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Conserved domains on  [gi|808182030|gb|AKD01704|]
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globulin-1, partial [Zea mays]

Protein Classification

cupin domain-containing protein( domain architecture ID 14388889)

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

Graphical summary

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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 ...
121-250 1.06e-59

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: 186.56  E-value: 1.06e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808182030 121 EQGSLWVLRPFDEVSRLLRGIRDYRVAVLEANPRSFVVPSHTDAHCICYVAEGEGVVTTIENGERRSYTIKQGHVFVAPA 200
Cdd:cd02244    5 EAGEIRVLERFDGRSRLLRGIENYRLAFITMEPNTLFLPHHLDADMVFYVHTGRGTITWVDEDKRESYNLERGDVYRIPA 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 808182030 201 GAVTYLANTDGRKKLVITKILHTIS--VPGEFQFFFGPGGRNPESFLSSFSK 250
Cdd:cd02244   85 GSTFYLVNTDENEKLRIIALFDPVNslTPGPFQSFFGAGGQNPESLLSGFSK 136
 
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 ...
121-250 1.06e-59

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: 186.56  E-value: 1.06e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808182030 121 EQGSLWVLRPFDEVSRLLRGIRDYRVAVLEANPRSFVVPSHTDAHCICYVAEGEGVVTTIENGERRSYTIKQGHVFVAPA 200
Cdd:cd02244    5 EAGEIRVLERFDGRSRLLRGIENYRLAFITMEPNTLFLPHHLDADMVFYVHTGRGTITWVDEDKRESYNLERGDVYRIPA 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 808182030 201 GAVTYLANTDGRKKLVITKILHTIS--VPGEFQFFFGPGGRNPESFLSSFSK 250
Cdd:cd02244   85 GSTFYLVNTDENEKLRIIALFDPVNslTPGPFQSFFGAGGQNPESLLSGFSK 136
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
136-250 1.22e-09

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: 55.36  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808182030   136 RLLRGIrDYRVAVLEANPRSFVVPS-HTDAHCICYVAEGEGVVTTI-ENGERR-SYTIKQGHVFVAPAGAVTYLANTdGR 212
Cdd:smart00835  23 PALNGL-GISAARVNLEPGGMLPPHyHPRATELLYVVRGEGRVGVVdPNGNKVyDARLREGDVFVVPQGHPHFQVNS-GD 100
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 808182030   213 KKLVItkILHTISVPGEFQFFFGpggrnPESFLSSFSK 250
Cdd:smart00835 101 ENLEF--VAFNTNDPNRRFFLAG-----RNSVLRGLPP 131
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
152-217 1.85e-04

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: 40.78  E-value: 1.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808182030  152 NPRSFVVPS-HTDAHCICYVAEGEG-VVTTIENGERRSY--TIKQGHVFVAPAGAVTYLANTDGRKKLVI 217
Cdd:pfam00190  41 APGGMNPPHwHPNATEILYVLQGRGrVGFVVPGNGNRVFhkVLREGDVFVVPQGLPHFQYNIGDEPAVAF 110
 
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 ...
121-250 1.06e-59

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: 186.56  E-value: 1.06e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808182030 121 EQGSLWVLRPFDEVSRLLRGIRDYRVAVLEANPRSFVVPSHTDAHCICYVAEGEGVVTTIENGERRSYTIKQGHVFVAPA 200
Cdd:cd02244    5 EAGEIRVLERFDGRSRLLRGIENYRLAFITMEPNTLFLPHHLDADMVFYVHTGRGTITWVDEDKRESYNLERGDVYRIPA 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 808182030 201 GAVTYLANTDGRKKLVITKILHTIS--VPGEFQFFFGPGGRNPESFLSSFSK 250
Cdd:cd02244   85 GSTFYLVNTDENEKLRIIALFDPVNslTPGPFQSFFGAGGQNPESLLSGFSK 136
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
136-250 1.22e-09

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: 55.36  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808182030   136 RLLRGIrDYRVAVLEANPRSFVVPS-HTDAHCICYVAEGEGVVTTI-ENGERR-SYTIKQGHVFVAPAGAVTYLANTdGR 212
Cdd:smart00835  23 PALNGL-GISAARVNLEPGGMLPPHyHPRATELLYVVRGEGRVGVVdPNGNKVyDARLREGDVFVVPQGHPHFQVNS-GD 100
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 808182030   213 KKLVItkILHTISVPGEFQFFFGpggrnPESFLSSFSK 250
Cdd:smart00835 101 ENLEF--VAFNTNDPNRRFFLAG-----RNSVLRGLPP 131
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
152-249 1.31e-08

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: 53.36  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808182030 152 NPRSFVVPSHTDAHCICYVAEGEGVV--------TTIENGERRS-------------YTIKQGHVFVAPAGAVTYLANtD 210
Cdd:cd02242   43 EPRGLLLPSYSNAPKLAYVLQGRGIVgvvfpgcpETFQSSQQSQgqgqrfrdqhqkvRRIRKGDVIAVPAGVVHWWYN-D 121
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808182030 211 GRKKLVITKILHTIS----VPGEFQFFF------------GPGGRNPESFLSSFS 249
Cdd:cd02242  122 GDSDLVIVFLGDTSNnanqLDGNFRRFFlagnpqqeqqgqGQEQSGGGNIFSGFS 176
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
161-209 5.23e-05

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: 42.19  E-value: 5.23e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 808182030 161 HTDAHCICYVAEGEGVVTTIEN-GERRSYTIKQGHVFVAPAGAVTYLANT 209
Cdd:cd20306   52 HPNANELGYVISGEARVSILDPtGSLDTFTVKPGQVVFIPQGWLHWIENV 101
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
152-217 1.85e-04

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: 40.78  E-value: 1.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808182030  152 NPRSFVVPS-HTDAHCICYVAEGEG-VVTTIENGERRSY--TIKQGHVFVAPAGAVTYLANTDGRKKLVI 217
Cdd:pfam00190  41 APGGMNPPHwHPNATEILYVLQGRGrVGFVVPGNGNRVFhkVLREGDVFVVPQGLPHFQYNIGDEPAVAF 110
cupin_TM1112-like cd02227
Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial ...
150-201 4.48e-04

Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial and plant proteins homologous to TM1112, a Thermotoga maritima protein of unknown function with a cupin beta barrel domain. TM1112 (also known as DUF861) is a subfamily of RmlC-like cupins with a conserved "jelly roll-like" beta-barrel fold; structures indicate that a monomer is the biologically-relevant form.


Pssm-ID: 380356 [Multi-domain]  Cd Length: 69  Bit Score: 37.56  E-value: 4.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 808182030 150 EANPRSFvvPSHTDAHCICYVAEGEGVVTTiENGErrSYTIKQGHVFVAPAG 201
Cdd:cd02227    6 ECTPGKF--PWNYDEDEFCYILEGEVRVTP-EDGE--PVTFKAGDLVVFPAG 52
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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