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Conserved domains on  [gi|573919041|ref|XP_006647142|]
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glutelin type-B 4-like [Oryza brachyantha]

Protein Classification

cupin domain-containing protein( domain architecture ID 11476485)

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PLN00212 PLN00212
glutelin; Provisional
 2-484 0e+00

glutelin; Provisional


:

Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 910.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041   2 ATTTFSRFSIYFCVLLLCHGSMAQLFSPTLNPWHSSRRGGSRDCRFDRLQAFEPLRRVRSEAGVTEYFDERNEQFQCTGT 81
Cdd:PLN00212   1 ASSAFSRLSICFCVLLLCHGSMAQLFSQSTNPWQSPRQGSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNEQFQCTGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041  82 FVIRRVIEPQGLLVPRYTNTPGVVYIMQGRGSMGLTFPGCPATYQQQFQQFLPEGQSQSQKFRDEHQKIHQFRQGDIVAL 161
Cdd:PLN00212  81 FVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQFLTEGQSQSQKFRDEHQKIHQFRQGDVVAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 162 PAGVAHWFYNEGDTPVVALYVFDINNSANQLEPRQKDFLLAGNNNREQQVYGRSIEKHSGQNIFSGFNHELLSEALGIST 241
Cdd:PLN00212 161 PAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNNRQQQVYGRSIEQHSGQNIFSGFSTELLSEALGINA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 242 LAAKRLQGQNDHRGEIIRVRNGLQLLKPTFTQ-----QQEQAQSQYQVQYSEKQQESTRCNGLDENFCTINARLNIENPS 316
Cdd:PLN00212 241 QVAKRLQSQNDQRGEIIRVKNGLQLLQPTLTQqqeqaQQQQQRLYQQVQYQQSQQTSGRWNGLDENFCTIKVRLNIENPS 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 317 RADTYNPRAGRITHLNNQKFPILNLVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARVQVVSNLGKTVFNSVLRPG 396
Cdd:PLN00212 321 RADTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGKTVFNGVLRPG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 397 QLLIIPQHYVVLKKAEREGCQYIAFKTNANSIVSQLAGKNSILRAMPVDVVANAYRISREQARDLKNNRGEELGAFTPKF 476
Cdd:PLN00212 401 QLLIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRGDELGAFTPRF 480


                 ....*...
gi 573919041 477 EQQSYPGL 484
Cdd:PLN00212 481 QQQSYQGF 488
 
Name Accession Description Interval E-value
PLN00212 PLN00212
glutelin; Provisional
 2-484 0e+00

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 910.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041   2 ATTTFSRFSIYFCVLLLCHGSMAQLFSPTLNPWHSSRRGGSRDCRFDRLQAFEPLRRVRSEAGVTEYFDERNEQFQCTGT 81
Cdd:PLN00212   1 ASSAFSRLSICFCVLLLCHGSMAQLFSQSTNPWQSPRQGSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNEQFQCTGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041  82 FVIRRVIEPQGLLVPRYTNTPGVVYIMQGRGSMGLTFPGCPATYQQQFQQFLPEGQSQSQKFRDEHQKIHQFRQGDIVAL 161
Cdd:PLN00212  81 FVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQFLTEGQSQSQKFRDEHQKIHQFRQGDVVAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 162 PAGVAHWFYNEGDTPVVALYVFDINNSANQLEPRQKDFLLAGNNNREQQVYGRSIEKHSGQNIFSGFNHELLSEALGIST 241
Cdd:PLN00212 161 PAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNNRQQQVYGRSIEQHSGQNIFSGFSTELLSEALGINA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 242 LAAKRLQGQNDHRGEIIRVRNGLQLLKPTFTQ-----QQEQAQSQYQVQYSEKQQESTRCNGLDENFCTINARLNIENPS 316
Cdd:PLN00212 241 QVAKRLQSQNDQRGEIIRVKNGLQLLQPTLTQqqeqaQQQQQRLYQQVQYQQSQQTSGRWNGLDENFCTIKVRLNIENPS 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 317 RADTYNPRAGRITHLNNQKFPILNLVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARVQVVSNLGKTVFNSVLRPG 396
Cdd:PLN00212 321 RADTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGKTVFNGVLRPG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 397 QLLIIPQHYVVLKKAEREGCQYIAFKTNANSIVSQLAGKNSILRAMPVDVVANAYRISREQARDLKNNRGEELGAFTPKF 476
Cdd:PLN00212 401 QLLIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRGDELGAFTPRF 480


                 ....*...
gi 573919041 477 EQQSYPGL 484
Cdd:PLN00212 481 QQQSYQGF 488
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
 47-262 2.57e-103

