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Conserved domains on  [gi|15241636|ref|NP_198727|]
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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. ...
24-220 1.94e-95

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: 276.40  E-value: 1.94e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636  24 DPSPLQDFCVAigDLKNGVFVNGKFCKDPKQAKAEDFFYSGLNQAGTTNNKVKSNVTTVNVDQIPGLNTLGISLVRIDYA 103
Cdd:cd02241   1 DPDPLQDFCVA--DLSSPRTPNGYPCKDPALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636 104 PYGQNPPHTHPRATEILVLVEGTLYVGFVSSNqdNNRLFAKVLNPGDVFVFPIGMIHFQVNIGKTPAVAFAGLSSQNAGV 183
Cdd:cd02241  79 PCGVNPPHTHPRATELLYVVEGTLYVGFVDEN--GNRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGT 156
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15241636 184 ITIADTVFGSTPPinPDILAQAFQLDVNVVKDLEAKF 220
Cdd:cd02241 157 QQIAQALFGLPPP--DDVLAAAFGLDGAQVEKLKSKF 191
 
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. ...
24-220 1.94e-95

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: 276.40  E-value: 1.94e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636  24 DPSPLQDFCVAigDLKNGVFVNGKFCKDPKQAKAEDFFYSGLNQAGTTNNKVKSNVTTVNVDQIPGLNTLGISLVRIDYA 103
Cdd:cd02241   1 DPDPLQDFCVA--DLSSPRTPNGYPCKDPALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636 104 PYGQNPPHTHPRATEILVLVEGTLYVGFVSSNqdNNRLFAKVLNPGDVFVFPIGMIHFQVNIGKTPAVAFAGLSSQNAGV 183
Cdd:cd02241  79 PCGVNPPHTHPRATELLYVVEGTLYVGFVDEN--GNRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGT 156
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15241636 184 ITIADTVFGSTPPinPDILAQAFQLDVNVVKDLEAKF 220
Cdd:cd02241 157 QQIAQALFGLPPP--DDVLAAAFGLDGAQVEKLKSKF 191
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
63-214 7.96e-61

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: 187.54  E-value: 7.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636    63 SGLNQAGTTNNKVKSNVTTVNVDQIPGLNTLGISLVRIDYAPYGQNPPHTHPRATEILVLVEGTLYVGFVSSNQDNnRLF 142
Cdd:pfam00190   1 LNLLEPGPTYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVGFVVPGNGN-RVF 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15241636   143 AKVLNPGDVFVFPIGMIHFQVNIGKTPAVAFAGLSSQNAGVITIADTVFGSTPPINPDILAQAFQLDVNVVK 214
Cdd:pfam00190  80 HKVLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
79-214 8.18e-34

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: 118.15  E-value: 8.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636     79 VTTVNVDQIPGLNTLGISLVRIDYAPYGQNPPHTHPRATEILVLVEGTLYVGFVSSNQdnNRLFAKVLNPGDVFVFPIGM 158
Cdd:smart00835  14 LREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNG--NKVYDARLREGDVFVVPQGH 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 15241636    159 IHFQVNIGKTPAVaFAGLSSQNAGVITIADTVFGSTPPINPDILAQAFQLDVNVVK 214
Cdd:smart00835  92 PHFQVNSGDENLE-FVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
94-171 4.94e-11

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 57.84  E-value: 4.94e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241636  94 GISLVRIDYAPYGQNPPHTHPRATEILVLVEGTLYVgfvssnQDNNRLFakVLNPGDVFVFPIGMIHFQVNIGKTPAV 171
Cdd:COG0662  26 RLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEV------TIGDEEV--ELKAGDSVYIPAGVPHRLRNPGDEPLE 95
 
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. ...
24-220 1.94e-95

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: 276.40  E-value: 1.94e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636  24 DPSPLQDFCVAigDLKNGVFVNGKFCKDPKQAKAEDFFYSGLNQAGTTNNKVKSNVTTVNVDQIPGLNTLGISLVRIDYA 103
Cdd:cd02241   1 DPDPLQDFCVA--DLSSPRTPNGYPCKDPALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636 104 PYGQNPPHTHPRATEILVLVEGTLYVGFVSSNqdNNRLFAKVLNPGDVFVFPIGMIHFQVNIGKTPAVAFAGLSSQNAGV 183
Cdd:cd02241  79 PCGVNPPHTHPRATELLYVVEGTLYVGFVDEN--GNRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGT 156
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15241636 184 ITIADTVFGSTPPinPDILAQAFQLDVNVVKDLEAKF 220
Cdd:cd02241 157 QQIAQALFGLPPP--DDVLAAAFGLDGAQVEKLKSKF 191
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
63-214 7.96e-61

