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Conserved domains on  [gi|641755681|ref|XP_008164253|]
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uncharacterized LOC101935274 isoform X1 [Chrysemys picta bellii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 153-251 8.57e-24

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


The actual alignment was detected with superfamily member cd20306:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 151  Bit Score: 97.28  E-value: 8.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 153 LRIKSKGLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSiVTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLFLLFFtTHEE 232
Cdd:cd20306   39 LRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGS-LDTFTVKPGQVVFIPQGWLHWIENVGDEEAHLLIFF-NHET 116

                         90
                 ....*....|....*....
gi 641755681 233 LQTLDVDDVFFSTPEDIAA 251
Cdd:cd20306  117 PEDIGLSDSLRATPPEVLG 135
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 353-453 4.29e-19

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


The actual alignment was detected with superfamily member cd20306:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 151  Bit Score: 83.79  E-value: 4.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 353 IRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITTDFDIGIGDVVFFPIGTQHYIKSTCDEDLLMILAFSTGNQl 432
Cdd:cd20306   39 LRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGSLDTFTVKPGQVVFIPQGWLHWIENVGDEEAHLLIFFNHETP- 117

                         90       100
                 ....*....|....*....|.
gi 641755681 433 QTLDMDDYFHATADHILAQLF 453
Cdd:cd20306  118 EDIGLSDSLRATPPEVLGNTY 138
CLLAC pfam15675
CLLAC-motif containing domain; This short domain is found in chordates. It carries a highly ...
 34-62 2.84e-09

CLLAC-motif containing domain; This short domain is found in chordates. It carries a highly conserved CLLAC sequence motif. The function is not known.


:

Pssm-ID: 434849  Cd Length: 30  Bit Score: 52.40  E-value: 2.84e-09
                          10        20
                  ....*....|....*....|....*....
gi 641755681   34 WSLMNIFLVCLLACFISTIIGVLIISSVY 62
Cdd:pfam15675   2 WSLWKIFLVCLLACLIATAIGVLILSLVY 30
 
Name Accession Description Interval E-value
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 153-251 8.57e-24

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: 97.28  E-value: 8.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 153 LRIKSKGLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSiVTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLFLLFFtTHEE 232
Cdd:cd20306   39 LRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGS-LDTFTVKPGQVVFIPQGWLHWIENVGDEEAHLLIFF-NHET 116

                         90
                 ....*....|....*....
gi 641755681 233 LQTLDVDDVFFSTPEDIAA 251
Cdd:cd20306  117 PEDIGLSDSLRATPPEVLG 135
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 112-426 1.20e-22

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


Pssm-ID: 274565 [Multi-domain]  Cd Length: 367  Bit Score: 99.32  E-value: 1.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  112 FPGGdiqWARfRYDVKDYPSDEEMefgTSINnqrskmtfgtLRIKSKGLRAPHWHFNAnEHGFLLKGSAWIGVVDAGGSi 191
Cdd:TIGR03404  48 ENGG---WAR-EVTVRDLPISTAI---AGVN----------MRLEPGAIRELHWHKEA-EWAYVLYGSCRITAVDENGR- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  192 VTTYNVTAGQVIFFPKNTLHWVKNVgEDDCLFLLFFT--THEELQTLDVDDVFFSTPEDIAARSLkpqgGVNfIRTFKKQ 269
Cdd:TIGR03404 109 NYIDDVGAGDLWYFPPGIPHSLQGL-DEGCEFLLVFDdgNFSEDGTFLVTDWLAHTPKDVLAKNF----GVP-ESAFDNL 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  270 TEDQAI----NLPPNLvelvqNASYVQSPDKLVWR-YFYNLKDSTEFKLSGGVIQWARFRkngvglndNEKIfseslqmh 344
Cdd:TIGR03404 183 PLKELYifpgTVPGPL-----DEEAVTGPAGEVPGpFTYHLSEQKPKQVPGGTVRIADST--------NFPV-------- 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  345 enSLTLAT--IRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITTDFDIGIGDVVFFPIGTQHYIKSTCDEDLLM 422
Cdd:TIGR03404 242 --SKTIAAaiVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVF 319


                  ....
gi 641755681  423 ILAF 426
Cdd:TIGR03404 320 LEVF 323
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 147-253 1.64e-19

