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Conserved domains on  [gi|489510148|ref|WP_003415007|]
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MULTISPECIES: vitamin K epoxide reductase family protein [Mycobacterium]

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 ...
 24-156 5.87e-56

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: 173.92  E-value: 5.87e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  24 WWVLIGGVIGLFASMTLTVEKVRILLDPIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVLAVAKV 103
Cdd:cd12922    1 WLLLVAGLIGLVASFVLTVEKIQLLEDPDYVLSCDINPVVSCGSVMQSWQASLFGFPNPLIGLAAFAVVITVGVALLAGA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489510148 104 PLPRWYWIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVV 156
Cdd:cd12922   81 RLPRWFWVGLQAGLAAGLVFVHWLIYQSLFVIGALCPYCMVVWAVTIPLFWYV 133
 
Name Accession Description Interval E-value
VKOR_5 cd12922
Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide ...
 24-156 5.87e-56

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: 173.92  E-value: 5.87e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  24 WWVLIGGVIGLFASMTLTVEKVRILLDPIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVLAVAKV 103
Cdd:cd12922    1 WLLLVAGLIGLVASFVLTVEKIQLLEDPDYVLSCDINPVVSCGSVMQSWQASLFGFPNPLIGLAAFAVVITVGVALLAGA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489510148 104 PLPRWYWIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVV 156
Cdd:cd12922   81 RLPRWFWVGLQAGLAAGLVFVHWLIYQSLFVIGALCPYCMVVWAVTIPLFWYV 133
COG4243 COG4243
Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond ...
 13-156 2.14e-45

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: 147.84  E-value: 2.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  13 PAAVRVPVPSAWWVLIGGVIGLFASMTLTVEKVRILLdPIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVV 92
Cdd:COG4243    2 TSTRRRSRWLAWLLLVLALIGLLASFYLTLEKLTLLA-PGGVLSCDINPVVSCGSVLNSPQASVFGFPNALLGLAAFAVV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489510148  93 VVTGVLAVAKVPLPRWYWIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVV 156
Cdd:COG4243   81 ITLAVALLAGARLPRWLWLALLAGALAGVVFSVWLIYQSLFVIGALCPYCLVVWAVTIPLFVLT 144
VKc smart00756
Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase; ...
 19-160 2.82e-43

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: 142.09  E-value: 2.82e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148    19 PVPSAWWVLIGGVIGLFASMTLTVEKVRILLDPIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVL 98
Cdd:smart00756   1 PRWTRWILLILGLIGLLASLYLTYEKLTLLEDPDYVASCDINPVVSCGKVLSSPYASIFGIPLSLLGIAAYLVVLALAVL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489510148    99 AVAKVPLPRWYWIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVVASIV 160
Cdd:smart00756  81 GLLGVTLPRWTWRLLFLGSLAGAVFSVYLIYLLVFVIKALCLYCILSAVVSISLFILVTIGR 142
VKOR pfam07884
Vitamin K epoxide reductase family; Vitamin K epoxide reductase (VKOR) recycles reduced ...
 24-156 8.34e-39

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: 130.04  E-value: 8.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148   24 WWVLIGGVIGLFASMTLTVEKVRilLDPIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVLAVAKV 103
Cdd:pfam07884   1 LLLLVLALIGLLASAYLTLEKLG--PDPGYAASCDINGVVSCGKVLTSPYASVFGIPNALLGLLAYAVVAVLALAGLAGA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489510148  104 PLPRWYWIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVV 156
Cdd:pfam07884  79 RLPRWPWLLLLLGSLAGVVFSLYLIYISLFVIGALCPYCLVSAVVSLLLFVLT 131
PRK14889 PRK14889
VKOR family protein; Provisional
 30-158 1.73e-07

