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Conserved domains on  [gi|767946904|ref|XP_011514133|]
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vitamin K epoxide reductase complex subunit 1-like protein 1 isoform X2 [Homo sapiens]

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 ...
 36-127 1.14e-54

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: 168.16  E-value: 1.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946904  36 KWGRGFGLLGSIFGKDGVLNQPNSVFGLIFYILQLLLGMTASAVAALILMTSSIMSVVGSLYLAYILYFVLKEFCIICIV 115
Cdd:cd12917   49 RYGRGFGLLGLILGKDSILNQPNSVFGIIFYILQLLLGLTNSAVAALLLLTLSILSVVGSLYLAYILYFVLKDFCIVCVS 128

                         90
                 ....*....|..
gi 767946904 116 TYVLNFLLLIIN 127
Cdd:cd12917  129 TYVVNFLLLILN 140
 
Name Accession Description Interval E-value
VKOR_euk cd12917
Vitamin K epoxide reductase family in eukaryotes, excluding plants; This family includes ...
 36-127 1.14e-54

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: 168.16  E-value: 1.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946904  36 KWGRGFGLLGSIFGKDGVLNQPNSVFGLIFYILQLLLGMTASAVAALILMTSSIMSVVGSLYLAYILYFVLKEFCIICIV 115
Cdd:cd12917   49 RYGRGFGLLGLILGKDSILNQPNSVFGIIFYILQLLLGLTNSAVAALLLLTLSILSVVGSLYLAYILYFVLKDFCIVCVS 128

                         90
                 ....*....|..
gi 767946904 116 TYVLNFLLLIIN 127
Cdd:cd12917  129 TYVVNFLLLILN 140
VKOR pfam07884
Vitamin K epoxide reductase family; Vitamin K epoxide reductase (VKOR) recycles reduced ...
 53-128 2.97e-18

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: 75.34  E-value: 2.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946904   53 VLNQPNSVFGLIFYILQLLLGMTASAVA------ALILMTSSIMSVVGSLYLAYILYFVLKEFCIICIVTYVLNFLLLII 126
Cdd:pfam07884  51 VFGIPNALLGLLAYAVVAVLALAGLAGArlprwpWLLLLLGSLAGVVFSLYLIYISLFVIGALCPYCLVSAVVSLLLFVL 130


                  ..
gi 767946904  127 NY 128
Cdd:pfam07884 131 TL 132
VKc smart00756
Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase; ...
 53-126 1.81e-14

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: 65.82  E-value: 1.81e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946904    53 VLNQPNSVFGLIFYILQLLLGMTASA------VAALILMTSSIMSVVGSLYLAYILYFVLKEFCIICIVTYVLNFLLLII 126
Cdd:smart00756  58 IFGIPLSLLGIAAYLVVLALAVLGLLgvtlprWTWRLLFLGSLAGAVFSVYLIYLLVFVIKALCLYCILSAVVSISLFIL 137
COG4243 COG4243
Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond ...
 53-126 4.24e-10

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: 54.62  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946904  53 VLNQPNSVFGLIFYILQLLLGMTASAVAAL------ILMTSSIMSVVGSLYLAYILYFVLKEFCIICIVTYVLNFLLLII 126
Cdd:COG4243   64 VFGFPNALLGLAAFAVVITLAVALLAGARLprwlwlALLAGALAGVVFSVWLIYQSLFVIGALCPYCLVVWAVTIPLFVL 143
 
Name Accession Description Interval E-value
VKOR_euk cd12917
Vitamin K epoxide reductase family in eukaryotes, excluding plants; This family includes ...
 36-127 1.14e-54

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: 168.16  E-value: 1.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946904  36 KWGRGFGLLGSIFGKDGVLNQPNSVFGLIFYILQLLLGMTASAVAALILMTSSIMSVVGSLYLAYILYFVLKEFCIICIV 115
Cdd:cd12917   49 RYGRGFGLLGLILGKDSILNQPNSVFGIIFYILQLLLGLTNSAVAALLLLTLSILSVVGSLYLAYILYFVLKDFCIVCVS 128

                         90
                 ....*....|..
gi 767946904 116 TYVLNFLLLIIN 127
Cdd:cd12917  129 TYVVNFLLLILN 140
VKOR pfam07884
Vitamin K epoxide reductase family; Vitamin K epoxide reductase (VKOR) recycles reduced ...
 53-128 2.97e-18

