ID TRMB_CAEEL Reviewed; 256 AA. AC Q23126; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 147. 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=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=metl-1 {ECO:0000312|WormBase:W02B12.10}; GN ORFNames=W02B12.10 {ECO:0000312|WormBase:W02B12.10}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). 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 -!- 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; BX284602; CAA91400.1; -; Genomic_DNA. DR PIR; T26090; T26090. DR RefSeq; NP_496448.1; NM_064047.3. DR AlphaFoldDB; Q23126; -. DR SMR; Q23126; -. DR BioGRID; 40060; 9. DR STRING; 6239.W02B12.10.1; -. DR EPD; Q23126; -. DR PaxDb; 6239-W02B12-10; -. DR PeptideAtlas; Q23126; -. DR EnsemblMetazoa; W02B12.10.1; W02B12.10.1; WBGene00012205. DR GeneID; 174753; -. DR KEGG; cel:CELE_W02B12.10; -. DR UCSC; W02B12.10; c. elegans. DR AGR; WB:WBGene00012205; -. DR WormBase; W02B12.10; CE03770; WBGene00012205; metl-1. DR eggNOG; KOG3115; Eukaryota. DR GeneTree; ENSGT00390000017840; -. DR HOGENOM; CLU_050910_3_1_1; -. DR InParanoid; Q23126; -. DR OMA; LPNYFAK; -. DR OrthoDB; 116813at2759; -. DR PhylomeDB; Q23126; -. DR UniPathway; UPA00989; -. DR PRO; PR:Q23126; -. DR Proteomes; UP000001940; Chromosome II. DR Bgee; WBGene00012205; Expressed in germ line (C elegans) and 4 other cell types or tissues. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central. DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; ISS:UniProtKB. 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 GO; GO:0006400; P:tRNA modification; ISS:UniProtKB. 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..256 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_0000171433" FT REGION 17..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 155 FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 74 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 97..98 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 132..133 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 152 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 230..232 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" SQ SEQUENCE 256 AA; 30041 MW; 4F4FAF58CB25FD24 CRC64; MDITPALTEM ELDHKPTCET VPGLPQKKHY RQRAHSNPHS DHDIEYPLTP NHMDWTKYYG DYTKGRQVDF ADIGCGYGGL LMRLSPKYPD NLMIGMEIRV KVSDYVNEKI QALRKHHAEA GHYRNVAVLR SNAMKYMPNY FHKGQLSKMF FLFPDPHFKN KKHKWRIITP TLLSEYAYVL REGGIIYTIT DVKDLHEWMV KHLSEHPLFE RLTEEEMKKD PIVEMLFEST EEGQKVTRND GGKWPAIFRR LPNPAL //