ID TRMB_LEPBJ Reviewed; 217 AA. AC Q04W54; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057}; DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_01057}; DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057}; DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057}; GN Name=trmB {ECO:0000255|HAMAP-Rule:MF_01057}; GN OrderedLocusNames=LBJ_0122; OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197). OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae; OC Leptospira. OX NCBI_TaxID=355277; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JB197; RX PubMed=16973745; DOI=10.1073/pnas.0603979103; RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., RA Rood J.I., Davies J.K., Adler B.; RT "Genome reduction in Leptospira borgpetersenii reflects limited RT transmission potential."; RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006). CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46 CC (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_01057}. CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)- CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, CC ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01057}; CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01057}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_01057}. 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; CP000350; ABJ74866.1; -; Genomic_DNA. DR RefSeq; WP_011671187.1; NC_008510.1. DR AlphaFoldDB; Q04W54; -. DR SMR; Q04W54; -. DR KEGG; lbj:LBJ_0122; -. DR HOGENOM; CLU_050910_2_0_12; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000000656; Chromosome 1. DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR HAMAP; MF_01057; tRNA_methyltr_TrmB; 1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb. DR PANTHER; PTHR23417; 3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE; 1. DR PANTHER; PTHR23417:SF14; PPR_LONG DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF02390; Methyltransf_4; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51625; SAM_MT_TRMB; 1. PE 3: Inferred from homology; KW Methyltransferase; S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1..217 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_0000288169" FT ACT_SITE 123 FT /evidence="ECO:0000250" FT BINDING 48 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 73 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 100 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 123 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 127 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 159 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" SQ SEQUENCE 217 AA; 26000 MW; CE903272344ADD04 CRC64; MSQDLEQKLW SIASGIPFVS DYFLQASPAR KLKKENLFSK VFETYFLELG SGWGEVAIAM ALQRRNTGFV LMEKKFDRIR HTIREIEKHS LDNVKILCVN FNWFLADVFE ENLFSEILLN FPDPWPKKRH HKKRTINSKF IESLRVLLPE KGKFSFATDY GPYARKTIRL FRDSEIFKPE TMEFRLERKE IPVSHFERKK RKEGKRIYYI DQILIRK //