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Conserved domains on  [gi|818399085|gb|KKQ77830|]
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MAG: Membrane protein-like protein [Parcubacteria group bacterium GW2011_GWA1_38_7]

Protein Classification

vitamin K epoxide reductase family protein( domain architecture ID 10191592)

vitamin K epoxide reductase (VKOR) family protein similar to human VKOR complex subunit 1 (VKORC1), an integral membrane protein and the catalytic subunit of the VKOR complex that reduces inactive vitamin K 2,3-epoxide to active vitamin K

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VKOR_5 cd12922
Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide ...
 7-138 5.09e-54

Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide reductase (VKOR) mostly present in actinobacteria. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade.


:

Pssm-ID: 240605  Cd Length: 133  Bit Score: 168.53  E-value: 5.09e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085   7 ILIVGSIIGLLASFLLTLDTIKLIKNPNVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLSIGIMLYSGGR 86
Cdd:cd12922    2 LLLVAGLIGLVASFVLTVEKIQLLEDPDYVLSCDINPVVSCGSVMQSWQASLFGFPNPLIGLAAFAVVITVGVALLAGAR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 818399085  87 SRKPLWLLVNLGTLASMIFIMWFFYQSVYNIGSLCIYCMIVWTVTWPLFLYT 138
Cdd:cd12922   82 LPRWFWVGLQAGLAAGLVFVHWLIYQSLFVIGALCPYCMVVWAVTIPLFWYV 133
 
Name Accession Description Interval E-value
VKOR_5 cd12922
Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide ...
 7-138 5.09e-54

Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide reductase (VKOR) mostly present in actinobacteria. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade.


Pssm-ID: 240605  Cd Length: 133  Bit Score: 168.53  E-value: 5.09e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085   7 ILIVGSIIGLLASFLLTLDTIKLIKNPNVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLSIGIMLYSGGR 86
Cdd:cd12922    2 LLLVAGLIGLVASFVLTVEKIQLLEDPDYVLSCDINPVVSCGSVMQSWQASLFGFPNPLIGLAAFAVVITVGVALLAGAR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 818399085  87 SRKPLWLLVNLGTLASMIFIMWFFYQSVYNIGSLCIYCMIVWTVTWPLFLYT 138
Cdd:cd12922   82 LPRWFWVGLQAGLAAGLVFVHWLIYQSLFVIGALCPYCMVVWAVTIPLFWYV 133
COG4243 COG4243
Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond ...
 6-153 6.12e-44

Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond formation [General function prediction only];


Pssm-ID: 443385  Cd Length: 161  Bit Score: 143.60  E-value: 6.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085   6 YILIVGSIIGLLASFLLTLDTIKLIKnPNVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLSIGIMLYSGG 85
Cdd:COG4243   13 WLLLVLALIGLLASFYLTLEKLTLLA-PGGVLSCDINPVVSCGSVLNSPQASVFGFPNALLGLAAFAVVITLAVALLAGA 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818399085  86 RSRKPLWLLVNLGTLASMIFIMWFFYQSVYNIGSLCIYCMIVWTVTWPLFLYTTIWNFRENHFVLQSL 153
Cdd:COG4243   92 RLPRWLWLALLAGALAGVVFSVWLIYQSLFVIGALCPYCLVVWAVTIPLFVLTTLGNLRRGWLDLGRL 159
VKOR pfam07884
Vitamin K epoxide reductase family; Vitamin K epoxide reductase (VKOR) recycles reduced ...
 7-139 1.36e-36

Vitamin K epoxide reductase family; Vitamin K epoxide reductase (VKOR) recycles reduced vitamin K, which is used subsequently as a co-factor in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. VKORC1 is a member of a large family of predicted enzymes that are present in vertebrates, Drosophila, plants, bacteria and archaea. Four cysteine residues and one residue, which is either serine or threonine, are identified as likely active-site residues. In some plant and bacterial homologs the VKORC1 homologous domain is fused with domains of the thioredoxin family of oxidoreductases.


