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Conserved domains on  [gi|30690288|ref|NP_850875|]
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RmlC-like cupins superfamily protein [Arabidopsis thaliana]

Protein Classification

germin family protein( domain architecture ID 14388826)

germin family protein is a cupin domain-containing protein similar to oxalate oxidase (also called germin) that catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide

CATH:  2.60.120.10
Gene Ontology:  GO:0046872
PubMed:  14697267|19478949
SCOP:  3001825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 21-206 4.55e-85

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: 249.82  E-value: 4.55e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  21 SAEMLQDVCVADLSNAVKVNGYTCKDSTQITPEDFYFKGLANIAATNTSTGSVVTGANVEKLPGLNTLGLSMSRIDYAPN 100
Cdd:cd02241   1 DPDPLQDFCVADLSSPRTPNGYPCKDPALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLAPC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288 101 GLNPPHVHPRASEIIFVLEGQLYVGFVTTAG-KLIAKNLNKGDVFTFPKGLIHFQKNIANSPASVLAAFDSQLPGTQSLV 179
Cdd:cd02241  81 GVNPPHTHPRATELLYVVEGTLYVGFVDENGnRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGTQQIA 160

                       170       180
                ....*....|....*....|....*...
gi 30690288 180 ASLFGA-LPDDILAKSFQLKHKQVKKIK 206
Cdd:cd02241 161 QALFGLpPPDDVLAAAFGLDGAQVEKLK 188
 
Name Accession Description Interval E-value
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 21-206 4.55e-85

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: 249.82  E-value: 4.55e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  21 SAEMLQDVCVADLSNAVKVNGYTCKDSTQITPEDFYFKGLANIAATNTSTGSVVTGANVEKLPGLNTLGLSMSRIDYAPN 100
Cdd:cd02241   1 DPDPLQDFCVADLSSPRTPNGYPCKDPALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLAPC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288 101 GLNPPHVHPRASEIIFVLEGQLYVGFVTTAG-KLIAKNLNKGDVFTFPKGLIHFQKNIANSPASVLAAFDSQLPGTQSLV 179
Cdd:cd02241  81 GVNPPHTHPRATELLYVVEGTLYVGFVDENGnRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGTQQIA 160

                       170       180
                ....*....|....*....|....*...
gi 30690288 180 ASLFGA-LPDDILAKSFQLKHKQVKKIK 206
Cdd:cd02241 161 QALFGLpPPDDVLAAAFGLDGAQVEKLK 188
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 59-203 1.68e-56

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: 175.99  E-value: 1.68e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288    59 GLANIAATNTSTGSVVTGANVEKLPGLNTLGLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAG--KLIAK 136
Cdd:pfam00190   2 NLLEPGPTYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVGFVVPGNgnRVFHK 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288   137 NLNKGDVFTFPKGLIHFQKNIANSPASVLAAFDSQLPGTQSLVASLFG---ALPDDILAKSFQLKHKQVK 203
Cdd:pfam00190  82 VLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSILAGGFSslpALPPEVLAKAFQLAGEEVK 151
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 66-203 1.11e-39

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


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 133.17  E-value: 1.11e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288     66 TNTSTGSVVTGANVEKLPGLNTLGLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAG-KLIAKNLNKGDVF 144
Cdd:smart00835   6 DFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGnKVYDARLREGDVF 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30690288    145 TFPKGLIHFQKNIANSPAsVLAAFDSQLPGTQSLVA---SLFGALPDDILAKSFQLKHKQVK 203
Cdd:smart00835  86 VVPQGHPHFQVNSGDENL-EFVAFNTNDPNRRFFLAgrnSVLRGLPPEVLAAAFGVSAEEVR 146
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 89-170 2.39e-12

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: 61.14  E-value: 2.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  89 GLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAGKLIAKNLNKGDVFTFPKGLIHFQKNIANSPASVLAAF 168
Cdd:COG2140   2 TLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVF 81


                ..
gi 30690288 169 DS 170
Cdd:COG2140  82 DD 83
PLN00212 PLN00212
glutelin; Provisional
 74-206 3.15e-08

