AC MF_00587; DC Protein; auto TR HAMAP; MF_00587; -; 1; level=0 XX Names: tRNA_methyltr_TrmY XX case ID TRMY DE RecName: Full=tRNA (pseudouridine(54)-N(1))-methyltransferase; DE EC=2.1.1.257; GN Name=trmY; else case ID TRMYL DE RecName: Full=Putative pseudouridine methyltransferase; DE EC=2.1.1.-; end case XX case CC -!- FUNCTION: Specifically catalyzes the N1-methylation of pseudouridine at CC position 54 (Psi54) in tRNAs. CC -!- CATALYTIC ACTIVITY: CC Reaction=pseudouridine(54) in tRNA + S-adenosyl-L-methionine = H(+) + CC N(1)-methylpseudouridine(54) in tRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:55292, Rhea:RHEA-COMP:14140, Rhea:RHEA-COMP:14141, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:65314, ChEBI:CHEBI:74890; EC=2.1.1.257; CC -!- SUBUNIT: Homodimer. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. TrmY family. XX DR Pfam; PF04013; Methyltrn_RNA_2; 1; trigger=no XX KW Cytoplasm KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase case KW tRNA processing end case XX case GO GO:0030488; P:tRNA methylation GO GO:0008175; F:tRNA methyltransferase activity end case GO GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity GO GO:0005737; C:cytoplasm XX FT From: TRMY_METJA (Q59034) FT BINDING 179..184 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Optional; Condition: [LIV]-S-P-L-[ES]-L FT BINDING 136 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Optional; Condition: [LM] FT BINDING 156 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Optional; Condition: G FT BINDING 189 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Optional; Condition: C XX Size: 192-211; Related: None; Template: Q59034; D4GTL8; Scope: Bacteria; Gammaproteobacteria Archaea Fusion: Nter: Cter: None Duplicate: None Plasmid: None Comments: Formation of 1-methylpseudouridine at position 54 of tRNA has never been identified in any bacterial tRNA sequenced so far. The bacterial and archaeal homologs may fulfill different functions. See PubMed:22274953. Unknown N-terminal domain in ARCFU. Divergent PYRAE not shown in alignment and not used in size range. XX # Revision 1.28 2022/11/19 //