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Conserved domains on  [gi|112677|sp|P13744|]
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RecName: Full=11S globulin subunit beta; Contains: RecName: Full=11S globulin gamma chain; AltName: Full=11S globulin acidic chain; Contains: RecName: Full=11S globulin delta chain; AltName: Full=11S globulin basic chain; Flags: Precursor

Protein Classification

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

Graphical summary

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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 ...
 2-476 1.20e-157

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 PLN00212:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 493  Bit Score: 456.58  E-value: 1.20e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677      2 ARSSLFTFLCLAVFINGCLSQIEQQspwefqGSEVWQQHRYQSPRACRLENLRAQDPVRRAEAEAIFTEVWDQDNDEFQC 81
Cdd:PLN00212   4 AFSRLSICFCVLLLCHGSMAQLFSQ------STNPWQSPRQGSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNEQFQC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677     82 AGVNMIRHTIRPKGLLLPGFSNAPKLIFVAQGFGIRGIAIPGCAETYQTDLRRSQSAGSA----FKDQHQKIRPFREGDL 157
Cdd:PLN00212  78 TGVFVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQFLTEGQSqsqkFRDEHQKIHQFRQGDV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    158 LVVPAGVSHWMYNRGQSDLVLIVFADTRNVANQIDPYLRKFYLAGRPEqveRGVEEWERSSRKGSSGeksgNIFSGFADE 237
Cdd:PLN00212 158 VALPAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNN---RQQQVYGRSIEQHSGQ----NIFSGFSTE 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    238 FLEEAFQIDGGLVRKLKGEDDERDRIVQVDEDFEVLLP------EKDEEERSR----GRYIESESES--ENGLEETICTL 305
Cdd:PLN00212 231 LLSEALGINAQVAKRLQSQNDQRGEIIRVKNGLQLLQPtltqqqEQAQQQQQRlyqqVQYQQSQQTSgrWNGLDENFCTI 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    306 RLKQNIGRSVRADVFNPRGGRISTANYHTLPILRQVRLSAERGVLYSNAMVAPHYTVNSHSVMYATRGNARVQVVDNFGQ 385
Cdd:PLN00212 311 KVRLNIENPSRADTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGK 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    386 SVFDGEVREGQVLMIPQNFVVIKRASDRGFEWIAFKTNDNAITNLLAGRVSQMRMLPLGVLSNMYRISREEAQRLKYGQ- 464
Cdd:PLN00212 391 TVFNGVLRPGQLLIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRg 470

                        490
                 ....*....|..
gi 112677    465 QEMRVLSPGRSQ 476
Cdd:PLN00212 471 DELGAFTPRFQQ 482
 
Name Accession Description Interval E-value
PLN00212 PLN00212
glutelin; Provisional
 2-476 1.20e-157

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 456.58  E-value: 1.20e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677      2 ARSSLFTFLCLAVFINGCLSQIEQQspwefqGSEVWQQHRYQSPRACRLENLRAQDPVRRAEAEAIFTEVWDQDNDEFQC 81
Cdd:PLN00212   4 AFSRLSICFCVLLLCHGSMAQLFSQ------STNPWQSPRQGSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNEQFQC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677     82 AGVNMIRHTIRPKGLLLPGFSNAPKLIFVAQGFGIRGIAIPGCAETYQTDLRRSQSAGSA----FKDQHQKIRPFREGDL 157
Cdd:PLN00212  78 TGVFVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQFLTEGQSqsqkFRDEHQKIHQFRQGDV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    158 LVVPAGVSHWMYNRGQSDLVLIVFADTRNVANQIDPYLRKFYLAGRPEqveRGVEEWERSSRKGSSGeksgNIFSGFADE 237
Cdd:PLN00212 158 VALPAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNN---RQQQVYGRSIEQHSGQ----NIFSGFSTE 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    238 FLEEAFQIDGGLVRKLKGEDDERDRIVQVDEDFEVLLP------EKDEEERSR----GRYIESESES--ENGLEETICTL 305
Cdd:PLN00212 231 LLSEALGINAQVAKRLQSQNDQRGEIIRVKNGLQLLQPtltqqqEQAQQQQQRlyqqVQYQQSQQTSgrWNGLDENFCTI 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    306 RLKQNIGRSVRADVFNPRGGRISTANYHTLPILRQVRLSAERGVLYSNAMVAPHYTVNSHSVMYATRGNARVQVVDNFGQ 385
Cdd:PLN00212 311 KVRLNIENPSRADTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGK 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    386 SVFDGEVREGQVLMIPQNFVVIKRASDRGFEWIAFKTNDNAITNLLAGRVSQMRMLPLGVLSNMYRISREEAQRLKYGQ- 464
Cdd:PLN00212 391 TVFNGVLRPGQLLIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRg 470

