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Conserved domains on  [gi|266618564]
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Chain D, Prunin

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 ...
 19-520 9.20e-125

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: 374.15  E-value: 9.20e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564  19 AREPDNRIQAEAGQIETWNFNQGDFQCAGVAASRITIQRNGLHLPSYSNAPQLIYIVQGRGVLGAVFSGCPETFEESQQS 98
Cdd:PLN00212  51 AFEPLRKVRSEAGVTEYFDEKNEQFQCTGVFVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQ 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564  99 sqqgrqqeqeqerqqqqqgeqGRQQGQQEQQQERqgrqqgrqqqeegrqqeqqqgqqgrpqqqqqfrqlDRHQKTRRIRE 178
Cdd:PLN00212 131 ---------------------FLTEGQSQSQKFR-----------------------------------DEHQKIHQFRQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 179 GDVVAIPAGVAYWSYNDGDQELVAVNLFHVSSDHNQLDQNPRKFYLAGNPENEfnqqgqsqprqqgeqgrpgqhQQPFGR 258
Cdd:PLN00212 155 GDVVALPAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNNRQ---------------------QQVYGR 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 259 prqQEQQGNGNNVFSGFNTQLLAQALNVNEETARNLQGQNDNRNQIIQVRGNLDFVQPPRGRQEREHEERQQEQLQQERQ 338
Cdd:PLN00212 214 ---SIEQHSGQNIFSGFSTELLSEALGINAQVAKRLQSQNDQRGEIIRVKNGLQLLQPTLTQQQEQAQQQQQRLYQQVQY 290

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 339 QQGEQLMA--NGLEETFCSLRLKENIGNPERADIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAH 416
Cdd:PLN00212 291 QQSQQTSGrwNGLDENFCTIKVRLNIENPSRADTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAH 370

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 417 SVVYVIRGNARVQVVNENGDAILDQEVQQGQLFIVPQNHGVIQQAGNQGFEYFAFKTEENAFINTLAGRTSFLRALPDEV 496
Cdd:PLN00212 371 SVVYITQGRARVQVVSNNGKTVFNGVLRPGQLLIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDV 450

                        490       500
                 ....*....|....*....|....
gi 266618564 497 LANAYQISREQARQLKYNRQETIA 520
Cdd:PLN00212 451 IANAYRISREEARRLKNNRGDELG 474
 
Name Accession Description Interval E-value
PLN00212 PLN00212
glutelin; Provisional
 19-520 9.20e-125

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 374.15  E-value: 9.20e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564  19 AREPDNRIQAEAGQIETWNFNQGDFQCAGVAASRITIQRNGLHLPSYSNAPQLIYIVQGRGVLGAVFSGCPETFEESQQS 98
Cdd:PLN00212  51 AFEPLRKVRSEAGVTEYFDEKNEQFQCTGVFVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQ 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564  99 sqqgrqqeqeqerqqqqqgeqGRQQGQQEQQQERqgrqqgrqqqeegrqqeqqqgqqgrpqqqqqfrqlDRHQKTRRIRE 178
Cdd:PLN00212 131 ---------------------FLTEGQSQSQKFR-----------------------------------DEHQKIHQFRQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 179 GDVVAIPAGVAYWSYNDGDQELVAVNLFHVSSDHNQLDQNPRKFYLAGNPENEfnqqgqsqprqqgeqgrpgqhQQPFGR 258
Cdd:PLN00212 155 GDVVALPAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNNRQ---------------------QQVYGR 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 259 prqQEQQGNGNNVFSGFNTQLLAQALNVNEETARNLQGQNDNRNQIIQVRGNLDFVQPPRGRQEREHEERQQEQLQQERQ 338
Cdd:PLN00212 214 ---SIEQHSGQNIFSGFSTELLSEALGINAQVAKRLQSQNDQRGEIIRVKNGLQLLQPTLTQQQEQAQQQQQRLYQQVQY 290

