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Conserved domains on  [gi|42627869|ref|NP_976083|]
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vitamin K epoxide reductase complex subunit 1-like protein 1 [Rattus norvegicus]

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 ...
 18-156 3.59e-77

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: 226.33  E-value: 3.59e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  18 ARYAVCAAGILLSIYAYHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGLLGSIFGKDGVLNQPNSVFGLIFYIL 97
Cdd:cd12917   2 LRLALCLAGLLLSLYALYVELKKERDPDYRALCDISESISCSKVFSSRYGRGFGLLGLILGKDSILNQPNSVFGIIFYIL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42627869  98 QLLLGMTASAVAALVLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLIIN 156
Cdd:cd12917  82 QLLLGLTNSAVAALLLLTLSILSVVGSLYLAYILYFVLKDFCIVCVSTYVVNFLLLILN 140
 
Name Accession Description Interval E-value
VKOR_euk cd12917
Vitamin K epoxide reductase family in eukaryotes, excluding plants; This family includes ...
 18-156 3.59e-77

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: 226.33  E-value: 3.59e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  18 ARYAVCAAGILLSIYAYHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGLLGSIFGKDGVLNQPNSVFGLIFYIL 97
Cdd:cd12917   2 LRLALCLAGLLLSLYALYVELKKERDPDYRALCDISESISCSKVFSSRYGRGFGLLGLILGKDSILNQPNSVFGIIFYIL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42627869  98 QLLLGMTASAVAALVLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLIIN 156
Cdd:cd12917  82 QLLLGLTNSAVAALLLLTLSILSVVGSLYLAYILYFVLKDFCIVCVSTYVVNFLLLILN 140
VKc smart00756
Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase; ...
 12-155 8.82e-29

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: 103.57  E-value: 8.82e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869     12 PRWERVARYAVCAAGILLSIYAYHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGllgsifgkdgvlnQPNSVFG 91
Cdd:smart00756   1 PRWTRWILLILGLIGLLASLYLTYEKLTLLEDPDYVASCDINPVVSCGKVLSSPYASIFG-------------IPLSLLG 67

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869     92 LIFYILQLLLGMTASA------VAALVLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLII 155
Cdd:smart00756  68 IAAYLVVLALAVLGLLgvtlprWTWRLLFLGSLAGAVFSVYLIYLLVFVIKALCLYCILSAVVSISLFIL 137
VKOR pfam07884
Vitamin K epoxide reductase family; Vitamin K epoxide reductase (VKOR) recycles reduced ...
 21-157 2.72e-26

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: 96.91  E-value: 2.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869    21 AVCAAGILLSIYAYHVEREkeRDPEHRALCDLGPWVKCSAALASRWGRgfgllgsifgkdgVLNQPNSVFGLIFYILQLL 100
Cdd:pfam07884   5 VLALIGLLASAYLTLEKLG--PDPGYAASCDINGVVSCGKVLTSPYAS-------------VFGIPNALLGLLAYAVVAV 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42627869   101 LGMTASAVA------ALVLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLIINY 157
Cdd:pfam07884  70 LALAGLAGArlprwpWLLLLLGSLAGVVFSLYLIYISLFVIGALCPYCLVSAVVSLLLFVLTL 132
COG4243 COG4243
Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond ...
 12-155 4.57e-17

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: 73.88  E-value: 4.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  12 PRWERVARYAVCAAGILLSIYAyHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGLlgsifgkdgvlnqPNSVFG 91
Cdd:COG4243   8 SRWLAWLLLVLALIGLLASFYL-TLEKLTLLAPGGVLSCDINPVVSCGSVLNSPQASVFGF-------------PNALLG 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  92 LIFYILQLLLGMTASAVAAL------VLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLII 155
Cdd:COG4243  74 LAAFAVVITLAVALLAGARLprwlwlALLAGALAGVVFSVWLIYQSLFVIGALCPYCLVVWAVTIPLFVL 143
PRK14889 PRK14889
VKOR family protein; Provisional
 21-155 5.57e-04

VKOR family protein; Provisional


Pssm-ID: 184883  Cd Length: 143  Bit Score: 38.53  E-value: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869   21 AVCAAGILLSIYAYHVEREKERDPehrALCDLGPWVKCSAALASRWGRGFGLlgsifgkdgvlnqPNSVFGLIFYILQLL 100
Cdd:PRK14889  14 AFSLVGLIASIASYLLFTLLVKPP---PFCTINSVINCSSVLSSPYARFLGI-------------PLDYLGAAWFSANIA 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42627869  101 LGM----TASAVAALVLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLII 155
Cdd:PRK14889  78 LALlgvgTLKRILGRVISLWSIIGLAIVPYLVYLEVFVLGAICIYCTIAHVSILAAFIL 136
 
