ID TRMB_CHAGB Reviewed; 293 AA. AC Q2GS86; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 24-JAN-2024, entry version 85. 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=CHGG_09168; OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / OS NRRL 1970) (Soil fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium. OX NCBI_TaxID=306901; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970; RX PubMed=25720678; DOI=10.1128/genomea.00021-15; RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.; RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum."; RL Genome Announc. 3:E0002115-E0002115(2015). 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; CH408034; EAQ85154.1; -; Genomic_DNA. DR RefSeq; XP_001227095.1; XM_001227094.1. DR AlphaFoldDB; Q2GS86; -. DR SMR; Q2GS86; -. DR STRING; 306901.Q2GS86; -. DR GeneID; 4395245; -. DR VEuPathDB; FungiDB:CHGG_09168; -. DR eggNOG; KOG3115; Eukaryota. DR HOGENOM; CLU_050910_3_1_1; -. DR InParanoid; Q2GS86; -. DR OMA; LPNYFAK; -. DR OrthoDB; 116813at2759; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000001056; Unassembled WGS sequence. 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..293 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_0000370593" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 68..97 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 72..95 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 192 FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 111 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 134..135 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 169..170 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 189 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 267..269 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" SQ SEQUENCE 293 AA; 33667 MW; B6250E938A788357 CRC64; MGGDKIKKDK RQKREDYRAA MRKDDISELP RKKFYRQRAH ANPFSDHQLI YPPHPDQMDW SSLYPHYIVD EPTTTSPPPP PPVPEQTPSE PDLTPLRPKP LSKEVSVADI GCGFGGLLIA LAPTMPEALI LGLEIRVSVT HFVEDRIKAL RAQNQAAGLY RNVGVLRANT MKFLPNFFRK AQLEKVFICF PDPHFKIRKH KQRIVSTTLN SEYAYVVKPG GIVYTITDVL DLHEWMVQHF DAHPSFERVS EEEQEADPCV AIMRTETEEG KKVERHKGEK HVALFRRLED PAW //