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Conserved domains on  [gi|75268099|sp|Q9ZWA9|]
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RecName: Full=12S seed storage protein CRD; AltName: Full=Cruciferin D; AltName: Full=Legumin-type globulin storage protein CRD; Contains: RecName: Full=12S seed storage protein CRD alpha chain; AltName: Full=12S seed storage protein CRD acidic chain; Contains: RecName: Full=12S seed storage protein CRD beta chain; AltName: Full=12S seed storage protein CRD 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 ...
 6-448 3.10e-122

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: 364.91  E-value: 3.10e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099    6 FSLLSVVsLSFLLFFHGAEAR-------QREAP---FPNACHFSQINSLAPAQATKFEAGQMEVWDHMSPELRCAGVTVA 75
Cdd:PLN00212   5 FSRLSIC-FCVLLLCHGSMAQlfsqstnPWQSPrqgSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNEQFQCTGVFVI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099   76 RITLQPNSIFLPAFFSPPALAYVVQGEGVMGTIASGCPETFAEVeGSSGRGGGGDPGRRFEDMHQKLENFRRGDVFASLA 155
Cdd:PLN00212  84 RRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQ-FQQFLTEGQSQSQKFRDEHQKIHQFRQGDVVALPA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099  156 GVSQWWYNRGDSDAVIVIVLDVTNRENQLDQVPRMFQLAG---SRTQEEEQPLTWPSGNNAFSGFDPNIIAEAFKINIET 232
Cdd:PLN00212 163 GVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGnnnRQQQVYGRSIEQHSGQNIFSGFSTELLSEALGINAQV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099  233 AKQLQNQKDNRGNIIRANGPLHFVIPP---------------------PREWQQDGIANGIEETYCTAKIHENIDDPERS 291
Cdd:PLN00212 243 AKRLQSQNDQRGEIIRVKNGLQLLQPTltqqqeqaqqqqqrlyqqvqyQQSQQTSGRWNGLDENFCTIKVRLNIENPSRA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099  292 DHFSTRAGRISTLNSLNLPVLRLVRLNALRGYLYSGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQSVFNEQVGQGQI 371
Cdd:PLN00212 323 DTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGKTVFNGVLRPGQL 402

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75268099  372 IVIPQGFAVSKTAGETGFEWISFKTNDNAYINTLSGQTSYLRAVPVDVIKASYGVNEEEAKRIKFSQQETMLSMTPS 448
Cdd:PLN00212 403 LIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRGDELGAFTPR 479
 
Name Accession Description Interval E-value
PLN00212 PLN00212
glutelin; Provisional
 6-448 3.10e-122

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 364.91  E-value: 3.10e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099    6 FSLLSVVsLSFLLFFHGAEAR-------QREAP---FPNACHFSQINSLAPAQATKFEAGQMEVWDHMSPELRCAGVTVA 75
Cdd:PLN00212   5 FSRLSIC-FCVLLLCHGSMAQlfsqstnPWQSPrqgSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNEQFQCTGVFVI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099   76 RITLQPNSIFLPAFFSPPALAYVVQGEGVMGTIASGCPETFAEVeGSSGRGGGGDPGRRFEDMHQKLENFRRGDVFASLA 155
Cdd:PLN00212  84 RRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQ-FQQFLTEGQSQSQKFRDEHQKIHQFRQGDVVALPA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099  156 GVSQWWYNRGDSDAVIVIVLDVTNRENQLDQVPRMFQLAG---SRTQEEEQPLTWPSGNNAFSGFDPNIIAEAFKINIET 232
Cdd:PLN00212 163 GVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGnnnRQQQVYGRSIEQHSGQNIFSGFSTELLSEALGINAQV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099  233 AKQLQNQKDNRGNIIRANGPLHFVIPP---------------------PREWQQDGIANGIEETYCTAKIHENIDDPERS 291
Cdd:PLN00212 243 AKRLQSQNDQRGEIIRVKNGLQLLQPTltqqqeqaqqqqqrlyqqvqyQQSQQTSGRWNGLDENFCTIKVRLNIENPSRA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099  292 DHFSTRAGRISTLNSLNLPVLRLVRLNALRGYLYSGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQSVFNEQVGQGQI 371
Cdd:PLN00212 323 DTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGKTVFNGVLRPGQL 402

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75268099  372 IVIPQGFAVSKTAGETGFEWISFKTNDNAYINTLSGQTSYLRAVPVDVIKASYGVNEEEAKRIKFSQQETMLSMTPS 448
Cdd:PLN00212 403 LIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRGDELGAFTPR 479
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
 38-251 4.95e-90

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: 272.15  E-value: 4.95e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099  38 FSQINSLAPAQATKFEAGQMEVWDHMSPELRCAGVTVARITLQPNSIFLPAFFSPPALAYVVQGEGVMGTIASGCPETFA 117
Cdd:cd02242   1 LDRLPALEPTRRIESEGGSYEYWDPNNPQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGCPETFQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099 118 EvegssgRGGGGDPGRRFEDMHQKLENFRRGDVFASLAGVSQWWYNRGDSDAVIVIVLDVTNRENQLDQVPRMFQLAGSR 197
Cdd:cd02242  81 S------SQQSQGQGQRFRDQHQKVRRIRKGDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNNANQLDGNFRRFFLAGNP 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75268099 198 TQEE-EQPLTWPSGNNAFSGFDPNIIAEAFKINIETAKQLQNQKDNRGNIIRANG 251
Cdd:cd02242 155 QQEQqGQGQEQSGGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGLIVKVEE 209
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 289-432 2.63e-44

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: 151.66  E-value: 2.63e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099    289 ERSDHFSTRAGRISTLNSLNLPVLRLVRLNALRGYLYSGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQSVFNEQVGQ 368
Cdd:smart00835   2 EPRPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVYDARLRE 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75268099    369 GQIIVIPQGFAVSKTA-GETGFEWISFKTNDNAYINTLSGQTSYLRAVPVDVIKASYGVNEEEAK 432
Cdd:smart00835  82 GDVFVVPQGHPHFQVNsGDENLEFVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 283-432 5.20e-40

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: 140.55  E-value: 5.20e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099   283 ENIDDPERSdhFSTRAGRISTLNSLNLPVLRLVRLNALRGYLYSGGMVLPQWTANAHTVLYVTGGQAK-IQVVDDNGQSV 361
Cdd:pfam00190   1 LNLLEPGPT--YNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRvGFVVPGNGNRV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75268099   362 FNEQVGQGQIIVIPQGFAVSKTA--GETGFEWISFKTNDNAYINTLSGQTSYLRAVPVDVIKASYGVNEEEAK 432
Cdd:pfam00190  79 FHKVLREGDVFVVPQGLPHFQYNigDEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 343-434 1.05e-04

bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins as they have two copies of the cupin domain (pfam00190). Two different known activities for members of this family are oxalate decarboxylase (EC 4.1.1.2) and oxalate oxidase (EC 1.2.3.4), although the latter activity has more often been found in distantly related monocupin (germin) proteins.


Pssm-ID: 274565 [Multi-domain]  Cd Length: 367  Bit Score: 44.23  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099   343 YVTGGQAKIQVVDDNGQSvFNEQVGQGQIIVIPQGFAVSKTAGETGFEW-ISFKTNDNAYINTLSgQTSYLRAVPVDVIK 421
Cdd:TIGR03404  92 YVLYGSCRITAVDENGRN-YIDDVGAGDLWYFPPGIPHSLQGLDEGCEFlLVFDDGNFSEDGTFL-VTDWLAHTPKDVLA 169

                          90
                  ....*....|...
gi 75268099   422 ASYGVNEEEAKRI 434
Cdd:TIGR03404 170 KNFGVPESAFDNL 182
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 324-379 6.94e-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: 39.18  E-value: 6.94e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75268099 324 LYSGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQsVFNEQVGQGQIIVIPQGFA 379
Cdd:COG2140  10 LEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGR-ARTVDVGPGDVVYVPPGYG 64
 
Name Accession Description Interval E-value
PLN00212 PLN00212
glutelin; Provisional
 6-448 3.10e-122

