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Conserved domains on  [gi|1333133355|ref|XP_023541363|]
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putative germin-like protein 2-1 [Cucurbita pepo subsp. pepo]

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. ...
 24-217 1.03e-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: 251.75  E-value: 1.03e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  24 DQSPIQDFCVANNGSTVLLNGLTCKDPKEVVADDFSFSGLHLAANTSNALGCHVTPVTPSEMPGLNTLGLSIVRIDYAPQ 103
Cdd:cd02241     1 DPDPLQDFCVADLSSPRTPNGYPCKDPALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLAPC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355 104 GINPLHTHPRASEILIVLEGSLEVGFITSfPENRHIGKVLQKGDAFVFPVGLVHYQRNPGPTNAVAIAALSSQNPGVIIV 183
Cdd:cd02241    81 GVNPPHTHPRATELLYVVEGTLYVGFVDE-NGNRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGTQQI 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1333133355 184 ANAVFGSipNISSNILEKSFQINKKAIGYLQTKF 217
Cdd:cd02241   160 AQALFGL--PPPDDVLAAAFGLDGAQVEKLKSKF 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. ...
 24-217 1.03e-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: 251.75  E-value: 1.03e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  24 DQSPIQDFCVANNGSTVLLNGLTCKDPKEVVADDFSFSGLHLAANTSNALGCHVTPVTPSEMPGLNTLGLSIVRIDYAPQ 103
Cdd:cd02241     1 DPDPLQDFCVADLSSPRTPNGYPCKDPALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLAPC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355 104 GINPLHTHPRASEILIVLEGSLEVGFITSfPENRHIGKVLQKGDAFVFPVGLVHYQRNPGPTNAVAIAALSSQNPGVIIV 183
Cdd:cd02241    81 GVNPPHTHPRATELLYVVEGTLYVGFVDE-NGNRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGTQQI 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1333133355 184 ANAVFGSipNISSNILEKSFQINKKAIGYLQTKF 217
Cdd:cd02241   160 AQALFGL--PPPDDVLAAAFGLDGAQVEKLKSKF 191
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 61-210 5.72e-49

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: 157.11  E-value: 5.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  61 SGLHLAANTSNALGCHVTPVTPSEMPGLNTLGLSIVRIDYAPQGINPLHTHPRASEILIVLEGSLEVGFITSFPENRHIG 140
Cdd:pfam00190   1 LNLLEPGPTYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVGFVVPGNGNRVFH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355 141 KVLQKGDAFVFPVGLVHYQRNPGPTNAVAIAALSSQNPGVIIVANAVFGSIPNISSNILEKSFQINKKAI 210
Cdd:pfam00190  81 KVLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEV 150
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 68-210 1.94e-32

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: 114.69  E-value: 1.94e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355   68 NTSNALGCHVTPVTPSEMPGLNTLGLSIVRIDYAPQGINPLHTHPRASEILIVLEGSLEVGFITSFPeNRHIGKVLQKGD 147
Cdd:smart00835   5 PDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNG-NKVYDARLREGD 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333133355  148 AFVFPVGLVHYQRNPGPTNAVaIAALSSQNPGVIIVANAVFGSIPNISSNILEKSFQINKKAI 210
Cdd:smart00835  84 VFVVPQGHPHFQVNSGDENLE-FVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEV 145
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
92-171 1.09e-12

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 62.08  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  92 GLSIVRIDYAPQGINPLHTHPRASEILIVLEGSLEVgfitsfpenrHIG---KVLQKGDAFVFPVGLVHYQRNPGPTNAV 168
Cdd:COG0662    26 RLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEV----------TIGdeeVELKAGDSVYIPAGVPHRLRNPGDEPLE 95


