ID TRMB_BACLD Reviewed; 213 AA. AC Q65G12; Q62RG7; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 117. 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=BLi03141, BL00042; OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15383718; DOI=10.1159/000079829; RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.; RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism RT with great industrial potential."; RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:R77.1-R77.12(2004). 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; AE017333; AAU42002.1; -; Genomic_DNA. DR EMBL; CP000002; AAU24643.1; -; Genomic_DNA. DR RefSeq; WP_003184473.1; NC_006322.1. DR AlphaFoldDB; Q65G12; -. DR SMR; Q65G12; -. DR STRING; 279010.BL00042; -. DR GeneID; 66214885; -. DR KEGG; bld:BLi03141; -. DR KEGG; bli:BL00042; -. DR eggNOG; COG0220; Bacteria. DR HOGENOM; CLU_050910_2_1_9; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000000606; Chromosome. 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 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..213 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_0000229154" FT REGION 124..129 FT /note="Interaction with RNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT ACT_SITE 118 FT /evidence="ECO:0000250" FT BINDING 44 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 69 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 96 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 118 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 122 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 154 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 191..194 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" SQ SEQUENCE 213 AA; 24431 MW; DABC74446D43BA28 CRC64; MRMRHKPWAD DYLAENSHIV ISEPSQYKGK WHSVFGNDNP IHIEVGTGKG QFISGMALQN PDVNYIGIEL FKSVIVTAVD KVKQTEAPNV KLLNINANML SDVFADGEVD RVYLNFSDPW PKKRHEKRRL TNHAFLKKYE QVLGGKGAIH FKTDNRGLFE YSLTSFSEYG LVLTFVSLDL HQSDFEGNVM TEYEEKFAAK GQPIYRVEAE WRT //