Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyArginase/deacetylase-like 8100520 3000260 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyArginase/deacetylase-like 8100520 3000260 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AHist_deacetyle5g12A1 A: a/b three-layered sandwichesX: HAD domain-likeH: HAD domain-relatedT: Arginase/deacetylaseF: Hist_deacetylECOD (1.6)
BHist_deacetyle5g12B1 A: a/b three-layered sandwichesX: HAD domain-likeH: HAD domain-relatedT: Arginase/deacetylaseF: Hist_deacetylECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.800.20 Alpha Beta 3-Layer(aba) Sandwich Arginase Chain ACATH (4.3.0)
B3.40.800.20 Alpha Beta 3-Layer(aba) Sandwich Arginase Chain ACATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00850Histone deacetylase domain (Hist_deacetyl)Histone deacetylase domainHistones can be reversibly acetylated on several lysine residues. Regulation of transcription is caused in part by this mechanism. Histone deacetylases catalyse the removal of the acetyl group. Histone deacetylases are related to other proteins [1]. ...Histones can be reversibly acetylated on several lysine residues. Regulation of transcription is caused in part by this mechanism. Histone deacetylases catalyse the removal of the acetyl group. Histone deacetylases are related to other proteins [1].
Domain