ID TRMB_CLOBH Reviewed; 217 AA. AC A5HZ44; A7G137; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 94. 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=CBO0499, CLC_0573; OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441771; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A; RX PubMed=17519437; DOI=10.1101/gr.6282807; RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A., RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., RA White B., Whithead S., Parkhill J.; RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain RT Hall A and comparative analysis of the clostridial genomes."; RL Genome Res. 17:1082-1092(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A; RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). 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; CP000727; ABS38078.1; -; Genomic_DNA. DR EMBL; AM412317; CAL82053.1; -; Genomic_DNA. DR RefSeq; WP_003355768.1; NC_009698.1. DR RefSeq; YP_001253043.1; NC_009495.1. DR RefSeq; YP_001386456.1; NC_009698.1. DR AlphaFoldDB; A5HZ44; -. DR SMR; A5HZ44; -. DR GeneID; 5184754; -. DR KEGG; cbh:CLC_0573; -. DR KEGG; cbo:CBO0499; -. DR PATRIC; fig|413999.7.peg.502; -. DR HOGENOM; CLU_050910_2_1_9; -. DR UniPathway; UPA00989; -. DR PRO; PR:A5HZ44; -. DR Proteomes; UP000001986; Chromosome. DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central. DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central. DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central. 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 NCBIfam; TIGR00091; tRNA (guanosine(46)-N7)-methyltransferase TrmB; 1. 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; Reference proteome; S-adenosyl-L-methionine; KW Transferase; tRNA processing. FT CHAIN 1..217 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_1000136346" FT REGION 129..134 FT /note="Interaction with RNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 43 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 68 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 101 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" FT BINDING 196..199 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" SQ SEQUENCE 217 AA; 26259 MW; C9CEDFA575906AD2 CRC64; MRLRKKWWAR PEIEASDKFA EEPKELRGKW NKEFNNNNDI HLELGCGRGG FISQLVEKNK DINYVGIDLK DEVIVYAIRK VKEKEEEVKR EFKNIKFVTM NIMGIAEVFD KNEISKIYIN FCNPWPKERH NKRRLTHTKL LTEYKKFLKP NTEIWFKTDD KELFEDSQEY FKESGFNIEY ITYDLHNSDF KENIKTEYET KFETMGMKIM FLKARLL //