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: 75.34  E-value: 2.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946904   53 VLNQPNSVFGLIFYILQLLLGMTASAVA------ALILMTSSIMSVVGSLYLAYILYFVLKEFCIICIVTYVLNFLLLII 126
Cdd:pfam07884  51 VFGIPNALLGLLAYAVVAVLALAGLAGArlprwpWLLLLLGSLAGVVFSLYLIYISLFVIGALCPYCLVSAVVSLLLFVL 130


                  ..
gi 767946904  127 NY 128
Cdd:pfam07884 131 TL 132
VKc smart00756
Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase; ...
 53-126 1.81e-14

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: 65.82  E-value: 1.81e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946904    53 VLNQPNSVFGLIFYILQLLLGMTASA------VAALILMTSSIMSVVGSLYLAYILYFVLKEFCIICIVTYVLNFLLLII 126
Cdd:smart00756  58 IFGIPLSLLGIAAYLVVLALAVLGLLgvtlprWTWRLLFLGSLAGAVFSVYLIYLLVFVIKALCLYCILSAVVSISLFIL 137
COG4243 COG4243
Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond ...
 53-126 4.24e-10

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: 54.62  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946904  53 VLNQPNSVFGLIFYILQLLLGMTASAVAAL------ILMTSSIMSVVGSLYLAYILYFVLKEFCIICIVTYVLNFLLLII 126
Cdd:COG4243   64 VFGFPNALLGLAAFAVVITLAVALLAGARLprwlwlALLAGALAGVVFSVWLIYQSLFVIGALCPYCLVVWAVTIPLFVL 143
VKOR cd10546
Vitamin K epoxide reductase (VKOR) family; VKOR (also named VKORC1) is an integral membrane ...
 43-125 4.01e-09

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: 51.27  E-value: 4.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946904  43 LLGSIFGKdgVLNQPNSVFGLIFYILQLLLGMTASAVAAL---ILMTSSIMSVVGSLYLAYILYFVLKEFCIICIVTYVL 119
Cdd:cd10546   41 VLTSRWSR--IFGVPLSLLGALYYLVVLGLLLSPPAGARLrwtALAAATFAGLGAAAWLIYLQLFVLGAFCPYCLVAHAA 118


                 ....*.
gi 767946904 120 NFLLLI 125
Cdd:cd10546  119 GLALLA 124
VKOR_1 cd12916
Vitamin K epoxide reductase family in bacteria and plants; This family includes vitamin K ...
 53-126 5.93e-09

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: 51.10  E-value: 5.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946904  53 VLNQPNSVFGLIFYILQLLLGMTASAVAA---------LILMTSSIMSVVgSLYLAYILYFVLKEFCIICIVTYVLNFLL 123
Cdd:cd12916   48 LLGIPLSLFGFLAYLAILVLAVLPLLLKSeklerwtwlLLFGLATAGVVF-SAYLTYLLAFVIGAFCPYCLTSAVLSTLL 126


                 ...
gi 767946904 124 LII 126
Cdd:cd12916  127 FLL 129
VKOR_3 cd12920
Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide ...
 53-128 7.37e-08

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: 48.07  E-value: 7.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946904  53 VLNQPNSVFGLIFY-------ILQLLLGMTASAVAALILMTSSIMsVVGSLYLAYILYFVLKEFCIICIVTYVLNFLLLI 125
Cdd:cd12920   53 IGGVPIALWGLLAYgflaalfLLALISREDSERAAGLLFLVLLVG-LVADLVLGLISVTAIGALCILCAGTYIVSAALLF 131


                 ...
gi 767946904 126 INY 128
Cdd:cd12920  132 GAW 134
VKOR_arc cd12918
Vitamin K epoxide reductase family in archaea and some bacteria; This family includes vitamin ...
 57-126 8.85e-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: 36.91  E-value: 8.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767946904  57 PNSVFGLIFYILQLLLGMTASAVAALILMTSSIMSVVGS---LYLAYILYFVLKEFCIICIVTYVLNFLLLII 126
Cdd:cd12918   53 PLAVLGLAWFAVLLVLSLLAALRVRLLLGALLYWSILGIafvPYLVYLELFLIGAICLYCTVAHVIILALFII 125
VKOR_4 cd12921
Vitamin K epoxide reductase (VKOR) family in bacteria; This family includes vitamin K epoxide ...
 59-127 1.23e-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: 36.53  E-value: 1.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767946904  59 SVFGLIFYILQLLLGMTASAVAAL--ILMTSSIMSVVGSLYLAYILYFVLKEFCIICIVTYVLNFLLLIIN 127
Cdd:cd12921   58 SELGLLYFFGLLLLLLLSPLNSSLlfLLSLLLLLALPAELYSIYYQKFVIKKWCPLCLSIQAILWLLFLLL 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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