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: 83.86  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 147 KMTFGTLRIKSKGLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSIVTtYNVTAGQVIFFPKNTLHWVKNVGEDDCLFLLF 226
Cdd:COG2140    2 TLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRART-VDVGPGDVVYVPPGYGHYIINTGDEPLVFLAV 80

                         90       100
                 ....*....|....*....|....*....
gi 641755681 227 FTTH--EELQTLDVDDVFFSTPEDIAARS 253
Cdd:COG2140   81 FDDDagSDYGTISLSGWLAHTPPEVLAVD 109
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 353-453 4.29e-19

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


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 83.79  E-value: 4.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 353 IRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITTDFDIGIGDVVFFPIGTQHYIKSTCDEDLLMILAFSTGNQl 432
Cdd:cd20306   39 LRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGSLDTFTVKPGQVVFIPQGWLHWIENVGDEEAHLLIFFNHETP- 117

                         90       100
                 ....*....|....*....|.
gi 641755681 433 QTLDMDDYFHATADHILAQLF 453
Cdd:cd20306  118 EDIGLSDSLRATPPEVLGNTY 138
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 144-254 1.81e-18

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: 81.94  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681   144 QRSKMTFGTLRIKSKGLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSIVTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLF 223
Cdd:smart00835  26 NGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVYDARLREGDVFVVPQGHPHFQVNSGDENLEF 105

                           90       100       110
                   ....*....|....*....|....*....|...
gi 641755681   224 LLFFTTHEELQTLDV--DDVFFSTPEDIAARSL 254
Cdd:smart00835 106 VAFNTNDPNRRFFLAgrNSVLRGLPPEVLAAAF 138
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 348-454 4.36e-18

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: 80.84  E-value: 4.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  348 LTLATIRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITTDFD--IGIGDVVFFPIGTQHYIKSTCDEDLLMILA 425
Cdd:pfam00190  33 ISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVGFVVPGNGNRVFHkvLREGDVFVVPQGLPHFQYNIGDEPAVAFVA 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 641755681  426 FST---GNQLQTLDMDDYFHATADHILAQLFF 454
Cdd:pfam00190 113 FDTnnpGNQSILAGGFSSLPALPPEVLAKAFQ 144
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 343-430 1.33e-15

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: 72.69  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 343 MHensLTLATIRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITTDFDIGIGDVVFFPIGTQHYIKSTCDEDLLM 422
Cdd:COG2140    1 MT---LAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVF 77


                 ....*...
gi 641755681 423 ILAFSTGN 430
Cdd:COG2140   78 LAVFDDDA 85
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 347-431 7.40e-14

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


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 68.85  E-value: 7.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681   347 SLTLATIRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITT-DFDIGIGDVVFFPIGTQHYIKSTCDEDLLmILA 425
Cdd:smart00835  29 GISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVyDARLREGDVFVVPQGHPHFQVNSGDENLE-FVA 107


                   ....*.
gi 641755681   426 FSTGNQ 431
Cdd:smart00835 108 FNTNDP 113
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 159-254 8.19e-13

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: 65.82  E-value: 8.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  159 GLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSiVTTYN--VTAGQVIFFPKNTLHWVKNVGEDDCL-FLLFFTTHEELQT 235
Cdd:pfam00190  44 GMNPPHWHPNATEILYVLQGRGRVGFVVPGNG-NRVFHkvLREGDVFVVPQGLPHFQYNIGDEPAVaFVAFDTNNPGNQS 122

                          90       100
                  ....*....|....*....|.
gi 641755681  236 --LDVDDVFFSTPEDIAARSL 254
Cdd:pfam00190 123 ilAGGFSSLPALPPEVLAKAF 143
CLLAC pfam15675
CLLAC-motif containing domain; This short domain is found in chordates. It carries a highly ...
 34-62 2.84e-09

CLLAC-motif containing domain; This short domain is found in chordates. It carries a highly conserved CLLAC sequence motif. The function is not known.


