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Conserved domains on  [gi|2524728712|gb|WJK72083|]
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vitamin K epoxide reductase complex subunit 1 [Lasiopodomys brandtii]

Protein Classification

vitamin K epoxide reductase family protein( domain architecture ID 10191574)

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_euk cd12917
Vitamin K epoxide reductase family in eukaryotes, excluding plants; This family includes ...
 10-149 3.30e-68

Vitamin K epoxide reductase family in eukaryotes, excluding 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. 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: 240600 [Multi-domain]  Cd Length: 140  Bit Score: 203.22  E-value: 3.30e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  10 RVRFALCLAGFALSLYALHVKAARARDEDYRALCDVGTSISCSRVFSSRWGRGFGLVEHVLGADSVLNQSNSIFGCMFYT 89
Cdd:cd12917     1 LLRLALCLAGLLLSLYALYVELKKERDPDYRALCDISESISCSKVFSSRYGRGFGLLGLILGKDSILNQPNSVFGIIFYI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  90 IQLLLGCLRGRWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAINVGLMLLS 149
Cdd:cd12917    81 LQLLLGLTNSAVAALLLLTLSILSVVGSLYLAYILYFVLKDFCIVCVSTYVVNFLLLILN 140
 
Name Accession Description Interval E-value
VKOR_euk cd12917
Vitamin K epoxide reductase family in eukaryotes, excluding plants; This family includes ...
 10-149 3.30e-68

Vitamin K epoxide reductase family in eukaryotes, excluding 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. 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: 240600 [Multi-domain]  Cd Length: 140  Bit Score: 203.22  E-value: 3.30e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  10 RVRFALCLAGFALSLYALHVKAARARDEDYRALCDVGTSISCSRVFSSRWGRGFGLVEHVLGADSVLNQSNSIFGCMFYT 89
Cdd:cd12917     1 LLRLALCLAGLLLSLYALYVELKKERDPDYRALCDISESISCSKVFSSRYGRGFGLLGLILGKDSILNQPNSVFGIIFYI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  90 IQLLLGCLRGRWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAINVGLMLLS 149
Cdd:cd12917    81 LQLLLGLTNSAVAALLLLTLSILSVVGSLYLAYILYFVLKDFCIVCVSTYVVNFLLLILN 140
VKc smart00756
Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase; ...
 5-150 9.94e-33

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: 113.20  E-value: 9.94e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712    5 WRNPGRVRFALCLAGFALSLYALHVKAARARDEDYRALCDVGTSISCSRVFSSRWGRGFGlvehvlgadsvlnQSNSIFG 84
Cdd:smart00756   1 PRWTRWILLILGLIGLLASLYLTYEKLTLLEDPDYVASCDINPVVSCGKVLSSPYASIFG-------------IPLSLLG 67

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524728712   85 CMFYTIQLLLGCLRG------RWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAINVGLMLLSF 150
Cdd:smart00756  68 IAAYLVVLALAVLGLlgvtlpRWTWRLLFLGSLAGAVFSVYLIYLLVFVIKALCLYCILSAVVSISLFILVT 139
VKOR pfam07884
Vitamin K epoxide reductase family; Vitamin K epoxide reductase (VKOR) recycles reduced ...
 11-150 5.59e-24

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: 90.36  E-value: 5.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  11 VRFALCLAGFALSLYALHVKaaRARDEDYRALCDVGTSISCSRVFSSRWGrgfglvehvlgadSVLNQSNSIFGCMFYTI 90
Cdd:pfam07884   2 LLLVLALIGLLASAYLTLEK--LGPDPGYAASCDINGVVSCGKVLTSPYA-------------SVFGIPNALLGLLAYAV 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524728712  91 QLLLGCLRG------RWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAINVGLMLLSF 150
Cdd:pfam07884  67 VAVLALAGLagarlpRWPWLLLLLGSLAGVVFSLYLIYISLFVIGALCPYCLVSAVVSLLLFVLTL 132
COG4243 COG4243
Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond ...
 1-150 6.38e-14

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: 65.41  E-value: 6.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712   1 MGTTWRNPGRVR---FALCLAGFALSLYaLHVKAARARDEDYRALCDVGTSISCSRVFSSRWGRGFGLvehvlgadsvln 77
Cdd:COG4243     1 MTSTRRRSRWLAwllLVLALIGLLASFY-LTLEKLTLLAPGGVLSCDINPVVSCGSVLNSPQASVFGF------------ 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524728712  78 qSNSIFGCMFYTIQL------LLGCLRGRWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAINVGLMLLSF 150
Cdd:COG4243    68 -PNALLGLAAFAVVItlavalLAGARLPRWLWLALLAGALAGVVFSVWLIYQSLFVIGALCPYCLVVWAVTIPLFVLTT 145
PRK14889 PRK14889
VKOR family protein; Provisional
 13-141 2.77e-03