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 52.89  E-value: 3.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288   74 VTGANVEKLPGLNTLGLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAGKLIAKN-LNKGDVFTFPKGLIH 152
Cdd:PLN00212 332 ITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGKTVFNGvLRPGQLLIIPQHYAV 411

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30690288  153 FQKNIANSPASVL-----AAFDSQLPGtqslVASLFGALPDDILAKSFQLKHKQVKKIK 206
Cdd:PLN00212 412 LKKAEREGCQYIAfktnaNAMVSHIAG----KNSIFRALPVDVIANAYRISREEARRLK 466
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 78-197 1.59e-05

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: 44.62  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288    78 NVEKLPGLNTL-GLSMSridYAPNGLNPPHVHpRASEIIFVLEGQLYVGFVTTAGKLIAKNLNKGDVFTFPKGLIHFQKN 156
Cdd:TIGR03404  57 TVRDLPISTAIaGVNMR---LEPGAIRELHWH-KEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQG 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 30690288   157 IANSpASVLAAFDSqlpGTQS-----LVASLFGALPDDILAKSFQL 197
Cdd:TIGR03404 133 LDEG-CEFLLVFDD---GNFSedgtfLVTDWLAHTPKDVLAKNFGV 174
 
Name Accession Description Interval E-value
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 21-206 4.55e-85

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: 249.82  E-value: 4.55e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  21 SAEMLQDVCVADLSNAVKVNGYTCKDSTQITPEDFYFKGLANIAATNTSTGSVVTGANVEKLPGLNTLGLSMSRIDYAPN 100
Cdd:cd02241   1 DPDPLQDFCVADLSSPRTPNGYPCKDPALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLAPC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288 101 GLNPPHVHPRASEIIFVLEGQLYVGFVTTAG-KLIAKNLNKGDVFTFPKGLIHFQKNIANSPASVLAAFDSQLPGTQSLV 179
Cdd:cd02241  81 GVNPPHTHPRATELLYVVEGTLYVGFVDENGnRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGTQQIA 160

                       170       180
                ....*....|....*....|....*...
gi 30690288 180 ASLFGA-LPDDILAKSFQLKHKQVKKIK 206
Cdd:cd02241 161 QALFGLpPPDDVLAAAFGLDGAQVEKLK 188
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 59-203 1.68e-56

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: 175.99  E-value: 1.68e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288    59 GLANIAATNTSTGSVVTGANVEKLPGLNTLGLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAG--KLIAK 136
Cdd:pfam00190   2 NLLEPGPTYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVGFVVPGNgnRVFHK 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288   137 NLNKGDVFTFPKGLIHFQKNIANSPASVLAAFDSQLPGTQSLVASLFG---ALPDDILAKSFQLKHKQVK 203
Cdd:pfam00190  82 VLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSILAGGFSslpALPPEVLAKAFQLAGEEVK 151
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 66-203 1.11e-39

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


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 133.17  E-value: 1.11e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288     66 TNTSTGSVVTGANVEKLPGLNTLGLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAG-KLIAKNLNKGDVF 144
Cdd:smart00835   6 DFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGnKVYDARLREGDVF 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30690288    145 TFPKGLIHFQKNIANSPAsVLAAFDSQLPGTQSLVA---SLFGALPDDILAKSFQLKHKQVK 203
Cdd:smart00835  86 VVPQGHPHFQVNSGDENL-EFVAFNTNDPNRRFFLAgrnSVLRGLPPEVLAAAFGVSAEEVR 146
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 71-197 3.35e-20

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: 83.02  E-value: 3.35e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  71 GSVVTGANVEKLPGLNtlGLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAGKLIAKNLNKGDVFTFPKGL 150
Cdd:cd20306  17 GGSIRQATADQLPVLK--GLSIYRLRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGSLDTFTVKPGQVVFIPQGW 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 30690288 151 IHFQKNIANSPASVLAAFDSQLPGTQSLVASLfGALPDDILAKSFQL 197
Cdd:cd20306  95 LHWIENVGDEEAHLLIFFNHETPEDIGLSDSL-RATPPEVLGNTYGV 140
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 67-197 2.26e-19