Pssm-ID: 434849  Cd Length: 30  Bit Score: 52.40  E-value: 2.84e-09
                          10        20
                  ....*....|....*....|....*....
gi 641755681   34 WSLMNIFLVCLLACFISTIIGVLIISSVY 62
Cdd:pfam15675   2 WSLWKIFLVCLLACLIATAIGVLILSLVY 30
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 354-464 2.36e-08

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


Pssm-ID: 274565 [Multi-domain]  Cd Length: 367  Bit Score: 55.79  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  354 RIYSNGLRQPHFHFNAnEMGYVISGCGKVGIIVSSKITTDFDIGIGDVVFFPIGTQHYIKSTcDEDLLMILAFSTGNQ-- 431
Cdd:TIGR03404  73 RLEPGAIRELHWHKEA-EWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGL-DEGCEFLLVFDDGNFse 150

                          90       100       110
                  ....*....|....*....|....*....|...
gi 641755681  432 LQTLDMDDYFHATADHILAQLFFKKQEEFKKIP 464
Cdd:TIGR03404 151 DGTFLVTDWLAHTPKDVLAKNFGVPESAFDNLP 183
 
Name Accession Description Interval E-value
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 153-251 8.57e-24

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: 97.28  E-value: 8.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 153 LRIKSKGLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSiVTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLFLLFFtTHEE 232
Cdd:cd20306   39 LRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGS-LDTFTVKPGQVVFIPQGWLHWIENVGDEEAHLLIFF-NHET 116

                         90
                 ....*....|....*....
gi 641755681 233 LQTLDVDDVFFSTPEDIAA 251
Cdd:cd20306  117 PEDIGLSDSLRATPPEVLG 135
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 112-426 1.20e-22

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


Pssm-ID: 274565 [Multi-domain]  Cd Length: 367  Bit Score: 99.32  E-value: 1.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  112 FPGGdiqWARfRYDVKDYPSDEEMefgTSINnqrskmtfgtLRIKSKGLRAPHWHFNAnEHGFLLKGSAWIGVVDAGGSi 191
Cdd:TIGR03404  48 ENGG---WAR-EVTVRDLPISTAI---AGVN----------MRLEPGAIRELHWHKEA-EWAYVLYGSCRITAVDENGR- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  192 VTTYNVTAGQVIFFPKNTLHWVKNVgEDDCLFLLFFT--THEELQTLDVDDVFFSTPEDIAARSLkpqgGVNfIRTFKKQ 269
Cdd:TIGR03404 109 NYIDDVGAGDLWYFPPGIPHSLQGL-DEGCEFLLVFDdgNFSEDGTFLVTDWLAHTPKDVLAKNF----GVP-ESAFDNL 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  270 TEDQAI----NLPPNLvelvqNASYVQSPDKLVWR-YFYNLKDSTEFKLSGGVIQWARFRkngvglndNEKIfseslqmh 344
Cdd:TIGR03404 183 PLKELYifpgTVPGPL-----DEEAVTGPAGEVPGpFTYHLSEQKPKQVPGGTVRIADST--------NFPV-------- 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  345 enSLTLAT--IRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITTDFDIGIGDVVFFPIGTQHYIKSTCDEDLLM 422
Cdd:TIGR03404 242 --SKTIAAaiVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVF 319


                  ....
gi 641755681  423 ILAF 426
Cdd:TIGR03404 320 LEVF 323
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 147-253 1.64e-19

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: 83.86  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 147 KMTFGTLRIKSKGLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSIVTtYNVTAGQVIFFPKNTLHWVKNVGEDDCLFLLF 226
Cdd:COG2140    2 TLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRART-VDVGPGDVVYVPPGYGHYIINTGDEPLVFLAV 80

                         90       100
                 ....*....|....*....|....*....
gi 641755681 227 FTTH--EELQTLDVDDVFFSTPEDIAARS 253
Cdd:COG2140   81 FDDDagSDYGTISLSGWLAHTPPEVLAVD 109
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 353-453 4.29e-19

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


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 83.79  E-value: 4.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 353 IRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITTDFDIGIGDVVFFPIGTQHYIKSTCDEDLLMILAFSTGNQl 432
Cdd:cd20306   39 LRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGSLDTFTVKPGQVVFIPQGWLHWIENVGDEEAHLLIFFNHETP- 117

                         90       100
                 ....*....|....*....|.
gi 641755681 433 QTLDMDDYFHATADHILAQLF 453
Cdd:cd20306  118 EDIGLSDSLRATPPEVLGNTY 138
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 144-254 1.81e-18

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: 81.94  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681   144 QRSKMTFGTLRIKSKGLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSIVTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLF 223
Cdd:smart00835  26 NGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVYDARLREGDVFVVPQGHPHFQVNSGDENLEF 105