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: 307.59  E-value: 2.57e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041  47 FDRLQAFEPLRRVRSEAGVTEYFDERNEQFQCTGTFVIRRVIEPQGLLVPRYTNTPGVVYIMQGRGSMGLTFPGCPATYQ 126
Cdd:cd02242    1 LDRLPALEPTRRIESEGGSYEYWDPNNPQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGCPETFQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 127 QQFQQflpegQSQSQKFRDEHQKIHQFRQGDIVALPAGVAHWFYNEGDTPVVALYVFDINNSANQLEPRQKDFLLAGNNN 206
Cdd:cd02242   81 SSQQS-----QGQGQRFRDQHQKVRRIRKGDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNNANQLDGNFRRFFLAGNPQ 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 573919041 207 REQQvyGRSIEKHSGQNIFSGFNHELLSEALGISTLAAKRLQGQNDHRGEIIRVRN 262
Cdd:cd02242  156 QEQQ--GQGQEQSGGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGLIVKVEE 209
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 316-459 5.61e-43

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: 148.97  E-value: 5.61e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041   316 SRADTYNPRAGRITHLNNQKFPILNLVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARVQVVSNLGKTVFNSVLRP 395
Cdd:smart00835   2 EPRPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVYDARLRE 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 573919041   396 GQLLIIPQHYVVLKKA-EREGCQYIAFKTNANSIVSQLAGKNSILRAMPVDVVANAYRISREQAR 459
Cdd:smart00835  82 GDVFVVPQGHPHFQVNsGDENLEFVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 310-459 1.27e-41

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: 145.55  E-value: 1.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041  310 LNIENPSRadTYNPRAGRITHLNNQKFPILNLVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARV-QVVSNLGKTV 388
Cdd:pfam00190   1 LNLLEPGP--TYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVgFVVPGNGNRV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 573919041  389 FNSVLRPGQLLIIPQHYVVLKKA--EREGCQYIAFKTNANSIVSQLAGKNSILRAMPVDVVANAYRISREQAR 459
Cdd:pfam00190  79 FHKVLREGDVFVVPQGLPHFQYNigDEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
148-183 9.01e-07

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 47.15  E-value: 9.01e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 573919041 148 QKIHQFRQGDIVALPAGVAHWFYNEGDTPVVALYVF 183
Cdd:COG1917   60 GEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVF 95
 
Name Accession Description Interval E-value
PLN00212 PLN00212
glutelin; Provisional
 2-484 0e+00

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 910.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041   2 ATTTFSRFSIYFCVLLLCHGSMAQLFSPTLNPWHSSRRGGSRDCRFDRLQAFEPLRRVRSEAGVTEYFDERNEQFQCTGT 81
Cdd:PLN00212   1 ASSAFSRLSICFCVLLLCHGSMAQLFSQSTNPWQSPRQGSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNEQFQCTGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041  82 FVIRRVIEPQGLLVPRYTNTPGVVYIMQGRGSMGLTFPGCPATYQQQFQQFLPEGQSQSQKFRDEHQKIHQFRQGDIVAL 161
Cdd:PLN00212  81 FVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQFLTEGQSQSQKFRDEHQKIHQFRQGDVVAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 162 PAGVAHWFYNEGDTPVVALYVFDINNSANQLEPRQKDFLLAGNNNREQQVYGRSIEKHSGQNIFSGFNHELLSEALGIST 241
Cdd:PLN00212 161 PAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNNRQQQVYGRSIEQHSGQNIFSGFSTELLSEALGINA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 242 LAAKRLQGQNDHRGEIIRVRNGLQLLKPTFTQ-----QQEQAQSQYQVQYSEKQQESTRCNGLDENFCTINARLNIENPS 316
Cdd:PLN00212 241 QVAKRLQSQNDQRGEIIRVKNGLQLLQPTLTQqqeqaQQQQQRLYQQVQYQQSQQTSGRWNGLDENFCTIKVRLNIENPS 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 317 RADTYNPRAGRITHLNNQKFPILNLVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARVQVVSNLGKTVFNSVLRPG 396
Cdd:PLN00212 321 RADTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGKTVFNGVLRPG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 397 QLLIIPQHYVVLKKAEREGCQYIAFKTNANSIVSQLAGKNSILRAMPVDVVANAYRISREQARDLKNNRGEELGAFTPKF 476
Cdd:PLN00212 401 QLLIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRGDELGAFTPRF 480


                 ....*...
gi 573919041 477 EQQSYPGL 484
Cdd:PLN00212 481 QQQSYQGF 488
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
 47-262 2.57e-103

