ID TRMD_CLOBB Reviewed; 238 AA. AC B2TJ31; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=tRNA (guanine-N(1)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605}; DE EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_00605}; DE AltName: Full=M1G-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605}; DE AltName: Full=tRNA [GM37] methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605}; GN Name=trmD {ECO:0000255|HAMAP-Rule:MF_00605}; GN OrderedLocusNames=CLL_A1249; OS Clostridium botulinum (strain Eklund 17B / Type B). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=935198; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Eklund 17B / Type B; RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., RA Smith T.J., Sutton G., Brettin T.S.; RT "Complete sequence of Clostridium botulinum strain Eklund."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs. CC {ECO:0000255|HAMAP-Rule:MF_00605}. CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)- CC methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00605}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00605}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00605}. CC -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family. CC {ECO:0000255|HAMAP-Rule:MF_00605}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001056; ACD23339.1; -; Genomic_DNA. DR AlphaFoldDB; B2TJ31; -. DR SMR; B2TJ31; -. DR KEGG; cbk:CLL_A1249; -. DR HOGENOM; CLU_047363_0_1_9; -. DR Proteomes; UP000001195; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052906; F:tRNA (guanine(37)-N1)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule. DR CDD; cd18080; TrmD-like; 1. DR Gene3D; 3.40.1280.10; -; 1. DR Gene3D; 1.10.1270.20; tRNA(m1g37)methyltransferase, domain 2; 1. DR HAMAP; MF_00605; TrmD; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR023148; tRNA_m1G_MeTrfase_C_sf. DR InterPro; IPR002649; tRNA_m1G_MeTrfase_TrmD. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10. DR NCBIfam; TIGR00088; trmD; 1. DR PANTHER; PTHR46417; TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE; 1. DR PANTHER; PTHR46417:SF1; TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE; 1. DR Pfam; PF01746; tRNA_m1G_MT; 1. DR PIRSF; PIRSF000386; tRNA_mtase; 1. DR SUPFAM; SSF75217; alpha/beta knot; 1. PE 3: Inferred from homology; KW Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1..238 FT /note="tRNA (guanine-N(1)-)-methyltransferase" FT /id="PRO_1000130151" FT BINDING 110 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605" FT BINDING 129..134 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605" SQ SEQUENCE 238 AA; 27431 MW; 5ACDDB01CEE101B9 CRC64; MKISILTLFP EMFSIFNHSI IGRAQENNIV ELELLNIRDN TLDKHKKVDD YPYGGGAGMV MAPQPIIDTI RKAKENNKGK VIFLGPRGKT FNQKMAMDLS KEENLIFLCG HYEGIDERVY KHIDMEVSLG DFILTGGEMA AIPVIDSILR LIPGVLGKEE SFVDESFSED LLEYPQYTRP YEFEGEHVPE ILLSGHHENI RKWRRLQSLD LTRKRRPDLY KNVILTKEDK KLLGRKNK //