                           90       100       110
                   ....*....|....*....|....*....|...
gi 641755681   224 LLFFTTHEELQTLDV--DDVFFSTPEDIAARSL 254
Cdd:smart00835 106 VAFNTNDPNRRFFLAgrNSVLRGLPPEVLAAAF 138
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 348-454 4.36e-18

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: 80.84  E-value: 4.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  348 LTLATIRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITTDFD--IGIGDVVFFPIGTQHYIKSTCDEDLLMILA 425
Cdd:pfam00190  33 ISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVGFVVPGNGNRVFHkvLREGDVFVVPQGLPHFQYNIGDEPAVAFVA 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 641755681  426 FST---GNQLQTLDMDDYFHATADHILAQLFF 454
Cdd:pfam00190 113 FDTnnpGNQSILAGGFSSLPALPPEVLAKAFQ 144
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 153-254 1.56e-17

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: 79.44  E-value: 1.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 153 LRIKSKGLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSIvTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLFLLFFtTHEE 232
Cdd:cd02240   32 VRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRF-ETFNLGAGDVGYVPSGSGHHIENIGDEDAEFLLIF-DDGT 109

                         90       100
                 ....*....|....*....|..
gi 641755681 233 LQTLDVDDVFFSTPEDIAARSL 254
Cdd:cd02240  110 FADVSLPWWLAMTPEEVLAATL 131
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 139-227 2.29e-17

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: 79.17  E-value: 2.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 139 TSINNQRSK-MTFGTLRIKSKGLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSiVTTYNVTAGQVIFFPKNTLHWVKNVG 217
Cdd:cd20305   24 DSKNFPISTtIAAALVTLEPGALRELHWHPNADEWQYYISGKARMTVFASGGR-ARTFDFQAGDVGYVPRGYGHYIENTG 102

                         90
                 ....*....|
gi 641755681 218 EDDCLFLLFF 227
Cdd:cd20305  103 DEPLEFLEVF 112
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 348-453 1.78e-16

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: 76.36  E-value: 1.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 348 LTLATIRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITTDFDIGIGDVVFFPIGTQHYIKSTCDEDLLMILAFS 427
Cdd:cd02240   27 LSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRFETFNLGAGDVGYVPSGSGHHIENIGDEDAEFLLIFD 106

                         90       100
                 ....*....|....*....|....*.
gi 641755681 428 TGnQLQTLDMDDYFHATADHILAQLF 453
Cdd:cd02240  107 DG-TFADVSLPWWLAMTPEEVLAATL 131
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 348-465 6.39e-16

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: 74.93  E-value: 6.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 348 LTLATIRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITTDFDIGIGDVVFFPIGTQHYIKSTCDEDLLMILAFS 427
Cdd:cd20305   34 IAAALVTLEPGALRELHWHPNADEWQYYISGKARMTVFASGGRARTFDFQAGDVGYVPRGYGHYIENTGDEPLEFLEVFN 113

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 641755681 428 TGNqLQTLDMDDYFHATADHILAQLFFKKQEEFKKIPR 465
Cdd:cd20305  114 SGR-YQDISLSQWLALTPPDLVAAHLGLPDDTIAKLPK 150
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 343-430 1.33e-15

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: 72.69  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 343 MHensLTLATIRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITTDFDIGIGDVVFFPIGTQHYIKSTCDEDLLM 422
Cdd:COG2140    1 MT---LAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVF 77


                 ....*...
gi 641755681 423 ILAFSTGN 430
Cdd:COG2140   78 LAVFDDDA 85
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 347-431 7.40e-14

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


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 68.85  E-value: 7.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681   347 SLTLATIRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITT-DFDIGIGDVVFFPIGTQHYIKSTCDEDLLmILA 425
Cdd:smart00835  29 GISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVyDARLREGDVFVVPQGHPHFQVNSGDENLE-FVA 107


                   ....*.
gi 641755681   426 FSTGNQ 431
Cdd:smart00835 108 FNTNDP 113
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 95-255 3.90e-13

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


Pssm-ID: 274565 [Multi-domain]  Cd Length: 367  Bit Score: 70.81  E-value: 3.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681   95 DVKFQFLNHLGKSKVFQFPGGDIQWArfryDVKDYPSdeemefgtsinnqrSKMTFGTL-RIKSKGLRAPHWHFNANEHG 173
Cdd:TIGR03404 209 EVPGPFTYHLSEQKPKQVPGGTVRIA----DSTNFPV--------------SKTIAAAIvTVEPGAMRELHWHPNADEWQ 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  174 FLLKGSAWIGVVDAGGSiVTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLFLLFFttheelQTLDVDDVFFS-----TPED 248
Cdd:TIGR03404 271 YFIQGQARMTVFAAGGN-ARTFDYQAGDVGYVPRNMGHYVENTGDETLVFLEVF------KADRFADVSLNqwlalTPPQ 343


                  ....*..
gi 641755681  249 IAARSLK 255
Cdd:TIGR03404 344 LVAAHLN 350
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 159-254 8.19e-13

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: 65.82  E-value: 8.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  159 GLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSiVTTYN--VTAGQVIFFPKNTLHWVKNVGEDDCL-FLLFFTTHEELQT 235
Cdd:pfam00190  44 GMNPPHWHPNATEILYVLQGRGRVGFVVPGNG-NRVFHkvLREGDVFVVPQGLPHFQYNIGDEPAVaFVAFDTNNPGNQS 122

                          90       100
                  ....*....|....*....|.
gi 641755681  236 --LDVDDVFFSTPEDIAARSL 254
Cdd:pfam00190 123 ilAGGFSSLPALPPEVLAKAF 143
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 103-254 1.33e-12

Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-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: 380438  Cd Length: 155  Bit Score: 65.32  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 103 HLGKSKVFQFPGGdiqWARfRYDVKDYPSDEEMEfGTSinnqrskmtfgtLRIKSKGLRAPHWHfNANEHGFLLKGSAWI 182
Cdd:cd20304    3 SFSDSHNRLESGG---WAR-EVTVRDLPISTGIA-GVN------------MRLEPGAIRELHWH-AAAEWAYVLSGRCRI 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641755681 183 GVVDAGGSiVTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLFLLFFT--THEELQTLDVDDVFFSTPEDIAARSL 254
Cdd:cd20304   65 TAVDPEGR-SFIDDVGPGDLWYFPRGHPHSIQGLGPDGCEFLLVFDdgNFSEFGTFSITDWLAHTPKEVLAKNF 137
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
123-248 1.39e-10

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 58.61  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 123 RYDVKDYPSDEEMEFgTSINNQRSKMTFGTLRIKSKGLRAPHWHFNANEHGFLLKGSawiGVVDAGGSIVTtynVTAGQV 202
Cdd:COG0662    3 DVNIEELKAIGWGSY-EVLGEGGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGT---GEVTIGDEEVE---LKAGDS 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 641755681 203 IFFPKNTLHWVKNVGEDDCLFLLFFTTHEelqtLDVDDVffsTPED 248
Cdd:COG0662   76 VYIPAGVPHRLRNPGDEPLELLEVQAPAY----LGEDDI---VRED 114
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 150-227 7.25e-10

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: 55.18  E-value: 7.25e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641755681 150 FGTLRIKSKGLRAPHWHFNANEHGFLLKGSAWIGVVDAGgsivtTYNVTAGQVIFFPKNTLHWVKNVGEDDCLFLLFF 227
Cdd:cd02208    1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDGE-----TVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
145-228 7.70e-10

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 56.01  E-value: 7.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 145 RSKMTFGTLRIKSKGLRAPHWHfNANEHGFLLKGSAWIGVvdaGGsivTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLFL 224
Cdd:COG1917   20 EDELEVVRVTFEPGARTPWHSH-PGEELIYVLEGEGEVEV---GG---EEYELKPGDVVFIPPGVPHAFRNLGDEPAVLL 92


                 ....
gi 641755681 225 LFFT 228
Cdd:COG1917   93 VVFS 96
CLLAC pfam15675
CLLAC-motif containing domain; This short domain is found in chordates. It carries a highly ...
 34-62 2.84e-09

CLLAC-motif containing domain; This short domain is found in chordates. It carries a highly conserved CLLAC sequence motif. The function is not known.


