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Conserved domains on  [gi|1002239619|ref|XP_015624048|]
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glutelin type-B 2-like [Oryza sativa Japonica Group]

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
 2-490 0e+00

glutelin; Provisional


:

Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 908.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619   2 TISVFSRFSIYFCVLLLCNGSMAQLFDPATNQWQTHRQGSFRECRFERLQAFEPLQNVRSEAGVTEYFDETNELFQCTGT 81
Cdd:PLN00212    1 ASSAFSRLSICFCVLLLCHGSMAQLFSQSTNPWQSPRQGSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNEQFQCTGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619  82 FVIRRVIQPQGLLIPRYANTPGMVYIIQGRGSMGLTFPGCPATYQQQSQQFLFQGESQSQKFIDEHQKIHQFRQGDIVVL 161
Cdd:PLN00212   81 FVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQFLTEGQSQSQKFRDEHQKIHQFRQGDVVAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 162 PTGVAHWFYNDGDTPVVALYVYDINNSANQLEPRHREFLLAGKNNRVQQVYGRSIQQHSGQNIFNGFSVEPLSEALNINT 241
Cdd:PLN00212  161 PAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNNRQQQVYGRSIEQHSGQNIFSGFSTELLSEALGINA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 242 VTTKRLQSQNDQRGEIIHVKNGLQLLKPTLTQ----RQEQEQAQYQEVQYSEKPQTSSRWNGLEENLCTIKTRLNIENPS 317
Cdd:PLN00212  241 QVAKRLQSQNDQRGEIIRVKNGLQLLQPTLTQqqeqAQQQQQRLYQQVQYQQSQQTSGRWNGLDENFCTIKVRLNIENPS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 318 RADSYDPRAGRITSLDSQKFPILNIIQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARVQVVSNFGKTVFDGVLRPE 397
Cdd:PLN00212  321 RADTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGKTVFNGVLRPG 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 398 QLLIIPQNYVVLKKAQHEGCQYIAINTNANAFVSHLAGVDSVFHALPVDVIANAYCISREEARRLKNNRGDEYGPFPPRL 477
Cdd:PLN00212  401 QLLIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRGDELGAFTPRF 480

                         490
                  ....*....|...
gi 1002239619 478 QQQIYPEFSNESK 490
Cdd:PLN00212  481 QQQSYQGFSNESE 493
 
Name Accession Description Interval E-value
PLN00212 PLN00212
glutelin; Provisional
 2-490 0e+00

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 908.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619   2 TISVFSRFSIYFCVLLLCNGSMAQLFDPATNQWQTHRQGSFRECRFERLQAFEPLQNVRSEAGVTEYFDETNELFQCTGT 81
Cdd:PLN00212    1 ASSAFSRLSICFCVLLLCHGSMAQLFSQSTNPWQSPRQGSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNEQFQCTGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619  82 FVIRRVIQPQGLLIPRYANTPGMVYIIQGRGSMGLTFPGCPATYQQQSQQFLFQGESQSQKFIDEHQKIHQFRQGDIVVL 161
Cdd:PLN00212   81 FVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQFLTEGQSQSQKFRDEHQKIHQFRQGDVVAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 162 PTGVAHWFYNDGDTPVVALYVYDINNSANQLEPRHREFLLAGKNNRVQQVYGRSIQQHSGQNIFNGFSVEPLSEALNINT 241
Cdd:PLN00212  161 PAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNNRQQQVYGRSIEQHSGQNIFSGFSTELLSEALGINA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 242 VTTKRLQSQNDQRGEIIHVKNGLQLLKPTLTQ----RQEQEQAQYQEVQYSEKPQTSSRWNGLEENLCTIKTRLNIENPS 317
Cdd:PLN00212  241 QVAKRLQSQNDQRGEIIRVKNGLQLLQPTLTQqqeqAQQQQQRLYQQVQYQQSQQTSGRWNGLDENFCTIKVRLNIENPS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 318 RADSYDPRAGRITSLDSQKFPILNIIQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARVQVVSNFGKTVFDGVLRPE 397
Cdd:PLN00212  321 RADTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGKTVFNGVLRPG 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 398 QLLIIPQNYVVLKKAQHEGCQYIAINTNANAFVSHLAGVDSVFHALPVDVIANAYCISREEARRLKNNRGDEYGPFPPRL 477
Cdd:PLN00212  401 QLLIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRGDELGAFTPRF 480

                         490
                  ....*....|...
gi 1002239619 478 QQQIYPEFSNESK 490
Cdd:PLN00212  481 QQQSYQGFSNESE 493
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
 47-262 8.49e-97

11S legumin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal domains of 11S legumin seed storage proteins that supply nutrition for seed germination, such as glycinin and legumin, including many common food allergens such as the peanut major allergen Ara h 3, almond allergen Pru du 6, Pecan allergen Car i 4, hazelnut nut allergen Cor a 9, Brazil nut allergen Ber e 2, cashew allergen Ana o 2, pistachio allergen Pis v 2/5, and walnut allergen Jug n/r 4. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). They are synthesized as propeptides in the endoplasmic reticulum and transported to the secretory vesicles as a homotrimer. The propeptides are processed as they are sorted in the secretory vesicles. The homotrimer binds another homotrimer to form a homohexamer with 32-point symmetry formed by a face-to-face stacking of the two trimers. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380369  Cd Length: 209  Bit Score: 291.03  E-value: 8.49e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619  47 FERLQAFEPLQNVRSEAGVTEYFDETNELFQCTGTFVIRRVIQPQGLLIPRYANTPGMVYIIQGRGSMGLTFPGCPATYq 126
Cdd:cd02242     1 LDRLPALEPTRRIESEGGSYEYWDPNNPQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGCPETF- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 127 qqsqQFLFQGESQSQKFIDEHQKIHQFRQGDIVVLPTGVAHWFYNDGDTPVVALYVYDINNSANQLEPRHREFLLAGKNN 206
Cdd:cd02242    80 ----QSSQQSQGQGQRFRDQHQKVRRIRKGDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNNANQLDGNFRRFFLAGNPQ 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002239619 207 RVQQvyGRSIQQHSGQNIFNGFSVEPLSEALNINTVTTKRLQSQNDQRGEIIHVKN 262
Cdd:cd02242   156 QEQQ--GQGQEQSGGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGLIVKVEE 209
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 317-460 3.50e-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: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 144.35  E-value: 3.50e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619  317 SRADSYDPRAGRITSLDSQKFPILNIIQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARVQVVSNFGKTVFDGVLRP 396
Cdd:smart00835   2 EPRPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVYDARLRE 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002239619  397 EQLLIIPQNYVVLKKA-QHEGCQYIAINTNANAFVSHLAGVDSVFHALPVDVIANAYCISREEAR 460
Cdd:smart00835  82 GDVFVVPQGHPHFQVNsGDENLEFVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 311-460 5.04e-39

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


Pssm-ID: 395138  Cd Length: 151  Bit Score: 139.01  E-value: 5.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 311 LNIENPSRadSYDPRAGRITSLDSQKFPILNIIQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARV-QVVSNFGKTV 389
Cdd:pfam00190   1 LNLLEPGP--TYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVgFVVPGNGNRV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002239619 390 FDGVLRPEQLLIIPQNYVVLKKAQH--EGCQYIAINTNANAFVSHLAGVDSVFHALPVDVIANAYCISREEAR 460
Cdd:pfam00190  79 FHKVLREGDVFVVPQGLPHFQYNIGdePAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
148-183 1.62e-06

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 46.38  E-value: 1.62e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1002239619 148 QKIHQFRQGDIVVLPTGVAHWFYNDGDTPVVALYVY 183
Cdd:COG1917    60 GEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVF 95
 
Name Accession Description Interval E-value
PLN00212 PLN00212
glutelin; Provisional
 2-490 0e+00

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 908.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619   2 TISVFSRFSIYFCVLLLCNGSMAQLFDPATNQWQTHRQGSFRECRFERLQAFEPLQNVRSEAGVTEYFDETNELFQCTGT 81
Cdd:PLN00212    1 ASSAFSRLSICFCVLLLCHGSMAQLFSQSTNPWQSPRQGSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNEQFQCTGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619  82 FVIRRVIQPQGLLIPRYANTPGMVYIIQGRGSMGLTFPGCPATYQQQSQQFLFQGESQSQKFIDEHQKIHQFRQGDIVVL 161
Cdd:PLN00212   81 FVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQFLTEGQSQSQKFRDEHQKIHQFRQGDVVAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 162 PTGVAHWFYNDGDTPVVALYVYDINNSANQLEPRHREFLLAGKNNRVQQVYGRSIQQHSGQNIFNGFSVEPLSEALNINT 241
Cdd:PLN00212  161 PAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNNRQQQVYGRSIEQHSGQNIFSGFSTELLSEALGINA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 242 VTTKRLQSQNDQRGEIIHVKNGLQLLKPTLTQ----RQEQEQAQYQEVQYSEKPQTSSRWNGLEENLCTIKTRLNIENPS 317
Cdd:PLN00212  241 QVAKRLQSQNDQRGEIIRVKNGLQLLQPTLTQqqeqAQQQQQRLYQQVQYQQSQQTSGRWNGLDENFCTIKVRLNIENPS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 318 RADSYDPRAGRITSLDSQKFPILNIIQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARVQVVSNFGKTVFDGVLRPE 397
Cdd:PLN00212  321 RADTYNPRAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGKTVFNGVLRPG 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 398 QLLIIPQNYVVLKKAQHEGCQYIAINTNANAFVSHLAGVDSVFHALPVDVIANAYCISREEARRLKNNRGDEYGPFPPRL 477
Cdd:PLN00212  401 QLLIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRGDELGAFTPRF 480

                         490
                  ....*....|...
gi 1002239619 478 QQQIYPEFSNESK 490
Cdd:PLN00212  481 QQQSYQGFSNESE 493
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
 47-262 8.49e-97

11S legumin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal domains of 11S legumin seed storage proteins that supply nutrition for seed germination, such as glycinin and legumin, including many common food allergens such as the peanut major allergen Ara h 3, almond allergen Pru du 6, Pecan allergen Car i 4, hazelnut nut allergen Cor a 9, Brazil nut allergen Ber e 2, cashew allergen Ana o 2, pistachio allergen Pis v 2/5, and walnut allergen Jug n/r 4. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). They are synthesized as propeptides in the endoplasmic reticulum and transported to the secretory vesicles as a homotrimer. The propeptides are processed as they are sorted in the secretory vesicles. The homotrimer binds another homotrimer to form a homohexamer with 32-point symmetry formed by a face-to-face stacking of the two trimers. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380369  Cd Length: 209  Bit Score: 291.03  E-value: 8.49e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619  47 FERLQAFEPLQNVRSEAGVTEYFDETNELFQCTGTFVIRRVIQPQGLLIPRYANTPGMVYIIQGRGSMGLTFPGCPATYq 126
Cdd:cd02242     1 LDRLPALEPTRRIESEGGSYEYWDPNNPQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGCPETF- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 127 qqsqQFLFQGESQSQKFIDEHQKIHQFRQGDIVVLPTGVAHWFYNDGDTPVVALYVYDINNSANQLEPRHREFLLAGKNN 206
Cdd:cd02242    80 ----QSSQQSQGQGQRFRDQHQKVRRIRKGDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNNANQLDGNFRRFFLAGNPQ 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002239619 207 RVQQvyGRSIQQHSGQNIFNGFSVEPLSEALNINTVTTKRLQSQNDQRGEIIHVKN 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 ...
 320-474 4.81e-75

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: 233.13  E-value: 4.81e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 320 DSYDPRAGRITSLDSQKFPILNIIQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARVQVVSNFGKTVFDGVLRPEQL 399
Cdd:cd02243     1 DVYVPRGGRITTLNSFKLPILRFVGLSAERVKLEPNAMFAPHWNANAHQVIYVTRGSGRVQVVGDNGKRVLDGEVREGQL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002239619 400 LIIPQNYVVLKKAQHEGCQYIAINTNANAFVSHLAGVDSVFHALPVDVIANAYCISREEARRLKNNRGDEYGPFP 474
Cdd:cd02243    81 LVVPQFFAVAKIAGEEGFEWVSFKTSDNPIFSELAGRTSVLRALPPEVLANSYNISPEEAKQLKSNREKETVLFP 155
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 317-460 3.50e-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: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 144.35  E-value: 3.50e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619  317 SRADSYDPRAGRITSLDSQKFPILNIIQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARVQVVSNFGKTVFDGVLRP 396
Cdd:smart00835   2 EPRPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVYDARLRE 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002239619  397 EQLLIIPQNYVVLKKA-QHEGCQYIAINTNANAFVSHLAGVDSVFHALPVDVIANAYCISREEAR 460
Cdd:smart00835  82 GDVFVVPQGHPHFQVNsGDENLEFVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 311-460 5.04e-39

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


Pssm-ID: 395138  Cd Length: 151  Bit Score: 139.01  E-value: 5.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 311 LNIENPSRadSYDPRAGRITSLDSQKFPILNIIQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARV-QVVSNFGKTV 389
Cdd:pfam00190   1 LNLLEPGP--TYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVgFVVPGNGNRV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002239619 390 FDGVLRPEQLLIIPQNYVVLKKAQH--EGCQYIAINTNANAFVSHLAGVDSVFHALPVDVIANAYCISREEAR 460
Cdd:pfam00190  79 FHKVLREGDVFVVPQGLPHFQYNIGdePAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 50-207 1.31e-22

