A0A0N4Z2Q9 · A0A0N4Z2Q9_PARTI
- ProteinMultifunctional fusion protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1021 (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
- H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Molecular Function | histone H3K79 trimethyltransferase activity | |
Molecular Function | myosin phosphatase activity | |
Biological Process | methylation |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameHistone-lysine N-methyltransferase, H3 lysine-79 specific
- EC number
- Alternative names
- Recommended nameSerine/threonine-protein phosphatase
- EC number
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Tylenchina > Panagrolaimomorpha > Strongyloidoidea > Strongyloididae > Parastrongyloides
Accessions
- Primary accessionA0A0N4Z2Q9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 295-313 | Helical | ||||
Sequence: WTKLYMMCFIVVIINSYFY |
Keywords
- Cellular component
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-320 | DOT1 | ||||
Sequence: ARIRLFQWCVLKSTKDFIPFCKDTSEFYLEEINLYTENAWNKKLPDSTIYFDFILFLGSMVQYDCDTRDYFAYKYKNIYPMPDQTPRGGSMDSDLADEVSNLLKAIITNRETVLKNYYQGSTEFTYGELKLQTLLELVNRSKMKFANENNFIDCGSGISNLQAGVAITQSVNSSIGVEINPLIGSAGKLYLHSFYLLARFANYSFSPTIHIIGDFNNNALDNLYNAKASIFFVNNFLLNDNTTLKLLDKISDTELSTTGIILTLNIGVGLRKFDYFANRKFEKQKFTLKDCVSWTKLYMMCFIVVIINSYFYQMFFANN | ||||||
Region | 329-385 | Disordered | ||||
Sequence: QKSKNKNKDEIAGTTVKKRDNLIPKEKHKGKRKTKDKGSANHRTDGTDTSARASKNL | ||||||
Compositional bias | 331-351 | Basic and acidic residues | ||||
Sequence: SKNKNKDEIAGTTVKKRDNLI | ||||||
Compositional bias | 997-1014 | Polar residues | ||||
Sequence: ESDVSEGSGESSSSHSKT | ||||||
Region | 997-1021 | Disordered | ||||
Sequence: ESDVSEGSGESSSSHSKTLTSDTEE |
Sequence similarities
Belongs to the PPP phosphatase family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,021
- Mass (Da)116,319
- Last updated2015-12-09 v1
- Checksum3CA0A5C89CCE4615
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 331-351 | Basic and acidic residues | ||||
Sequence: SKNKNKDEIAGTTVKKRDNLI | ||||||
Compositional bias | 997-1014 | Polar residues | ||||
Sequence: ESDVSEGSGESSSSHSKT |