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: 187.54  E-value: 7.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636    63 SGLNQAGTTNNKVKSNVTTVNVDQIPGLNTLGISLVRIDYAPYGQNPPHTHPRATEILVLVEGTLYVGFVSSNQDNnRLF 142
Cdd:pfam00190   1 LNLLEPGPTYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVGFVVPGNGN-RVF 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15241636   143 AKVLNPGDVFVFPIGMIHFQVNIGKTPAVAFAGLSSQNAGVITIADTVFGSTPPINPDILAQAFQLDVNVVK 214
Cdd:pfam00190  80 HKVLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEVK 151
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
79-214 8.18e-34

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: 118.15  E-value: 8.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636     79 VTTVNVDQIPGLNTLGISLVRIDYAPYGQNPPHTHPRATEILVLVEGTLYVGFVSSNQdnNRLFAKVLNPGDVFVFPIGM 158
Cdd:smart00835  14 LREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNG--NKVYDARLREGDVFVVPQGH 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 15241636    159 IHFQVNIGKTPAVaFAGLSSQNAGVITIADTVFGSTPPINPDILAQAFQLDVNVVK 214
Cdd:smart00835  92 PHFQVNSGDENLE-FVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
79-219 1.77e-14

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: 68.00  E-value: 1.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636  79 VTTVNVDQIPGLNtlGISLVRIDYAPYGQNPPHTHPRATEILVLVEGTLYVGFVSSNqdnNRLFAKVLNPGDVFVFPIGM 158
Cdd:cd20306  20 IRQATADQLPVLK--GLSIYRLRLSPGGIREPHWHPNANELGYVISGEARVSILDPT---GSLDTFTVKPGQVVFIPQGW 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241636 159 IHFQVNIGKTPAVAFAGLSSQNAGVITIADtVFGSTPpinPDILAQAFQLDVNVVKDLEAK 219
Cdd:cd20306  95 LHWIENVGDEEAHLLIFFNHETPEDIGLSD-SLRATP---PEVLGNTYGVDAFFAAPAFPT 151
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
94-171 4.94e-11

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 57.84  E-value: 4.94e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241636  94 GISLVRIDYAPYGQNPPHTHPRATEILVLVEGTLYVgfvssnQDNNRLFakVLNPGDVFVFPIGMIHFQVNIGKTPAV 171
Cdd:COG0662  26 RLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEV------TIGDEEV--ELKAGDSVYIPAGVPHRLRNPGDEPLE 95
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
79-171 8.17e-10

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: 55.18  E-value: 8.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636  79 VTTVNVDQIPGLNTLGISLVRIdyAPYGQNPPHTHPRATEILVLVEGTLYVGFVSSNqdnNRLFAKVLNPGDVFVFPIGM 158
Cdd:cd02240  13 VRIATVTNFPISKDLSSALVRV--APGAMRELHWHPNTAEWQYVISGSARVTVFDED---GRFETFNLGAGDVGYVPSGS 87
                        90
                ....*....|...
gi 15241636 159 IHFQVNIGKTPAV 171
Cdd:cd02240  88 GHHIENIGDEDAE 100
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
98-174 1.39e-09

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: 52.65  E-value: 1.39e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241636    98 VRIDYAPYGQNPPHTHPRATEILVLVEGTLYVgfvssNQDNNRLfakVLNPGDVFVFPIGMIHFQVNIGKTPAVAFA 174
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFYVLEGEGEL-----TVDGEEV---VLKAGDSVYFPAGVPHRFRNTGDEPARLLD 69
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
95-174 1.46e-09

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 53.31  E-value: 1.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636  95 ISLVRIDYAPYGQNPPHTHPrATEILVLVEGTLYVgfvssnQDNNRLFakVLNPGDVFVFPIGMIHFQVNIGKTPAVAFA 174
Cdd:COG1917  23 LEVVRVTFEPGARTPWHSHP-GEELIYVLEGEGEV------EVGGEEY--ELKPGDVVFIPPGVPHAFRNLGDEPAVLLV 93
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
97-173 1.31e-08

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: 50.17  E-value: 1.31e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241636  97 LVRIDYAPYGQNPPHTHPRATEILVLVEGTLYVGFVSSNQdnnrlfaKVLNPGDVFVFPIGMIHFQVNIGKTPAVAF 173
Cdd:cd02208   1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDGET-------VELKAGDIVLIPPGVPHSFVNTSDEPAVFL 70
cupin_CV2614-like cd02236
Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes ...
95-175 3.56e-08

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: 49.80  E-value: 3.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636  95 ISLVRIDYAPYGQNPPHTHPRATEILVLvEGTLYVgfvsSNQDNNRlfaKVLNPGDVFVFPIGMIHFQVNIGKTPA---V 171
Cdd:cd02236  22 ITVLRITIPPGAELPWHTHPVPNAGYVL-SGELTV----EYEDGKK---RTFKAGDAFVEAVNTWHRGRNGGDEPVellV 93