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 364.91  E-value: 3.10e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099    6 FSLLSVVsLSFLLFFHGAEAR-------QREAP---FPNACHFSQINSLAPAQATKFEAGQMEVWDHMSPELRCAGVTVA 75
Cdd:PLN00212   5 FSRLSIC-FCVLLLCHGSMAQlfsqstnPWQSPrqgSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNEQFQCTGVFVI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099   76 RITLQPNSIFLPAFFSPPALAYVVQGEGVMGTIASGCPETFAEVeGSSGRGGGGDPGRRFEDMHQKLENFRRGDVFASLA 155
Cdd:PLN00212  84 RRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQ-FQQFLTEGQSQSQKFRDEHQKIHQFRQGDVVALPA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099  156 GVSQWWYNRGDSDAVIVIVLDVTNRENQLDQVPRMFQLAG---SRTQEEEQPLTWPSGNNAFSGFDPNIIAEAFKINIET 232
Cdd:PLN00212 163 GVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGnnnRQQQVYGRSIEQHSGQNIFSGFSTELLSEALGINAQV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099  233 AKQLQNQKDNRGNIIRANGPLHFVIPP---------------------PREWQQDGIANGIEETYCTAKIHENIDDPERS 291
Cdd:PLN00212 243 AKRLQSQNDQRGEIIRVKNGLQLLQPTltqqqeqaqqqqqrlyqqvqyQQSQQTSGRWNGLDENFCTIKVRLNIENPSRA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099  292 DHFSTRAGRISTLNSLNLPVLRLVRLNALRGYLYSGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQSVFNEQVGQGQI 371
Cdd:PLN00212 323 DTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGKTVFNGVLRPGQL 402

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75268099  372 IVIPQGFAVSKTAGETGFEWISFKTNDNAYINTLSGQTSYLRAVPVDVIKASYGVNEEEAKRIKFSQQETMLSMTPS 448
Cdd:PLN00212 403 LIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRGDELGAFTPR 479
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
 38-251 4.95e-90

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: 272.15  E-value: 4.95e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099  38 FSQINSLAPAQATKFEAGQMEVWDHMSPELRCAGVTVARITLQPNSIFLPAFFSPPALAYVVQGEGVMGTIASGCPETFA 117
Cdd:cd02242   1 LDRLPALEPTRRIESEGGSYEYWDPNNPQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGCPETFQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099 118 EvegssgRGGGGDPGRRFEDMHQKLENFRRGDVFASLAGVSQWWYNRGDSDAVIVIVLDVTNRENQLDQVPRMFQLAGSR 197
Cdd:cd02242  81 S------SQQSQGQGQRFRDQHQKVRRIRKGDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNNANQLDGNFRRFFLAGNP 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75268099 198 TQEE-EQPLTWPSGNNAFSGFDPNIIAEAFKINIETAKQLQNQKDNRGNIIRANG 251
Cdd:cd02242 155 QQEQqGQGQEQSGGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGLIVKVEE 209
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
 292-442 6.45e-77

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: 236.60  E-value: 6.45e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099 292 DHFSTRAGRISTLNSLNLPVLRLVRLNALRGYLYSGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQSVFNEQVGQGQI 371
Cdd:cd02243   1 DVYVPRGGRITTLNSFKLPILRFVGLSAERVKLEPNAMFAPHWNANAHQVIYVTRGSGRVQVVGDNGKRVLDGEVREGQL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75268099 372 IVIPQGFAVSKTAGETGFEWISFKTNDNAYINTLSGQTSYLRAVPVDVIKASYGVNEEEAKRIKFSQQETM 442
Cdd:cd02243  81 LVVPQFFAVAKIAGEEGFEWVSFKTSDNPIFSELAGRTSVLRALPPEVLANSYNISPEEAKQLKSNREKET 151
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 289-432 2.63e-44

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: 151.66  E-value: 2.63e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099    289 ERSDHFSTRAGRISTLNSLNLPVLRLVRLNALRGYLYSGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQSVFNEQVGQ 368
Cdd:smart00835   2 EPRPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVYDARLRE 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75268099    369 GQIIVIPQGFAVSKTA-GETGFEWISFKTNDNAYINTLSGQTSYLRAVPVDVIKASYGVNEEEAK 432
Cdd:smart00835  82 GDVFVVPQGHPHFQVNsGDENLEFVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 283-432 5.20e-40