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: 80.60  E-value: 2.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  67 NTSTGSVVTgANVEKLPGLNtlGLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAGKLIAKNLNKGDVFTF 146
Cdd:cd02240   7 ENAGGSVRI-ATVTNFPISK--DLSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRFETFNLGAGDVGYV 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 30690288 147 PKGLIHFQKNIANSPASVLAAFDSQLPGTQSLVASLfGALPDDILAKSFQL 197
Cdd:cd02240  84 PSGSGHHIENIGDEDAEFLLIFDDGTFADVSLPWWL-AMTPEEVLAATLDL 133
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 89-170 2.39e-12

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: 61.14  E-value: 2.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  89 GLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAGKLIAKNLNKGDVFTFPKGLIHFQKNIANSPASVLAAF 168
Cdd:COG2140   2 TLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVF 81


                ..
gi 30690288 169 DS 170
Cdd:COG2140  82 DD 83
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 94-168 3.78e-12

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: 59.58  E-value: 3.78e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30690288    94 RIDYAPNGLNPPHVHPRASEIIFVLEGQLYvgfVTTAGKLIAknLNKGDVFTFPKGLIHFQKNIANSPASVLAAF 168
Cdd:pfam07883   2 LVTLPPGESSPPHRHPGEDEFFYVLEGEGE---LTVDGEEVV--LKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 92-165 1.29e-11

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: 58.26  E-value: 1.29e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30690288  92 MSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVgfvtTAGKLIAKNLNKGDVFTFPKGLIHFQKNIANSPASVL 165
Cdd:cd02208   1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGEL----TLDDGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFL 70
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
90-168 1.79e-11

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 58.32  E-value: 1.79e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30690288  90 LSMSRIDYAPNGLNPPHVHPrASEIIFVLEGQLYvgfVTTAGKLIAknLNKGDVFTFPKGLIHFQKNIANSPASVLAAF 168
Cdd:COG1917  23 LEVVRVTFEPGARTPWHSHP-GEELIYVLEGEGE---VEVGGEEYE--LKPGDVVFIPPGVPHAFRNLGDEPAVLLVVF 95
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 90-199 1.62e-10

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: 57.21  E-value: 1.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  90 LSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAGKLIAKNLNKGDVFTFPKGLIHFQKNIANSPASVLAAFD 169
Cdd:cd20305  34 IAAALVTLEPGALRELHWHPNADEWQYYISGKARMTVFASGGRARTFDFQAGDVGYVPRGYGHYIENTGDEPLEFLEVFN 113

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 30690288 170 SQ----------LPGT-QSLVASLFGaLPDDILAKSFQLKH 199
Cdd:cd20305 114 SGryqdislsqwLALTpPDLVAAHLG-LPDDTIAKLPKKKQ 153
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
89-166 2.23e-10

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 55.92  E-value: 2.23e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30690288  89 GLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQlyvGFVTTAGKLIAknLNKGDVFTFPKGLIHFQKNIANSPASVLA 166
Cdd:COG0662  26 RLSVKRITVPPGAELSLHVHPHRDEFFYVLEGT---GEVTIGDEEVE--LKAGDSVYIPAGVPHRLRNPGDEPLELLE 98
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 92-166 2.69e-08

Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens 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: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 49.88  E-value: 2.69e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30690288  92 MSRIDYAPNGLNPPHVHPrASEIIFVLEGQLYVgfvTTAGKlIAKNLNKGDVFTFPKGLIHFQKNIANSPASVLA 166
Cdd:cd02235  21 QVRVEIPPGAVAGRHTHP-GEESGYVLEGSLEL---EVDGQ-PPVTLKAGDSFFIPAGTVHNAKNVGSGPAKLLA 90
PLN00212 PLN00212
glutelin; Provisional
 74-206 3.15e-08

glutelin; Provisional


Pssm-ID: 215106 [Multi-domain]  Cd Length: 493  Bit Score: 52.89  E-value: 3.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288   74 VTGANVEKLPGLNTLGLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAGKLIAKN-LNKGDVFTFPKGLIH 152
Cdd:PLN00212 332 ITRLNSQKFPILNLIQMSATRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGKTVFNGvLRPGQLLIIPQHYAV 411

