Reviewed,
UniProtKB/Swiss-Prot Q4P2W8 (DOT1_USTMA)
Last modified
June 16, 2009.
Version 27.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Histone-lysine N-methyltransferase, H3 lysine-79 specific EC=2.1.1.43 Alternative name(s): Histone H3-K79 methyltransferase H3-K79-HMTase | ||||
| Gene names |
| ||||
| Organism | Ustilago maydis (Smut fungus) [Complete proteome] | ||||
| Taxonomic identifier | 5270 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago |
Protein attributes
| Sequence length | 798 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Histone methyltransferase that specifically methylates histone H3 to form H3K79me. 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 histones By similarity. |
| Catalytic activity | S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine. |
| Enzyme regulation | Ubiquitination of histone H2B to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3 By similarity. |
| Subcellular location | Nucleus By similarity. |
| Miscellaneous | In contrast to other lysine histone methyltransferase, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones. |
| Sequence similarities | Belongs to the DOT1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Domain | Repeat |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Chromatin regulator Methyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW transcriptionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | histone-lysine N-methyltransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 798 | 798 | Histone-lysine N-methyltransferase, H3 lysine-79 specific | PRO_0000270616 | |||||
Regions | |||||||||
| Motif | 577 – 588 | 12 | SAM-binding motif 1 By similarity | ||||||
| Motif | 657 – 666 | 10 | SAM-binding motif 2 By similarity | ||||||
Sites | |||||||||
| Binding site | 581 | 1 | S-adenosyl-L-homocysteine By similarity | ||||||
| Binding site | 605 | 1 | S-adenosyl-L-homocysteine By similarity | ||||||
Sequences
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References
| [1] | "Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis." Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. Birren B.W.Nature 444:97-101(2006) [PubMed: 17080091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521. |
Cross-references
Sequence databases | |
|---|---|
| AACP01000200 Genomic DNA. Translation: EAK86305.1. | |
| RefSeq | XP_761692.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3633676. |
| KEGG | uma:UM05545.1. |
Enzyme and pathway databases | |
| BRENDA | 2.1.1.43. 2320. |
Family and domain databases | |
| InterPro | IPR013110. DOT1. [Graphical view] |
| Pfam | PF08123. DOT1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DOT1_USTMA | ||||||||
| Accession | Primary (citable) accession number: Q4P2W8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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