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: 140.55  E-value: 5.20e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099   283 ENIDDPERSdhFSTRAGRISTLNSLNLPVLRLVRLNALRGYLYSGGMVLPQWTANAHTVLYVTGGQAK-IQVVDDNGQSV 361
Cdd:pfam00190   1 LNLLEPGPT--YNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRvGFVVPGNGNRV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75268099   362 FNEQVGQGQIIVIPQGFAVSKTA--GETGFEWISFKTNDNAYINTLSGQTSYLRAVPVDVIKASYGVNEEEAK 432
Cdd:pfam00190  79 FHKVLREGDVFVVPQGLPHFQYNigDEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 42-234 5.30e-24

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: 97.40  E-value: 5.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099    42 NSLAPAQATKFEAGQMEVWDHMS-PELRCAGVTVARITLQPNSIFLPAFFS-PPALAYVVQGEGVMGTIASGCPetfaev 119
Cdd:pfam00190   2 NLLEPGPTYNPEGGRVTTVNSKNlPGLNTLGISAARVDLAPGGMNPPHWHPnATEILYVLQGRGRVGFVVPGNG------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099   120 egssgrggggdpgrrFEDMHQKLenfRRGDVFASLAGVSQWWYNRGDSDAVIVIVLDVTNRENQldqvprmFQLAGsrtq 199
Cdd:pfam00190  76 ---------------NRVFHKVL---REGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQ-------SILAG---- 126

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 75268099   200 eeeqpltwpsGNNAFSGFDPNIIAEAFKINIETAK 234
Cdd:pfam00190 127 ----------GFSSLPALPPEVLAKAFQLAGEEVK 151
cupin_7S_11S_C cd20285
7S and 11S seed storage globulin, C-terminal cupin domain; This family contains the C-terminal ...
 299-406 7.48e-21

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: 87.28  E-value: 7.48e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099 299 GRISTLNSLNLPVLRLVRLNALRGYLYSGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQSVFNEQVGQGQIIVIPQGF 378
Cdd:cd20285   1 GNVTERTSNDFPILKSLNLLASSISLEEGAMFVPHYYSKAIVILVVNEGRAHIQVVGPKGYESYDAELSKGDVFVVPAAF 80

                        90       100
                ....*....|....*....|....*....
gi 75268099 379 AVSKTAGETGFEWISFKTN-DNAYINTLS 406
Cdd:cd20285  81 PVAIKSTSHNVEFTGFGTNaNNNNRNLLA 109
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 44-234 1.26e-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: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 79.25  E-value: 1.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099     44 LAPAQATKFEAGQMEVWD-HMSPELRCAGVTVARITLQPNSIFLPAFFS-PPALAYVVQGEGVMGTIASGCPETFAEveg 121
Cdd:smart00835   1 LEPRPDFSNEGGRLREADpTNFPALNGLGISAARVNLEPGGMLPPHYHPrATELLYVVRGEGRVGVVDPNGNKVYDA--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099    122 ssgrggggdpgrrfedmhqkleNFRRGDVFASLAGVSQWWYNRGDSDAVIVIVLdvTNRENqldqvpRMFQLAGsrtqee 201
Cdd:smart00835  78 ----------------------RLREGDVFVVPQGHPHFQVNSGDENLEFVAFN--TNDPN------RRFFLAG------ 121

                          170       180       190
                   ....*....|....*....|....*....|...
gi 75268099    202 eqpltwpsGNNAFSGFDPNIIAEAFKINIETAK 234
Cdd:smart00835 122 --------RNSVLRGLPPEVLAAAFGVSAEEVR 146
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 294-431 2.69e-15

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: 73.01  E-value: 2.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099 294 FSTRAGRISTLNSLNLPVLRlvRLNALRGYLYSGGMVLPQWTANAHTVLYVTGGQAKIQVVdDNGQSVFNEQVGQGQIIV 373
Cdd:cd20306  13 FESEGGSIRQATADQLPVLK--GLSIYRLRLSPGGIREPHWHPNANELGYVISGEARVSIL-DPTGSLDTFTVKPGQVVF 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75268099 374 IPQGFAVSKTA-GETGFEWISFKtnDNAYINTLSGQTSyLRAVPVDVIKASYGVNEEEA 431
Cdd:cd20306  90 IPQGWLHWIENvGDEEAHLLIFF--NHETPEDIGLSDS-LRATPPEVLGNTYGVDAFFA 145
cupin_7S_vicilin-like_C cd02245
7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal ...
 294-440 1.53e-08