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30690288  153 FQKNIANSPASVL-----AAFDSQLPGtqslVASLFGALPDDILAKSFQLKHKQVKKIK 206
Cdd:PLN00212 412 LKKAEREGCQYIAfktnaNAMVSHIAG----KNSIFRALPVDVIANAYRISREEARRLK 466
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
84-166 1.26e-07

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 48.48  E-value: 1.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  84 GLNTLGLSMSRIdyAPNG-LNPPHVHPRASEIIFVLEGQLYvgfVTTAGKLIAknLNKGDVFTFPKGLIHFQKNIANSPA 162
Cdd:COG3837  24 GLTRLGVNLITL--PPGAsSSPYHAHSAEEEFVYVLEGELT---LRIGGEEYV--LEPGDSVGFPAGVPHRLRNRGDEPA 96


                ....
gi 30690288 163 SVLA 166
Cdd:COG3837  97 RYLV 100
cupin_MAE_RS03005 cd06987
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ...
 97-165 1.73e-07

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: 48.41  E-value: 1.73e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30690288  97 YAPNGLNPPHVHPRASEIIFVLEGQlyvGFVTTAGKLIAknLNKGDVFTFPKGLIHFqknIANSPASVL 165
Cdd:cd06987  35 FDPGGRTPPNTHPAAHEMFFVLAGE---GRAYCDGQRVP--LRPGDALVVPPGSEHV---IENTGSGRL 95
cupin_PA3510-like cd02225
Pseudomonas aeruginosa PA3510 and related proteins, cupin domain; This family includes ...
 103-175 4.25e-07

Pseudomonas aeruginosa PA3510 and related proteins, cupin domain; This family includes bacterial proteins homologous to PA3510, a Pseudomonas aeruginosa protein of unknown function with a beta-barrel fold that belongs to the cupin superfamily.


Pssm-ID: 380354  Cd Length: 150  Bit Score: 47.66  E-value: 4.25e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30690288 103 NPPHVHPrASEIIFVLEGQLYVgFVTTAGKLIAKNLNKGDVFTFPKGLIHFQKNIANSPASVLAAFDSQLPGT 175
Cdd:cd02225  66 GALHTHE-VEEVFFVLQGRLTV-FWEDEGEEHERELGPRDMISVPAGVYRGFKNIGEEDALMQVMLGTGKPGR 136
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 70-213 1.17e-06

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: 46.45  E-value: 1.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  70 TGSVVTGANVEKLPGLNTL-GLSMSridYAPNGLNPPHVHpRASEIIFVLEGQLYVGFVTTAGKLIAKNLNKGDVFTFPK 148
Cdd:cd20304  13 SGGWAREVTVRDLPISTGIaGVNMR---LEPGAIRELHWH-AAAEWAYVLSGRCRITAVDPEGRSFIDDVGPGDLWYFPR 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288 149 GLIHFQKNIANSPASVLAAFDSqlpGTQS-----LVASLFGALPDDILAKSFQLKHKQVKKIklryaPKK 213
Cdd:cd20304  89 GHPHSIQGLGPDGCEFLLVFDD---GNFSefgtfSITDWLAHTPKEVLAKNFGVPAEAFDNL-----PKK 150
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
 71-206 4.75e-06