Name Accession Description Interval E-value
VKOR_euk cd12917
Vitamin K epoxide reductase family in eukaryotes, excluding plants; This family includes ...
 18-156 3.59e-77

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: 226.33  E-value: 3.59e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  18 ARYAVCAAGILLSIYAYHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGLLGSIFGKDGVLNQPNSVFGLIFYIL 97
Cdd:cd12917   2 LRLALCLAGLLLSLYALYVELKKERDPDYRALCDISESISCSKVFSSRYGRGFGLLGLILGKDSILNQPNSVFGIIFYIL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42627869  98 QLLLGMTASAVAALVLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLIIN 156
Cdd:cd12917  82 QLLLGLTNSAVAALLLLTLSILSVVGSLYLAYILYFVLKDFCIVCVSTYVVNFLLLILN 140
VKc smart00756
Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase; ...
 12-155 8.82e-29

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: 103.57  E-value: 8.82e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869     12 PRWERVARYAVCAAGILLSIYAYHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGllgsifgkdgvlnQPNSVFG 91
Cdd:smart00756   1 PRWTRWILLILGLIGLLASLYLTYEKLTLLEDPDYVASCDINPVVSCGKVLSSPYASIFG-------------IPLSLLG 67

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869     92 LIFYILQLLLGMTASA------VAALVLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLII 155
Cdd:smart00756  68 IAAYLVVLALAVLGLLgvtlprWTWRLLFLGSLAGAVFSVYLIYLLVFVIKALCLYCILSAVVSISLFIL 137
VKOR pfam07884
Vitamin K epoxide reductase family; Vitamin K epoxide reductase (VKOR) recycles reduced ...
 21-157 2.72e-26

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: 96.91  E-value: 2.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869    21 AVCAAGILLSIYAYHVEREkeRDPEHRALCDLGPWVKCSAALASRWGRgfgllgsifgkdgVLNQPNSVFGLIFYILQLL 100
Cdd:pfam07884   5 VLALIGLLASAYLTLEKLG--PDPGYAASCDINGVVSCGKVLTSPYAS-------------VFGIPNALLGLLAYAVVAV 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42627869   101 LGMTASAVA------ALVLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLIINY 157
Cdd:pfam07884  70 LALAGLAGArlprwpWLLLLLGSLAGVVFSLYLIYISLFVIGALCPYCLVSAVVSLLLFVLTL 132
COG4243 COG4243
Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond ...
 12-155 4.57e-17

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: 73.88  E-value: 4.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  12 PRWERVARYAVCAAGILLSIYAyHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGLlgsifgkdgvlnqPNSVFG 91
Cdd:COG4243   8 SRWLAWLLLVLALIGLLASFYL-TLEKLTLLAPGGVLSCDINPVVSCGSVLNSPQASVFGF-------------PNALLG 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  92 LIFYILQLLLGMTASAVAAL------VLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLII 155
Cdd:COG4243  74 LAAFAVVITLAVALLAGARLprwlwlALLAGALAGVVFSVWLIYQSLFVIGALCPYCLVVWAVTIPLFVL 143
VKOR cd10546
Vitamin K epoxide reductase (VKOR) family; VKOR (also named VKORC1) is an integral membrane ...
 21-154 2.15e-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: 60.90  E-value: 2.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  21 AVCAAGILLSIYAYHVEREKERDpehrALCDLGPWVKCSAALASRWGRGFGLlgsifgkdgvlnqPNSVFGLIFYILQLL 100
Cdd:cd10546   5 LLAAIGLLVSLYLTYYELTEGAV----AGCDAGPSSSCDLVLTSRWSRIFGV-------------PLSLLGALYYLVVLG 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42627869 101 LGMTASAVAAL---VLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLI 154
Cdd:cd10546  68 LLLSPPAGARLrwtALAAATFAGLGAAAWLIYLQLFVLGAFCPYCLVAHAAGLALLA 124
VKOR_1 cd12916
Vitamin K epoxide reductase family in bacteria and plants; This family includes vitamin K ...
 58-155 8.67e-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: 51.49  E-value: 8.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  58 CSAALASRWGRgfgllgsifgkdgVLNQPNSVFGLIFYILQLLLGMTASAVAA--------LVLMTSSIVSVVGSLYLAY 129
Cdd:cd12916  37 CDTVLNSPYAT-------------LLGIPLSLFGFLAYLAILVLAVLPLLLKSeklerwtwLLLFGLATAGVVFSAYLTY 103

