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Conserved domains on  [gi|357470433|ref|XP_003605501|]
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glutelin type-D 1 [Medicago truncatula]

Protein Classification

11S seed storage family protein( domain architecture ID 14388877)

11S seed storage family protein is a bicupin domain-containing protein that supply nutrition for seed germination such as glycinin and legumin

CATH:  2.60.120.10
Gene Ontology:  GO:0045735
SCOP:  3001825

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
198-353 1.90e-77

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


:

Pssm-ID: 380370  Cd Length: 155  Bit Score: 234.68  E-value: 1.90e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433 198 DVDIKNGGRVVVLNTKNLPLVGEVGLGADLVRIDGRSMCSPGFSCdSALQVTYIVRGSGRVQVVGVDGKRVLETTLKAGD 277
Cdd:cd02243    1 DVYVPRGGRITTLNSFKLPILRFVGLSAERVKLEPNAMFAPHWNA-NAHQVIYVTRGSGRVQVVGDNGKRVLDGEVREGQ 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357470433 278 LFIVPRFFVVSKIADNDGMEWFSIITTPNPVFTHMAGSSSVWKALSPTVLQAAFNVDPEVEKLFRSKRTADAIFFP 353
Cdd:cd02243   80 LLVVPQFFAVAKIAGEEGFEWVSFKTSDNPIFSELAGRTSVLRALPPEVLANSYNISPEEAKQLKSNREKETVLFP 155
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
4-173 4.83e-71

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: 220.53  E-value: 4.83e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433   4 NLSPQLAKKVYGGDGGSYYAWSPSElPMLREGNIGAAKLALEKNGFAVPRYSDSSKVAYVLQGSGVAGIVLPE------- 76
Cdd:cd02242    3 RLPALEPTRRIESEGGSYEYWDPNN-PQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGcpetfqs 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433  77 -------------SKEKVVAIKEGDALALPFGVVTWWYNKEDTELVVLFLGDTSK--AHKAGEFTDFFLTG--------- 132
Cdd:cd02242   82 sqqsqgqgqrfrdQHQKVRRIRKGDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNnaNQLDGNFRRFFLAGnpqqeqqgq 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 357470433 133 ------PNGIFTGFSTEFVGRAWDLDENNVKTLVGKQSAKG-IVKLDG 173
Cdd:cd02242  162 gqeqsgGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGlIVKVEE 209
 
Name Accession Description Interval E-value
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
198-353 1.90e-77

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


Pssm-ID: 380370  Cd Length: 155  Bit Score: 234.68  E-value: 1.90e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433 198 DVDIKNGGRVVVLNTKNLPLVGEVGLGADLVRIDGRSMCSPGFSCdSALQVTYIVRGSGRVQVVGVDGKRVLETTLKAGD 277
Cdd:cd02243    1 DVYVPRGGRITTLNSFKLPILRFVGLSAERVKLEPNAMFAPHWNA-NAHQVIYVTRGSGRVQVVGDNGKRVLDGEVREGQ 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357470433 278 LFIVPRFFVVSKIADNDGMEWFSIITTPNPVFTHMAGSSSVWKALSPTVLQAAFNVDPEVEKLFRSKRTADAIFFP 353
Cdd:cd02243   80 LLVVPQFFAVAKIAGEEGFEWVSFKTSDNPIFSELAGRTSVLRALPPEVLANSYNISPEEAKQLKSNREKETVLFP 155
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
4-173 4.83e-71

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: 220.53  E-value: 4.83e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433   4 NLSPQLAKKVYGGDGGSYYAWSPSElPMLREGNIGAAKLALEKNGFAVPRYSDSSKVAYVLQGSGVAGIVLPE------- 76
Cdd:cd02242    3 RLPALEPTRRIESEGGSYEYWDPNN-PQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGcpetfqs 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433  77 -------------SKEKVVAIKEGDALALPFGVVTWWYNKEDTELVVLFLGDTSK--AHKAGEFTDFFLTG--------- 132
Cdd:cd02242   82 sqqsqgqgqrfrdQHQKVRRIRKGDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNnaNQLDGNFRRFFLAGnpqqeqqgq 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 357470433 133 ------PNGIFTGFSTEFVGRAWDLDENNVKTLVGKQSAKG-IVKLDG 173
Cdd:cd02242  162 gqeqsgGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGlIVKVEE 209
PLN00212 PLN00212
glutelin; Provisional
41-354 5.35e-43

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 155.36  E-value: 5.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433  41 KLALEKNGFAVPRYSDSSKVAYVLQGSGVAGIVLP-------------------------ESKEKVVAIKEGDALALPFG 95
Cdd:PLN00212  84 RRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPgcpatyqqqfqqfltegqsqsqkfrDEHQKIHQFRQGDVVALPAG 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433  96 VVTWWYNKEDTELVVLFLGDTSKAHKAGE--FTDFFLTGPN-----------------GIFTGFSTEFVGRAWDLDENNV 156
Cdd:PLN00212 164 VAHWFYNDGDAPVVALYVYDINNNANQLEprQREFLLAGNNnrqqqvygrsieqhsgqNIFSGFSTELLSEALGINAQVA 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433 157 KTLVGKQSAKG-IVKLDGKISLPQP-------------------IEEHKKGMALNC----------------LEAPLDVD 200
Cdd:PLN00212 244 KRLQSQNDQRGeIIRVKNGLQLLQPtltqqqeqaqqqqqrlyqqVQYQQSQQTSGRwngldenfctikvrlnIENPSRAD 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433 201 IKN--GGRVVVLNTKNLPLVGEVGLGADLVRIDGRSMCSPgFSCDSALQVTYIVRGSGRVQVVGVDGKRVLETTLKAGDL 278
Cdd:PLN00212 324 TYNprAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSP-FWNVNAHSVVYITQGRARVQVVSNNGKTVFNGVLRPGQL 402
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357470433 279 FIVPRFFVVSKIADNDGMEWFSIITTPNPVFTHMAGSSSVWKALSPTVLQAAFNVDPEVEKLFRSKRTADAIFFPP 354
Cdd:PLN00212 403 LIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRGDELGAFTP 478
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
11-157 4.02e-30

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: 112.37  E-value: 4.02e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433    11 KKVYGGDGGSYYAWSPSELPMLREGNIGAAKLALEKNGFAVPRY-SDSSKVAYVLQGSGVAGIVLPESKEKVVA-IKEGD 88
Cdd:smart00835   4 RPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYhPRATELLYVVRGEGRVGVVDPNGNKVYDArLREGD 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357470433    89 ALALPFGVVTWWYNKEDTELVVLFLGDTSKAHKageftdFFLTGPNGIFTGFSTEFVGRAWDLDENNVK 157
Cdd:smart00835  84 VFVVPQGHPHFQVNSGDENLEFVAFNTNDPNRR------FFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
190-339 1.39e-28

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: 108.58  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433  190 LNCLEaPLDVDIKNGGRVVVLNTKNLPLVGEVGLGADLVRIDGRSMCSPGFSCdSALQVTYIVRGSGRV-QVVGVDGKRV 268
Cdd:pfam00190   1 LNLLE-PGPTYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHP-NATEILYVLQGRGRVgFVVPGNGNRV 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357470433  269 LETTLKAGDLFIVPRFFVVSKIA--DNDGMEWFSIITTPNPVFTHMAGSSSVWKALSPTVLQAAFNVDPEVEK 339
Cdd:pfam00190  79 FHKVLREGDVFVVPQGLPHFQYNigDEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
10-157 2.38e-25

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: 99.72  E-value: 2.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433   10 AKKVYGGDGGSYYAWSPSELPMLREGNIGAAKLALEKNGFAVPRY-SDSSKVAYVLQGSGVAGIVLPESKEKVVA--IKE 86
Cdd:pfam00190   6 PGPTYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWhPNATEILYVLQGRGRVGFVVPGNGNRVFHkvLRE 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357470433   87 GDALALPFGVVTWWYNKEDTELVVLFLGDTSKAHKAGEFtdfflTGPNGIFTGFSTEFVGRAWDLDENNVK 157
Cdd:pfam00190  86 GDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSIL-----AGGFSSLPALPPEVLAKAFQLAGEEVK 151
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
203-336 4.82e-24

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


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 96.20  E-value: 4.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433   203 NGGRVVVLNTKNLPLVGEVGLGADLVRIDGRSMCSPGFSCDSAlQVTYIVRGSGRVQVVGVDGKRVLETTLKAGDLFIVP 282
Cdd:smart00835  10 EGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRAT-ELLYVVRGEGRVGVVDPNGNKVYDARLREGDVFVVP 88
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 357470433   283 RFFVVSKIA-DNDGMEWFSIITTPNPVFTHMAGSSSVWKALSPTVLQAAFNVDPE 336
Cdd:smart00835  89 QGHPHFQVNsGDENLEFVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAE 143
 
Name Accession Description Interval E-value
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
198-353 1.90e-77

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


Pssm-ID: 380370  Cd Length: 155  Bit Score: 234.68  E-value: 1.90e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433 198 DVDIKNGGRVVVLNTKNLPLVGEVGLGADLVRIDGRSMCSPGFSCdSALQVTYIVRGSGRVQVVGVDGKRVLETTLKAGD 277
Cdd:cd02243    1 DVYVPRGGRITTLNSFKLPILRFVGLSAERVKLEPNAMFAPHWNA-NAHQVIYVTRGSGRVQVVGDNGKRVLDGEVREGQ 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357470433 278 LFIVPRFFVVSKIADNDGMEWFSIITTPNPVFTHMAGSSSVWKALSPTVLQAAFNVDPEVEKLFRSKRTADAIFFP 353
Cdd:cd02243   80 LLVVPQFFAVAKIAGEEGFEWVSFKTSDNPIFSELAGRTSVLRALPPEVLANSYNISPEEAKQLKSNREKETVLFP 155
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
4-173 4.83e-71

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: 220.53  E-value: 4.83e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433   4 NLSPQLAKKVYGGDGGSYYAWSPSElPMLREGNIGAAKLALEKNGFAVPRYSDSSKVAYVLQGSGVAGIVLPE------- 76
Cdd:cd02242    3 RLPALEPTRRIESEGGSYEYWDPNN-PQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGVVFPGcpetfqs 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433  77 -------------SKEKVVAIKEGDALALPFGVVTWWYNKEDTELVVLFLGDTSK--AHKAGEFTDFFLTG--------- 132
Cdd:cd02242   82 sqqsqgqgqrfrdQHQKVRRIRKGDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNnaNQLDGNFRRFFLAGnpqqeqqgq 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 357470433 133 ------PNGIFTGFSTEFVGRAWDLDENNVKTLVGKQSAKG-IVKLDG 173
Cdd:cd02242  162 gqeqsgGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGlIVKVEE 209
PLN00212 PLN00212
glutelin; Provisional
41-354 5.35e-43

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 155.36  E-value: 5.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433  41 KLALEKNGFAVPRYSDSSKVAYVLQGSGVAGIVLP-------------------------ESKEKVVAIKEGDALALPFG 95
Cdd:PLN00212  84 RRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPgcpatyqqqfqqfltegqsqsqkfrDEHQKIHQFRQGDVVALPAG 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433  96 VVTWWYNKEDTELVVLFLGDTSKAHKAGE--FTDFFLTGPN-----------------GIFTGFSTEFVGRAWDLDENNV 156
Cdd:PLN00212 164 VAHWFYNDGDAPVVALYVYDINNNANQLEprQREFLLAGNNnrqqqvygrsieqhsgqNIFSGFSTELLSEALGINAQVA 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433 157 KTLVGKQSAKG-IVKLDGKISLPQP-------------------IEEHKKGMALNC----------------LEAPLDVD 200
Cdd:PLN00212 244 KRLQSQNDQRGeIIRVKNGLQLLQPtltqqqeqaqqqqqrlyqqVQYQQSQQTSGRwngldenfctikvrlnIENPSRAD 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433 201 IKN--GGRVVVLNTKNLPLVGEVGLGADLVRIDGRSMCSPgFSCDSALQVTYIVRGSGRVQVVGVDGKRVLETTLKAGDL 278
Cdd:PLN00212 324 TYNprAGRITRLNSQKFPILNLIQMSATRVNLYQNALLSP-FWNVNAHSVVYITQGRARVQVVSNNGKTVFNGVLRPGQL 402
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357470433 279 FIVPRFFVVSKIADNDGMEWFSIITTPNPVFTHMAGSSSVWKALSPTVLQAAFNVDPEVEKLFRSKRTADAIFFPP 354
Cdd:PLN00212 403 LIIPQHYAVLKKAEREGCQYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRGDELGAFTP 478
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
11-157 4.02e-30

