AC MF_00735; DC Protein; auto TR HAMAP; MF_00735; -; 1; level=0 XX Names: Methyltr_PrmA XX ID PRMA DE RecName: Full=Ribosomal protein L11 methyltransferase; DE Short=L11 Mtase; DE EC=2.1.1.-; GN Name=prmA; XX CC -!- FUNCTION: Methylates ribosomal protein L11. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + CC N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA- CC COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family. XX DR PIRSF; PIRSF000401; RPL11_MTase; 0-1; trigger=no DR NCBIfam; TIGR00406; PrmA; 1; trigger=no XX KW Cytoplasm KW S-adenosyl-L-methionine KW Transferase KW Methyltransferase XX GO GO:0008276; F:protein methyltransferase activity GO GO:0005737; C:cytoplasm XX FT From: PRMA_THET8 (Q84BQ9) FT BINDING 107 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Group: 1; Condition: T FT BINDING 128 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Group: 1; Condition: G FT BINDING 149 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Group: 1; Condition: D FT BINDING 191 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Group: 1; Condition: N XX Size: 220-400; Related: None; Template: P0A8T1; Q84BQ9; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: 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). XX # Revision 1.21 2023/06/01 //