TRM5_PUCGT
ID TRM5_PUCGT Reviewed; 510 AA.
AC E3KWE1;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
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};
GN Name=TRM5 {ECO:0000255|HAMAP-Rule:MF_03152}; ORFNames=PGTG_14821;
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL;
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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; DS178315; EFP88616.2; -; Genomic_DNA.
DR RefSeq; XP_003333035.2; XM_003332987.2.
DR AlphaFoldDB; E3KWE1; -.
DR SMR; E3KWE1; -.
DR STRING; 5297.GMQ_08063T0; -.
DR PRIDE; E3KWE1; -.
DR EnsemblFungi; EFP88616; EFP88616; PGTG_14821.
DR GeneID; 10541244; -.
DR KEGG; pgr:PGTG_14821; -.
DR VEuPathDB; FungiDB:PGTG_14821; -.
DR eggNOG; KOG2078; Eukaryota.
DR HOGENOM; CLU_022610_2_3_1; -.
DR InParanoid; E3KWE1; -.
DR OrthoDB; 788980at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
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..510
FT /note="tRNA (guanine(37)-N1)-methyltransferase"
FT /id="PRO_0000414170"
FT REGION 61..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 299
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 338..339
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 366..367
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 400
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ SEQUENCE 510 AA; 58198 MW; 560F0BE3D6B84EDA CRC64;
MEEELICRGF DSVEVLFVDV FEKSRLSVGG DGERMLQTPQ TGSLMLSSLL TTRRTISSMA
ALQQPSRHRF PPPNNIQRLP LRPDGQQEPI KLTEAIKQQF KQSIPLLAAR VPSPSITKFK
TNPEIRKALL NSKNLRSVEP DPDSTDNAFK LLLLNTPHKD QIPESTLKVF QEHDIQIKNT
KLDLDWEYWM ADEIIERLLP DQLTDIPASF TMIGHIAHFN LRDEYLPYKY LIGQVILEKN
LAIKTVVNKI DNINSQFRFF EMELLAGEPD YTVTLWQSGC RYRFDFSKVY YNPRLSTEHD
LLSSMIEKDE VVVDAFAGVG PFAMRAAANR KAWVLASDLN PASVEALETN VRLNKLQGRV
AVSGGDGREK IREAVRTLWL DKPFKTPNSS PLLPDHFIIN LPDSSIQFLD AFRDLYHPLS
DSEGFLNAVK KKSRLPLLHC YCFTKQVDEP ESDICQRVSE VMKVEISPST VARFELKFVR
AVAPHKDMYR ITFELPLKLL FSSSSEESRA
