9GL0

Crystal Structure of Acetylpolyamine aminohydrolase (ApaH) from Legionella pneumophila

External Resource: Annotation


Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D
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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D
Acetylpolyamine aminohydrolase - -

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, B, C, D
IPR023696Ureohydrolase domain superfamilyHomologous Superfamily
A, B, C, D
IPR023801Histone deacetylase domainDomain
A, B, C, D
IPR037138Histone deacetylase domain superfamilyHomologous Superfamily