Pssm-ID: 434849  Cd Length: 30  Bit Score: 52.40  E-value: 2.84e-09
                          10        20
                  ....*....|....*....|....*....
gi 641755681   34 WSLMNIFLVCLLACFISTIIGVLIISSVY 62
Cdd:pfam15675   2 WSLWKIFLVCLLACLIATAIGVLILSLVY 30
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 351-464 1.69e-08

Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-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: 380438  Cd Length: 155  Bit Score: 53.38  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 351 ATIRIYSNGLRQPHFHfNANEMGYVISGCGKVGIIVSSKITTDFDIGIGDVVFFPIGTQHYIKSTCDEDLLMILAFSTGN 430
Cdd:cd20304   34 VNMRLEPGAIRELHWH-AAAEWAYVLSGRCRITAVDPEGRSFIDDVGPGDLWYFPRGHPHSIQGLGPDGCEFLLVFDDGN 112

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 641755681 431 --QLQTLDMDDYFHATADHILAQLFFKKQEEFKKIP 464
Cdd:cd20304  113 fsEFGTFSITDWLAHTPKEVLAKNFGVPAEAFDNLP 148
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 354-464 2.36e-08

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


Pssm-ID: 274565 [Multi-domain]  Cd Length: 367  Bit Score: 55.79  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681  354 RIYSNGLRQPHFHFNAnEMGYVISGCGKVGIIVSSKITTDFDIGIGDVVFFPIGTQHYIKSTcDEDLLMILAFSTGNQ-- 431
Cdd:TIGR03404  73 RLEPGAIRELHWHKEA-EWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGL-DEGCEFLLVFDDGNFse 150

                          90       100       110
                  ....*....|....*....|....*....|...
gi 641755681  432 LQTLDMDDYFHATADHILAQLFFKKQEEFKKIP 464
Cdd:TIGR03404 151 DGTFLVTDWLAHTPKDVLAKNFGVPESAFDNLP 183
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
339-436 4.44e-08

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 51.30  E-value: 4.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 339 ESLQMHENSLTLATIRIYSNGLRQPHFHFNANEMGYVISGCGKVgiIVSSKittDFDIGIGDVVFFPIGTQHYIKSTCDE 418
Cdd:COG0662   18 EVLGEGGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEV--TIGDE---EVELKAGDSVYIPAGVPHRLRNPGDE 92

                         90
                 ....*....|....*...
gi 641755681 419 DlLMILAFSTGNQLQTLD 436
Cdd:COG0662   93 P-LELLEVQAPAYLGEDD 109
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 163-227 2.03e-07

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: 48.02  E-value: 2.03e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641755681  163 PHWHFNANEHGFLLKGSawiGVVDAGGsivTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLFLLFF 227
Cdd:pfam07883  13 PHRHPGEDEFFYVLEGE---GELTVDG---EEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 350-423 8.57e-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: 8.57e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641755681 350 LATIRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSKITtdfdIGIGDVVFFPIGTQHYIKSTCDEDLLMI 423
Cdd:cd02208    1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDGETVE----LKAGDIVLIPPGVPHSFVNTSDEPAVFL 70
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
336-427 3.26e-06

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 45.61  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 336 IFSESLQMHENSLTLATIRIYSNGLRQPHFHfNANEMGYVISGCGKVGIIvsskiTTDFDIGIGDVVFFPIGTQHYIKST 415
Cdd:COG1917   11 VSVRVLADGEDELEVVRVTFEPGARTPWHSH-PGEELIYVLEGEGEVEVG-----GEEYELKPGDVVFIPPGVPHAFRNL 84

                         90
                 ....*....|..
gi 641755681 416 CDEDLLMILAFS 427
Cdd:COG1917   85 GDEPAVLLVVFS 96
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 164-241 3.70e-06

Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif.


Pssm-ID: 380343 [Multi-domain]  Cd Length: 126  Bit Score: 46.01  E-value: 3.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 164 HWHFNANEHGFLLKGSAwigVVDAGGSIVTtynVTAGQVIFFPKNTLHWVKNVGEDDCLFLlffttheELQT---LDVDD 240
Cdd:cd02213   56 QRHHHRSEHWVVVSGTA---EVTLDGKEKL---LKEGESIYIPKGTKHRLENPGKIPLEII-------EVQTgeyLGEDD 122


                 .
gi 641755681 241 V 241
Cdd:cd02213  123 I 123
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 159-268 5.93e-06

