cocosin 1 [Oryza sativa Japonica Group]
cupin domain-containing protein( domain architecture ID 1562428)
cupin domain-containing protein, part of a functionally diverse superfamily with the active site generally located at the center of a conserved domain forming a beta-barrel fold
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
cupin_RmlC-like super family | cl40423 | RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ... |
211-347 | 9.02e-34 | ||||
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. The actual alignment was detected with superfamily member cd02243: Pssm-ID: 477354 Cd Length: 155 Bit Score: 122.20 E-value: 9.02e-34
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cupin_RmlC-like super family | cl40423 | RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ... |
12-165 | 9.17e-34 | ||||
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. The actual alignment was detected with superfamily member cd02242: Pssm-ID: 477354 Cd Length: 209 Bit Score: 123.85 E-value: 9.17e-34
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Name | Accession | Description | Interval | E-value | ||||||
cupin_11S_legumin_C | cd02243 | 11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ... |
211-347 | 9.02e-34 | ||||||
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the C-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: 380370 Cd Length: 155 Bit Score: 122.20 E-value: 9.02e-34
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cupin_11S_legumin_N | cd02242 | 11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ... |
12-165 | 9.17e-34 | ||||||
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: 123.85 E-value: 9.17e-34
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Cupin_1 | smart00835 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
195-344 | 3.61e-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: 214845 [Multi-domain] Cd Length: 146 Bit Score: 90.80 E-value: 3.61e-22
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Cupin_1 | smart00835 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
7-158 | 4.98e-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: 71.16 E-value: 4.98e-15
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PLN00212 | PLN00212 | glutelin; Provisional |
40-347 | 4.53e-11 | ||||||
glutelin; Provisional Pssm-ID: 215106 [Multi-domain] Cd Length: 493 Bit Score: 63.68 E-value: 4.53e-11
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Cupin_1 | pfam00190 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
9-156 | 4.74e-11 | ||||||
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: 60.43 E-value: 4.74e-11
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Cupin_1 | pfam00190 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
198-344 | 5.08e-11 | ||||||
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: 60.04 E-value: 5.08e-11
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QdoI | COG1917 | Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
50-114 | 4.67e-05 | ||||||
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 41.76 E-value: 4.67e-05
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Name | Accession | Description | Interval | E-value | ||||||
cupin_11S_legumin_C | cd02243 | 11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ... |
211-347 | 9.02e-34 | ||||||
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the C-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: 380370 Cd Length: 155 Bit Score: 122.20 E-value: 9.02e-34
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cupin_11S_legumin_N | cd02242 | 11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ... |
12-165 | 9.17e-34 | ||||||
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: 123.85 E-value: 9.17e-34
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Cupin_1 | smart00835 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
195-344 | 3.61e-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: 214845 [Multi-domain] Cd Length: 146 Bit Score: 90.80 E-value: 3.61e-22
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Cupin_1 | smart00835 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
7-158 | 4.98e-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: 71.16 E-value: 4.98e-15
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PLN00212 | PLN00212 | glutelin; Provisional |
40-347 | 4.53e-11 | ||||||
glutelin; Provisional Pssm-ID: 215106 [Multi-domain] Cd Length: 493 Bit Score: 63.68 E-value: 4.53e-11
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Cupin_1 | pfam00190 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
9-156 | 4.74e-11 | ||||||
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: 60.43 E-value: 4.74e-11
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Cupin_1 | pfam00190 | Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ... |
198-344 | 5.08e-11 | ||||||
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: 60.04 E-value: 5.08e-11
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cupin_7S_vicilin-like_N | cd02244 | 7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ... |
38-149 | 2.94e-09 | ||||||
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: 55.59 E-value: 2.94e-09
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cupin_OxDC-like | cd20306 | Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ... |
9-147 | 5.30e-06 | ||||||
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: 45.66 E-value: 5.30e-06
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cupin_7S_vicilin-like_C | cd02245 | 7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal ... |
213-346 | 6.32e-06 | ||||||
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: 45.97 E-value: 6.32e-06
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QdoI | COG1917 | Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
50-114 | 4.67e-05 | ||||||
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 41.76 E-value: 4.67e-05
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cupin_RmlC-like | cd02208 | RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ... |
38-113 | 1.90e-03 | ||||||
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: 36.69 E-value: 1.90e-03
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cupin_OxDC-like | cd20306 | Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ... |
212-341 | 4.70e-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: 37.19 E-value: 4.70e-03
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Cupin_2 | pfam07883 | Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ... |
38-107 | 9.29e-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: 34.54 E-value: 9.29e-03
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Blast search parameters | ||||
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