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 339 QQGEQLMA--NGLEETFCSLRLKENIGNPERADIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAH 416
Cdd:PLN00212 291 QQSQQTSGrwNGLDENFCTIKVRLNIENPSRADTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAH 370

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 417 SVVYVIRGNARVQVVNENGDAILDQEVQQGQLFIVPQNHGVIQQAGNQGFEYFAFKTEENAFINTLAGRTSFLRALPDEV 496
Cdd:PLN00212 371 SVVYITQGRARVQVVSNNGKTVFNGVLRPGQLLIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDV 450

                        490       500
                 ....*....|....*....|....
gi 266618564 497 LANAYQISREQARQLKYNRQETIA 520
Cdd:PLN00212 451 IANAYRISREEARRLKNNRGDELG 474
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
 19-309 6.74e-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: 274.46  E-value: 6.74e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564  19 AREPDNRIQAEAGQIETWNFNQGDFQCAGVAASRITIQRNGLHLPSYSNAPQLIYIVQGRGVLGAVFSGCPETFEESQQS 98
Cdd:cd02242    6 ALEPTRRIESEGGSYEYWDPNNPQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGCPETFQSSQQS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564  99 SQQGRQQEqeqerqqqqqgeqgrqqgqqeqqqerqgrqqgrqqqeegrqqeqqqgqqgrpqqqqqfrqlDRHQKTRRIRE 178
Cdd:cd02242   86 QGQGQRFR-------------------------------------------------------------DQHQKVRRIRK 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 179 GDVVAIPAGVAYWSYNDGDQELVAVNLFHVSSDHNQLDQNPRKFYLAGNPENEFnqqgqsqprqqgeqgrpgqhqqpfgr 258
Cdd:cd02242  105 GDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNNANQLDGNFRRFFLAGNPQQEQ-------------------------- 158

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 266618564 259 PRQQEQQGNGNNVFSGFNTQLLAQALNVNEETARNLQGQNDNRNQIIQVRG 309
Cdd:cd02242  159 QGQGQEQSGGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGLIVKVEE 209
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 366-509 2.16e-46

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: 158.98  E-value: 2.16e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564   366 ERADIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDQEVQQ 445
Cdd:smart00835   2 EPRPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVYDARLRE 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 266618564   446 GQLFIVPQNHGVIQQA-GNQGFEYFAFKTEENAFINTLAGRTSFLRALPDEVLANAYQISREQAR 509
Cdd:smart00835  82 GDVFVVPQGHPHFQVNsGDENLEFVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 360-509 2.44e-42

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: 148.25  E-value: 2.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564  360 ENIGNPERadIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARV-QVVNENGDAI 438
Cdd:pfam00190   1 LNLLEPGP--TYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVgFVVPGNGNRV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 266618564  439 LDQEVQQGQLFIVPQNHGVIQQAGNQ--GFEYFAFKTEENAFINTLAGRTSFLRALPDEVLANAYQISREQAR 509
Cdd:pfam00190  79 FHKVLREGDVFVVPQGLPHFQYNIGDepAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 400-498 1.76e-10

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: 58.44  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 400 FFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDqEVQQGQLFIVPQNHG-VIQQAGNQGFEYFAFKTEENAF 478
Cdd:COG2140    9 VLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTV-DVGPGDVVYVPPGYGhYIINTGDEPLVFLAVFDDDAGS 87

                         90       100
                 ....*....|....*....|
gi 266618564 479 INTLAGRTSFLRALPDEVLA 498
Cdd:COG2140   88 DYGTISLSGWLAHTPPEVLA 107
 
Name Accession Description Interval E-value
PLN00212 PLN00212
glutelin; Provisional
 19-520 9.20e-125