                        490
                 ....*....|..
gi 112677    465 QEMRVLSPGRSQ 476
Cdd:PLN00212 471 DELGAFTPRFQQ 482
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
 50-268 8.04e-97

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: 290.64  E-value: 8.04e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    50 LENLRAQDPVRRAEAEAIFTEVWDQDNDEFQCAGVNMIRHTIRPKGLLLPGFSNAPKLIFVAQGFGIRGIAIPGCAETYQ 129
Cdd:cd02242   1 LDRLPALEPTRRIESEGGSYEYWDPNNPQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGCPETFQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677   130 TDlRRSQSAGSAFKDQHQKIRPFREGDLLVVPAGVSHWMYNRGQSDLVLIVFADTRNVANQIDPYLRKFYLAGRPEQVER 209
Cdd:cd02242  81 SS-QQSQGQGQRFRDQHQKVRRIRKGDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNNANQLDGNFRRFFLAGNPQQEQQ 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 112677   210 gveewerssRKGSSGEKSGNIFSGFADEFLEEAFQIDGGLVRKLKGEDDERDRIVQVDE 268
Cdd:cd02242 160 ---------GQGQEQSGGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGLIVKVEE 209
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 316-458 3.27e-47

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: 160.14  E-value: 3.27e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677      316 RADVFNPRGGRISTANYHTLPILRQVRLSAERGVLYSNAMVAPHYTVNSHSVMYATRGNARVQVVDNFGQSVFDGEVREG 395
Cdd:smart00835   3 PRPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVYDARLREG 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112677      396 QVLMIPQNFVVIKRAS-DRGFEWIAFKTNDNAITNLLAGRVSQMRMLPLGVLSNMYRISREEAQ 458
Cdd:smart00835  83 DVFVVPQGHPHFQVNSgDENLEFVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 318-458 4.19e-39

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: 138.62  E-value: 4.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677     318 DVFNPRGGRISTANYHTLPILRQVRLSAERGVLYSNAMVAPHYTVNSHSVMYATRGNARV-QVVDNFGQSVFDGEVREGQ 396
Cdd:pfam00190   8 PTYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVgFVVPGNGNRVFHKVLREGD 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112677     397 VLMIPQNFVVIKRASDR--GFEWIAFKTNDNAITNLLAGRVSQMRMLPLGVLSNMYRISREEAQ 458
Cdd:pfam00190  88 VFVVPQGLPHFQYNIGDepAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 349-404 3.24e-04

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: 40.33  E-value: 3.24e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 112677   349 VLYSNAMVAPHYTVNSHSVMYATRGNARVQVVDNFGQSVFDgEVREGQVLMIPQNF 404
Cdd:COG2140   9 VLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTV-DVGPGDVVYVPPGY 63
 
Name Accession Description Interval E-value
PLN00212 PLN00212
glutelin; Provisional
 2-476 1.20e-157