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: 44.77  E-value: 4.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  71 GSVVTgANVEKLPGLNTLGLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAGKLI-AKNLNKGDVFTFPKg 149
Cdd:cd02243   8 GRITT-LNSFKLPILRFVGLSAERVKLEPNAMFAPHWNANAHQVIYVTRGSGRVQVVGDNGKRVlDGEVREGQLLVVPQ- 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30690288 150 lihfqkniaNSPASVLAAFD---------SQLPGTQSLV--ASLFGALPDDILAKSFQLKHKQVKKIK 206
Cdd:cd02243  86 ---------FFAVAKIAGEEgfewvsfktSDNPIFSELAgrTSVLRALPPEVLANSYNISPEEAKQLK 144
cupin_DRT102 cd06989
Arabidopsis thaliana DRT102 and related proteins, cupin domain; This family includes bacterial ...
 89-153 1.33e-05

Arabidopsis thaliana DRT102 and related proteins, cupin domain; This family includes bacterial and eukaryotic proteins homologous to DNA-damage-repair/toleration protein DRT102 found in Arabidopsis thaliana. DRT102 may be involved in DNA repair from UV damage. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380394  Cd Length: 97  Bit Score: 42.52  E-value: 1.33e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30690288  89 GLSMSRIDYAPNGLNPPHVHPrASEIIFVLEGQLYVGFVTTAGKLIAKNLNKGDVFTFPKGLIHF 153
Cdd:cd06989  17 GPFVVRLKFPAGYKIPPHTHP-DDERVTVISGTFYLGMGDKFDEAKAKALPAGSFFTLPAGTPHF 80
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 78-197 1.59e-05

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: 44.62  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288    78 NVEKLPGLNTL-GLSMSridYAPNGLNPPHVHpRASEIIFVLEGQLYVGFVTTAGKLIAKNLNKGDVFTFPKGLIHFQKN 156
Cdd:TIGR03404  57 TVRDLPISTAIaGVNMR---LEPGAIRELHWH-KEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQG 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 30690288   157 IANSpASVLAAFDSqlpGTQS-----LVASLFGALPDDILAKSFQL 197
Cdd:TIGR03404 133 LDEG-CEFLLVFDD---GNFSedgtfLVTDWLAHTPKDVLAKNFGV 174
cupin_RemF-like cd06979
Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is ...
 90-165 2.08e-05

Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is a manganese-containing polyketide cyclase present in bacteria that is involved in the biosynthesis of resistomycin, the aromatic pentacyclic metabolite in Streptomyces resistomycificus. Structure of this enzyme shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold that forms a homodimer. It contains an unusual octahedral zinc-binding site in a large hydrophobic pocket that may represent the active site. The zinc ion, coordinated to four histidine side chains and two water molecules, could act as a Lewis acid in the aldol condensation reaction catalyzed by RemF, reminiscent of class II aldolases.


Pssm-ID: 380384 [Multi-domain]  Cd Length: 93  Bit Score: 41.68  E-value: 2.08e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30690288  90 LSMSRIDYAPN-GLNPPHVHPRASEIIFVLEGQLYvgfVTTAGKLIAknLNKGDVFTFPKGLIHFQKNIANSPASVL 165
Cdd:cd06979  17 FDLFEFEVSPNaGMPPPHYHEDWEETIYGLEGSVT---LTLPGKTVE--VGPGDSIFIPRGEVHGFVNRSGGPTCRL 88
cupin_7S_11S_C cd20285
7S and 11S seed storage globulin, C-terminal cupin domain; This family contains the C-terminal ...
 74-160 2.85e-05

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: 41.83  E-value: 2.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  74 VTGANVEKLPGLNTLGLSMSRIDYAPNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAGKLIAK-NLNKGDVFTFPKGLIH 152
Cdd:cd20285   3 VTERTSNDFPILKSLNLLASSISLEEGAMFVPHYYSKAIVILVVNEGRAHIQVVGPKGYESYDaELSKGDVFVVPAAFPV 82


                ....*...
gi 30690288 153 FQKNIANS 160
Cdd:cd20285  83 AIKSTSHN 90
cupin_BLR7677-like cd02234
Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain; This family includes ...
 72-168 3.45e-04

Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLR7677, a Bradyrhizobium japonicum 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: 380362 [Multi-domain]  Cd Length: 103  Bit Score: 38.64  E-value: 3.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  72 SVVTGANVEKLPGLNTLGLSMSRIDYAPNGLNPPHVHPrASEIIFVLEGQLYVGFVTTAgkliAKNLNKGDVFTFPKGLI 151
Cdd:cd02234   1 ETVTVLYSQPLPNIPGKEVTVLLVTYPPGAASPPHRHP-GFVFAYVLEGEVRSQVNGGP----PRVYKAGESFYEPPGAH 75

                        90       100
                ....*....|....*....|.
gi 30690288 152 HFQ-KNiaNS---PASVLAAF 168
Cdd:cd02234  76 HRVsRN--ASatePAKLLAVF 94
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 99-206 4.01e-04

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: 40.38  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288    99 PNGLNPPHVHPRASEIIFVLEGQLYVGFVTTAGKLIAKNLNKGDVFTFPKGLIHFQKNIANSPASVLAAFDSQLPGTQSL 178
Cdd:TIGR03404 254 PGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVFLEVFKADRFADVSL 333

                          90       100
                  ....*....|....*....|....*...
gi 30690288   179 vASLFGALPDDILAKSFQLKHKQVKKIK 206
Cdd:TIGR03404 334 -NQWLALTPPQLVAAHLNLDDEVIDSLK 360
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 106-165 4.75e-04

Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also 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: 380355 [Multi-domain]  Cd Length: 94  Bit Score: 37.81  E-value: 4.75e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30690288 106 HVHPRASEIIFVLEGQLYVGF----VTtagkliaknLNKGDVFTFPKGLIHfqKNIANSPASVL 165
Cdd:cd02226  38 HKHDDEDELFLVLEGELTIDFrdrdVT---------LGPGEFFVVPKGVEH--RPVAEEETVVL 90
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 104-154 5.31e-04

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380345 [Multi-domain]  Cd Length: 122  Bit Score: 38.29  E-value: 5.31e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 30690288 104 PPHVHPRASEIIFVLEGQLYVgFVTTAGKLiaknLNKGDVFTFPKGLIH-FQ 154
Cdd:cd02215  46 PPHYHKRHHETFYVLEGRLQL-WLDGESRL----LTPGDFASVPPGTIHaYR 92
cupin_CV2614-like cd02236
Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes ...
 90-168 7.38e-04

Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to CV2614, a Chromobacterium violaceum 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: 380364 [Multi-domain]  Cd Length: 102  Bit Score: 37.47  E-value: 7.38e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30690288  90 LSMSRIDYAPNGLNPPHVHPrASEIIFVLEGQLYVgfVTTAGKliAKNLNKGDVFTFPKGLIHFQKNIANSPASVLAAF 168
Cdd:cd02236  22 ITVLRITIPPGAELPWHTHP-VPNAGYVLSGELTV--EYEDGK--KRTFKAGDAFVEAVNTWHRGRNGGDEPVELLVFY 95
cupin_7S_vicilin-like_N cd02244
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ...
 104-208 8.00e-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: 38.64  E-value: 8.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288 104 PPHVHprASEIIFVLEGQLYVGFVTTaGKLIAKNLNKGDVFTFPKGLIHFqknIANSP-------ASVLAAFDSQLPGTQ 176
Cdd:cd02244  43 PHHLD--ADMVFYVHTGRGTITWVDE-DKRESYNLERGDVYRIPAGSTFY---LVNTDeneklriIALFDPVNSLTPGPF 116

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 30690288 177 SLVASLFGALP--------DDILAKSFQLKHKQVKKIKLR 208
Cdd:cd02244 117 QSFFGAGGQNPesllsgfsKEILEAAFNVSEEELERLLSQ 156
cupin_ChrR_1 cd20303
Marinobacter hydrocarbonoclasticus anti-ECFsigma factor ChrR, and similar proteins; 2 ...
 97-122 1.03e-03

