ID   TRM5_AJECG              Reviewed;         483 AA.
AC   C0NUP2;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 41.
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=HCBG_06656;
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; GG663372; EEH04705.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NUP2; -.
DR   SMR; C0NUP2; -.
DR   STRING; 447093.C0NUP2; -.
DR   EnsemblFungi; EEH04705; EEH04705; HCBG_06656.
DR   VEuPathDB; FungiDB:HCBG_06656; -.
DR   HOGENOM; CLU_022610_2_2_1; -.
DR   InParanoid; C0NUP2; -.
DR   OrthoDB; 788980at2759; -.
DR   Proteomes; UP000001631; 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   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..483
FT                   /note="tRNA (guanine(37)-N1)-methyltransferase"
FT                   /id="PRO_0000414158"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         252
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT   BINDING         290..291
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT   BINDING         379
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ   SEQUENCE   483 AA;  55500 MW;  23D632FD14ECD86D CRC64;
     MEEAATLQSL SISSSSPFPN NSSPVVTAAN TISTSESDMF RAPVNRMMRT LDRSFFKKTV
     PLSAATIFDK QSIGSIKSEL LQSQDLLLAN RIIPVRAARE GPLENVTDHW YGRKDGKQDG
     RKCLLLREGI KADDVTTWSP TIQKLVEAKS VEVRPFNLLL DYDYFTYTHF NLREQYLPYK
     YLLGEILRDK HPQARTVINK TDDVGSHSEF RTFSYEVLAG EDDMLVTVHE QDCEYSFDYS
     KVYWNTRLAT EHERMVSRFK KGEAVCDVMA GVGPFSIPAG KKQVFVWAND LNPYGYECLE
     RGAAKNKVRE FVKAHNMNGR DFIRFATERL YQGNPRTVVH RTKVPKAERE NSPIRQRKPK
     AFDTEYLTCP RTFDHFVMNL PATAIEFLDA FRGLYAGMQE LFEPYTDRKL PLIHVYCFST
     NSEDEALERK DICERISERL GFKITPEDEG RELEIRSVRL VSPTKKMFCA SFRLPAEVAF
     KKA