ID TRMB_PICGU Reviewed; 272 AA. AC A5DC23; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 2. DT 04-NOV-2026, entry version 94. 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}; ORFNames=PGUG_00828; OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes; OC Debaryomycetaceae; Meyerozyma. OX NCBI_TaxID=294746; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL RC Y-324; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B., RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., RA Birren B.W., Kellis M., Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(2009). 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; CH408155; EDK36730.2; -; Genomic_DNA. DR RefSeq; XP_001487451.2; XM_001487401.1. DR SMR; A5DC23; -. DR STRING; 294746.A5DC23; -. DR GeneID; 5128595; -. DR KEGG; pgu:PGUG_00828; -. DR VEuPathDB; FungiDB:PGUG_00828; -. DR eggNOG; KOG3115; Eukaryota. DR HOGENOM; CLU_050910_3_1_1; -. DR InParanoid; A5DC23; -. DR OMA; AADPCVN; -. DR OrthoDB; 47276at2759; -. DR UniPathway; UPA00989; -. DR CDD; cd02440; AdoMet_MTases; 1. DR FunFam; 3.40.50.150:FF:000060; tRNA (guanine-N(7)-)-methyltransferase; 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 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 NCBIfam; TIGR00091; tRNA (guanosine(46)-N7)-methyltransferase TrmB; 1. DR PROSITE; PS51625; SAM_MT_TRMB; 1. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0106143; C:tRNA (m7G46) methyltransferase complex; IEA:EnsemblFungi. DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. DR Proteomes; UP000001997; Unassembled WGS sequence. DR AlphaFoldDB; A5DC23; -. DR FunCoup; A5DC23; 529. 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..272 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_0000370602" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..20 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 171 FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 89 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 112..113 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 148..149 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 168 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 246..248 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" SQ SEQUENCE 272 AA; 31916 MW; 87C52BB3B272D3A2 CRC64; MSTDSESKRR AYREEKEGAR KKSVKLAPEA TPESKPDLPR KRYYRQRAHS NPFSDHSLDY PRNPDAMEWG KLYPEYANTD KKVEIADIGC GYGGLMIGLA KEYPQTMILG MEIRVQVTQY VEDRIIALRE KHEKDEVNYQ NIAVLRGNAM KFLPNFFHRG QLKKMFFCFP DPHFKQRKHK ARIITTTLLS EYAYVLREEG VLYTITDVED LHIWMVKHLD DHPLFERLDK EWEKNDKCVS IMYGSTEEGQ KVARNKGSKF VACFRRVANP EE //