Marinobacter hydrocarbonoclasticus anti-ECFsigma factor ChrR, and similar proteins; 2 heterologous tandem repeats of cupin domain; This family contains bacterial anti-sigma factor such as ChrR from Marinobacter hydrocarbonoclasticus. Anti-sigma factor ChrR is a member of the ZAS (Zn2+ anti-sigma) subfamily of group IV anti-sigmas. It inhibits transcriptional activity by binding to the ECF sigma factor E (sigmaE), an essential factor to mount a transcriptional response to a singlet oxygen and for viability when carotenoids are limiting. This protein family likely contains two distinct homologous functional domains belonging to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380437 [Multi-domain]  Cd Length: 102  Bit Score: 37.19  E-value: 1.03e-03
                        10        20
                ....*....|....*....|....*.
gi 30690288  97 YAPNGLNPPHVHPRASEiIFVLEGQL 122
Cdd:cd20303  40 WAPGTRFPPHSHPGGEE-ILVLEGTF 64
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 104-153 1.62e-03

AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.


Pssm-ID: 396749 [Multi-domain]  Cd Length: 134  Bit Score: 37.41  E-value: 1.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 30690288   104 PPHVHPRAsEIIFVLEGQlyvGFVTTAGKLIakNLNKGDVFTFPKGLIHF 153
Cdd:pfam02311  17 PPHVHDFY-VIGYIERGV---GRFRLNGRTY--HLGPGDLFLLPPGEPHD 60
cupin_WbuC TIGR04366
cupin fold metalloprotein, WbuC family; Members of this family show sequence similarity to ...
 104-152 2.51e-03

cupin fold metalloprotein, WbuC family; Members of this family show sequence similarity to cupin fold proteins (see pfam07883), including conserved His residues likely to serve as metal-binding ligands. Many members occur in bacterial O-antigen biosynthesis regions. Some members have acquired the gene symbol wbuC (e.g. Jarvis, et al, 2011), but publications using this term do not ascribe a function.


Pssm-ID: 275159  Cd Length: 132  Bit Score: 36.77  E-value: 2.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 30690288   104 PPHVHPRASEIIFVLEGQLYVGFVTTAGKLIAK-NLNKGD---VFTFPKGLIH 152
Cdd:TIGR04366  48 RPHRHPHKSETFIVLEGELDVLLFDDDGEVTERvVLSPGGgtfGVEIPPGTWH 100
EutQ COG4766
Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid ...
 113-168 3.21e-03

Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid transport and metabolism];


Pssm-ID: 443798  Cd Length: 123  Bit Score: 36.12  E-value: 3.21e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30690288 113 EIIFVLEGQLYVgfVTTAGKLIAKnlnKGDVFTFPKGL-IHFQknianSPASVLAAF 168
Cdd:COG4766  69 EVDYVLEGTLTI--EIDGETVTAG---PGDVIYIPKGSsITFS-----TPEKARFFY 115
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 83-168 4.86e-03

XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380339 [Multi-domain]  Cd Length: 90  Bit Score: 35.18  E-value: 4.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690288  83 PGLNTLGLSMSRIDYAPNG-LNPPHVHPrASEIIFVLEGQLYVgfvTTAGKLIAknLNKGDVFTFPKGLIHFQKNIANSP 161
Cdd:cd02209   9 PGLPGRKMEPFLVTLPPGGsGGEPYSHE-GEEFGYVLEGELEL---TVGGETYV--LEAGDSIYFDSDVPHRYRNPGDEP 82


                ....*..
gi 30690288 162 ASVLAAF 168
Cdd:cd02209  83 ARVLWVI 89
Cupin_7 pfam12973
ChrR Cupin-like domain; Members of this family are part of the cupin superfamily. This family ...
 97-120 8.63e-03

ChrR Cupin-like domain; Members of this family are part of the cupin superfamily. This family includes the transcriptional activator ChrR.


Pssm-ID: 463764 [Multi-domain]  Cd Length: 91  Bit Score: 34.53  E-value: 8.63e-03
                          10        20
                  ....*....|....*....|....
gi 30690288    97 YAPNGLNPPHVHPRASEiIFVLEG 120
Cdd:pfam12973  31 YAPGSRFPAHRHPGGEE-ILVLEG 53
 
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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