Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
A [auth B]SCOP2 FamilySlx4 domain-like8044990 4004239 SCOP2 (2022-06-29)
A [auth B]SCOP2 SuperfamilySlx4 domain-like8053986 3002259 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
B [auth A]PF01541e4xlgA1 A: a+b three layersX: GIY-YIG endonuclease (From Topology)H: GIY-YIG endonuclease (From Topology)T: GIY-YIG endonucleaseF: PF01541ECOD (1.6)
B [auth A]PF21202e4xlgA2 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: RING/U-boxF: PF21202ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A [auth B]PF09494Slx4 endonuclease (Slx4)Slx4 endonucleaseThe Slx4 protein is a heteromeric structure-specific endonuclease found from fungi to mammals. Slx4 with Slx1 acts as a nuclease on branched DNA substrates, particularly simple-Y, 5'-flap, or replication fork structures by cleaving the strand bearin ...The Slx4 protein is a heteromeric structure-specific endonuclease found from fungi to mammals. Slx4 with Slx1 acts as a nuclease on branched DNA substrates, particularly simple-Y, 5'-flap, or replication fork structures by cleaving the strand bearing the 5' non-homologous arm at the branch junction and thus generating ligatable nicked products from 5'-flap or replication fork substrates [1].
Domain
B [auth A]PF21202Structure-specific endonuclease subunit SLX1, C-terminal (SLX1_C)Structure-specific endonuclease subunit SLX1, C-terminalSlx1 is a catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. It has endonuclease activity towards branched DNA substrates, introducing single-strand ...Slx1 is a catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. It has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA [1-3]. This is the RING zinc finger domain.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A [auth B]Structure-specific endonuclease subunit SLX4-
B [auth A]Structure-specific endonuclease subunit SLX1