                  ...
gi 1333133355 169 AIA 171
Cdd:COG0662    96 LLE 98
 
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. ...
 24-217 1.03e-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: 251.75  E-value: 1.03e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  24 DQSPIQDFCVANNGSTVLLNGLTCKDPKEVVADDFSFSGLHLAANTSNALGCHVTPVTPSEMPGLNTLGLSIVRIDYAPQ 103
Cdd:cd02241     1 DPDPLQDFCVADLSSPRTPNGYPCKDPALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLAPC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355 104 GINPLHTHPRASEILIVLEGSLEVGFITSfPENRHIGKVLQKGDAFVFPVGLVHYQRNPGPTNAVAIAALSSQNPGVIIV 183
Cdd:cd02241    81 GVNPPHTHPRATELLYVVEGTLYVGFVDE-NGNRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGTQQI 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1333133355 184 ANAVFGSipNISSNILEKSFQINKKAIGYLQTKF 217
Cdd:cd02241   160 AQALFGL--PPPDDVLAAAFGLDGAQVEKLKSKF 191
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 61-210 5.72e-49

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: 157.11  E-value: 5.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  61 SGLHLAANTSNALGCHVTPVTPSEMPGLNTLGLSIVRIDYAPQGINPLHTHPRASEILIVLEGSLEVGFITSFPENRHIG 140
Cdd:pfam00190   1 LNLLEPGPTYNPEGGRVTTVNSKNLPGLNTLGISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVGFVVPGNGNRVFH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355 141 KVLQKGDAFVFPVGLVHYQRNPGPTNAVAIAALSSQNPGVIIVANAVFGSIPNISSNILEKSFQINKKAI 210
Cdd:pfam00190  81 KVLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEV 150
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 68-210 1.94e-32

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: 114.69  E-value: 1.94e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355   68 NTSNALGCHVTPVTPSEMPGLNTLGLSIVRIDYAPQGINPLHTHPRASEILIVLEGSLEVGFITSFPeNRHIGKVLQKGD 147
Cdd:smart00835   5 PDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNG-NKVYDARLREGD 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333133355  148 AFVFPVGLVHYQRNPGPTNAVaIAALSSQNPGVIIVANAVFGSIPNISSNILEKSFQINKKAI 210
Cdd:smart00835  84 VFVVPQGHPHFQVNSGDENLE-FVAFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEV 145
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
92-171 1.09e-12

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 62.08  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  92 GLSIVRIDYAPQGINPLHTHPRASEILIVLEGSLEVgfitsfpenrHIG---KVLQKGDAFVFPVGLVHYQRNPGPTNAV 168
Cdd:COG0662    26 RLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEV----------TIGdeeVELKAGDSVYIPAGVPHRLRNPGDEPLE 95


                  ...
gi 1333133355 169 AIA 171
Cdd:COG0662    96 LLE 98
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
93-174 2.29e-12

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 61.02  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  93 LSIVRIDYAPQGINPLHTHPrASEILIVLEGSLEVgfitsfpenrHIGK---VLQKGDAFVFPVGLVHYQRNPGPTNAVA 169
Cdd:COG1917    23 LEVVRVTFEPGARTPWHSHP-GEELIYVLEGEGEV----------EVGGeeyELKPGDVVFIPPGVPHAFRNLGDEPAVL 91


                  ....*
gi 1333133355 170 IAALS 174
Cdd:COG1917    92 LVVFS 96
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 96-171 1.39e-11

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: 58.04  E-value: 1.39e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333133355  96 VRIDYAPQGINPLHTHPRASEILIVLEGSLEVgfitsfpenrHIG---KVLQKGDAFVFPVGLVHYQRNPGPTNAVAIA 171
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFYVLEGEGEL----------TVDgeeVVLKAGDSVYFPAGVPHRFRNTGDEPARLLD 69
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 80-205 4.67e-11

