178 Bit Score: 213.52 E-value: 3.22e-67
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cupin_7S_vicilin-like_C | cd02245 | 7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal ... |
285-457 | 4.92e-62 | ||||
7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal domain of plant 7S seed storage protein such as vicilin and includes beta-conglycinin, phaseolin, canavalin, conglutin-beta, a chromatin protein in Pisum sativum called P54, and a sucrose binding protein in soybean called SBP. These 7S globulins also include soybean allergen beta-conglycinin, peanut allergen conarachin (Ara h 1), walnut allergen Jug r 2 and lentil allergen Len c 1. Proteins in this family perform various functions, including a role in sucrose binding, desiccation, defense against microbes and oxidative stress. The vicilin peptides formed by trypsin or chymotrypsin digestion exhibit antihypertensive effects. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). Storage proteins are the cause of well-known allergic reactions to peanuts and cereals. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380372 Cd Length: 166 Bit Score: 199.67 E-value: 4.92e-62
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Cupin_1 | smart00835 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
281-448 | 2.07e-35 | ||||
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant. Pssm-ID: 214845 [Multi-domain] Cd Length: 146 Bit Score: 128.94 E-value: 2.07e-35
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Cupin_1 | pfam00190 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
278-448 | 3.00e-22 | ||||
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant. Pssm-ID: 395138 Cd Length: 151 Bit Score: 92.78 E-value: 3.00e-22
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Cupin_1 | smart00835 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
75-222 | 3.42e-15 | ||||
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant. Pssm-ID: 214845 [Multi-domain] Cd Length: 146 Bit Score: 72.70 E-value: 3.42e-15
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cupin_11S_legumin_N | cd02242 | 11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ... |
110-238 | 3.46e-13 | ||||
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal domains of 11S legumin seed storage proteins that supply nutrition for seed germination, such as glycinin and legumin, including many common food allergens such as the peanut major allergen Ara h 3, almond allergen Pru du 6, Pecan allergen Car i 4, hazelnut nut allergen Cor a 9, Brazil nut allergen Ber e 2, cashew allergen Ana o 2, pistachio allergen Pis v 2/5, and walnut allergen Jug n/r 4. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). They are synthesized as propeptides in the endoplasmic reticulum and transported to the secretory vesicles as a homotrimer. The propeptides are processed as they are sorted in the secretory vesicles. The homotrimer binds another homotrimer to form a homohexamer with 32-point symmetry formed by a face-to-face stacking of the two trimers. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380369 Cd Length: 209 Bit Score: 68.38 E-value: 3.46e-13
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cupin_7S_11S_C | cd20285 | 7S and 11S seed storage globulin, C-terminal cupin domain; This family contains the C-terminal ... |
292-422 | 1.33e-12 | ||||
7S and 11S seed storage globulin, C-terminal cupin domain; This family contains the C-terminal cupin domains of 7S and 11S seed storage proteins. The 7S globulins include soybean allergen beta-conglycinin, peanut allergen conarachin (Ara h 1), walnut allergen Jug r 2, and lentil allergen Len c 1. Proteins in this family perform various functions, including a role in sucrose binding, desiccation, defense against microbes and oxidative stress. The 11S globulins include many common food allergens such as the peanut major allergen Ara h 3, almond allergen Pru du 6, pecan allergen Car i 4, hazelnut nut allergen Cor a 9, Brazil nut allergen Ber e 2, cashew allergen Ana o 2, pistachio allergen Pis v 2/5, and walnut allergen Jug n/r 4. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). Storage proteins are the cause of well-known allergic reactions to peanuts and cereals. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380420 Cd Length: 109 Bit Score: 64.17 E-value: 1.33e-12
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ManC | COG0662 | Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism]; |
100-181 | 8.25e-07 | ||||
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 440426 [Multi-domain] Cd Length: 114 Bit Score: 47.83 E-value: 8.25e-07
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Cupin_1 | pfam00190 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
107-217 | 1.46e-06 | ||||
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant. Pssm-ID: 395138 Cd Length: 151 Bit Score: 47.71 E-value: 1.46e-06
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OxdD | COG2140 | Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ... |
103-191 | 4.00e-06 | ||||
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis Pssm-ID: 441743 [Multi-domain] Cd Length: 115 Bit Score: 45.73 E-value: 4.00e-06
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cupin_PA3510-like | cd02225 | Pseudomonas aeruginosa PA3510 and related proteins, cupin domain; This family includes ... |
90-160 | 9.44e-06 | ||||
Pseudomonas aeruginosa PA3510 and related proteins, cupin domain; This family includes bacterial proteins homologous to PA3510, a Pseudomonas aeruginosa protein of unknown function with a beta-barrel fold that belongs to the cupin superfamily. Pssm-ID: 380354 Cd Length: 150 Bit Score: 45.34 E-value: 9.44e-06
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QdoI | COG1917 | Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
95-182 | 1.14e-05 | ||||
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 44.07 E-value: 1.14e-05
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cupin_MJ1618 | cd02214 | Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ... |
103-181 | 1.53e-05 | ||||
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. Pssm-ID: 380344 [Multi-domain] Cd Length: 100 Bit Score: 43.66 E-value: 1.53e-05
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cupin_RmlC-like | cd02208 | RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ... |
104-170 | 1.67e-05 | ||||
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation. Pssm-ID: 380338 [Multi-domain] Cd Length: 73 Bit Score: 42.86 E-value: 1.67e-05
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cupin_DddK | cd06988 | Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ... |
117-168 | 1.90e-05 | ||||
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380393 [Multi-domain] Cd Length: 76 Bit Score: 42.61 E-value: 1.90e-05
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cupin_yp_001338853-like | cd07008 | Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes ... |
109-179 | 9.74e-04 | ||||
Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes bacterial proteins homologous to Klebsiella pneumoniae yp_001338853.1, an uncharacterized conserved protein with double-stranded beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. Pssm-ID: 380411 [Multi-domain] Cd Length: 101 Bit Score: 38.39 E-value: 9.74e-04
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PLN00212 | PLN00212 | glutelin; Provisional |
109-238 | 1.60e-03 | ||||
glutelin; Provisional Pssm-ID: 215106 [Multi-domain] Cd Length: 493 Bit Score: 40.95 E-value: 1.60e-03
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Cupin_2 | pfam07883 | Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ... |
106-160 | 2.33e-03 | ||||
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). Pssm-ID: 462300 [Multi-domain] Cd Length: 71 Bit Score: 36.47 E-value: 2.33e-03
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EutQ | COG4766 | Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid ... |
108-183 | 2.94e-03 | ||||
Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid transport and metabolism]; Pssm-ID: 443798 Cd Length: 123 Bit Score: 37.66 E-value: 2.94e-03
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cupin_OxDC-like | cd20306 | Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ... |
61-220 | 4.88e-03 | ||||
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Pssm-ID: 380440 [Multi-domain] Cd Length: 151 Bit Score: 37.57 E-value: 4.88e-03
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cupin_Bh2720-like | cd02223 | Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ... |
119-187 | 6.71e-03 | ||||
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, archaeal, and eukaryotic proteins similar to Bh2720, a Bacillus halodurans protein of unknown function with a cupin beta-barrel fold. Pssm-ID: 380352 [Multi-domain] Cd Length: 98 Bit Score: 35.98 E-value: 6.71e-03
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cupin_YdbB-like | cd02226 | Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ... |
115-160 | 7.17e-03 | ||||
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. Pssm-ID: 380355 [Multi-domain] Cd Length: 94 Bit Score: 35.88 E-value: 7.17e-03
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Blast search parameters | ||||
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