Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
D [auth A]SCOP2B SuperfamilyPutative DNA-binding domain8038870 3000158 SCOP2B (2022-06-29)
E [auth B]SCOP2B SuperfamilyPutative DNA-binding domain8038870 3000158 SCOP2B (2022-06-29)
F [auth C]SCOP2B SuperfamilyPutative DNA-binding domain8038870 3000158 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
D [auth A]Exce2iefA1 A: alpha arraysX: HTHH: HTHT: Putative DNA-binding domainF: ExcECOD (1.6)
E [auth B]Exce2iefB1 A: alpha arraysX: HTHH: HTHT: Putative DNA-binding domainF: ExcECOD (1.6)
F [auth C]Exce2iefC1 A: alpha arraysX: HTHH: HTHT: Putative DNA-binding domainF: ExcECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
D [auth A],
E [auth B],
F [auth C]
PF07825Excisionase-like protein (Exc)Excisionase-like proteinThe phage-encoded excisionase protein (Xis, Swiss:P03699) is involved in excisive recombination by regulating the assembly of the excisive intasome and by inhibiting viral integration. It adopts an unusual 'winged'-helix structure in which two alpha ...The phage-encoded excisionase protein (Xis, Swiss:P03699) is involved in excisive recombination by regulating the assembly of the excisive intasome and by inhibiting viral integration. It adopts an unusual 'winged'-helix structure in which two alpha helices are packed against two extended strands. Also present in the structure is a two-stranded anti-parallel beta-sheet, whose strands are connected by a four-residue 'wing'. During interaction with DNA, helix alpha2 is thought to insert into the major groove, while the wing contacts the adjacent minor groove or phosphodiester backbone. The C-terminal region of Xis is involved in interaction with phage-encoded integrase (Int), and a putative C-terminal alpha helix may fold upon interaction with Int and/or DNA [1].
Domain