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: 307.59  E-value: 2.57e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041  47 FDRLQAFEPLRRVRSEAGVTEYFDERNEQFQCTGTFVIRRVIEPQGLLVPRYTNTPGVVYIMQGRGSMGLTFPGCPATYQ 126
Cdd:cd02242    1 LDRLPALEPTRRIESEGGSYEYWDPNNPQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGCPETFQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 127 QQFQQflpegQSQSQKFRDEHQKIHQFRQGDIVALPAGVAHWFYNEGDTPVVALYVFDINNSANQLEPRQKDFLLAGNNN 206
Cdd:cd02242   81 SSQQS-----QGQGQRFRDQHQKVRRIRKGDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNNANQLDGNFRRFFLAGNPQ 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 573919041 207 REQQvyGRSIEKHSGQNIFSGFNHELLSEALGISTLAAKRLQGQNDHRGEIIRVRN 262
Cdd:cd02242  156 QEQQ--GQGQEQSGGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGLIVKVEE 209
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
 319-473 1.74e-76

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: 1.74e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 319 DTYNPRAGRITHLNNQKFPILNLVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARVQVVSNLGKTVFNSVLRPGQL 398
Cdd:cd02243    1 DVYVPRGGRITTLNSFKLPILRFVGLSAERVKLEPNAMFAPHWNANAHQVIYVTRGSGRVQVVGDNGKRVLDGEVREGQL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 573919041 399 LIIPQHYVVLKKAEREGCQYIAFKTNANSIVSQLAGKNSILRAMPVDVVANAYRISREQARDLKNNRGEELGAFT 473
Cdd:cd02243   81 LVVPQFFAVAKIAGEEGFEWVSFKTSDNPIFSELAGRTSVLRALPPEVLANSYNISPEEAKQLKSNREKETVLFP 155
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 316-459 5.61e-43

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: 148.97  E-value: 5.61e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041   316 SRADTYNPRAGRITHLNNQKFPILNLVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARVQVVSNLGKTVFNSVLRP 395
Cdd:smart00835   2 EPRPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVYDARLRE 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 573919041   396 GQLLIIPQHYVVLKKA-EREGCQYIAFKTNANSIVSQLAGKNSILRAMPVDVVANAYRISREQAR 459
Cdd:smart00835  82 GDVFVVPQGHPHFQVNsGDENLEFVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 310-459 1.27e-41

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: 145.55  E-value: 1.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041  310 LNIENPSRadTYNPRAGRITHLNNQKFPILNLVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARV-QVVSNLGKTV 388
Cdd:pfam00190   1 LNLLEPGP--TYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVgFVVPGNGNRV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 573919041  389 FNSVLRPGQLLIIPQHYVVLKKA--EREGCQYIAFKTNANSIVSQLAGKNSILRAMPVDVVANAYRISREQAR 459
Cdd:pfam00190  79 FHKVLREGDVFVVPQGLPHFQYNigDEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 50-207 2.04e-26

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: 104.34  E-value: 2.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041   50 LQAFEPLRRVRSEAGVTEYFDERNEQ--FQCTGTFViRRVIEPQGLLVPRYT-NTPGVVYIMQGRGSMGLTFPGCPatyq 126
Cdd:pfam00190   1 LNLLEPGPTYNPEGGRVTTVNSKNLPglNTLGISAA-RVDLAPGGMNPPHWHpNATEILYVLQGRGRVGFVVPGNG---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041  127 qqfqqflpegqsqsqkFRDEHQKihqFRQGDIVALPAGVAHWFYNEGDTPVVALYVFDINNSANQ--------------L 192
Cdd:pfam00190  76 ----------------NRVFHKV---LREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQsilaggfsslpalpP 136

                         170
                  ....*....|....*
gi 573919041  193 EPRQKDFLLAGNNNR 207
Cdd:pfam00190 137 EVLAKAFQLAGEEVK 151
cupin_7S_11S_C cd20285
7S and 11S seed storage globulin, C-terminal cupin domain; This family contains the C-terminal ...
 326-426 1.41e-18

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: 81.12  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 326 GRITHLNNQKFPILNLVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARVQVVSNLGKTVFNSVLRPGQLLIIPQHY 405
Cdd:cd20285    1 GNVTERTSNDFPILKSLNLLASSISLEEGAMFVPHYYSKAIVILVVNEGRAHIQVVGPKGYESYDAELSKGDVFVVPAAF 80

