ID TRMB_EREGS Reviewed; 282 AA. AC Q74ZK8; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 120. DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055}; DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_03055}; DE AltName: Full=Transfer RNA methyltransferase 8 {ECO:0000255|HAMAP-Rule:MF_03055}; DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055}; DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055}; GN Name=TRM8 {ECO:0000255|HAMAP-Rule:MF_03055}; GN OrderedLocusNames=AGR192C; OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL OS Y-1056) (Yeast) (Ashbya gossypii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=284811; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces RT cerevisiae genome."; RL Science 304:304-307(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=23749448; DOI=10.1534/g3.112.002881; RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.; RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type RT loci, numerous translocations, lack of transposons, and distinct gene RT duplications."; RL G3 (Bethesda) 3:1225-1239(2013). CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46 CC (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_03055}. 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_03055}; CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_03055}. CC -!- SUBUNIT: Forms a complex with TRM82. {ECO:0000255|HAMAP-Rule:MF_03055}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03055}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_03055}. 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; AE016820; AAS54682.1; -; Genomic_DNA. DR RefSeq; NP_986858.1; NM_211920.1. DR AlphaFoldDB; Q74ZK8; -. DR SMR; Q74ZK8; -. DR STRING; 284811.Q74ZK8; -. DR EnsemblFungi; AAS54682; AAS54682; AGOS_AGR192C. DR GeneID; 4623160; -. DR KEGG; ago:AGOS_AGR192C; -. DR eggNOG; KOG3115; Eukaryota. DR HOGENOM; CLU_050910_3_1_1; -. DR InParanoid; Q74ZK8; -. DR OMA; LPNYFAK; -. DR OrthoDB; 116813at2759; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000000591; Chromosome VII. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0106143; C:tRNA (m7G46) methyltransferase complex; IEA:EnsemblFungi. 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:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central. DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR025763; Trm8_euk. 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:SF16; TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE; 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; Nucleus; Reference proteome; RNA-binding; KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding. FT CHAIN 1..282 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_0000370583" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 11..31 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 180 FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 99 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 122..123 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 157..158 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 177 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 255..257 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" SQ SEQUENCE 282 AA; 32889 MW; 6935EABEDB0BD2FF CRC64; MSLTDDQASK RQAYRAAKEA NRKELKHVKI DDALPNKSSE LDLPKKKFYR QRAHSNPFSD HQLEYPLSPA EMDWSKLYPH YYDAATNTMT KKVTVADIGC GYGGLMVELS RELPENLILG MEIRVQVTNY VEDRIIALRT NHAAQKEYQN INVLRGNAMK FLPNFFEKSQ LEKMFFCFPD PHFKQRKHKA RIITNTLLSE YAYVLKEGGV IYTITDVLDL HNWMVEHLNM HPLFDRLGDE WLDQDPCVRI MRHATEEGKK VARKQGDKFV ACFRRLPNPE LV //