                ....
gi 15241636 172 AFAG 175
Cdd:cd02236  94 FYAG 97
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
110-174 1.36e-07

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: 48.42  E-value: 1.36e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15241636 110 PHTHPRATEILVLVEGTLYVGFVSSNqdnNRLFAKVLNPGDVFVFPIGMIHFQVNIGKTPAVAFA 174
Cdd:COG2140  18 EHWHPNAAEWYYVLSGEARMTVQDPP---GRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLA 79
cupin_PA3510-like cd02225
Pseudomonas aeruginosa PA3510 and related proteins, cupin domain; This family includes ...
102-190 7.80e-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: 47.27  E-value: 7.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636 102 YAPYGQ-NPPHTHPrATEILVLVEGTLYVGFvssnQDNNRLFAKVLNPGDVFVFPIGMIHFQVNIGKTPAVAFAGLSSQN 180
Cdd:cd02225  59 RLPPGQgGALHTHE-VEEVFFVLQGRLTVFW----EDEGEEHERELGPRDMISVPAGVYRGFKNIGEEDALMQVMLGTGK 133
                        90
                ....*....|
gi 15241636 181 AGVITIADTV 190
Cdd:cd02225 134 PGRPTYPDDS 143
cupin_DRT102 cd06989
Arabidopsis thaliana DRT102 and related proteins, cupin domain; This family includes bacterial ...
94-161 9.03e-07

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: 45.60  E-value: 9.03e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15241636  94 GISLVRIDYAPYGQNPPHTHPrATEILVLVEGTLYVG----FVSSNqdnnrlfAKVLNPGDVFVFPIGMIHF 161
Cdd:cd06989  17 GPFVVRLKFPAGYKIPPHTHP-DDERVTVISGTFYLGmgdkFDEAK-------AKALPAGSFFTLPAGTPHF 80
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
89-174 9.83e-07

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 46.16  E-value: 9.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636  89 GLNTLGISLVRIdyAP-YGQNPPHTHPRATEILVLVEGTLYVgfvssnQDNNRLFakVLNPGDVFVFPIGMIHFQVNIGK 167
Cdd:COG3837  24 GLTRLGVNLITL--PPgASSSPYHAHSAEEEFVYVLEGELTL------RIGGEEY--VLEPGDSVGFPAGVPHRLRNRGD 93

                ....*..
gi 15241636 168 TPAVAFA 174
Cdd:COG3837  94 EPARYLV 100
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
97-174 2.64e-06

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: 44.49  E-value: 2.64e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241636  97 LVRIDYAPYGQNPPHTHPrATEILVLVEGTLyVGFVSSNQDnnrlfaKVLNPGDVFVFPIGMIHFQVNIGKTPAVAFA 174
Cdd:cd02235  21 QVRVEIPPGAVAGRHTHP-GEESGYVLEGSL-ELEVDGQPP------VTLKAGDSFFIPAGTVHNAKNVGSGPAKLLA 90
cupin_MAE_RS03005 cd06987
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ...
95-167 1.60e-05

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: 43.02  E-value: 1.60e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15241636  95 ISLVRIdYAPYGQNPPHTHPRATEILVLVEGTlYVGFVssnqDNNRLfakVLNPGDVFVFPIGMIHFQVNIGK 167
Cdd:cd06987  29 TVVVEI-FDPGGRTPPNTHPAAHEMFFVLAGE-GRAYC----DGQRV---PLRPGDALVVPPGSEHVIENTGS 92
cupin_ChrR_1 cd20303
Marinobacter hydrocarbonoclasticus anti-ECFsigma factor ChrR, and similar proteins; 2 ...
78-127 1.00e-04

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: 40.27  E-value: 1.00e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15241636  78 NVTTVNVDQIPGLNTlgiSLVRidYAPYGQNPPHTHPRATEILVLvEGTL 127
Cdd:cd20303  21 GVERLPLHRFGAEAT---ALVR--WAPGTRFPPHSHPGGEEILVL-EGTF 64
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
78-222 3.18e-04

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: 39.88  E-value: 3.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636  78 NVTTVNVDQIPGLNTLGISLVRIDyaPYGQNPPHTHPRATEILVLVEGTLYVGfVSSNQDNNRLFAkvLNPGDVFVFPIG 157
Cdd:cd20305  19 SVRIVDSKNFPISTTIAAALVTLE--PGALRELHWHPNADEWQYYISGKARMT-VFASGGRARTFD--FQAGDVGYVPRG 93
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241636 158 MIHFQVNIGKTPAVAFAGLssqNAGV---ITIADTVfGSTPpinPDILAQAFQLDvnvvKDLEAKFKN 222
Cdd:cd20305  94 YGHYIENTGDEPLEFLEVF---NSGRyqdISLSQWL-ALTP---PDLVAAHLGLP----DDTIAKLPK 150
cupin_7S_11S_C cd20285
7S and 11S seed storage globulin, C-terminal cupin domain; This family contains the C-terminal ...
78-155 5.45e-04

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: 38.36  E-value: 5.45e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241636  78 NVTTVNVDQIPGLNTLGISLVRIDYAPYGQNPPHTHPRATEILVLVEGTLYVGFVssNQDNNRLFAKVLNPGDVFVFP 155
Cdd:cd20285   2 NVTERTSNDFPILKSLNLLASSISLEEGAMFVPHYYSKAIVILVVNEGRAHIQVV--GPKGYESYDAELSKGDVFVVP 77
Cupin_7 pfam12973
ChrR Cupin-like domain; Members of this family are part of the cupin superfamily. This family ...
75-127 7.71e-04

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: 37.61  E-value: 7.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15241636    75 VKSNVTTVNV---DQIPGLNTLGISLVRidYAPYGQNPPHTHPRATEILVLvEGTL 127
Cdd:pfam12973   3 VPSPVPGVERkplHRDGGEKARATSLVR--YAPGSRFPAHRHPGGEEILVL-EGVF 55
cupin_BLR7677-like cd02234
Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain; This family includes ...
77-160 2.48e-03

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: 36.33  E-value: 2.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636  77 SNVTTVNVDQIPGLNTLGISLVRIDYAPYGQNPPHTHPRATEILVLvEGTLYVGFVSSNqdnnrlfAKVLNPGDVFVFPI 156
Cdd:cd02234   1 ETVTVLYSQPLPNIPGKEVTVLLVTYPPGAASPPHRHPGFVFAYVL-EGEVRSQVNGGP-------PRVYKAGESFYEPP 72

                ....
gi 15241636 157 GMIH 160
Cdd:cd02234  73 GAHH 76
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
109-163 2.92e-03

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: 36.36  E-value: 2.92e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15241636 109 PPHTHPRATEILVLVEG--TLYVgfvssnQDNNRlfakVLNPGDvFVF-PIGMIH-FQV 163
Cdd:cd02215  46 PPHYHKRHHETFYVLEGrlQLWL------DGESR----LLTPGD-FASvPPGTIHaYRM 93
cupin_7S_vicilin-like_C cd02245
7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal ...
110-157 4.56e-03

7S vicilin seed storage globulin, C-terminal cupin domain; This family contains C-terminal domain of plant 7S seed storage protein such as vicilin and includes beta-conglycinin, phaseolin, canavalin, conglutin-beta, a chromatin protein in Pisum sativum called P54, and a sucrose binding protein in soybean called SBP. These 7S globulins also include soybean allergen beta-conglycinin, peanut allergen conarachin (Ara h 1), walnut allergen Jug r 2 and lentil allergen Len c 1. Proteins in this family perform various functions, including a role in sucrose binding, desiccation, defense against microbes and oxidative stress. The vicilin peptides formed by trypsin or chymotrypsin digestion exhibit antihypertensive effects. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). Storage proteins are the cause of well-known allergic reactions to peanuts and cereals. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380372  Cd Length: 166  Bit Score: 36.73  E-value: 4.56e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636 110 PHTHPRATEILVLVEGTLYVGFVSSN---------QDNNRLFAKV---LNPGDVFVFPIG 157
Cdd:cd02245  41 PHYNSRATEIAVVVEGEGYVEMVCPHlssqsqqgeEEGSGEYQKVrarLSEGDVFVVPAG 100
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
111-160 5.76e-03

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: 35.11  E-value: 5.76e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15241636 111 HTHPRATEILVLVEGTLYVGFvssnqdnnRLFAKVLNPGDVFVFPIGMIH 160
Cdd:cd02226  38 HKHDDEDELFLVLEGELTIDF--------RDRDVTLGPGEFFVVPKGVEH 79
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
88-172 6.52e-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: 34.79  E-value: 6.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241636  88 PGLNTLGISLVRIDYAPYG-QNPPHTHPrATEILVLVEGTLYVGFvssnqDNNRLfakVLNPGDVFVFPIGMIHFQVNIG 166
Cdd:cd02209   9 PGLPGRKMEPFLVTLPPGGsGGEPYSHE-GEEFGYVLEGELELTV-----GGETY---VLEAGDSIYFDSDVPHRYRNPG 79

                ....*.
gi 15241636 167 KTPAVA 172
Cdd:cd02209  80 DEPARV 85
 
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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