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 374.15  E-value: 9.20e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564  19 AREPDNRIQAEAGQIETWNFNQGDFQCAGVAASRITIQRNGLHLPSYSNAPQLIYIVQGRGVLGAVFSGCPETFEESQQS 98
Cdd:PLN00212  51 AFEPLRKVRSEAGVTEYFDEKNEQFQCTGVFVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQ 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564  99 sqqgrqqeqeqerqqqqqgeqGRQQGQQEQQQERqgrqqgrqqqeegrqqeqqqgqqgrpqqqqqfrqlDRHQKTRRIRE 178
Cdd:PLN00212 131 ---------------------FLTEGQSQSQKFR-----------------------------------DEHQKIHQFRQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 179 GDVVAIPAGVAYWSYNDGDQELVAVNLFHVSSDHNQLDQNPRKFYLAGNPENEfnqqgqsqprqqgeqgrpgqhQQPFGR 258
Cdd:PLN00212 155 GDVVALPAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNNRQ---------------------QQVYGR 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 259 prqQEQQGNGNNVFSGFNTQLLAQALNVNEETARNLQGQNDNRNQIIQVRGNLDFVQPPRGRQEREHEERQQEQLQQERQ 338
Cdd:PLN00212 214 ---SIEQHSGQNIFSGFSTELLSEALGINAQVAKRLQSQNDQRGEIIRVKNGLQLLQPTLTQQQEQAQQQQQRLYQQVQY 290

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 339 QQGEQLMA--NGLEETFCSLRLKENIGNPERADIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAH 416
Cdd:PLN00212 291 QQSQQTSGrwNGLDENFCTIKVRLNIENPSRADTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAH 370

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 417 SVVYVIRGNARVQVVNENGDAILDQEVQQGQLFIVPQNHGVIQQAGNQGFEYFAFKTEENAFINTLAGRTSFLRALPDEV 496
Cdd:PLN00212 371 SVVYITQGRARVQVVSNNGKTVFNGVLRPGQLLIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDV 450

                        490       500
                 ....*....|....*....|....
gi 266618564 497 LANAYQISREQARQLKYNRQETIA 520
Cdd:PLN00212 451 IANAYRISREEARRLKNNRGDELG 474
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
 19-309 6.74e-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: 274.46  E-value: 6.74e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564  19 AREPDNRIQAEAGQIETWNFNQGDFQCAGVAASRITIQRNGLHLPSYSNAPQLIYIVQGRGVLGAVFSGCPETFEESQQS 98
Cdd:cd02242    6 ALEPTRRIESEGGSYEYWDPNNPQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGCPETFQSSQQS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564  99 SQQGRQQEqeqerqqqqqgeqgrqqgqqeqqqerqgrqqgrqqqeegrqqeqqqgqqgrpqqqqqfrqlDRHQKTRRIRE 178
Cdd:cd02242   86 QGQGQRFR-------------------------------------------------------------DQHQKVRRIRK 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 179 GDVVAIPAGVAYWSYNDGDQELVAVNLFHVSSDHNQLDQNPRKFYLAGNPENEFnqqgqsqprqqgeqgrpgqhqqpfgr 258
Cdd:cd02242  105 GDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNNANQLDGNFRRFFLAGNPQQEQ-------------------------- 158

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 266618564 259 PRQQEQQGNGNNVFSGFNTQLLAQALNVNEETARNLQGQNDNRNQIIQVRG 309
Cdd:cd02242  159 QGQGQEQSGGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGLIVKVEE 209
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
 369-521 3.63e-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: 262.80  E-value: 3.63e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 369 DIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDQEVQQGQL 448
Cdd:cd02243    1 DVYVPRGGRITTLNSFKLPILRFVGLSAERVKLEPNAMFAPHWNANAHQVIYVTRGSGRVQVVGDNGKRVLDGEVREGQL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 266618564 449 FIVPQNHGVIQQAGNQGFEYFAFKTEENAFINTLAGRTSFLRALPDEVLANAYQISREQARQLKYNRQETIAL 521
Cdd:cd02243   81 LVVPQFFAVAKIAGEEGFEWVSFKTSDNPIFSELAGRTSVLRALPPEVLANSYNISPEEAKQLKSNREKETVL 153
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 366-509 2.16e-46

