TRM5_CAEEL
ID TRM5_CAEEL Reviewed; 474 AA.
AC A8WHT1;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=tRNA (guanine(37)-N1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=M1G-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA [GM37] methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA methyltransferase 5 homolog {ECO:0000255|HAMAP-Rule:MF_03152};
GN ORFNames=C53A5.17;
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: Specifically methylates the N1 position of guanosine-37 in
CC various cytoplasmic and mitochondrial tRNAs. Methylation is not
CC dependent on the nature of the nucleoside 5' of the target nucleoside.
CC This is the first step in the biosynthesis of wybutosine (yW), a
CC modified base adjacent to the anticodon of tRNAs and required for
CC accurate decoding. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03152};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03152}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03152}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_03152}. Note=Predominantly in the
CC mitochondria and in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000305}.
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DR EMBL; Z81486; CAP16267.1; -; Genomic_DNA.
DR EMBL; Z78015; CAP16267.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001256592.1; NM_001269663.1.
DR AlphaFoldDB; A8WHT1; -.
DR SMR; A8WHT1; -.
DR STRING; 6239.C53A5.17; -.
DR EPD; A8WHT1; -.
DR PaxDb; A8WHT1; -.
DR PeptideAtlas; A8WHT1; -.
DR EnsemblMetazoa; C53A5.17.1; C53A5.17.1; WBGene00194707.
DR GeneID; 13216595; -.
DR KEGG; cel:CELE_C53A5.17; -.
DR UCSC; C53A5.2c; c. elegans.
DR CTD; 13216595; -.
DR WormBase; C53A5.17; CE41622; WBGene00194707; -.
DR eggNOG; KOG2078; Eukaryota.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000153304; -.
DR HOGENOM; CLU_022610_2_3_1; -.
DR InParanoid; A8WHT1; -.
DR OMA; DMYKIVV; -.
DR OrthoDB; 788980at2759; -.
DR PhylomeDB; A8WHT1; -.
DR PRO; PR:A8WHT1; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00194707; Expressed in adult organism and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070901; P:mitochondrial tRNA methylation; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03152; TRM5; 1.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025792; tRNA_Gua_MeTrfase_euk.
DR Pfam; PF02475; Met_10; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Mitochondrion; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..474
FT /note="tRNA (guanine(37)-N1)-methyltransferase"
FT /id="PRO_0000414132"
FT REGION 452..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 274..275
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 303..304
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 345
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ SEQUENCE 474 AA; 55008 MW; F09972BE5F583413 CRC64;
MIILKRLFSN MSILQPPEVV RGMTKLEKEA FRMPVDFPVI EIEARDAGIV GRRVRLEPYL
IGHKLKPLKN LVDSEKDGKK YLVFHPDKVQ EDETRFKILE LLKRELGNEK LLDWTTLSKD
LTFENWDAKS IFKAVLPVGI DYSSYTQTGH IIHCNFADEI LPFRFIIAEV LLDKVNNCKT
VVQKGNIITN VYRNLDLELL AGEDNYVTEV KETGLRFKMD FSKVYWNSRL SHEHERVSGM
FNTQSLVYDA CCGIGPFVLP ATLKRKPKRV VANDLNPESV KWLKVNVGLN KIKEERIEIH
NMDAKMFIKE NVADDVVRLM LEESTAGEFE NEVPKPMSEV HVVMNLPAYA VNFLPAFRGA
LSRFKDEIEK VPLDKRYKWN VYCYLFAKSH VDVPDSWYED EARRMCDEKT KWERSLVVKC
HNVRTVSSRK EMFCAQLELP YEFLLAEPFP DEPEAQCESE EAEEPSSKRI KVDT
