We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU00902
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00902
General rule information
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| Accession | PRU00902 |
| Dates | 25-NOV-2011 (Created)
03-SEP-2024 (Last updated, Version 25) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51569; DOT1 |
Name | Histone-lysine N-methyltransferase DOT1 (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) | Q04089; |
Propagated annotation
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Identifier, protein and gene names
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| case <FTGroup:1> | |
| Protein name | + RecName: EC=2.1.1.-; |
Comments
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| 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 I-like SAM-binding methyltransferase superfamily. DOT1 family. |
| end case | |
Keywords
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Gene Ontology
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| case <FTGroup:1> | |
| 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
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| From: PS51569 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="DOT1 #" | |||||||||
| case <FTGroup:1> | ||||||||||||
| BINDING | 120 | 123 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
Y-G-E-x | ||||||||
| BINDING | 143 | 152 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
[FLV]-x-D-x-G-[ACS]-G-x-G-x | ||||||||
| BINDING | 206 | 207 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
x-F | ||||||||
| end case | ||||||||||||
| BINDING | 170 | 170 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
[DE] | 1 | |||||||
Additional information
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| 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
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- UniProtKB/Swiss-Prot sets
Eukaryota [21] All [ 21 ]
- Retrieve set of proteins with 3D structure for this domain