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: 46.82  E-value: 5.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 159 GLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSIVTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLFLLFFtTHEELQTLDV 238
Cdd:cd02241   81 GVNPPHTHPRATELLYVVEGTLYVGFVDENGNRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAF-NSEDPGTQQI 159

                         90       100       110
                 ....*....|....*....|....*....|..
gi 641755681 239 DDVFFST--PEDIAARSLkpQGGVNFIRTFKK 268
Cdd:cd02241  160 AQALFGLppPDDVLAAAF--GLDGAQVEKLKS 189
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 350-420 1.98e-05

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 43.27  E-value: 1.98e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641755681 350 LATIRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSkittdFDIGIGDVVFFPIGTQHYIKSTCDEDL 420
Cdd:cd02214   21 LAHARVPPGESTLPHRLKGSEEVYYILEGEGTMEIDGEP-----REVGPGDAVLIPPGAVQRIENTGEEDL 86
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 346-463 3.51e-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: 44.51  E-value: 3.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 346 NSLTLATIRIYSNGLRQPHFHFNANEMGYVISGCGKVGIIVSSK---ITTdfDIGIGDVVFFPIGTQHYIKSTCDEDLLM 422
Cdd:cd02241   68 LGISMARGDLAPCGVNPPHTHPRATELLYVVEGTLYVGFVDENGnrlFTK--TLNPGDVFVFPQGLIHFQFNPGCEPAVF 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 641755681 423 ILAFS-----TGNQLQTLdmddyFHAT-ADHILAQLFFKKQEEFKKI 463
Cdd:cd02241  146 VAAFNsedpgTQQIAQAL-----FGLPpPDDVLAAAFGLDGAQVEKL 187
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
 149-208 3.80e-05

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: 44.00  E-value: 3.80e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 149 TFGTLRikSKGLRAPHWHFNANEHGFLLKGSAWIGVVDAGGSIVTTYNVTAGQVIFFPKN 208
Cdd:cd02243   29 ERVKLE--PNAMFAPHWNANAHQVIYVTRGSGRVQVVGDNGKRVLDGEVREGQLLVVPQF 86
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 362-426 5.10e-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: 5.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641755681  362 QPHFHFNANEMGYVISGCGKVgiIVSSKittDFDIGIGDVVFFPIGTQHYIKSTCDEDLLMILAF 426
Cdd:pfam07883  12 PPHRHPGEDEFFYVLEGEGEL--TVDGE---EVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 165-224 6.01e-05

Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 41.67  E-value: 6.01e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641755681 165 WHFNANEHG-FLLKGSawiGVVDAGGsivTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLFL 224
Cdd:cd02222   32 LHTHPWEHEvYVLRGK---GVVVIGG---EEYPVKPGDVVYIPPNEPHQFRNTGDEPLGFL 86
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 162-224 8.31e-05

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 41.73  E-value: 8.31e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641755681 162 APHWHFNANEHGFLLKGSawiGVVDAGGsivTTYNVTAGQVIFFPKNTLHWVKNVGEDDCLFL 224
Cdd:cd02214   33 LPHRLKGSEEVYYILEGE---GTMEIDG---EPREVGPGDAVLIPPGAVQRIENTGEEDLVFL 89
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 363-422 8.33e-05

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: 40.68  E-value: 8.33e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 363 PHFHfNANEMGYVISGcgkVGIIVSSKITTDFdiGIGDVVFFPIGTQHYIKSTCDEDLLM 422
Cdd:cd06988   17 PHSH-HEYEIFIVISG---KGIVVVDGEREPV--KAGDVVYIPPGTEHYVKNDGDEDFEF 70
cupin_MAE_RS03005 cd06987
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ...
 353-423 3.06e-04

Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes bacterial and some eukaryotic proteins homologous to MAE_RS03005, a Microcystis aeruginosa protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380392 [Multi-domain]  Cd Length: 122  Bit Score: 40.33  E-value: 3.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641755681 353 IRIYSNGLRQP-HFHFNANEMGYVISGCGKVgiIVSSKittDFDIGIGDVVFFPIGTQHYIKSTCDEDLLMI 423
Cdd:cd06987   32 VEIFDPGGRTPpNTHPAAHEMFFVLAGEGRA--YCDGQ---RVPLRPGDALVVPPGSEHVIENTGSGRLYCL 98
cupin_11S_legumin_N cd02242
11S legumin seed storage globulin, N-terminal cupin domain; This family contains the ...
 352-436 4.48e-04

