ProRule PRU00911
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00911
General rule information
[?]
| Accession | PRU00911 |
| Dates | 25-NOV-2011 (Created)
03-SEP-2024 (Last updated, Version 15) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51578; SAM_MT43_SET2_2 |
Name | Histone-lysine N-methyltransferase (EC 2.1.1.43) |
| Function | Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. |
| Scope(s) |
Eukaryota |
| Example(s) | Q945S8 (ASHH3_ARATH); |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
| Protein name | + RecName: EC=2.1.1.-; |
Comments
[?]
| CATALYTIC ACTIVITY | Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = N(6)-methyl-L- lysyl-[histone] + S-adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; |
| SIMILARITY | Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily. |
Keywords
[?]
Gene Ontology
[?]
| GO:0032259; Biological process:methylation |
| GO:0042054; Molecular function:histone methyltransferase activity |
| GO:0016740; Molecular function:transferase activity |
| GO:0008168; Molecular function:methyltransferase activity |
| GO:0046500; Biological process:S-adenosylmethionine metabolic process |
Features
[?]
Additional information
[?]
| Size range | unlimited amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
[?]
- UniProtKB/Swiss-Prot sets
Eukaryota [3] All [ 3 ]
- Retrieve set of proteins with 3D structure for this domain