Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyDsbC/DsbG C-terminal domain-like8027539 4000486 SCOP2 (2022-06-29)
ASCOP2 FamilyDsbC/DsbG N-terminal domain-like8027541 4001018 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyThioredoxin-like8039918 3000031 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyDsbC/DsbG N-terminal domain-like8039920 3000466 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ADsbC_Ne1t3bA1 A: a+b two layersX: Cystatin-likeH: DsbC/DsbG N-terminal domain-like (From Topology)T: DsbC/DsbG N-terminal domain-likeF: DsbC_NECOD (1.6)
ADSBA_1e1t3bA2 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)
A3.10.450.70 Alpha Beta Roll Nuclear Transport Factor 2 Chain: A,CATH (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
PF10411Disulfide bond isomerase protein N-terminus (DsbC_N)Disulfide bond isomerase protein N-terminusThis is the N-terminal domain of the disulfide bond isomerase DsbC. The whole molecule is V-shaped, where each arm is a DsbC monomer of two domains linked by a hinge; and the N-termini of each monomer join to form the dimer interface at the base of t ...This is the N-terminal domain of the disulfide bond isomerase DsbC. The whole molecule is V-shaped, where each arm is a DsbC monomer of two domains linked by a hinge; and the N-termini of each monomer join to form the dimer interface at the base of the V, so are vital for dimerisation [1]. DsbC is required for disulfide bond formation and functions as a disulfide bond isomerase during oxidative protein-folding in bacterial periplasm. It also has chaperone activity [2].
Domain
PF13098Thioredoxin-like domain (Thioredoxin_2)Thioredoxin-like domain- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Thiol:disulfide interchange protein dsbC- -