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: 93.94  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619  50 LQAFEPLQNVRSEAGVTEYFDETNE--LFQCTGTFViRRVIQPQGLLIPRY-ANTPGMVYIIQGRGSMGLTFPGCPATyq 126
Cdd:pfam00190   1 LNLLEPGPTYNPEGGRVTTVNSKNLpgLNTLGISAA-RVDLAPGGMNPPHWhPNATEILYVLQGRGRVGFVVPGNGNR-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 127 qqsqqflfqgesqsqkfiDEHQKihqFRQGDIVVLPTGVAHWFYNDGDTPVVALYVYDINNSANQ--------------L 192
Cdd:pfam00190  78 ------------------VFHKV---LREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQsilaggfsslpalpP 136

                         170
                  ....*....|....*
gi 1002239619 193 EPRHREFLLAGKNNR 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 ...
 327-427 1.10e-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: 86.89  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 327 GRITSLDSQKFPILNIIQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARVQVVSNFGKTVFDGVLRPEQLLIIPQNY 406
Cdd:cd20285     1 GNVTERTSNDFPILKSLNLLASSISLEEGAMFVPHYYSKAIVILVVNEGRAHIQVVGPKGYESYDAELSKGDVFVVPAAF 80

                          90       100
                  ....*....|....*....|.
gi 1002239619 407 VVLKKAQHEGCQYIAINTNAN 427
Cdd:cd20285    81 PVAIKSTSHNVEFTGFGTNAN 101
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 53-240 6.75e-16

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: 74.62  E-value: 6.75e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619   53 FEPLQNVRSEAGVTEYFD-ETNELFQCTGTFVIRRVIQPQGLLIPRY-ANTPGMVYIIQGRGSMGLTFPGCpatyqqqsq 130
Cdd:smart00835   1 LEPRPDFSNEGGRLREADpTNFPALNGLGISAARVNLEPGGMLPPHYhPRATELLYVVRGEGRVGVVDPNG--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619  131 qflfqgesqsqkfidEHQKIHQFRQGDIVVLPTGVAHWFYNDGDTPVValYVYDINNSANqleprhREFLLAGKNnrvqq 210
Cdd:smart00835  72 ---------------NKVYDARLREGDVFVVPQGHPHFQVNSGDENLE--FVAFNTNDPN------RRFFLAGRN----- 123

                          170       180       190
                   ....*....|....*....|....*....|
gi 1002239619  211 vygrsiqqhsgqNIFNGFSVEPLSEALNIN 240
Cdd:smart00835 124 ------------SVLRGLPPEVLAAAFGVS 141
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 326-459 1.30e-11

Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues.


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 62.61  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 326 AGRITSLDSQKFPILNiiQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARVQVVSNFGKT-VFDgvLRPEQLLIIPQ 404
Cdd:cd20306    17 GGSIRQATADQLPVLK--GLSIYRLRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGSLdTFT--VKPGQVVFIPQ 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002239619 405 NYVvlkkaqH-------EGCQYIAINTNANAFVSHLAGVDSVFhalPVDVIANAYCISREEA 459
Cdd:cd20306    93 GWL------HwienvgdEEAHLLIFFNHETPEDIGLSDSLRAT---PPEVLGNTYGVDAFFA 145
cupin_7S_vicilin-like_C cd02245
7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal ...
 327-469 6.12e-07

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: 49.44  E-value: 6.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 327 GRITSLDSQKFPILNIIQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARVQVV----------SNFGKTV----FDG 392
Cdd:cd02245     8 GWLYEADPEDYKQLKDLDVGVSFVNITQGSMMAPHYNSRATEIAVVVEGEGYVEMVcphlssqsqqGEEEGSGeyqkVRA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 393 VLRPEQLLIIPQNY-VVLKKAQHEGCQYIAINTNA--NAFVsHLAGVDSVFHALPVDVIANAYCISREEARRLKNNRGDE 469
Cdd:cd02245    88 RLSEGDVFVVPAGHpVAQVASSNENLEFVGFGINAqnNERQ-FLAGKNNVLRQLDREAKELAFNVPAEEVEEVLNAQDES 166
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
148-183 1.62e-06