                         90       100
                 ....*....|....*....|.
gi 573919041 406 VVLKKAEREGCQYIAFKTNAN 426
Cdd:cd20285   81 PVAIKSTSHNVEFTGFGTNAN 101
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 53-240 3.96e-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: 78.09  E-value: 3.96e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041    53 FEPLRRVRSEAGVTEYFD-ERNEQFQCTGTFVIRRVIEPQGLLVPRY-TNTPGVVYIMQGRGSMGLTFPGCpatyqqqfq 130
Cdd:smart00835   1 LEPRPDFSNEGGRLREADpTNFPALNGLGISAARVNLEPGGMLPPHYhPRATELLYVVRGEGRVGVVDPNG--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041   131 qflpegqsqsqkfrdEHQKIHQFRQGDIVALPAGVAHWFYNEGDTPVVALYvFDINNSANQleprqkdFLLAGNNnreqq 210
Cdd:smart00835  72 ---------------NKVYDARLREGDVFVVPQGHPHFQVNSGDENLEFVA-FNTNDPNRR-------FFLAGRN----- 123

                          170       180       190
                   ....*....|....*....|....*....|
gi 573919041   211 vygrsiekhsgqNIFSGFNHELLSEALGIS 240
Cdd:smart00835 124 ------------SVLRGLPPEVLAAAFGVS 141
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 325-458 6.34e-16

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: 74.94  E-value: 6.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 325 AGRITHLNNQKFPILNlvQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARVQVVSNlGKTVFNSVLRPGQLLIIPQ- 403
Cdd:cd20306   17 GGSIRQATADQLPVLK--GLSIYRLRLSPGGIREPHWHPNANELGYVISGEARVSILDP-TGSLDTFTVKPGQVVFIPQg 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 573919041 404 --HYVVlkKAEREGCQYIAFKTNANSIVSQLAGknsILRAMPVDVVANAYRISREQA 458
Cdd:cd20306   94 wlHWIE--NVGDEEAHLLIFFNHETPEDIGLSD---SLRATPPEVLGNTYGVDAFFA 145
cupin_7S_vicilin-like_C cd02245
7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal ...
 326-468 3.63e-10

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: 58.68  E-value: 3.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 326 GRITHLNNQKFPILNLVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARVQVV--------------SNLGKTVFNS 391
Cdd:cd02245    8 GWLYEADPEDYKQLKDLDVGVSFVNITQGSMMAPHYNSRATEIAVVVEGEGYVEMVcphlssqsqqgeeeGSGEYQKVRA 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 573919041 392 VLRPGQLLIIPQHYVVLKKAEREGC-QYIAFKTNA-NSIVSQLAGKNSILRAMPVDVVANAYRISREQARDLKNNRGEE 468
Cdd:cd02245   88 RLSEGDVFVVPAGHPVAQVASSNENlEFVGFGINAqNNERQFLAGKNNVLRQLDREAKELAFNVPAEEVEEVLNAQDES 166
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 314-464 1.51e-09

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: 57.61  E-value: 1.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 314 NPSRADTYNPRAGRITHLNNQKFPILNLVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGhaRVQV--VSNLGKTVFNS 391
Cdd:cd02241   40 LNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLAPCGVNPPHTHPRATELLYVVEG--TLYVgfVDENGNRLFTK 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 392 VLRPGQLLIIPQ---HYvvlkkaeregcQYIAFKTNANSIV---SQLAGKNSILRAM-----PVDVVANAYRISREQARD 460
Cdd:cd02241  118 TLNPGDVFVFPQgliHF-----------QFNPGCEPAVFVAafnSEDPGTQQIAQALfglppPDDVLAAAFGLDGAQVEK 186


                 ....
gi 573919041 461 LKNN 464
Cdd:cd02241  187 LKSK 190
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
148-183 9.01e-07

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 47.15  E-value: 9.01e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 573919041 148 QKIHQFRQGDIVALPAGVAHWFYNEGDTPVVALYVF 183
Cdd:COG1917   60 GEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVF 95
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 142-183 9.45e-07

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: 46.32  E-value: 9.45e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 573919041 142 KFRDEHQKIHQFRQGDIVALPAGVAHWFYNEGDTPVVALYVF 183
Cdd:cd02208   32 ELTLDDGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
cupin_7S_vicilin-like_N cd02244
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ...
 58-260 1.99e-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: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041  58 RVRSEAG---VTEYFDERNEQFQCTGTFvirRV----IEPQGLLVPRYTNTPGVVYIMQGRGSMGLTFPGcpatyqqqfq 130
Cdd:cd02244    1 VVRTEAGeirVLERFDGRSRLLRGIENY---RLafitMEPNTLFLPHHLDADMVFYVHTGRGTITWVDED---------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 131 qflpegqsqsqkfRDEHQKIhqfRQGDIVALPAGVAHWFYNEGDTpvVALYVFDINNSANQLEPRQ-KDFLLAGNNNReq 209
Cdd:cd02244   68 -------------KRESYNL---ERGDVYRIPAGSTFYLVNTDEN--EKLRIIALFDPVNSLTPGPfQSFFGAGGQNP-- 127