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 456.58  E-value: 1.20e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677      2 ARSSLFTFLCLAVFINGCLSQIEQQspwefqGSEVWQQHRYQSPRACRLENLRAQDPVRRAEAEAIFTEVWDQDNDEFQC 81
Cdd:PLN00212   4 AFSRLSICFCVLLLCHGSMAQLFSQ------STNPWQSPRQGSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNEQFQC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677     82 AGVNMIRHTIRPKGLLLPGFSNAPKLIFVAQGFGIRGIAIPGCAETYQTDLRRSQSAGSA----FKDQHQKIRPFREGDL 157
Cdd:PLN00212  78 TGVFVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQFLTEGQSqsqkFRDEHQKIHQFRQGDV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    158 LVVPAGVSHWMYNRGQSDLVLIVFADTRNVANQIDPYLRKFYLAGRPEqveRGVEEWERSSRKGSSGeksgNIFSGFADE 237
Cdd:PLN00212 158 VALPAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNN---RQQQVYGRSIEQHSGQ----NIFSGFSTE 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    238 FLEEAFQIDGGLVRKLKGEDDERDRIVQVDEDFEVLLP------EKDEEERSR----GRYIESESES--ENGLEETICTL 305
Cdd:PLN00212 231 LLSEALGINAQVAKRLQSQNDQRGEIIRVKNGLQLLQPtltqqqEQAQQQQQRlyqqVQYQQSQQTSgrWNGLDENFCTI 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    306 RLKQNIGRSVRADVFNPRGGRISTANYHTLPILRQVRLSAERGVLYSNAMVAPHYTVNSHSVMYATRGNARVQVVDNFGQ 385
Cdd:PLN00212 311 KVRLNIENPSRADTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGK 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    386 SVFDGEVREGQVLMIPQNFVVIKRASDRGFEWIAFKTNDNAITNLLAGRVSQMRMLPLGVLSNMYRISREEAQRLKYGQ- 464
Cdd:PLN00212 391 TVFNGVLRPGQLLIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRg 470

                        490
                 ....*....|..
gi 112677    465 QEMRVLSPGRSQ 476
Cdd:PLN00212 471 DELGAFTPRFQQ 482
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
 50-268 8.04e-97

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: 290.64  E-value: 8.04e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    50 LENLRAQDPVRRAEAEAIFTEVWDQDNDEFQCAGVNMIRHTIRPKGLLLPGFSNAPKLIFVAQGFGIRGIAIPGCAETYQ 129
Cdd:cd02242   1 LDRLPALEPTRRIESEGGSYEYWDPNNPQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGCPETFQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677   130 TDlRRSQSAGSAFKDQHQKIRPFREGDLLVVPAGVSHWMYNRGQSDLVLIVFADTRNVANQIDPYLRKFYLAGRPEQVER 209
Cdd:cd02242  81 SS-QQSQGQGQRFRDQHQKVRRIRKGDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNNANQLDGNFRRFFLAGNPQQEQQ 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 112677   210 gveewerssRKGSSGEKSGNIFSGFADEFLEEAFQIDGGLVRKLKGEDDERDRIVQVDE 268
Cdd:cd02242 160 ---------GQGQEQSGGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGLIVKVEE 209
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
 318-472 6.45e-86

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: 260.48  E-value: 6.45e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677   318 DVFNPRGGRISTANYHTLPILRQVRLSAERGVLYSNAMVAPHYTVNSHSVMYATRGNARVQVVDNFGQSVFDGEVREGQV 397
Cdd:cd02243   1 DVYVPRGGRITTLNSFKLPILRFVGLSAERVKLEPNAMFAPHWNANAHQVIYVTRGSGRVQVVGDNGKRVLDGEVREGQL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112677   398 LMIPQNFVVIKRASDRGFEWIAFKTNDNAITNLLAGRVSQMRMLPLGVLSNMYRISREEAQRLKYGQQEMRVLSP 472
Cdd:cd02243  81 LVVPQFFAVAKIAGEEGFEWVSFKTSDNPIFSELAGRTSVLRALPPEVLANSYNISPEEAKQLKSNREKETVLFP 155
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 316-458 3.27e-47

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: 160.14  E-value: 3.27e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677      316 RADVFNPRGGRISTANYHTLPILRQVRLSAERGVLYSNAMVAPHYTVNSHSVMYATRGNARVQVVDNFGQSVFDGEVREG 395
Cdd:smart00835   3 PRPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVYDARLREG 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112677      396 QVLMIPQNFVVIKRAS-DRGFEWIAFKTNDNAITNLLAGRVSQMRMLPLGVLSNMYRISREEAQ 458
Cdd:smart00835  83 DVFVVPQGHPHFQVNSgDENLEFVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 318-458 4.19e-39