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: 158.98  E-value: 2.16e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564   366 ERADIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDQEVQQ 445
Cdd:smart00835   2 EPRPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVYDARLRE 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 266618564   446 GQLFIVPQNHGVIQQA-GNQGFEYFAFKTEENAFINTLAGRTSFLRALPDEVLANAYQISREQAR 509
Cdd:smart00835  82 GDVFVVPQGHPHFQVNsGDENLEFVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 360-509 2.44e-42

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: 148.25  E-value: 2.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564  360 ENIGNPERadIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARV-QVVNENGDAI 438
Cdd:pfam00190   1 LNLLEPGP--TYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVgFVVPGNGNRV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 266618564  439 LDQEVQQGQLFIVPQNHGVIQQAGNQ--GFEYFAFKTEENAFINTLAGRTSFLRALPDEVLANAYQISREQAR 509
Cdd:pfam00190  79 FHKVLREGDVFVVPQGLPHFQYNIGDepAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
cupin_7S_11S_C cd20285
7S and 11S seed storage globulin, C-terminal cupin domain; This family contains the C-terminal ...
 376-483 1.13e-20

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: 1.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 376 GRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDQEVQQGQLFIVPQNH 455
Cdd:cd20285    1 GNVTERTSNDFPILKSLNLLASSISLEEGAMFVPHYYSKAIVILVVNEGRAHIQVVGPKGYESYDAELSKGDVFVVPAAF 80

                         90       100
                 ....*....|....*....|....*....
gi 266618564 456 GVIQQAGNQGFEYFAFKT-EENAFINTLA 483
Cdd:cd20285   81 PVAIKSTSHNVEFTGFGTnANNNNRNLLA 109
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 370-508 1.16e-19

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: 85.72  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 370 IFSPRAGRISTLNSHNLPILRflRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNeNGDAILDQEVQQGQLF 449
Cdd:cd20306   12 FFESEGGSIRQATADQLPVLK--GLSIYRLRLSPGGIREPHWHPNANELGYVISGEARVSILD-PTGSLDTFTVKPGQVV 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 266618564 450 IVPQN--HgVIQQAGNQGFEYFA-FKTEENAFIntlaGRTSFLRALPDEVLANAYQISREQA 508
Cdd:cd20306   89 FIPQGwlH-WIENVGDEEAHLLIfFNHETPEDI----GLSDSLRATPPEVLGNTYGVDAFFA 145
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 20-292 2.58e-15

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 73.08  E-value: 2.58e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564    20 REPDNRIQAEAGQIETWNFNQGD-FQCAGVAASRITIQRNGLHLPSY-SNAPQLIYIVQGRGVLGAVFSGCpetfeesqq 97
Cdd:smart00835   1 LEPRPDFSNEGGRLREADPTNFPaLNGLGISAARVNLEPGGMLPPHYhPRATELLYVVRGEGRVGVVDPNG--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564    98 ssqqgrqqeqeqerqqqqqgeqgrqqgqqeqqqerqgrqqgrqqqeegrqqeqqqgqqgrpqqqqqfrqldRHQKTRRIR 177
Cdd:smart00835  72 -----------------------------------------------------------------------NKVYDARLR 80

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564   178 EGDVVAIPAGVAYWSYNDGDQELVAVNLFhvssdhnqLDQNPRKFYLAGNpenefnqqgqsqprqqgeqgrpgqhqqpfg 257
Cdd:smart00835  81 EGDVFVVPQGHPHFQVNSGDENLEFVAFN--------TNDPNRRFFLAGR------------------------------ 122

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 266618564   258 rprqqeqqgngNNVFSGFNTQLLAQALNVNEETAR 292
Cdd:smart00835 123 -----------NSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 19-230 3.13e-14