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: 112.37  E-value: 4.02e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433    11 KKVYGGDGGSYYAWSPSELPMLREGNIGAAKLALEKNGFAVPRY-SDSSKVAYVLQGSGVAGIVLPESKEKVVA-IKEGD 88
Cdd:smart00835   4 RPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYhPRATELLYVVRGEGRVGVVDPNGNKVYDArLREGD 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357470433    89 ALALPFGVVTWWYNKEDTELVVLFLGDTSKAHKageftdFFLTGPNGIFTGFSTEFVGRAWDLDENNVK 157
Cdd:smart00835  84 VFVVPQGHPHFQVNSGDENLEFVAFNTNDPNRR------FFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
190-339 1.39e-28

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: 108.58  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433  190 LNCLEaPLDVDIKNGGRVVVLNTKNLPLVGEVGLGADLVRIDGRSMCSPGFSCdSALQVTYIVRGSGRV-QVVGVDGKRV 268
Cdd:pfam00190   1 LNLLE-PGPTYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHP-NATEILYVLQGRGRVgFVVPGNGNRV 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357470433  269 LETTLKAGDLFIVPRFFVVSKIA--DNDGMEWFSIITTPNPVFTHMAGSSSVWKALSPTVLQAAFNVDPEVEK 339
Cdd:pfam00190  79 FHKVLREGDVFVVPQGLPHFQYNigDEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
10-157 2.38e-25

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: 99.72  E-value: 2.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433   10 AKKVYGGDGGSYYAWSPSELPMLREGNIGAAKLALEKNGFAVPRY-SDSSKVAYVLQGSGVAGIVLPESKEKVVA--IKE 86
Cdd:pfam00190   6 PGPTYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWhPNATEILYVLQGRGRVGFVVPGNGNRVFHkvLRE 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357470433   87 GDALALPFGVVTWWYNKEDTELVVLFLGDTSKAHKAGEFtdfflTGPNGIFTGFSTEFVGRAWDLDENNVK 157
Cdd:pfam00190  86 GDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSIL-----AGGFSSLPALPPEVLAKAFQLAGEEVK 151
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
203-336 4.82e-24

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


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 96.20  E-value: 4.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433   203 NGGRVVVLNTKNLPLVGEVGLGADLVRIDGRSMCSPGFSCDSAlQVTYIVRGSGRVQVVGVDGKRVLETTLKAGDLFIVP 282
Cdd:smart00835  10 EGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRAT-ELLYVVRGEGRVGVVDPNGNKVYDARLREGDVFVVP 88
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 357470433   283 RFFVVSKIA-DNDGMEWFSIITTPNPVFTHMAGSSSVWKALSPTVLQAAFNVDPE 336
Cdd:smart00835  89 QGHPHFQVNsGDENLEFVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAE 143
cupin_7S_vicilin-like_C cd02245
7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal ...
245-345 2.32e-12

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: 64.46  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433 245 ALQVTYIVRGSGRVQVVGVDGK--------------RVLETTLKAGDLFIVPRFFVVSKIADNDG---MEWFSIITTPN- 306
Cdd:cd02245   47 ATEIAVVVEGEGYVEMVCPHLSsqsqqgeeegsgeyQKVRARLSEGDVFVVPAGHPVAQVASSNEnleFVGFGINAQNNe 126
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 357470433 307 PVFthMAGSSSVWKALSPTVLQAAFNVDP-EVEKLFRSKR 345
Cdd:cd02245  127 RQF--LAGKNNVLRQLDREAKELAFNVPAeEVEEVLNAQD 164
cupin_7S_vicilin-like_N cd02244
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ...
44-171 3.48e-11

