D3G9N3 · RT109_PNECA
- ProteinHistone acetyltransferase Rtt109
- GeneRtt109
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids375 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Histone chaperone-dependent acetylase that modifies 'Lys-56' of histone H3 (H3K56ac) (PubMed:20656950).
Histone H3 'Lys-56' acetylation may be required for S-phase-linked DNA damage tolerance (By similarity).
Also acetylates 'Lys-9' of histone H3 (H3K9ac) (By similarity).
Autoacetylates (PubMed:20656950).
Histone H3 'Lys-56' acetylation may be required for S-phase-linked DNA damage tolerance (By similarity).
Also acetylates 'Lys-9' of histone H3 (H3K9ac) (By similarity).
Autoacetylates (PubMed:20656950).
Catalytic activity
- acetyl-CoA + L-lysyl-[protein] = CoA + H+ + N6-acetyl-L-lysyl-[protein]This reaction proceeds in the forward direction.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | histone H3K56 acetyltransferase activity | |
Biological Process | DNA damage response | |
Biological Process | regulation of DNA-templated transcription |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone acetyltransferase Rtt109
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Pneumocystomycetes > Pneumocystaceae > Pneumocystis
Accessions
- Primary accessionD3G9N3
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 84 | Abolishes histone acetyltransferase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 218 | Mildly decreases histone acetyltransferase activity; when associated with A-219. | ||||
Sequence: D → A | ||||||
Mutagenesis | 219 | Mildly decreases histone acetyltransferase activity; when associated with A-218. | ||||
Sequence: D → A |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000453550 | 1-375 | Histone acetyltransferase Rtt109 | |||
Sequence: MDNLYTGISKSIESLPPEITFSYGYIFTNFKKLKWPWLNKRKIDNVYLSNHFFFILQEDAMAYAIEVLIFFSSELSVFYISKADSTGFFNRHGSPSPLKAVISTFLSYLIRRFSRKNIPSRISLFSRSQPQYLFPSSSLNPSKHILDDRELVRWWLKVLDSVNGSQCPKKYVLIPGMDPRETLKYTPQHVDTDLNWICGHPYESMGQSAGEIIPRFPDDPKTRFLDQLDRDGEVVSIDKFWELMAFRQECIHGRIVGFFSLEFPGNDQDGTNNTITEDLDLQNGIQINEKIYRMVYEKLLRSDFETLEKSKGATLDLINDINNSKDIKDSVDWIKKVSGKKTSEDKKRKAIDISEQLKPVNILNESLIRKKSKKK | ||||||
Modified residue | 221 | N6-acetyllysine; by autocatalysis | ||||
Sequence: K |
Keywords
- PTM
Interaction
Subunit
Forms a complex composed of two RTT109 subunits and one VPS75 homodimer (By similarity).
Interacts with ASF1 (By similarity).
Interacts with ASF1 (By similarity).
Structure
Sequence
- Sequence statusComplete
- Length375
- Mass (Da)43,516
- Last updated2010-03-23 v1
- ChecksumF5D2A87AD44E03D7