VKOR family protein; Provisional


Pssm-ID: 184883  Cd Length: 143  Bit Score: 48.54  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  30 GVIGLFASMTLTVEKVRILLDPiyvPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVLAVAKvpLPRWY 109
Cdd:PRK14889  16 SLVGLIASIASYLLFTLLVKPP---PFCTINSVINCSSVLSSPYARFLGIPLDYLGAAWFSANIALALLGVGT--LKRIL 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489510148 110 WIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVVAS 158
Cdd:PRK14889  91 GRVISLWSIIGLAIVPYLVYLEVFVLGAICIYCTIAHVSILAAFILILI 139
 
Name Accession Description Interval E-value
VKOR_5 cd12922
Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide ...
 24-156 5.87e-56

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: 173.92  E-value: 5.87e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  24 WWVLIGGVIGLFASMTLTVEKVRILLDPIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVLAVAKV 103
Cdd:cd12922    1 WLLLVAGLIGLVASFVLTVEKIQLLEDPDYVLSCDINPVVSCGSVMQSWQASLFGFPNPLIGLAAFAVVITVGVALLAGA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489510148 104 PLPRWYWIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVV 156
Cdd:cd12922   81 RLPRWFWVGLQAGLAAGLVFVHWLIYQSLFVIGALCPYCMVVWAVTIPLFWYV 133
COG4243 COG4243
Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond ...
 13-156 2.14e-45

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: 147.84  E-value: 2.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  13 PAAVRVPVPSAWWVLIGGVIGLFASMTLTVEKVRILLdPIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVV 92
Cdd:COG4243    2 TSTRRRSRWLAWLLLVLALIGLLASFYLTLEKLTLLA-PGGVLSCDINPVVSCGSVLNSPQASVFGFPNALLGLAAFAVV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489510148  93 VVTGVLAVAKVPLPRWYWIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVV 156
Cdd:COG4243   81 ITLAVALLAGARLPRWLWLALLAGALAGVVFSVWLIYQSLFVIGALCPYCLVVWAVTIPLFVLT 144
VKc smart00756
Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase; ...
 19-160 2.82e-43

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: 142.09  E-value: 2.82e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148    19 PVPSAWWVLIGGVIGLFASMTLTVEKVRILLDPIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVL 98
Cdd:smart00756   1 PRWTRWILLILGLIGLLASLYLTYEKLTLLEDPDYVASCDINPVVSCGKVLSSPYASIFGIPLSLLGIAAYLVVLALAVL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489510148    99 AVAKVPLPRWYWIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVVASIV 160
Cdd:smart00756  81 GLLGVTLPRWTWRLLFLGSLAGAVFSVYLIYLLVFVIKALCLYCILSAVVSISLFILVTIGR 142
VKOR pfam07884
Vitamin K epoxide reductase family; Vitamin K epoxide reductase (VKOR) recycles reduced ...
 24-156 8.34e-39

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: 130.04  E-value: 8.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148   24 WWVLIGGVIGLFASMTLTVEKVRilLDPIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVLAVAKV 103
Cdd:pfam07884   1 LLLLVLALIGLLASAYLTLEKLG--PDPGYAASCDINGVVSCGKVLTSPYASVFGIPNALLGLLAYAVVAVLALAGLAGA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489510148  104 PLPRWYWIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVV 156
Cdd:pfam07884  79 RLPRWPWLLLLLGSLAGVVFSLYLIYISLFVIGALCPYCLVSAVVSLLLFVLT 131
VKOR_arc cd12918
Vitamin K epoxide reductase family in archaea and some bacteria; This family includes vitamin ...
 27-156 1.12e-14