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 573919041 210 qvygrsiekhsgQNIFSGFNHELLSEALGISTLAAKRLQGQnDHRGEIIRV 260
Cdd:cd02244  128 ------------ESLLSGFSKEILEAAFNVSEEELERLLSQ-QKPGPIVKA 165
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
133-182 8.14e-06

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 45.01  E-value: 8.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 573919041 133 LPEGQSQSQKFRDEHQ-----------------KIHQFRQGDIVALPAGVAHWFYNEGDTPVVALYV 182
Cdd:COG3837   35 LPPGASSSPYHAHSAEeefvyvlegeltlriggEEYVLEPGDSVGFPAGVPHRLRNRGDEPARYLVV 101
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 323-465 1.32e-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: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 323 PRAGRITHLNNQKFPILnlVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARVQVVSNLGKT-VFNsvLRPGQLLII 401
Cdd:cd20305   15 PAGGSVRIVDSKNFPIS--TTIAAALVTLEPGALRELHWHPNADEWQYYISGKARMTVFASGGRArTFD--FQAGDVGYV 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 573919041 402 PQ---HYVvlkkaEREG---CQY-IAFKTNANSIVSqLagkNSILRAMPVDVVANAYRISREQARDLKNNR 465
Cdd:cd20305   91 PRgygHYI-----ENTGdepLEFlEVFNSGRYQDIS-L---SQWLALTPPDLVAAHLGLPDDTIAKLPKKK 152
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 87-200 3.00e-05

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: 43.42  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041  87 VIEPQGLLVPRY-TNTPGVVYIMQGRGSMGLtfpgcpatyqqqfqqFLPEGQsqsqkFRDEHqkihqFRQGDIVALPAGV 165
Cdd:COG2140    9 VLEPGGVREEHWhPNAAEWYYVLSGEARMTV---------------QDPPGR-----ARTVD-----VGPGDVVYVPPGY 63

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 573919041 166 AHWFYNEGDTPVVALYVFDINNSANQLEPRQKDFL 200
Cdd:COG2140   64 GHYIINTGDEPLVFLAVFDDDAGSDYGTISLSGWL 98
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 151-183 4.27e-05

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: 41.47  E-value: 4.27e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 573919041  151 HQFRQGDIVALPAGVAHWFYNEGDTPVVALYVF 183
Cdd:pfam07883  39 VVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 326-406 4.08e-04

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: 40.54  E-value: 4.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 326 GRITHLNNQKFPILNlvQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARVQVVSNLGkTVFNSVLRPGQLLIIPQ-- 403
Cdd:cd02240   11 GSVRIATVTNFPISK--DLSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDG-RFETFNLGAGDVGYVPSgs 87


                 ....
gi 573919041 404 -HYV 406
Cdd:cd02240   88 gHHI 91
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 351-448 7.85e-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: 7.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573919041 351 LYQNAILSPYWNVNAHSLVYMVQGHARVQVVSNLGKtVFNSVLRPGQLLIIPQ---HYVVlkKAEREGCQYIA-FKTNAN 426
Cdd:COG2140   10 LEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGR-ARTVDVGPGDVVYVPPgygHYII--NTGDEPLVFLAvFDDDAG 86

                         90       100
                 ....*....|....*....|..
gi 573919041 427 SIVSQLAGKNsILRAMPVDVVA 448
Cdd:COG2140   87 SDYGTISLSG-WLAHTPPEVLA 107
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 149-177 1.30e-03

Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380393 [Multi-domain]  Cd Length: 76  Bit Score: 37.60  E-value: 1.30e-03
                         10        20
                 ....*....|....*....|....*....
gi 573919041 149 KIHQFRQGDIVALPAGVAHWFYNEGDTPV 177
Cdd:cd06988   40 EREPVKAGDVVYIPPGTEHYVKNDGDEDF 68
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
149-183 1.49e-03

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 38.58  E-value: 1.49e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 573919041 149 KIHQFRQGDIVALPAGVAHWFYNEGDTPVVALYVF 183
Cdd:COG0662   66 EEVELKAGDSVYIPAGVPHRLRNPGDEPLELLEVQ 100
 
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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