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: 138.62  E-value: 4.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677     318 DVFNPRGGRISTANYHTLPILRQVRLSAERGVLYSNAMVAPHYTVNSHSVMYATRGNARV-QVVDNFGQSVFDGEVREGQ 396
Cdd:pfam00190   8 PTYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVgFVVPGNGNRVFHKVLREGD 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112677     397 VLMIPQNFVVIKRASDR--GFEWIAFKTNDNAITNLLAGRVSQMRMLPLGVLSNMYRISREEAQ 458
Cdd:pfam00190  88 VFVVPQGLPHFQYNIGDepAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
cupin_7S_11S_C cd20285
7S and 11S seed storage globulin, C-terminal cupin domain; This family contains the C-terminal ...
 325-432 4.23e-27

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: 105.00  E-value: 4.23e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677   325 GRISTANYHTLPILRQVRLSAERGVLYSNAMVAPHYTVNSHSVMYATRGNARVQVVDNFGQSVFDGEVREGQVLMIPQNF 404
Cdd:cd20285   1 GNVTERTSNDFPILKSLNLLASSISLEEGAMFVPHYYSKAIVILVVNEGRAHIQVVGPKGYESYDAELSKGDVFVVPAAF 80

                        90       100
                ....*....|....*....|....*....
gi 112677   405 VVIKRASDRGFEWIAFKTN-DNAITNLLA 432
Cdd:cd20285  81 PVAIKSTSHNVEFTGFGTNaNNNNRNLLA 109
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 54-251 2.38e-19

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: 84.25  E-value: 2.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677       54 RAQDPVrrAEAEAIFTEVWDQDN-DEFQCAGVNMIRHTIRPKGLLLPGF-SNAPKLIFVAQGFGIRGIAIPGCaetyqtd 131
Cdd:smart00835   1 LEPRPD--FSNEGGRLREADPTNfPALNGLGISAARVNLEPGGMLPPHYhPRATELLYVVRGEGRVGVVDPNG------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677      132 lrrsqsagsafkdQHQKIRPFREGDLLVVPAGVSHWMYNRGQSDLVLIVFADTRNVanqidpylRKFYLAGRpeqvergv 211
Cdd:smart00835  72 -------------NKVYDARLREGDVFVVPQGHPHFQVNSGDENLEFVAFNTNDPN--------RRFFLAGR-------- 122

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 112677      212 eewerssrkgssgeksGNIFSGFADEFLEEAFQIDGGLVR 251
Cdd:smart00835 123 ----------------NSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 51-207 4.06e-17

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: 78.15  E-value: 4.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677      51 ENLRAQDPVrrAEAEAIFTEVWDQDN--DEFQCAGVnMIRHTIRPKGLLLPGF-SNAPKLIFVAQGFGIRGIAIPGCAet 127
Cdd:pfam00190   1 LNLLEPGPT--YNPEGGRVTTVNSKNlpGLNTLGIS-AARVDLAPGGMNPPHWhPNATEILYVLQGRGRVGFVVPGNG-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677     128 yqtdlrrsqsagsaFKDQHQKIRPfreGDLLVVPAGVSHWMYNRGQSDLVLIVFADTRNVANQIDPYLRKFYLAGRPEQV 207
Cdd:pfam00190  76 --------------NRVFHKVLRE---GDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEV 138
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 319-457 7.37e-11

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: 60.30  E-value: 7.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677   319 VFNPRGGRISTANYHTLPILRqvRLSAERGVLYSNAMVAPHYTVNSHSVMYATRGNARVQVVDNFGQ-SVFDgeVREGQV 397
Cdd:cd20306  12 FFESEGGSIRQATADQLPVLK--GLSIYRLRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGSlDTFT--VKPGQV 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112677   398 LMIPQNFV-VIKRASDRGFEWIAFKTNDNAITNLLAGRVsqmRMLPLGVLSNMYRISREEA 457
Cdd:cd20306  88 VFIPQGWLhWIENVGDEEAHLLIFFNHETPEDIGLSDSL---RATPPEVLGNTYGVDAFFA 145
cupin_7S_vicilin-like_C cd02245
7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal ...
 325-466 8.79e-09

