ID TRMB_YERP3 Reviewed; 239 AA. AC A7FEX6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 27-MAR-2024, entry version 82. 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=YpsIP31758_0820; OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=349747; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP 31758; RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142; RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G., RA Fayolle C., Lindler L.E., Carniel E., Ravel J.; RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the RT causative agent of Far East scarlet-like fever."; RL PLoS Genet. 3:1508-1523(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 -!- SUBUNIT: Monomer. {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; CP000720; ABS47809.1; -; Genomic_DNA. DR RefSeq; WP_012104659.1; NC_009708.1. DR AlphaFoldDB; A7FEX6; -. DR SMR; A7FEX6; -. DR KEGG; ypi:YpsIP31758_0820; -. DR HOGENOM; CLU_050910_0_1_6; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000002412; Chromosome. DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule. 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; S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1..239 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_1000064416" FT REGION 150..155 FT /note="Interaction with RNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT ACT_SITE 144 FT /evidence="ECO:0000250" 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 94 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 121 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 144 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 148 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 180 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 217..220 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" SQ SEQUENCE 239 AA; 26989 MW; FBB9A479450D3A9A CRC64; MINDVISPEF DENGRALRRI RSFVRRQGRL TKGQQLALDS YWPVMGVEYQ AAPVDLNTLF GREAPIVLEI GFGMGTSLVT MAANNPQQNF LGIEVHSPGV GACLSSAHDA GLSNLRIMCH DAVEVLENMI PEASLDMVQL FFPDPWHKAR HNKRRIVQTP FVELVKSKLK VGGVFHMATD WQPYAEHMLE VMSGVSGYLN LSEQNDYVPR PDSRPLTKFE LRGQRLGHGV WDLMFERKE //