TRM5_FUSV7
ID TRM5_FUSV7 Reviewed; 465 AA.
AC C7YK87;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 48.
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 {ECO:0000255|HAMAP-Rule:MF_03152};
DE Flags: Precursor;
GN Name=TRM5 {ECO:0000255|HAMAP-Rule:MF_03152}; ORFNames=NECHADRAFT_98685;
OS Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS 45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex; Fusarium vanettenii.
OX NCBI_TaxID=660122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA VanEtten H.D.;
RT "The genome of Nectria haematococca: contribution of supernumerary
RT chromosomes to gene expansion.";
RL PLoS Genet. 5:E1000618-E1000618(2009).
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; GG698896; EEU48404.1; -; Genomic_DNA.
DR RefSeq; XP_003054117.1; XM_003054071.1.
DR AlphaFoldDB; C7YK87; -.
DR STRING; 140110.NechaP98685; -.
DR PRIDE; C7YK87; -.
DR EnsemblFungi; NechaT98685; NechaP98685; NechaG98685.
DR GeneID; 9664123; -.
DR KEGG; nhe:NECHADRAFT_98685; -.
DR eggNOG; KOG2078; Eukaryota.
DR HOGENOM; CLU_022610_2_2_1; -.
DR InParanoid; C7YK87; -.
DR OMA; PKKQMFC; -.
DR OrthoDB; 788980at2759; -.
DR Proteomes; UP000005206; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:0070901; P:mitochondrial tRNA methylation; IEA:EnsemblFungi.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IEA:EnsemblFungi.
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; Transit peptide; tRNA processing.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT CHAIN 21..465
FT /note="tRNA (guanine(37)-N1)-methyltransferase"
FT /id="PRO_0000414166"
FT REGION 326..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 238
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 304..305
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 359
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ SEQUENCE 465 AA; 52510 MW; 4F6A8CDFDF2BF133 CRC64;
MDKNSQLRDM NLFRAPAARA AKTLDRSVFA KTLNAAAASI SENRLLSKYR KELEKTQEVL
FMERFNPILP DPDPSLASQG RKCIVLSPQI KPASPETWSP TLQEASKLGE LKVVPYDLEI
TYDFWNYFDV VKSILPEELH GEIPSGFNTV GHVAHLNIRD QYLPYKNIIA QVLLDKNPHI
KTVINKIDNV GSENEFRTFA YEVLGGPDNM NVEVSEAGCI FRFDYSKVYW NSKLDTEHKR
ITSFFKPGEV VADVMAGIGP FAVPAGKKGV FVWANDKNPE SHRYLEDAIQ KNKVWEFVKP
FNHDGHDFIR TSADLVLEAS KRGDCAVIKP PRPPRKSAAP PPEPVRVPVP PTISHFVMNL
PASAIEFLHN YRGLYHGHED LFEPHTETKL PIVHVHCFSA KMDDDTPLKD ICERIHKEIG
VMLKPGDAEK EGEVLIYDVR DVAPAKRMFC ASFRLPREVA FAARA