Pssm-ID: 429714  Cd Length: 132  Bit Score: 123.88  E-value: 1.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085    7 ILIVGSIIGLLASFLLTLDtiKLIKNPNVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLSIGIMLYSGGR 86
Cdd:pfam07884   2 LLLVLALIGLLASAYLTLE--KLGPDPGYAASCDINGVVSCGKVLTSPYASVFGIPNALLGLLAYAVVAVLALAGLAGAR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 818399085   87 SRKPLWLLVNLGTLASMIFIMWFFYQSVYNIGSLCIYCMIVWTVTWPLFLYTT 139
Cdd:pfam07884  80 LPRWPWLLLLLGSLAGVVFSLYLIYISLFVIGALCPYCLVSAVVSLLLFVLTL 132
VKc smart00756
Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase; ...
 7-142 1.62e-30

Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase; Bacterial homologues are fused to members of the thioredoxin family of oxidoreductases.


Pssm-ID: 214805  Cd Length: 142  Bit Score: 108.96  E-value: 1.62e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085     7 ILIVGSIIGLLASFLLTLDTIKLIKNPNVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLSIGIMLYSGGR 86
Cdd:smart00756   7 ILLILGLIGLLASLYLTYEKLTLLEDPDYVASCDINPVVSCGKVLSSPYASIFGIPLSLLGIAAYLVVLALAVLGLLGVT 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 818399085    87 SRKPLWLLVNLGTLASMIFIMWFFYQSVYNIGSLCIYCMIVWTVTWPLFLYTTIWN 142
Cdd:smart00756  87 LPRWTWRLLFLGSLAGAVFSVYLIYLLVFVIKALCLYCILSAVVSISLFILVTIGR 142
PRK14889 PRK14889
VKOR family protein; Provisional
 6-126 4.20e-08

VKOR family protein; Provisional


Pssm-ID: 184883  Cd Length: 143  Bit Score: 50.08  E-value: 4.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085   6 YILIVGSIIGLLASFLLTLDTIKLIKNPNVslpCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLsIGIMLYSGG 85
Cdd:PRK14889  10 YLLLAFSLVGLIASIASYLLFTLLVKPPPF---CTINSVINCSSVLSSPYARFLGIPLDYLGAAWFSANI-ALALLGVGT 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 818399085  86 RSRKPLWLLVNLGTLASmIFIMWFFYQSVYNIGSLCIYCMI 126
Cdd:PRK14889  86 LKRILGRVISLWSIIGL-AIVPYLVYLEVFVLGAICIYCTI 125
 
Name Accession Description Interval E-value
VKOR_5 cd12922
Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide ...
 7-138 5.09e-54

Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide reductase (VKOR) mostly present in actinobacteria. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade.


Pssm-ID: 240605  Cd Length: 133  Bit Score: 168.53  E-value: 5.09e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085   7 ILIVGSIIGLLASFLLTLDTIKLIKNPNVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLSIGIMLYSGGR 86
Cdd:cd12922    2 LLLVAGLIGLVASFVLTVEKIQLLEDPDYVLSCDINPVVSCGSVMQSWQASLFGFPNPLIGLAAFAVVITVGVALLAGAR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 818399085  87 SRKPLWLLVNLGTLASMIFIMWFFYQSVYNIGSLCIYCMIVWTVTWPLFLYT 138
Cdd:cd12922   82 LPRWFWVGLQAGLAAGLVFVHWLIYQSLFVIGALCPYCMVVWAVTIPLFWYV 133
COG4243 COG4243
Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond ...
 6-153 6.12e-44

Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond formation [General function prediction only];


Pssm-ID: 443385  Cd Length: 161  Bit Score: 143.60  E-value: 6.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085   6 YILIVGSIIGLLASFLLTLDTIKLIKnPNVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLSIGIMLYSGG 85
Cdd:COG4243   13 WLLLVLALIGLLASFYLTLEKLTLLA-PGGVLSCDINPVVSCGSVLNSPQASVFGFPNALLGLAAFAVVITLAVALLAGA 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818399085  86 RSRKPLWLLVNLGTLASMIFIMWFFYQSVYNIGSLCIYCMIVWTVTWPLFLYTTIWNFRENHFVLQSL 153
Cdd:COG4243   92 RLPRWLWLALLAGALAGVVFSVWLIYQSLFVIGALCPYCLVVWAVTIPLFVLTTLGNLRRGWLDLGRL 159
VKOR pfam07884
Vitamin K epoxide reductase family; Vitamin K epoxide reductase (VKOR) recycles reduced ...
 7-139 1.36e-36

Vitamin K epoxide reductase family; Vitamin K epoxide reductase (VKOR) recycles reduced vitamin K, which is used subsequently as a co-factor in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. VKORC1 is a member of a large family of predicted enzymes that are present in vertebrates, Drosophila, plants, bacteria and archaea. Four cysteine residues and one residue, which is either serine or threonine, are identified as likely active-site residues. In some plant and bacterial homologs the VKORC1 homologous domain is fused with domains of the thioredoxin family of oxidoreductases.


