A0A2S6BY91 · A0A2S6BY91_9PEZI
- ProteinHistone-lysine N-methyltransferase, H3 lysine-79 specific
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids469 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
Miscellaneous
In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
Catalytic activity
- L-lysyl79-[histone H3] + 3 S-adenosyl-L-methionine = N6,N6,N6-trimethyl-L-lysyl79-[histone H3] + 3 S-adenosyl-L-homocysteine + 3 H+
Activity regulation
Ubiquitination of histone H2B to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | histone H3K79 trimethyltransferase activity | |
Biological Process | DNA damage checkpoint signaling | |
Biological Process | DNA repair | |
Biological Process | methylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone-lysine N-methyltransferase, H3 lysine-79 specific
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Dothideomycetidae > Mycosphaerellales > Mycosphaerellaceae > Cercospora
Accessions
- Primary accessionA0A2S6BY91
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-30 | Disordered | ||||
Sequence: MGIMASMMTRNQKRKQQTESFNNTHQEATN | ||||||
Compositional bias | 9-30 | Polar residues | ||||
Sequence: TRNQKRKQQTESFNNTHQEATN | ||||||
Domain | 117-435 | DOT1 | ||||
Sequence: RHARPLDPIDDIVRTIQVFHIQVGKLTSPEIDTMGRMIYRTFEHFINTNNFYPLQRLITNLTDPAFFPLATHLSLSPPFDLTTHFLAQLHDRIIADAAHNLSRPSTSKNLEPTYGELLPPFLQTLFLQTNLNENSTYLDLGSGVGQTCLQASLTTGCLSYGIERESRSAGLAALHLGQFHERTKLWGLATEQENFEDRIVLRLGDFLKLECVKEWLGRADVVLVNNLKLEPETDLALVRMLGGREGVRKGTRVISTRGLVPVGRTRSGSKVGGKRKRGLEDDCEGKRRKVEKEKTNGKREKMQPQPEENEGENDIMAVR | ||||||
Region | 380-432 | Disordered | ||||
Sequence: RTRSGSKVGGKRKRGLEDDCEGKRRKVEKEKTNGKREKMQPQPEENEGENDIM | ||||||
Compositional bias | 389-432 | Basic and acidic residues | ||||
Sequence: GKRKRGLEDDCEGKRRKVEKEKTNGKREKMQPQPEENEGENDIM |
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length469
- Mass (Da)53,356
- Last updated2018-07-18 v1
- ChecksumEEC6C27C56EFD184
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 9-30 | Polar residues | ||||
Sequence: TRNQKRKQQTESFNNTHQEATN | ||||||
Compositional bias | 389-432 | Basic and acidic residues | ||||
Sequence: GKRKRGLEDDCEGKRRKVEKEKTNGKREKMQPQPEENEGENDIM |
Keywords
- Technical term