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: 70.06  E-value: 3.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564   19 AREPDNRIQAEAGQIETWNFNQ--GDFQCAGVAAsRITIQRNGLHLPSY-SNAPQLIYIVQGRGVLGAVFSGCPETfees 95
Cdd:pfam00190   3 LLEPGPTYNPEGGRVTTVNSKNlpGLNTLGISAA-RVDLAPGGMNPPHWhPNATEILYVLQGRGRVGFVVPGNGNR---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564   96 qqssqqgrqqeqeqerqqqqqgeqgrqqgqqeqqqerqgrqqgrqqqeegrqqeqqqgqqgrpqqqqqfrqlDRHQKtrr 175
Cdd:pfam00190  78 ------------------------------------------------------------------------VFHKV--- 82

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 266618564  176 IREGDVVAIPAGVAYWSYNDGDQELVAVNLFHVSSDHNQ--------------LDQNPRKFYLAGNPEN 230
Cdd:pfam00190  83 LREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQsilaggfsslpalpPEVLAKAFQLAGEEVK 151
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 376-506 8.14e-12

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: 62.88  E-value: 8.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 376 GRISTLNSHNLPILRflRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDqEVQQGQLFIVPQNH 455
Cdd:cd02240   11 GSVRIATVTNFPISK--DLSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRFETF-NLGAGDVGYVPSGS 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 266618564 456 G-VIQQAGNQGFEYF-AFKTEENAFIntlaGRTSFLRALPDEVLANAYQISRE 506
Cdd:cd02240   88 GhHIENIGDEDAEFLlIFDDGTFADV----SLPWWLAMTPEEVLAATLDLGKF 136
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 400-498 1.76e-10

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: 58.44  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 400 FFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDqEVQQGQLFIVPQNHG-VIQQAGNQGFEYFAFKTEENAF 478
Cdd:COG2140    9 VLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTV-DVGPGDVVYVPPGYGhYIINTGDEPLVFLAVFDDDAGS 87

                         90       100
                 ....*....|....*....|
gi 266618564 479 INTLAGRTSFLRALPDEVLA 498
Cdd:COG2140   88 DYGTISLSGWLAHTPPEVLA 107
cupin_7S_vicilin-like_C cd02245
7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal ...
 370-517 2.10e-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: 56.76  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 370 IFSPRAGRISTLNSHNLPILRFLRLsaerGFFYRN----GIYSPHWNVNAHSVVYVIRGNARVQVV-------NENGDAI 438
Cdd:cd02245    2 DFSNQYGWLYEADPEDYKQLKDLDV----GVSFVNitqgSMMAPHYNSRATEIAVVVEGEGYVEMVcphlssqSQQGEEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 439 LDQEVQQ-------GQLFIVPQNHGVIQQA-GNQGFEYFAFKTE-ENAFINTLAGRTSFLRALPDEVLANAYQISREQAR 509
Cdd:cd02245   78 GSGEYQKvrarlseGDVFVVPAGHPVAQVAsSNENLEFVGFGINaQNNERQFLAGKNNVLRQLDREAKELAFNVPAEEVE 157


                 ....*...
gi 266618564 510 QLKYNRQE 517
Cdd:cd02245  158 EVLNAQDE 165
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 363-512 4.90e-08

Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3.4) catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide (H2O2). It is widespread in fungi and various plant tissues and may play a role in plant signaling and defense. This enzyme has been employed in a widely used assay for detecting urinary oxalate levels. Also, the gene encoding OxOx from barley roots has been expressed in oilseed rape in order to provide a defense against externally supplied oxalic acid. In germin, the predominant protein produced during the early phase of wheat germination, it is believed that H2O2 production is employed as a defense mechanism in response to infection by pathogens. Germin is also a marker of growth onset in cell walls in germinating cereals. The H2O2 produced by OxOx, together with the Ca2+ released by degradation of calcium oxalate, are thought to mediate cell wall cross-linking at high concentrations. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380368  Cd Length: 191  Bit Score: 52.98  E-value: 4.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 363 GNPERADIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDQE 442
Cdd:cd02241   39 FLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLAPCGVNPPHTHPRATELLYVVEGTLYVGFVDENGNRLFTKT 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 443 VQQGQLFIVPQnhGVI--QQagNQGFE---YFAfkteenAFINTLAGRTSFLRAL-----PDEVLANAYQISREQARQLK 512
Cdd:cd02241  119 LNPGDVFVFPQ--GLIhfQF--NPGCEpavFVA------AFNSEDPGTQQIAQALfglppPDDVLAAAFGLDGAQVEKLK 188
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 404-516 1.33e-05

Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal cupin domain of oxalate decarboxylase (OxDC; EC 4.1.1.2), 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. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380439 [Multi-domain]  Cd Length: 153  Bit Score: 45.27  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 404 NGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDqEVQQGQLFIVPQNHG-VIQQAGNQGFEYF-AFKT---EENAF 478
Cdd:cd20305   44 GALRELHWHPNADEWQYYISGKARMTVFASGGRARTF-DFQAGDVGYVPRGYGhYIENTGDEPLEFLeVFNSgryQDISL 122

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 266618564 479 intlagrTSFLRALPDEVLANAYQISREQARQLKYNRQ 516
Cdd:cd20305  123 -------SQWLALTPPDLVAAHLGLPDDTIAKLPKKKQ 153
cupin_7S_vicilin-like_N cd02244
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ...
 172-289 1.35e-03

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: 39.80  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266618564 172 KTRRIREGDVVAIPAG-VAYWSYNDGDQELVAVNLFHVSSDhnqldqnprkfylagnpenefnqqgqsqprqqgeqGRPG 250
Cdd:cd02244   70 ESYNLERGDVYRIPAGsTFYLVNTDENEKLRIIALFDPVNS-----------------------------------LTPG 114

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 266618564 251 QHQQPFGRPRQqeqqgNGNNVFSGFNTQLLAQALNVNEE 289
Cdd:cd02244  115 PFQSFFGAGGQ-----NPESLLSGFSKEILEAAFNVSEE 148
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 170-206 1.58e-03

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 37.46  E-value: 1.58e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 266618564 170 HQKTRRIREGDVVAIPAGVAYWSYNDGDQELVAVNLF 206
Cdd:cd02208   37 DGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
YjlB COG4297
Uncharacterized conserved protein YjlB, cupin superfamily [Function unknown];
403-452 1.93e-03

Uncharacterized conserved protein YjlB, cupin superfamily [Function unknown];


Pssm-ID: 443438  Cd Length: 170  Bit Score: 39.09  E-value: 1.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 266618564 403 RNGIYS-PHWNVNAHSVVYVIRGNARVQVVNENGDAIldqEVQQGQLFIVP 452
Cdd:COG4297   58 RNGVFDyHHYHSTAHEVLGVASGSARLQLGGEGGREV---EVKAGDVLVLP 105
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
171-207 5.31e-03

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 36.75  E-value: 5.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 266618564 171 QKTRRIREGDVVAIPAGVAYWSYNDGDQELVAVNLFH 207
Cdd:COG1917   60 GEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVFS 96
cupin_YjlB-like cd02219
Bacillus subtilis YjlB and related proteins, cupin domain; This family includes bacterial and ...
 403-452 9.30e-03

Bacillus subtilis YjlB and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to YjlB, a Bacillus subtilis protein of unknown function with a cupin beta barrel fold. 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. 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: 380348  Cd Length: 154  Bit Score: 37.14  E-value: 9.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 266618564 403 RNGIYS-PHWNVNAHSVVYVIRGNARVQVVNENGDAIldqEVQQGQLFIVP 452
Cdd:cd02219   46 RNGIYDyHHYHSTTHEVLGVASGSATLQLGGPGGVEV---TVEAGDVVVLP 93
 
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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