HAMAP rule MF_00735
General rule information
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| Accession | MF_00735 |
| Dates | 24-NOV-2003 (Created)
1-JUN-2023 (Last updated, Version 21) |
| Name | Methyltr_PrmA |
| Scope(s) |
Bacteria |
| Template(s) | P0A8T1 (PRMA_ECOLI); Q84BQ9 (PRMA_THET8); [ Recover all ] |
| Triggered by |
HAMAP; MF_00735 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | PRMA |
| Protein name | RecName: Full=Ribosomal protein L11 methyltransferase; Short=L11 Mtase; EC=2.1.1.-; |
| Gene name | Name=prmA; |
Comments
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| FUNCTION | Methylates ribosomal protein L11. |
| CATALYTIC ACTIVITY | Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L- homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA- COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the methyltransferase superfamily. PrmA family. |
Keywords
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Gene Ontology
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| GO:0008276; Molecular function:protein methyltransferase activity |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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| PIRSF | PIRSF000401; RPL11_MTase; 0-1; |
| NCBIfam | TIGR00406; PrmA; 1; |
Features
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| From: PRMA_THET8 (Q84BQ9) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 107 | 107 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
T | 1 | |||||||
| BINDING | 128 | 128 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
G | 1 | |||||||
| BINDING | 149 | 149 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
D | 1 | |||||||
| BINDING | 191 | 191 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
N | 1 | |||||||
Additional information
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| Size range | 220-400 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | See: MEDLINE=20450294; PubMed=10997488; Bujnicki J.M.; "Sequence, structural, and evolutionary analysis of prokaryotic ribosomal protein L11 methyltransferases."; Acta Microbiol. Pol. 49:19-29(2000). |