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: 67.72  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  27 LIGGVIGLFASMTLTVEkvriLLDPIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVLAVAKVPLP 106
Cdd:cd12918    4 LALSLVGLLASAYLTYE----HYLKRPPLACTISGVINCEKVLSSPYSRILGVPLAVLGLAWFAVLLVLSLLAALRVRLL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489510148 107 RWYWIGLAVgilVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVV 156
Cdd:cd12918   80 LGALLYWSI---LGIAFVPYLVYLELFLIGAICLYCTVAHVIILALFIII 126
VKOR_3 cd12920
Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide ...
 26-155 1.91e-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: 67.33  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  26 VLIGGVIGLFASMTLTVEKVRILLDPIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVLAVAKVPL 105
Cdd:cd12920    3 ALVLALIGLAFSGLLTYHHYGILTDGVGSSFCAINEVVNCDKVAQSPYSAIGGVPIALWGLLAYGFLAALFLLALISRED 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489510148 106 PRWYWIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVV 155
Cdd:cd12920   83 SERAAGLLFLVLLVGLVADLVLGLISVTAIGALCILCAGTYIVSAALLFG 132
VKOR cd10546
Vitamin K epoxide reductase (VKOR) family; VKOR (also named VKORC1) is an integral membrane ...
 24-156 1.72e-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: 61.67  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  24 WWVLIGGVIGLFASMTLTVEKVRIlldpIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVLAVakv 103
Cdd:cd10546    1 LILLLLAAIGLLVSLYLTYYELTE----GAVAGCDAGPSSSCDLVLTSRWSRIFGVPLSLLGALYYLVVLGLLLSPP--- 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489510148 104 PLPRWYWIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVV 156
Cdd:cd10546   74 AGARLRWTALAAATFAGLGAAAWLIYLQLFVLGAFCPYCLVAHAAGLALLALT 126
VKOR_1 cd12916
Vitamin K epoxide reductase family in bacteria and plants; This family includes vitamin K ...
 64-159 4.61e-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: 49.95  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  64 SCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVLAVAKVP--LPRWYWIGLAVGILVGVAFVHWLIFQSLYRIGALCPY 141
Cdd:cd12916   36 GCDTVLNSPYATLLGIPLSLFGFLAYLAILVLAVLPLLLKSekLERWTWLLLFGLATAGVVFSAYLTYLLAFVIGAFCPY 115

                         90
                 ....*....|....*...
gi 489510148 142 CmVVWAVIATLLVVVASI 159
Cdd:cd12916  116 C-LTSAVLSTLLFLLTIL 132
PRK14889 PRK14889
VKOR family protein; Provisional
 30-158 1.73e-07

VKOR family protein; Provisional


Pssm-ID: 184883  Cd Length: 143  Bit Score: 48.54  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  30 GVIGLFASMTLTVEKVRILLDPiyvPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVLAVAKvpLPRWY 109
Cdd:PRK14889  16 SLVGLIASIASYLLFTLLVKPP---PFCTINSVINCSSVLSSPYARFLGIPLDYLGAAWFSANIALALLGVGT--LKRIL 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489510148 110 WIGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVVVAS 158
Cdd:PRK14889  91 GRVISLWSIIGLAIVPYLVYLEVFVLGAICIYCTIAHVSILAAFILILI 139
VKOR_4 cd12921
Vitamin K epoxide reductase (VKOR) family in bacteria; This family includes vitamin K epoxide ...
 31-155 1.42e-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: 37.30  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  31 VIGLFASMTLtVEKVRILLDPIYVPSCNVNPIVSCGSVMTTPQASLLGFPNPLLGIAGFTVVVVTGVLAvakvPLPRWYW 110
Cdd:cd12921    8 LIGLLISILL-LLKELGKSNKILKKFCSIGKKVDCNAVLKSKGAKIGGISLSELGLLYFFGLLLLLLLS----PLNSSLL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489510148 111 IGLAVGILVGVAFVHWLIFQSLYRIGALCPYCMVVWAVIATLLVV 155
Cdd:cd12921   83 FLLSLLLLLALPAELYSIYYQKFVIKKWCPLCLSIQAILWLLFLL 127
VKOR_euk cd12917
Vitamin K epoxide reductase family in eukaryotes, excluding plants; This family includes ...
 24-89 1.75e-03

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: 37.20  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510148  24 WWVLIGGVIGLFASM-TLTVEkVRILLDPIYVPSCNVNPIVSCGSVMTTPQASLLGF-------------PNPLLGIAGF 89
Cdd:cd12917    1 LLRLALCLAGLLLSLyALYVE-LKKERDPDYRALCDISESISCSKVFSSRYGRGFGLlglilgkdsilnqPNSVFGIIFY 79
 
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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