TRMB_CAEEL
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 03-AUG-2022, entry version 140.
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}.
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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; -.
DR EPD; Q23126; -.
DR PaxDb; Q23126; -.
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 CTD; 174753; -.
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; DLHNWMV; -.
DR OrthoDB; 1417652at2759; -.
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 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-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 Gene3D; 3.40.50.150; -; 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; PTHR23417; 1.
DR PANTHER; PTHR23417:SF16; PTHR23417:SF16; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00091; TIGR00091; 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
