ID TRMB_HAEIN Reviewed; 246 AA. AC P44648; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 134. 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=HI_0340; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C., RA Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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; L42023; AAC22002.1; -; Genomic_DNA. DR PIR; F64148; F64148. DR RefSeq; NP_438504.1; NC_000907.1. DR AlphaFoldDB; P44648; -. DR SMR; P44648; -. DR STRING; 71421.HI_0340; -. DR EnsemblBacteria; AAC22002; AAC22002; HI_0340. DR KEGG; hin:HI_0340; -. DR PATRIC; fig|71421.8.peg.357; -. DR eggNOG; COG0220; Bacteria. DR HOGENOM; CLU_050910_0_1_6; -. DR OrthoDB; 9802090at2; -. DR PhylomeDB; P44648; -. DR BioCyc; HINF71421:G1GJ1-356-MONOMER; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000000579; 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 1: Evidence at protein level; KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine; KW Transferase; tRNA processing. FT CHAIN 1..246 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_0000171333" FT ACT_SITE 152 FT /evidence="ECO:0000250" FT BINDING 77 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 102 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 129 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 152 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 156 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 188 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" FT BINDING 225..228 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057" SQ SEQUENCE 246 AA; 28053 MW; 1FF1DFD12FEC729D CRC64; MTQTFADQKR KTVETAEFTE DGRYKRKVRS FVLRTGRLSE FQRNMMNDNW GTLGLDYQTE PFDFAKIYGN DNPVVLEIGF GMGKSLVDMA FANPDKNYLG IEVHTPGVGA CIAYAVEKGV TNLRVICHDA TEILRDSIAD GALGGLQLFF PDPWHKAKHH KRRIVQPHFV TQVIQKLGEN GFIHMATDWE NYAEQMLEVL SANTDLVNTS KNGDYIPRPD FRPLTKFEAR GYKLGHGVWD LYFVKK //