VKOR family protein; Provisional


Pssm-ID: 184883  Cd Length: 143  Bit Score: 36.22  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  13 FALCLAGFALS-----LYALHVKAarardedyRALCDVGTSISCSRVFSSRWGRGFGLVEHVLGAdsvlnqsnsIFGCMF 87
Cdd:PRK14889   13 LAFSLVGLIASiasylLFTLLVKP--------PPFCTINSVINCSSVLSSPYARFLGIPLDYLGA---------AWFSAN 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2524728712  88 YTIQLLLGCLRGRWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAI 141
Cdd:PRK14889   76 IALALLGVGTLKRILGRVISLWSIIGLAIVPYLVYLEVFVLGAICIYCTIAHVS 129
 
Name Accession Description Interval E-value
VKOR_euk cd12917
Vitamin K epoxide reductase family in eukaryotes, excluding plants; This family includes ...
 10-149 3.30e-68

Vitamin K epoxide reductase family in eukaryotes, excluding 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. 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: 240600 [Multi-domain]  Cd Length: 140  Bit Score: 203.22  E-value: 3.30e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  10 RVRFALCLAGFALSLYALHVKAARARDEDYRALCDVGTSISCSRVFSSRWGRGFGLVEHVLGADSVLNQSNSIFGCMFYT 89
Cdd:cd12917     1 LLRLALCLAGLLLSLYALYVELKKERDPDYRALCDISESISCSKVFSSRYGRGFGLLGLILGKDSILNQPNSVFGIIFYI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  90 IQLLLGCLRGRWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAINVGLMLLS 149
Cdd:cd12917    81 LQLLLGLTNSAVAALLLLTLSILSVVGSLYLAYILYFVLKDFCIVCVSTYVVNFLLLILN 140
VKc smart00756
Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase; ...
 5-150 9.94e-33

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: 113.20  E-value: 9.94e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712    5 WRNPGRVRFALCLAGFALSLYALHVKAARARDEDYRALCDVGTSISCSRVFSSRWGRGFGlvehvlgadsvlnQSNSIFG 84
Cdd:smart00756   1 PRWTRWILLILGLIGLLASLYLTYEKLTLLEDPDYVASCDINPVVSCGKVLSSPYASIFG-------------IPLSLLG 67

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524728712   85 CMFYTIQLLLGCLRG------RWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAINVGLMLLSF 150
Cdd:smart00756  68 IAAYLVVLALAVLGLlgvtlpRWTWRLLFLGSLAGAVFSVYLIYLLVFVIKALCLYCILSAVVSISLFILVT 139
VKOR pfam07884
Vitamin K epoxide reductase family; Vitamin K epoxide reductase (VKOR) recycles reduced ...
 11-150 5.59e-24

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: 90.36  E-value: 5.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  11 VRFALCLAGFALSLYALHVKaaRARDEDYRALCDVGTSISCSRVFSSRWGrgfglvehvlgadSVLNQSNSIFGCMFYTI 90
Cdd:pfam07884   2 LLLVLALIGLLASAYLTLEK--LGPDPGYAASCDINGVVSCGKVLTSPYA-------------SVFGIPNALLGLLAYAV 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524728712  91 QLLLGCLRG------RWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAINVGLMLLSF 150
Cdd:pfam07884  67 VAVLALAGLagarlpRWPWLLLLLGSLAGVVFSLYLIYISLFVIGALCPYCLVSAVVSLLLFVLTL 132
COG4243 COG4243
Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond ...
 1-150 6.38e-14

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: 65.41  E-value: 6.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712   1 MGTTWRNPGRVR---FALCLAGFALSLYaLHVKAARARDEDYRALCDVGTSISCSRVFSSRWGRGFGLvehvlgadsvln 77
Cdd:COG4243     1 MTSTRRRSRWLAwllLVLALIGLLASFY-LTLEKLTLLAPGGVLSCDINPVVSCGSVLNSPQASVFGF------------ 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524728712  78 qSNSIFGCMFYTIQL------LLGCLRGRWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAINVGLMLLSF 150
Cdd:COG4243    68 -PNALLGLAAFAVVItlavalLAGARLPRWLWLALLAGALAGVVFSVWLIYQSLFVIGALCPYCLVVWAVTIPLFVLTT 145
VKOR cd10546
Vitamin K epoxide reductase (VKOR) family; VKOR (also named VKORC1) is an integral membrane ...
 13-149 3.08e-12

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: 60.13  E-value: 3.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  13 FALCLAGFALSLYALHVKAARARDedyrALCDVGTSISCSRVFSSRWGRGFGLvehvlgadsvlnqSNSIFGCMFYTIQL 92
Cdd:cd10546     4 LLLAAIGLLVSLYLTYYELTEGAV----AGCDAGPSSSCDLVLTSRWSRIFGV-------------PLSLLGALYYLVVL 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  93 LLGCLRG---RWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAINVGLMLLS 149
Cdd:cd10546    67 GLLLSPPagaRLRWTALAAATFAGLGAAAWLIYLQLFVLGAFCPYCLVAHAAGLALLALT 126
VKOR_1 cd12916
Vitamin K epoxide reductase family in bacteria and plants; This family includes vitamin K ...
 13-150 8.29e-08