Pssm-ID: 429714  Cd Length: 132  Bit Score: 123.88  E-value: 1.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085    7 ILIVGSIIGLLASFLLTLDtiKLIKNPNVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLSIGIMLYSGGR 86
Cdd:pfam07884   2 LLLVLALIGLLASAYLTLE--KLGPDPGYAASCDINGVVSCGKVLTSPYASVFGIPNALLGLLAYAVVAVLALAGLAGAR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 818399085   87 SRKPLWLLVNLGTLASMIFIMWFFYQSVYNIGSLCIYCMIVWTVTWPLFLYTT 139
Cdd:pfam07884  80 LPRWPWLLLLLGSLAGVVFSLYLIYISLFVIGALCPYCLVSAVVSLLLFVLTL 132
VKc smart00756
Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase; ...
 7-142 1.62e-30

Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase; Bacterial homologues are fused to members of the thioredoxin family of oxidoreductases.


Pssm-ID: 214805  Cd Length: 142  Bit Score: 108.96  E-value: 1.62e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085     7 ILIVGSIIGLLASFLLTLDTIKLIKNPNVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLSIGIMLYSGGR 86
Cdd:smart00756   7 ILLILGLIGLLASLYLTYEKLTLLEDPDYVASCDINPVVSCGKVLSSPYASIFGIPLSLLGIAAYLVVLALAVLGLLGVT 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 818399085    87 SRKPLWLLVNLGTLASMIFIMWFFYQSVYNIGSLCIYCMIVWTVTWPLFLYTTIWN 142
Cdd:smart00756  87 LPRWTWRLLFLGSLAGAVFSVYLIYLLVFVIKALCLYCILSAVVSISLFILVTIGR 142
VKOR cd10546
Vitamin K epoxide reductase (VKOR) family; VKOR (also named VKORC1) is an integral membrane ...
 6-138 1.02e-14

Vitamin K epoxide reductase (VKOR) family; VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. This family includes enzymes that are present in vertebrates, Drosophila, plants, bacteria, and archaea. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some plant and bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade. Warfarin, a widely used oral anticoagulant used in medicine as well as rodenticides, inhibits the activity of VKOR, resulting in decreased levels of reduced vitamin K, which is required for the function of several clotting factors. However, anticoagulation effect of warfarin is significantly associated with polymorphism of certain genes, including VKORC1. Interestingly, in rodents, an adaptive trait appears to have evolved convergently by selection on new or standing genetic polymorphisms in VKORC1 as well as by adaptive introgressive hybridization between species, likely brought about by human-mediated dispersal.


Pssm-ID: 240598  Cd Length: 126  Bit Score: 67.44  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085   6 YILIVGSIIGLLASFLLTLDTIKLIknpnVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLsigIMLYSGG 85
Cdd:cd10546    1 LILLLLAAIGLLVSLYLTYYELTEG----AVAGCDAGPSSSCDLVLTSRWSRIFGVPLSLLGALYYLVVL---GLLLSPP 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 818399085  86 RSRKPLWLLVNLGTLASMIFIMWFFYQSVYNIGSLCIYCMIVWTVTWPLFLYT 138
Cdd:cd10546   74 AGARLRWTALAAATFAGLGAAAWLIYLQLFVLGAFCPYCLVAHAAGLALLALT 126
VKOR_3 cd12920
Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide ...
 6-138 2.12e-14

Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide reductase (VKOR) present in proteobacteria and spirochetes. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade.