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


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 58.76  E-value: 4.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  80 VTPSEMPGLNtlGLSIVRIDYAPQGINPLHTHPRASEILIVLEGSLEVGFITsfPENRHIGKVLQKGDAFVFPVGLVHYQ 159
Cdd:cd20306    23 ATADQLPVLK--GLSIYRLRLSPGGIREPHWHPNANELGYVISGEARVSILD--PTGSLDTFTVKPGQVVFIPQGWLHWI 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333133355 160 RNPGPTNAVAIAALSSQNPGVIIVA-------NAVFGSIPNISSNILEKSFQI 205
Cdd:cd20306    99 ENVGDEEAHLLIFFNHETPEDIGLSdslratpPEVLGNTYGVDAFFAAPAFPT 151
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 90-171 1.17e-09

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: 54.20  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  90 TLGLSIVRIdyAPQGINPLHTHPRASEILIVLEGSLEVGFITSFPENRHIgkVLQKGDAFVFPVGLVHYQRNPGPTNAVA 169
Cdd:COG2140     2 TLAGGLTVL--EPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTV--DVGPGDVVYVPPGYGHYIINTGDEPLVF 77


                  ..
gi 1333133355 170 IA 171
Cdd:COG2140    78 LA 79
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
63-171 1.33e-09

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 53.87  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  63 LHLAANTSNALGCHVTPVtpSEMPGLNTLGLSIVRIdyAP-QGINPLHTHPRASEILIVLEGSLEVgfitSFPENRHigk 141
Cdd:COG3837     2 VNLDDLPGPEAGRRYRRL--GDALGLTRLGVNLITL--PPgASSSPYHAHSAEEEFVYVLEGELTL----RIGGEEY--- 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 1333133355 142 VLQKGDAFVFPVGLVHYQRNPGPTNAVAIA 171
Cdd:COG3837    71 VLEPGDSVGFPAGVPHRLRNRGDEPARYLV 100
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 95-170 6.04e-09

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: 50.94  E-value: 6.04e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333133355  95 IVRIDYAPQGINPLHTHPRASEILIVLEGSlevGFITSFPENRHigkVLQKGDAFVFPVGLVHYQRNPGPTNAVAI 170
Cdd:cd02208     1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGE---GELTLDDGETV---ELKAGDIVLIPPGVPHSFVNTSDEPAVFL 70
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 70-170 1.00e-08

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: 52.10  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  70 SNALGcHVTPVTPSEMPGLNtlGLSIVRIDYAPQGINPLHTHPRASEILIVLEGSLEVGFITsfPENRHIGKVLQKGDAF 149
Cdd:cd02240     7 ENAGG-SVRIATVTNFPISK--DLSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFD--EDGRFETFNLGAGDVG 81

                          90       100
                  ....*....|....*....|.
gi 1333133355 150 VFPVGLVHYQRNPGPTNAVAI 170
Cdd:cd02240    82 YVPSGSGHHIENIGDEDAEFL 102
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 86-174 1.06e-08

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: 50.58  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  86 PGLNTLGLSIVRIDYAPQG-INPLHTHPrASEILIVLEGSLEVGFitsfPENRHIgkvLQKGDAFVFPVGLVHYQRNPGP 164
Cdd:cd02209     9 PGLPGRKMEPFLVTLPPGGsGGEPYSHE-GEEFGYVLEGELELTV----GGETYV---LEAGDSIYFDSDVPHRYRNPGD 80

                          90
                  ....*....|
gi 1333133355 165 TNAVAIAALS 174
Cdd:cd02209    81 EPARVLWVIT 90
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 81-171 2.17e-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: 50.27  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  81 TPSEMPGLNTLglsIVRIDYAPQGINPLHTHPrASEILIVLEGSLEVgFITSFPEnrhigKVLQKGDAFVFPVGLVHYQR 160
Cdd:cd02235    10 TDLSVPGREVV---QVRVEIPPGAVAGRHTHP-GEESGYVLEGSLEL-EVDGQPP-----VTLKAGDSFFIPAGTVHNAK 79

                          90
                  ....*....|.
gi 1333133355 161 NPGPTNAVAIA 171
Cdd:cd02235    80 NVGSGPAKLLA 90
cupin_CV2614-like cd02236
Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes ...
 93-171 5.25e-07