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 46.38  E-value: 1.62e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1002239619 148 QKIHQFRQGDIVVLPTGVAHWFYNDGDTPVVALYVY 183
Cdd:COG1917    60 GEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVF 95
cupin_7S_vicilin-like_N cd02244
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ...
 59-260 1.92e-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: 48.27  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619  59 VRSEAG---VTEYFDETNELFQCTGTFVIRrVIQ--PQGLLIPRYANTPGMVYIIQGRGSMGLtfpgcpatyqqqsqqfl 133
Cdd:cd02244     2 VRTEAGeirVLERFDGRSRLLRGIENYRLA-FITmePNTLFLPHHLDADMVFYVHTGRGTITW----------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 134 fqgesqsqkfIDEHQKI-HQFRQGDIVVLPTGVAHWFYNDGDTpvVALYVYDINNSANQLEP-RHREFLLAGKNNRvqqv 211
Cdd:cd02244    64 ----------VDEDKREsYNLERGDVYRIPAGSTFYLVNTDEN--EKLRIIALFDPVNSLTPgPFQSFFGAGGQNP---- 127

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1002239619 212 ygrsiqqhsgQNIFNGFSVEPLSEALNINTVTTKRLQSQNDQrGEIIHV 260
Cdd:cd02244   128 ----------ESLLSGFSKEILEAAFNVSEEELERLLSQQKP-GPIVKA 165
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 142-183 8.18e-06

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: 43.63  E-value: 8.18e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1002239619 142 KFIDEHQKIHQFRQGDIVVLPTGVAHWFYNDGDTPVVALYVY 183
Cdd:cd02208    32 ELTLDDGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 324-465 2.50e-05

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: 44.89  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 324 PRAGRITSLDSQKFPILNIIQMSATRVNLYQNAILTPfwnvnaHS------LMYVIRGRARVQVVSNFGKTVFDGVLRPE 397
Cdd:cd02241    49 PLGGSVTLANVANFPALNGLGISMARGDLAPCGVNPP------HThprateLLYVVEGTLYVGFVDENGNRLFTKTLNPG 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002239619 398 QLLIIPQNyvvlkkAQHegCQYIAINTNA---NAFVSHLAGVDSVFHAL-----PVDVIANAYCISREEARRLKNN 465
Cdd:cd02241   123 DVFVFPQG------LIH--FQFNPGCEPAvfvAAFNSEDPGTQQIAQALfglppPDDVLAAAFGLDGAQVEKLKSK 190
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 327-406 4.64e-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: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 327 GRITSLDSQKFPILNiiQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARVQVVSNFGkTVFDGVLRPEQLLIIPQNY 406
Cdd:cd02240    11 GSVRIATVTNFPISK--DLSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDG-RFETFNLGAGDVGYVPSGS 87
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 151-183 6.04e-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: 41.09  E-value: 6.04e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1002239619 151 HQFRQGDIVVLPTGVAHWFYNDGDTPVVALYVY 183
Cdd:pfam07883  39 VVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 324-406 7.55e-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: 42.96  E-value: 7.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619 324 PRAGRITSLDSQKFPIlnIIQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARVQVVSNFGKT-VFDgvLRPEQLLII 402
Cdd:cd20305    15 PAGGSVRIVDSKNFPI--STTIAAALVTLEPGALRELHWHPNADEWQYYISGKARMTVFASGGRArTFD--FQAGDVGYV 90


                  ....
gi 1002239619 403 PQNY 406
Cdd:cd20305    91 PRGY 94
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
149-182 1.46e-04

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 41.16  E-value: 1.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1002239619 149 KIHQFRQGDIVVLPTGVAHWFYNDGDTPVVALYV 182
Cdd:COG3837    68 EEYVLEPGDSVGFPAGVPHRLRNRGDEPARYLVV 101
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 87-184 3.20e-04

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 40.33  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239619  87 VIQPQGLLIPRY-ANTPGMVYIIQGRGSMGLTfpgcpatyqqqsqqflfqgESQSQKFIDEhqkihqFRQGDIVVLPTGV 165
Cdd:COG2140     9 VLEPGGVREEHWhPNAAEWYYVLSGEARMTVQ-------------------DPPGRARTVD------VGPGDVVYVPPGY 63

                          90
                  ....*....|....*....
gi 1002239619 166 AHWFYNDGDTPVVALYVYD 184
Cdd:COG2140    64 GHYIINTGDEPLVFLAVFD 82
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
149-183 4.92e-04

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 39.74  E-value: 4.92e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1002239619 149 KIHQFRQGDIVVLPTGVAHWFYNDGDTPVVALYVY 183
Cdd:COG0662    66 EEVELKAGDSVYIPAGVPHRLRNPGDEPLELLEVQ 100
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 149-177 2.07e-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: 36.83  E-value: 2.07e-03
                          10        20
                  ....*....|....*....|....*....
gi 1002239619 149 KIHQFRQGDIVVLPTGVAHWFYNDGDTPV 177
Cdd:cd06988    40 EREPVKAGDVVYIPPGTEHYVKNDGDEDF 68
 
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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