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: 61.37  E-value: 3.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433  44 LEKNGFAVPRYSDSSKVAYVLQGSGVAGIVLPESKEKVVaIKEGDALALPFGVVTWWYNKEDTE---LVVLFlgDTSKAH 120
Cdd:cd02244   35 MEPNTLFLPHHLDADMVFYVHTGRGTITWVDEDKRESYN-LERGDVYRIPAGSTFYLVNTDENEklrIIALF--DPVNSL 111
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 357470433 121 KAGEFTDFFLTG---PNGIFTGFSTEFVGRAWDLDENNVKTLVGKQSAKGIVKL 171
Cdd:cd02244  112 TPGPFQSFFGAGgqnPESLLSGFSKEILEAAFNVSEEELERLLSQQKPGPIVKA 165
cupin_7S_11S_C cd20285
7S and 11S seed storage globulin, C-terminal cupin domain; This family contains the C-terminal ...
205-306 1.17e-10

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: 58.00  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433 205 GRVVVLNTKNLPLVGEVGLGADLVRIDGRSMCSPGFSCDSALqVTYIVRGSGRVQVVGVDGKRVLETTLKAGDLFIVPRF 284
Cdd:cd20285    1 GNVTERTSNDFPILKSLNLLASSISLEEGAMFVPHYYSKAIV-ILVVNEGRAHIQVVGPKGYESYDAELSKGDVFVVPAA 79
                         90       100
                 ....*....|....*....|..
gi 357470433 285 FVVSKIADNDGMEWFSIITTPN 306
Cdd:cd20285   80 FPVAIKSTSHNVEFTGFGTNAN 101
cupin_7S_vicilin-like_N cd02244
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ...
250-345 4.42e-08

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: 52.51  E-value: 4.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433 250 YIVRGSGRVQVVGVDGKRvlETTLKAGDLFIVPR---FFVVSkiadNDGMEWFSII--------TTPNPV--FTHMAGS- 315
Cdd:cd02244   53 YVHTGRGTITWVDEDKRE--SYNLERGDVYRIPAgstFYLVN----TDENEKLRIIalfdpvnsLTPGPFqsFFGAGGQn 126
                         90       100       110
                 ....*....|....*....|....*....|..
gi 357470433 316 -SSVWKALSPTVLQAAFNVDPE-VEKLFRSKR 345
Cdd:cd02244  127 pESLLSGFSKEILEAAFNVSEEeLERLLSQQK 158
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
244-344 6.53e-07

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: 48.36  E-value: 6.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433 244 SALQVTYIVRGSGRVQVVGVDGKrVLETTLKAGDLFIVPR--FFVVSKIADnDGMEWFSIITTPNPVFthmAGSSSVWKA 321
Cdd:cd20306   54 NANELGYVISGEARVSILDPTGS-LDTFTVKPGQVVFIPQgwLHWIENVGD-EEAHLLIFFNHETPED---IGLSDSLRA 128
                         90       100
                 ....*....|....*....|...
gi 357470433 322 LSPTVLQAAFNVDPEVEKLFRSK 344
Cdd:cd20306  129 TPPEVLGNTYGVDAFFAAPAFPT 151
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
204-344 1.84e-03

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: 38.23  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357470433 204 GGRVVVLNTKNLPLVGevGLGADLVRIDGRSMCSPGFSCDSAlQVTYIVRGSGRVQVVGVDGkRVLETTLKAGDLFIVPR 283
Cdd:cd02240   10 GGSVRIATVTNFPISK--DLSSALVRVAPGAMRELHWHPNTA-EWQYVISGSARVTVFDEDG-RFETFNLGAGDVGYVPS 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357470433 284 FFV--VSKIADNDGmewFSIITTPNPVFTHMAGSSSVwKALSPTVLQAAFNVDPEVEKLFRSK 344
Cdd:cd02240   86 GSGhhIENIGDEDA---EFLLIFDDGTFADVSLPWWL-AMTPEEVLAATLDLGKFIDALPKAK 144
 
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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