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: 46.33  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  93 LSIVRIDYAPQGINPLHTHPrASEILIVLEGSLEVgfitsfpENR-HIGKVLQKGDAFVFPVGLVHYQRNPGPTNAVAIA 171
Cdd:cd02236    22 ITVLRITIPPGAELPWHTHP-VPNAGYVLSGELTV-------EYEdGKKRTFKAGDAFVEAVNTWHRGRNGGDEPVELLV 93
cupin_PA3510-like cd02225
Pseudomonas aeruginosa PA3510 and related proteins, cupin domain; This family includes ...
 93-182 2.91e-06

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: 45.34  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  93 LSIVRIDyaPQGINPLHTHPrASEILIVLEGSLEVGFITsfpENRHIGKVLQKGDAFVFPVGLVHYQRNPGPTNAVAIAA 172
Cdd:cd02225    55 LSTMRLP--PGQGGALHTHE-VEEVFFVLQGRLTVFWED---EGEEHERELGPRDMISVPAGVYRGFKNIGEEDALMQVM 128

                          90
                  ....*....|
gi 1333133355 173 LSSQNPGVII 182
Cdd:cd02225   129 LGTGKPGRPT 138
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 93-168 1.59e-05

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 42.46  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  93 LSIVRIDYAPQGINPLHTHPraSE-ILIVLEGSLEVgfitsfpenrHIG---KVLQKGDAFVFPVGLVHYQRNPGPTNAV 168
Cdd:cd02238    27 LMLVEVRFEKGAVVPLHSHP--HEqIGYVLSGRFEF----------TIGgetRILKPGDSYYIPPNVPHGAEALEDSVLL 94
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 109-157 8.63e-05

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: 40.12  E-value: 8.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1333133355 109 HTHPRASEILIVLEGSLEVGFitsfpENRHIgkVLQKGDAFVFPVGLVH 157
Cdd:cd02226    38 HKHDDEDELFLVLEGELTIDF-----RDRDV--TLGPGEFFVVPKGVEH 79
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 80-175 1.03e-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: 41.03  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  80 VTPSEMPGLNTLGLSIVRIDyaPQGINPLHTHPRASEILIVLEGSLEVgfiTSFPENrhiGKV----LQKGDAFVFPVGL 155
Cdd:cd20305    23 VDSKNFPISTTIAAALVTLE--PGALRELHWHPNADEWQYYISGKARM---TVFASG---GRArtfdFQAGDVGYVPRGY 94

                          90       100
                  ....*....|....*....|
gi 1333133355 156 VHYQRNPGPTNAVAIAALSS 175
Cdd:cd20305    95 GHYIENTGDEPLEFLEVFNS 114
cupin_MAE_RS03005 cd06987
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ...
 94-163 1.12e-04

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


Pssm-ID: 380392 [Multi-domain]  Cd Length: 122  Bit Score: 40.33  E-value: 1.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333133355  94 SIVRIdYAPQGINPLHTHPRASEILIVLEGSLEV---GFITSfpenrhigkvLQKGDAFVFPVGLVHYQRNPG 163
Cdd:cd06987    30 VVVEI-FDPGGRTPPNTHPAAHEMFFVLAGEGRAycdGQRVP----------LRPGDALVVPPGSEHVIENTG 91
cupin_yp_001338853-like cd07008
Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes ...
 107-168 1.36e-04

Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes bacterial proteins homologous to Klebsiella pneumoniae yp_001338853.1, an uncharacterized conserved protein with double-stranded beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380411 [Multi-domain]  Cd Length: 101  Bit Score: 39.93  E-value: 1.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333133355 107 PLHTHPRASEILIVLEGSLEvgFITSFPENRHIgkvlQKGDAFVFPVGLVHYQRNPGPTNAV 168
Cdd:cd07008    41 AAHIHPHGQDTWIVLSGEGE--YLLGDGQTVPI----KAGDIVIAPAGQVHGARNTGDEPLV 96
cupin_BLR7677-like cd02234
Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain; This family includes ...
 77-165 1.51e-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: 39.80  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  77 VTPVTPSEMPGLNTLGLSIVRIDYAPQGINPLHTHPrASEILIVLEGSLEVGFITSfPEnrhigKVLQKGDAFVFPVGLV 156
Cdd:cd02234     3 VTVLYSQPLPNIPGKEVTVLLVTYPPGAASPPHRHP-GFVFAYVLEGEVRSQVNGG-PP-----RVYKAGESFYEPPGAH 75

                          90
                  ....*....|
gi 1333133355 157 HYQ-RNPGPT 165
Cdd:cd02234    76 HRVsRNASAT 85
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 109-174 2.74e-04

TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of the tetracenomycin (TCM) polyketide synthase (PKS) type II complex in Streptomyces glaucescens. TcmJ is a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III. Orthologs of TcmJ include the Streptomyces BenD (benastatin biosynthetic pathway), the Streptomyces olivaceus ElmJ (polyketide antibiotic elloramycin biosynthetic pathway), the Actinomadura hibisca PdmL (pradimicin biosynthetic pathway), the Streptomyces cyaneus CurC (curamycin biosynthetic pathway), the Streptomyces rishiriensis Lct30 (lactonamycin biosynthetic pathway), and the Streptomyces WhiE II (spore pigment polyketide biosynthetic pathway). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380396 [Multi-domain]  Cd Length: 105  Bit Score: 38.81  E-value: 2.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333133355 109 HTHPRASEILIVLEGSLEVgfitSFPENRHigkVLQKGDAFVFPVGLVHYQRNPGPTNAVAIAALS 174
Cdd:cd06991    35 HYHPYSEEFLYVVRGRLVV----RVDGEPV---VLEAGEALLVPRGVRHRLENAGDEPARLVFHLS 93
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 74-166 2.82e-04

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


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 38.65  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  74 GCHVTPVT-PSEMPGLNtlgLSIVRIDYAPQGINPLHTHPRASEILIVLEGSLEVgfitsfpenrHIGKV---LQKGDAF 149
Cdd:cd02214     2 GSLIRELLhPDNDGDPR---YSLAHARVPPGESTLPHRLKGSEEVYYILEGEGTM----------EIDGEpreVGPGDAV 68

                          90
                  ....*....|....*..
gi 1333133355 150 VFPVGLVHYQRNPGPTN 166
Cdd:cd02214    69 LIPPGAVQRIENTGEED 85
RmlC COG4101
Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];
91-183 3.19e-04

Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];


Pssm-ID: 443277  Cd Length: 146  Bit Score: 39.56  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  91 LGLSIVRIdyAPQGINPLHTHPRASEILIVLEGSLEvgfiTSFPENRHIGKVLQKGDaFVF-PVGLVHYQRNPGPTN-AV 168
Cdd:COG4101    46 LWMGLVTI--PPGARAKAHHHGEHETAIYVLSGRAE----TRYGERLEHRVVTEPGD-FIFiPPGVPHQEINLSDTEpAV 118

                          90
                  ....*....|....*
gi 1333133355 169 AIAALSSQNPGVIIV 183
Cdd:COG4101   119 AVIARTDPNEQESVV 133
cupin_ChrR_1 cd20303
Marinobacter hydrocarbonoclasticus anti-ECFsigma factor ChrR, and similar proteins; 2 ...
 81-126 5.12e-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: 37.96  E-value: 5.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333133355  81 TPSEMPGLNTLGL--------SIVRidYAPQGINPLHTHPRASEILiVLEGSLE 126
Cdd:cd20303    15 VPGPVPGVERLPLhrfgaeatALVR--WAPGTRFPPHSHPGGEEIL-VLEGTFS 65
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 101-159 7.65e-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: 37.90  E-value: 7.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333133355 101 APQGIN-PLHTHPRASEILIVLEGSLEVgfitsfpenrHIGK---VLQKGDaFVF-PVGLVH-YQ 159
Cdd:cd02215    39 GPKGDAiPPHYHKRHHETFYVLEGRLQL----------WLDGesrLLTPGD-FASvPPGTIHaYR 92
cupin_7S_vicilin-like_N cd02244
7S vicilin seed storage globulin, N-terminal cupin domain; This family contains the N-terminal ...
 107-211 1.86e-03