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: 41.42  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 352 TIRiySNGLRQPHFHfNANEMGYVISGCGKVGIIVSSKITTDFDIGI--------------------GDVVFFPIGTQHY 411
Cdd:cd02242   41 TIE--PRGLLLPSYS-NAPKLAYVLQGRGIVGVVFPGCPETFQSSQQsqgqgqrfrdqhqkvrrirkGDVIAVPAGVVHW 117

                         90       100
                 ....*....|....*....|....*
gi 641755681 412 IKSTCDEDLLMILAFSTGNQLQTLD 436
Cdd:cd02242  118 WYNDGDSDLVIVFLGDTSNNANQLD 142
cupin_7S_vicilin-like_N cd02244
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ...
 322-430 6.87e-04

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: 40.57  E-value: 6.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 322 RFRKNGVGLNDNEKIFSESLQMHENSLTLatiriysnglrqPHfHFNANEMGYVISGCGKVGIIVSSKITTdFDIGIGDV 401
Cdd:cd02244   14 RFDGRSRLLRGIENYRLAFITMEPNTLFL------------PH-HLDADMVFYVHTGRGTITWVDEDKRES-YNLERGDV 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 641755681 402 VFFPIGTQHYIKST-CDEDLLMILAFSTGN 430
Cdd:cd02244   80 YRIPAGSTFYLVNTdENEKLRIIALFDPVN 109
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 364-423 9.55e-04

Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif.


Pssm-ID: 380343 [Multi-domain]  Cd Length: 126  Bit Score: 39.08  E-value: 9.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 364 HFHFNANEMGYVISGCGKVgiIVSSKIttdFDIGIGDVVFFPIGTQHYIKSTCDEDLLMI 423
Cdd:cd02213   56 QRHHHRSEHWVVVSGTAEV--TLDGKE---KLLKEGESIYIPKGTKHRLENPGKIPLEII 110
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 364-423 3.61e-03

Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial proteins homologous to TM1287 decarboxylase, a Thermotoga maritima manganese-containing cupin thought to catalyze the conversion of oxalate to formate and carbon dioxide, due to its similarity to oxalate decarboxylase (OXDC) from Bacillus subtilis. TM1287 shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer.


Pssm-ID: 380350 [Multi-domain]  Cd Length: 93  Bit Score: 36.68  E-value: 3.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 364 HFHFNANEMGYVISGCGKVgiIVSSKITTdfdIGIGDVVFFPIGTQHYIKSTCDEDLLMI 423
Cdd:cd02221   35 HQHEGEFEIYYILSGEGLY--TDNGKEYE---VKAGDVTFTRDGESHGIENTGDEDLVFI 89
cupin_Bh2720-like cd02223
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ...
 374-420 4.72e-03

Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, archaeal, and eukaryotic proteins similar to Bh2720, a Bacillus halodurans protein of unknown function with a cupin beta-barrel fold.


Pssm-ID: 380352 [Multi-domain]  Cd Length: 98  Bit Score: 36.37  E-value: 4.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 641755681 374 YVISGCGKVgiIVSskiTTDFDIGIGDVVFFPIGTQHYIKSTCDEDL 420
Cdd:cd02223   37 RIEEGEGKA--IMG---GFESEVKDGDAIIVPAGTWHNVINTGNEPL 78
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 162-220 6.64e-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: 35.67  E-value: 6.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 641755681 162 APHWHfNANEHGFLLKGSAWIgVVDAGgsivtTYNVTAGQVIFFPKNTLHWVKNVGEDD 220
Cdd:cd06988   16 TPHSH-HEYEIFIVISGKGIV-VVDGE-----REPVKAGDVVYIPPGTEHYVKNDGDED 67
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
362-439 8.89e-03

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 36.15  E-value: 8.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641755681 362 QPHFHFNANEMGYVISGCGKVgiivsskiTTD---FDIGIGDVVFFPIGTQHYIKSTCDEDLLMILAFSTGNQLQTLDMD 438
Cdd:COG3837   43 PYHAHSAEEEFVYVLEGELTL--------RIGgeeYVLEPGDSVGFPAGVPHRLRNRGDEPARYLVVGTRAPYPDSFDYW 114


                 .
gi 641755681 439 D 439
Cdd:COG3837  115 D 115
 
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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