Pssm-ID: 240603  Cd Length: 134  Bit Score: 66.95  E-value: 2.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085   6 YILIVGSIIGLLASFLLTLDTIKLIKNPNVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLSIGIMLYSGG 85
Cdd:cd12920    1 AIALVLALIGLAFSGLLTYHHYGILTDGVGSSFCAINEVVNCDKVAQSPYSAIGGVPIALWGLLAYGFLAALFLLALISR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 818399085  86 RSRKPLWLLVNLGTLASMIFIMWFFYQSVYNIGSLCIYCMIVWTVTWPLFLYT 138
Cdd:cd12920   81 EDSERAAGLLFLVLLVGLVADLVLGLISVTAIGALCILCAGTYIVSAALLFGA 133
VKOR_arc cd12918
Vitamin K epoxide reductase family in archaea and some bacteria; This family includes vitamin ...
 6-127 1.41e-10

Vitamin K epoxide reductase family in archaea and some bacteria; This family includes vitamin K epoxide reductase (VKOR) mostly present in archaea and some bacteria. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade.


Pssm-ID: 240601  Cd Length: 126  Bit Score: 56.55  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085   6 YILIVGSIIGLLASFLLTLDTIklikNPNVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLlsIGIMLYSGG 85
Cdd:cd12918    1 LLGLALSLVGLLASAYLTYEHY----LKRPPLACTISGVINCEKVLSSPYSRILGVPLAVLGLAWFAVL--LVLSLLAAL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 818399085  86 RSRKPLWLLVNLGTLASmIFIMWFFYQSVYNIGSLCIYCMIV 127
Cdd:cd12918   75 RVRLLLGALLYWSILGI-AFVPYLVYLELFLIGAICLYCTVA 115
PRK14889 PRK14889
VKOR family protein; Provisional
 6-126 4.20e-08

VKOR family protein; Provisional


Pssm-ID: 184883  Cd Length: 143  Bit Score: 50.08  E-value: 4.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085   6 YILIVGSIIGLLASFLLTLDTIKLIKNPNVslpCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLsIGIMLYSGG 85
Cdd:PRK14889  10 YLLLAFSLVGLIASIASYLLFTLLVKPPPF---CTINSVINCSSVLSSPYARFLGIPLDYLGAAWFSANI-ALALLGVGT 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 818399085  86 RSRKPLWLLVNLGTLASmIFIMWFFYQSVYNIGSLCIYCMI 126
Cdd:PRK14889  86 LKRILGRVISLWSIIGL-AIVPYLVYLEVFVLGAICIYCTI 125
VKOR_1 cd12916
Vitamin K epoxide reductase family in bacteria and plants; This family includes vitamin K ...
 6-124 1.20e-05

Vitamin K epoxide reductase family in bacteria and plants; This family includes vitamin K epoxide reductase (VKOR) present in bacteria and plant. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some plant and bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade.


Pssm-ID: 240599  Cd Length: 133  Bit Score: 43.01  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085   6 YILIVGSIIGLLASFLLTLdtiklIKNPNVSLPCNinPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLSIGIM--LYS 83
Cdd:cd12916    3 RLIAGLALIGLLETAYLTY-----VKLTGSSAVCP--GGGGCDTVLNSPYATLLGIPLSLFGFLAYLAILVLAVLplLLK 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 818399085  84 GGRSRKPLWLLVNLGTLASMIFIMWFFYQSVYNIGSLCIYC 124
Cdd:cd12916   76 SEKLERWTWLLLFGLATAGVVFSAYLTYLLAFVIGAFCPYC 116
VKOR_4 cd12921
Vitamin K epoxide reductase (VKOR) family in bacteria; This family includes vitamin K epoxide ...
 6-137 7.04e-03

Vitamin K epoxide reductase (VKOR) family in bacteria; This family includes vitamin K epoxide reductase (VKOR) present only in bacteria. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade. This family also has a cysteine peptidase domain present at the N-terminus of the VKOR domain.


Pssm-ID: 240604  Cd Length: 128  Bit Score: 35.38  E-value: 7.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818399085   6 YILIVGSIIGLLASFLLTLDTIKlIKNPNVSLPCNINPFVSCTSVATAWQGEVFGFPNSLLGIVAFSMLLSIGIMLYSGG 85
Cdd:cd12921    1 LLLLLLSLIGLLISILLLLKELG-KSNKILKKFCSIGKKVDCNAVLKSKGAKIGGISLSELGLLYFFGLLLLLLLSPLNS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 818399085  86 RSRKPLWLLVnlgtLASMIFIMWFFYQSVYNIGSLCIYCMIVWTVTWPLFLY 137
Cdd:cd12921   80 SLLFLLSLLL----LLALPAELYSIYYQKFVIKKWCPLCLSIQAILWLLFLL 127
 
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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