ID TRMB_DEBHA Reviewed; 292 AA. AC Q6BX78; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 2. DT 24-JAN-2024, entry version 109. 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=DEHA2B05258g; OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Debaryomyces. OX NCBI_TaxID=284592; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC RC 2968; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., RA Weissenbach J., Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). 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; CR382134; CAG85186.2; -; Genomic_DNA. DR RefSeq; XP_457191.2; XM_457191.1. DR AlphaFoldDB; Q6BX78; -. DR SMR; Q6BX78; -. DR STRING; 284592.Q6BX78; -. DR GeneID; 2913004; -. DR KEGG; dha:DEHA2B05258g; -. DR VEuPathDB; FungiDB:DEHA2B05258g; -. DR eggNOG; KOG3115; Eukaryota. DR HOGENOM; CLU_050910_3_1_1; -. DR InParanoid; Q6BX78; -. DR OMA; LPNYFAK; -. DR OrthoDB; 116813at2759; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000000599; Chromosome B. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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 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..292 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_0000370595" FT REGION 1..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 189 FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 106 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 129..130 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 166..167 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 186 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 264..266 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" SQ SEQUENCE 292 AA; 34725 MW; 013E99298FE4683C CRC64; MGKIEATSKE EKLRVQKEAE ARRRAYRDLK KEARQMQKEV KFDTDDNSEL PKKRFYRQRA HSNPFSDHRL EYPRSPDTMD WSKFYPQYYD SESKKMTSEV EIADIGCGYG GLLINLAPEF PDKLLLGMEI RVQVTQYVED RIIALRNQYR NELQNNYQNI SVLRGNAMKF LPNFFHKAQL SKMFFCFPDP HFKQRKHKAR IITNTLLAEY AYVLKEGGII YTITDVEDLH NWMVKHLEEH PMFERLSKEW EKQDKCVSIM WNSTEEGKKV TRNKGSKWVA CFKRLPTPDD CE //