ID TRMB_CRYNJ Reviewed; 286 AA. AC P0CS80; Q55X18; Q5KMW7; DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 24-JAN-2024, entry version 58. 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=CNB00250; OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC OS MYA-565) (Filobasidiella neoformans). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Tremellales; Cryptococcaceae; Cryptococcus; OC Cryptococcus neoformans species complex. OX NCBI_TaxID=214684; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JEC21 / ATCC MYA-565; RX PubMed=15653466; DOI=10.1126/science.1103773; RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.; RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus RT neoformans."; RL Science 307:1321-1324(2005). 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; AE017342; AAW41459.1; -; Genomic_DNA. DR RefSeq; XP_568766.1; XM_568766.1. DR AlphaFoldDB; P0CS80; -. DR SMR; P0CS80; -. DR STRING; 214684.P0CS80; -. DR PaxDb; 214684-P0CS80; -. DR EnsemblFungi; AAW41459; AAW41459; CNB00250. DR GeneID; 3256005; -. DR KEGG; cne:CNB00250; -. DR eggNOG; KOG3115; Eukaryota. DR HOGENOM; CLU_050910_3_1_1; -. DR InParanoid; P0CS80; -. DR OMA; LPNYFAK; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000002149; Chromosome 2. 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..286 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_0000370594" FT ACT_SITE 181 FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 91 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 114..115 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 158..159 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 178 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 256..258 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" SQ SEQUENCE 286 AA; 32263 MW; ED46ACEFCD44A732 CRC64; MEAGPSTASP GVSVSPAPAL TAGEVQLLKV PQKRFYRQRA HANVFIDHEL DYPKRPELMD WSTHYPAYFS QPNEDGTITQ GEKKVEWADV GCGFGGLLMA LAPLFPEKLM LGMEIRTSVT KYVTDRIAAT RQAQSLLPAD SVDTKPGGYQ NVSVIKANSM KHMPNFFAKG QLEKIFFLFP DPHFKNRKHK ARIITPALLA EYAYVLRPGG ILYTVTDVKD LHEWMAHHLH AHPLFEYIPT ETLSDDPILE AARTATEEGQ KVERNKGDKW VACFRRKEDP KEEDED //