                        90       100
                ....*....|....*....|....*.
gi 42627869 130 ILYFVLKEFCIICVTTYVLNFLLLII 155
Cdd:cd12916 104 LLAFVIGAFCPYCLTSAVLSTLLFLL 129
VKOR_3 cd12920
Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide ...
 25-157 2.00e-07

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: 47.69  E-value: 2.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  25 AGILLSIY-AYHVEREKErDPEHRALCDLGPWVKCSAALASRWGRGFGLLGSIFGKDGVLnqpnsvFGLIFYILQLLLGM 103
Cdd:cd12920   9 IGLAFSGLlTYHHYGILT-DGVGSSFCAINEVVNCDKVAQSPYSAIGGVPIALWGLLAYG------FLAALFLLALISRE 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 42627869 104 TASAVAALVLMTSsIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLIINY 157
Cdd:cd12920  82 DSERAAGLLFLVL-LVGLVADLVLGLISVTAIGALCILCAGTYIVSAALLFGAW 134
VKOR_arc cd12918
Vitamin K epoxide reductase family in archaea and some bacteria; This family includes vitamin ...
 20-155 8.09e-07

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: 45.77  E-value: 8.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  20 YAVCAAGILLSIYAYHVEREKERdpehRALCDLGPWVKCSAALASRWGRGFGLlgsifgkdgvlnqPNSVFGLIFYILQL 99
Cdd:cd12918   4 LALSLVGLLASAYLTYEHYLKRP----PLACTISGVINCEKVLSSPYSRILGV-------------PLAVLGLAWFAVLL 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42627869 100 LLGMTASAVAALVLMTS---SIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLII 155
Cdd:cd12918  67 VLSLLAALRVRLLLGALlywSILGIAFVPYLVYLELFLIGAICLYCTVAHVIILALFII 125
VKOR_4 cd12921
Vitamin K epoxide reductase (VKOR) family in bacteria; This family includes vitamin K epoxide ...
 25-156 2.12e-06

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: 44.62  E-value: 2.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  25 AGILLSIYAYHVEREKERDPEHRaLCDLGPWVKCSAALASRwgrGFGLLGSIFgkdgvlnqpnSVFGLIFYILQLLLGMT 104
Cdd:cd12921   9 IGLLISILLLLKELGKSNKILKK-FCSIGKKVDCNAVLKSK---GAKIGGISL----------SELGLLYFFGLLLLLLL 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 42627869 105 ASAVAAL--VLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLIIN 156
Cdd:cd12921  75 SPLNSSLlfLLSLLLLLALPAELYSIYYQKFVIKKWCPLCLSIQAILWLLFLLL 128
VKOR_5 cd12922
Vitamin K epoxide reductase family in bacteria; This family includes vitamin K epoxide ...
 24-155 2.24e-04

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: 39.10  E-value: 2.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869  24 AAGILLSIYAYHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGLlgsifgkdgvlnqPNSVFGLIFYILQLLLGM 103
Cdd:cd12922   8 LIGLVASFVLTVEKIQLLEDPDYVLSCDINPVVSCGSVMQSWQASLFGF-------------PNPLIGLAAFAVVITVGV 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42627869 104 TASA---------VAALVLMTSSIVSVVgslYLAYILYFVLKEFCIICVTTYVLNFLLLII 155
Cdd:cd12922  75 ALLAgarlprwfwVGLQAGLAAGLVFVH---WLIYQSLFVIGALCPYCMVVWAVTIPLFWY 132
PRK14889 PRK14889
VKOR family protein; Provisional
 21-155 5.57e-04

VKOR family protein; Provisional


Pssm-ID: 184883  Cd Length: 143  Bit Score: 38.53  E-value: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627869   21 AVCAAGILLSIYAYHVEREKERDPehrALCDLGPWVKCSAALASRWGRGFGLlgsifgkdgvlnqPNSVFGLIFYILQLL 100
Cdd:PRK14889  14 AFSLVGLIASIASYLLFTLLVKPP---PFCTINSVINCSSVLSSPYARFLGI-------------PLDYLGAAWFSANIA 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42627869  101 LGM----TASAVAALVLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLII 155
Cdd:PRK14889  78 LALlgvgTLKRILGRVISLWSIIGLAIVPYLVYLEVFVLGAICIYCTIAHVSILAAFIL 136
 
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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