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: 48.40  E-value: 8.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  13 FALCLAGFALSLYALHVKAARARdedyrALCdvGTSISCSRVFSSRWGRgfglvehvlgadsVLNQSNSIFGCMFYTIQL 92
Cdd:cd12916     6 AGLALIGLLETAYLTYVKLTGSS-----AVC--PGGGGCDTVLNSPYAT-------------LLGIPLSLFGFLAYLAIL 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524728712  93 LLGCLRGRWASVLLVLSSLVSLAG--------SVYLAWILFFVLHDFCIVCITTYAINVGLMLLSF 150
Cdd:cd12916    66 VLAVLPLLLKSEKLERWTWLLLFGlatagvvfSAYLTYLLAFVIGAFCPYCLTSAVLSTLLFLLTI 131
VKOR_arc cd12918
Vitamin K epoxide reductase family in archaea and some bacteria; This family includes vitamin ...
 13-149 7.12e-04

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: 37.68  E-value: 7.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  13 FALCLAGFALSLYALHVkaarARDEDYRALCDVGTSISCSRVFSSRWGRGFGLVEHVLGAdsvlnqsnsiFGCMFYTIQL 92
Cdd:cd12918     4 LALSLVGLLASAYLTYE----HYLKRPPLACTISGVINCEKVLSSPYSRILGVPLAVLGL----------AWFAVLLVLS 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2524728712  93 LLGCLRGRWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAINVGLMLLS 149
Cdd:cd12918    70 LLAALRVRLLLGALLYWSILGIAFVPYLVYLELFLIGAICLYCTVAHVIILALFIII 126
VKOR_3 cd12920
Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide ...
 13-150 1.06e-03

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: 37.29  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  13 FALCLAGFALSLYaLHVKAARAR-DEDYRALCDVGTSISCSRVFSSRWGRGFGLVEHVLGAdsvlnqsnSIFGCMFYTIQ 91
Cdd:cd12920     4 LVLALIGLAFSGL-LTYHHYGILtDGVGSSFCAINEVVNCDKVAQSPYSAIGGVPIALWGL--------LAYGFLAALFL 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  92 LLLGCLRG-RWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAINVGLMLLSF 150
Cdd:cd12920    75 LALISREDsERAAGLLFLVLLVGLVADLVLGLISVTAIGALCILCAGTYIVSAALLFGAW 134
VKOR_5 cd12922
Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide ...
 17-141 1.95e-03

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: 36.41  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  17 LAGFALSLYALHVKAARARDEDYRALCDVGTSISCSRVFSSRWGRGFGLvehvlgadsvlnqSNSIFGCMFYTIQLLLGC 96
Cdd:cd12922     8 LIGLVASFVLTVEKIQLLEDPDYVLSCDINPVVSCGSVMQSWQASLFGF-------------PNPLIGLAAFAVVITVGV 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2524728712  97 L---RGRWASVLLVLSSLVSLAGSVYLAWILF---FVLHDFCIVCITTYAI 141
Cdd:cd12922    75 AllaGARLPRWFWVGLQAGLAAGLVFVHWLIYqslFVIGALCPYCMVVWAV 125
PRK14889 PRK14889
VKOR family protein; Provisional
 13-141 2.77e-03

VKOR family protein; Provisional


Pssm-ID: 184883  Cd Length: 143  Bit Score: 36.22  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  13 FALCLAGFALS-----LYALHVKAarardedyRALCDVGTSISCSRVFSSRWGRGFGLVEHVLGAdsvlnqsnsIFGCMF 87
Cdd:PRK14889   13 LAFSLVGLIASiasylLFTLLVKP--------PPFCTINSVINCSSVLSSPYARFLGIPLDYLGA---------AWFSAN 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2524728712  88 YTIQLLLGCLRGRWASVLLVLSSLVSLAGSVYLAWILFFVLHDFCIVCITTYAI 141
Cdd:PRK14889   76 IALALLGVGTLKRILGRVISLWSIIGLAIVPYLVYLEVFVLGAICIYCTIAHVS 129
VKOR_4 cd12921
Vitamin K epoxide reductase (VKOR) family in bacteria; This family includes vitamin K epoxide ...
 13-149 8.68e-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: 34.61  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524728712  13 FALCLAGFALSLYALHvKAARARDEDYRALCDVGTSISCSRVFSSRWGRGFGLvehvlgadsvlnqSNSIFGCMFYTIQL 92
Cdd:cd12921     4 LLLSLIGLLISILLLL-KELGKSNKILKKFCSIGKKVDCNAVLKSKGAKIGGI-------------SLSELGLLYFFGLL 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2524728712  93 LLGCLRGRWASVLLVLSSLVSLA--GSVYLAWILFFVLHDFCIVCITTYAINVGLMLLS 149
Cdd:cd12921    70 LLLLLSPLNSSLLFLLSLLLLLAlpAELYSIYYQKFVIKKWCPLCLSIQAILWLLFLLL 128
 
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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