Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BVKORe4nv5B2 A: alpha bundlesX: Bromodomain-likeH: Vitamin K epoxide reductase (VKOR) (From Topology)T: Vitamin K epoxide reductase (VKOR)F: VKORECOD (1.6)
BDSBA_1e4nv5B1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: DSBA_1ECOD (1.6)
AVKORe4nv5A2 A: alpha bundlesX: Bromodomain-likeH: Vitamin K epoxide reductase (VKOR) (From Topology)T: Vitamin K epoxide reductase (VKOR)F: VKORECOD (1.6)
ADSBA_1e4nv5A1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: DSBA_1ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B1.20.1440.130 Mainly Alpha Up-down Bundle de novo design (two linked rop proteins) VKOR domainCATH (4.3.0)
B3.40.30.10 Alpha Beta 3-Layer(aba) Sandwich Glutaredoxin GlutaredoxinCATH (4.3.0)
A1.20.1440.130 Mainly Alpha Up-down Bundle de novo design (two linked rop proteins) VKOR domainCATH (4.3.0)
A3.40.30.10 Alpha Beta 3-Layer(aba) Sandwich Glutaredoxin GlutaredoxinCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF07884Vitamin K epoxide reductase family (VKOR)Vitamin K epoxide reductase familyVitamin 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 ...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 [1]. Four cysteine residues and one residue, which is either serine or threonine, are identified as likely active-site residues [1]. In some plant and bacterial homologues the VKORC1 homologous domain is fused with domains of the thioredoxin family of oxidoreductases [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
VKORC1/thioredoxin domain protein -

InterPro: Protein Family Classification InterPro Database Homepage

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage