ID TRMB_CORGL Reviewed; 255 AA. AC Q8NLS3; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 114. 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=Cgl2865, cg3172; OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / OS JCM 1318 / LMG 3730 / NCIMB 10025). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196627; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1; RA Ikeda M., Nakagawa S.; RT "The Corynebacterium glutamicum genome: features and impacts on RT biotechnological processes."; RL Appl. Microbiol. Biotechnol. 62:99-109(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its RT impact on the production of L-aspartate-derived amino acids and vitamins."; RL J. Biotechnol. 104:5-25(2003). 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; BA000036; BAC00259.1; -; Genomic_DNA. DR EMBL; BX927156; CAF20890.1; -; Genomic_DNA. DR RefSeq; NP_602057.1; NC_003450.3. DR RefSeq; WP_011015448.1; NC_006958.1. DR AlphaFoldDB; Q8NLS3; -. DR SMR; Q8NLS3; -. DR STRING; 196627.cg3172; -. DR KEGG; cgb:cg3172; -. DR KEGG; cgl:Cgl2865; -. DR PATRIC; fig|196627.13.peg.2797; -. DR eggNOG; COG0220; Bacteria. DR HOGENOM; CLU_050910_0_2_11; -. DR OrthoDB; 9802090at2; -. DR BioCyc; CORYNE:G18NG-12483-MONOMER; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000000582; Chromosome. DR Proteomes; UP000001009; 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..255 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_0000171324" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 164..169 FT /note="Interaction with RNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT ACT_SITE 158 FT /evidence="ECO:0000250" FT BINDING 83 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 108 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 135 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 158 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 162 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 194 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 232..235 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" SQ SEQUENCE 255 AA; 28806 MW; 550F5003FAE01AA6 CRC64; MSISDNSRDQ LGELPAGRPL QSDFDNDLDY PRLGSVTFRR GTLTENQQTM WDEKWPELGR VLEDELIDVD AWFGREGAKT IVEIGSGTGT STAAMAPLEA DTNIVAVELY KPGLAKLMGS VVRGEIDNVR MVRGDGIEVL NRMFADGSLD GIRVYFPDPW PKARHNKRRI IQSGPLNLFA KKLKPGGVLH VATDHADYAE WINELVEVEP LLEYKGWPWE ECPQLTDRQV ITKFEGKGLE KDHVINEYLW QKVQN //