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: 53.67  E-value: 1.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099 294 FSTRAGRISTLNSLNLPVLRlvRLNALRGY--LYSGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQSVFNE------- 364
Cdd:cd02245   3 FSNQYGWLYEADPEDYKQLK--DLDVGVSFvnITQGSMMAPHYNSRATEIAVVVEGEGYVEMVCPHLSSQSQQgeeegsg 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099 365 -------QVGQGQIIVIPQGFAVSKTAGETG-FEWISFKTN-DNAYINTLSGQTSYLRAVPVDVIKASYGVNEEEAKRIK 435
Cdd:cd02245  81 eyqkvraRLSEGDVFVVPAGHPVAQVASSNEnLEFVGFGINaQNNERQFLAGKNNVLRQLDREAKELAFNVPAEEVEEVL 160


                ....*
gi 75268099 436 FSQQE 440
Cdd:cd02245 161 NAQDE 165
cupin_7S_vicilin-like_N cd02244
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ...
 294-440 2.04e-06

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: 47.89  E-value: 2.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099 294 FSTRAGRISTL-----NSLNLPVLRLVRL-------NALrgylysggmVLPQWTaNAHTVLYVTGGQAKIQVVDDNGQSV 361
Cdd:cd02244   2 VRTEAGEIRVLerfdgRSRLLRGIENYRLafitmepNTL---------FLPHHL-DADMVFYVHTGRGTITWVDEDKRES 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099 362 FNeqVGQGQIIVIPQGFA---VSKTAGETGFEWISFKTNDNAYINTLS--------GQTSYLRAVPVDVIKASYGVNEEE 430
Cdd:cd02244  72 YN--LERGDVYRIPAGSTfylVNTDENEKLRIIALFDPVNSLTPGPFQsffgaggqNPESLLSGFSKEILEAAFNVSEEE 149

                       170
                ....*....|
gi 75268099 431 AKRIKFSQQE 440
Cdd:cd02244 150 LERLLSQQKP 159
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 295-429 3.88e-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: 43.62  E-value: 3.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099 295 STRAGRISTLNSLNLPVLR-----LVRLNalrgylySGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQSvFNEQVGQG 369
Cdd:cd02240   7 ENAGGSVRIATVTNFPISKdlssaLVRVA-------PGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRF-ETFNLGAG 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75268099 370 QIIVIPQGFAVS-KTAGETGFEWISFktNDNAYINTLSGqTSYLRAVPVDVIKASYGVNEE 429
Cdd:cd02240  79 DVGYVPSGSGHHiENIGDEDAEFLLI--FDDGTFADVSL-PWWLAMTPEEVLAATLDLGKF 136
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 343-434 1.05e-04

bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins as they have two copies of the cupin domain (pfam00190). Two different known activities for members of this family are oxalate decarboxylase (EC 4.1.1.2) and oxalate oxidase (EC 1.2.3.4), although the latter activity has more often been found in distantly related monocupin (germin) proteins.


Pssm-ID: 274565 [Multi-domain]  Cd Length: 367  Bit Score: 44.23  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75268099   343 YVTGGQAKIQVVDDNGQSvFNEQVGQGQIIVIPQGFAVSKTAGETGFEW-ISFKTNDNAYINTLSgQTSYLRAVPVDVIK 421
Cdd:TIGR03404  92 YVLYGSCRITAVDENGRN-YIDDVGAGDLWYFPPGIPHSLQGLDEGCEFlLVFDDGNFSEDGTFL-VTDWLAHTPKDVLA 169

                          90
                  ....*....|...
gi 75268099   422 ASYGVNEEEAKRI 434
Cdd:TIGR03404 170 KNFGVPESAFDNL 182
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 324-379 6.94e-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: 39.18  E-value: 6.94e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75268099 324 LYSGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQsVFNEQVGQGQIIVIPQGFA 379
Cdd:COG2140  10 LEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGR-ARTVDVGPGDVVYVPPGYG 64
 
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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