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: 54.45  E-value: 8.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677   325 GRISTANYHTLPILRQVRLsaerGVLYSN----AMVAPHYtvNSHSVMYA--TRGNARVQVV------------DNFGQS 386
Cdd:cd02245   8 GWLYEADPEDYKQLKDLDV----GVSFVNitqgSMMAPHY--NSRATEIAvvVEGEGYVEMVcphlssqsqqgeEEGSGE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677   387 V--FDGEVREGQVLMIPQNF-VVIKRASDRGFEWIAFKTN-DNAITNLLAGRVSQMRMLPLGVLSNMYRISREEAQRLKY 462
Cdd:cd02245  82 YqkVRARLSEGDVFVVPAGHpVAQVASSNENLEFVGFGINaQNNERQFLAGKNNVLRQLDREAKELAFNVPAEEVEEVLN 161


                ....
gi 112677   463 GQQE 466
Cdd:cd02245 162 AQDE 165
cupin_7S_vicilin-like_N cd02244
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ...
 90-259 1.92e-05

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: 45.19  E-value: 1.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677    90 TIRPKGLLLPGFSNAPKLIFVAQGFGIRGIAIPGcaETYQTDLRRsqsagsafkdqhqkirpfreGDLLVVPAGVSHWMY 169
Cdd:cd02244  34 TMEPNTLFLPHHLDADMVFYVHTGRGTITWVDED--KRESYNLER--------------------GDVYRIPAGSTFYLV 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112677   170 NRGQSD-LVLIVFADTRNVANqIDPYlRKFYLAGrpeqvergveewerssrkgssGEKSGNIFSGFADEFLEEAFQIDGG 248
Cdd:cd02244  92 NTDENEkLRIIALFDPVNSLT-PGPF-QSFFGAG---------------------GQNPESLLSGFSKEILEAAFNVSEE 148

                       170
                ....*....|.
gi 112677   249 LVRKLKGEDDE 259
Cdd:cd02244 149 ELERLLSQQKP 159
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 142-181 5.36e-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: 41.31  E-value: 5.36e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 112677   142 FKDQHQKIRPFREGDLLVVPAGVSHWMYNRGQSDLVLIVF 181
Cdd:cd02208  33 LTLDDGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVV 72
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 324-401 9.17e-05

Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) 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 and both domains are included in this alignment. Each OxDC cupin domain contains one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380367 [Multi-domain]  Cd Length: 145  Bit Score: 42.47  E-value: 9.17e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112677   324 GGRISTANYHTLPILRQvrLSAERGVLYSNAMVAPHYTVNSHSVMYATRGNARVQVVDNFGQSvFDGEVREGQVLMIP 401
Cdd:cd02240  10 GGSVRIATVTNFPISKD--LSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRF-ETFNLGAGDVGYVP 84
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 349-404 3.24e-04

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: 40.33  E-value: 3.24e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 112677   349 VLYSNAMVAPHYTVNSHSVMYATRGNARVQVVDNFGQSVFDgEVREGQVLMIPQNF 404
Cdd:COG2140   9 VLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTV-DVGPGDVVYVPPGY 63
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
147-181 4.77e-04

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 39.45  E-value: 4.77e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 112677   147 QKIRPFREGDLLVVPAGVSHWMYNRGQSDLVLIVF 181
Cdd:COG1917  60 GEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVV 94
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
148-181 6.11e-04

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 39.35  E-value: 6.11e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 112677   148 KIRPFREGDLLVVPAGVSHWMYNRGQSDLVLIVF 181
Cdd:COG0662  66 EEVELKAGDSVYIPAGVPHRLRNPGDEPLELLEV 99
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 151-180 3.15e-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: 36.08  E-value: 3.15e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 112677     151 PFREGDLLVVPAGVSHWMYNRGQSDLVLIV 180
Cdd:pfam07883  40 VLKAGDSVYFPAGVPHRFRNTGDEPARLLD 69
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 144-179 6.02e-03

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: 36.34  E-value: 6.02e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 112677   144 DQHQKIRPfreGDLLVVPAGVSHWMYNRGQSDLVLI 179
Cdd:cd02214  57 GEPREVGP---GDAVLIPPGAVQRIENTGEEDLVFL 89
 
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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