A0A437APZ6 · A0A437APZ6_9MICR
- ProteinHistone deacetylase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids412 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- N6-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + acetate
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 92 | substrate | |||
Active site | 134 | Proton acceptor | |||
Binding site | 142 | substrate | |||
Binding site | 169 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 171 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 257 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 296 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | histone deacetylase activity | |
Molecular Function | metal ion binding | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone deacetylase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Microsporidia > Tubulinosematoidea > Tubulinosematidae > Tubulinosema
Accessions
- Primary accessionA0A437APZ6
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length412
- Mass (Da)46,762
- Last updated2019-05-08 v1
- MD5 ChecksumC9964041DE2F973376E903843F9E490E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
RCSS01000089 EMBL· GenBank· DDBJ | RVD93087.1 EMBL· GenBank· DDBJ | Genomic DNA |