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: 37.87  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355 107 PLHTHprASEILIVLEGSLEVGFITsfpENRHIGKVLQKGDAFVFPVGLVHYQRNPGPTNAVAIAAL----SSQNPGVII 182
Cdd:cd02244    43 PHHLD--ADMVFYVHTGRGTITWVD---EDKRESYNLERGDVYRIPAGSTFYLVNTDENEKLRIIALfdpvNSLTPGPFQ 117

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1333133355 183 VANAVFGSIPN-----ISSNILEKSFQINKKAIG 211
Cdd:cd02244   118 SFFGAGGQNPEsllsgFSKEILEAAFNVSEEELE 151
cupin_HNL-like cd02233
Granulicella tundricola hydroxynitrile lyase (GtHNL) and related proteins, cupin domain; This ...
 76-157 3.01e-03

Granulicella tundricola hydroxynitrile lyase (GtHNL) and related proteins, cupin domain; This family includes archaeal, eukaryotic, and bacterial proteins homologous to hydroxynitrile lyase from Granulicella tundricola (GtHNL), a novel class of HNLs that does not show any sequence or structural similarity to any other HNL and does not contain conserved motifs typical of HNLs. HNLs comprise a diverse group of enzymes that vary in terms of their substrate specificity, enantioselectivity and the need for a co-factor. In plants, they catalyze the reversible cleavage of cyanohydrins, yielding HCN and aldehydes or ketones. Also included in this family is TM1010 from Thermotoga maritima, a protein of unknown function. Some but not all members of this family have N- or C-terminal carboxymuconolactone decarboxylase domains in addition to the cupin domain. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380361 [Multi-domain]  Cd Length: 106  Bit Score: 35.99  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333133355  76 HVTPVTPSEMPGlntlGLSIVRIDYAPQGINPLHTHPRAsEILIVLEGsleVGFITSfpENRHIgKVLQKGDAFVFPVGL 155
Cdd:cd02233     6 WLDPLFPADEPS----RVSVANVTFEPGARTAWHTHPGG-QILIVTSG---VGWVQE--EGGPP-QELRPGDVVWIPPGV 74


                  ..
gi 1333133355 156 VH 157
Cdd:cd02233    75 KH 76
cupin_TTHA0104 cd06122
Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains ...
 107-168 4.66e-03

Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains bacterial proteins including TTHA0104 (also called TT1209), a putative antibiotic synthesis protein from Thermus thermophilus. TTHA0104 is a cupin-like protein. The 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).


Pssm-ID: 380377 [Multi-domain]  Cd Length: 102  Bit Score: 35.61  E-value: 4.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333133355 107 PLHTHPRASEILIVLEGSLEVgfitsfpenrHIG---KVLQKGDAFVFPVGLVHYQRNPGPTNAV 168
Cdd:cd06122    41 KVHAHAGSDKVYFVLEGEGRF----------TVGdeeRELGAGEAVLAPAGVPHGVRNTGAERLV 95
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 105-170 4.88e-03

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


Pssm-ID: 380343 [Multi-domain]  Cd Length: 126  Bit Score: 36.00  E-value: 4.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333133355 105 INP-----LHTHPRASEILIVLEGSLEVgfitsfpenRHIGKV--LQKGDAFVFPVGLVHYQRNPGPTNAVAI 170
Cdd:cd02213    47 VNPgkrlsLQRHHHRSEHWVVVSGTAEV---------TLDGKEklLKEGESIYIPKGTKHRLENPGKIPLEII 110
 
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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