ID   TRMD_ACIC1              Reviewed;         286 AA.
AC   A0LV70;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=tRNA (guanine-N(1)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605};
DE            EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_00605};
DE   AltName: Full=M1G-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605};
DE   AltName: Full=tRNA [GM37] methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605};
GN   Name=trmD {ECO:0000255|HAMAP-Rule:MF_00605}; OrderedLocusNames=Acel_1558;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
CC   -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_00605}.
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_00605};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00605}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00605}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC       {ECO:0000255|HAMAP-Rule:MF_00605}.
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DR   EMBL; CP000481; ABK53330.1; -; Genomic_DNA.
DR   RefSeq; WP_011720393.1; NC_008578.1.
DR   AlphaFoldDB; A0LV70; -.
DR   SMR; A0LV70; -.
DR   STRING; 351607.Acel_1558; -.
DR   EnsemblBacteria; ABK53330; ABK53330; Acel_1558.
DR   KEGG; ace:Acel_1558; -.
DR   eggNOG; COG0336; Bacteria.
DR   HOGENOM; CLU_047363_0_0_11; -.
DR   OMA; ILCGHYK; -.
DR   OrthoDB; 525632at2; -.
DR   Proteomes; UP000008221; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd18080; TrmD-like; 1.
DR   Gene3D; 1.10.1270.20; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_00605; TrmD; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR002649; tRNA_m1G_MeTrfase_bac.
DR   InterPro; IPR023148; tRNA_m1G_MeTrfase_C_sf.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR   PANTHER; PTHR46417; PTHR46417; 1.
DR   Pfam; PF01746; tRNA_m1G_MT; 1.
DR   PIRSF; PIRSF000386; tRNA_mtase; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   TIGRFAMs; TIGR00088; trmD; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..286
FT                   /note="tRNA (guanine-N(1)-)-methyltransferase"
FT                   /id="PRO_1000006442"
FT   REGION          232..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT   BINDING         140..145
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
SQ   SEQUENCE   286 AA;  30687 MW;  E0521B196FC8189E CRC64;
     MHVDIVSIFP EYFRPLELSL IGKARARGVL DVHLWDLRDF THDPHRTVDD TPYGGGPGMV
     MRPEPWGETL DAVRAEAARL GVDAPLLIVP TPAGELLTQR AAERYAAEPW LAFACGRYEG
     IDERVLLDAR RHMRVEEVSI GDYVLAGGEA ATLVIVEAVA RLLPGVVGNQ ASVLDDSHAQ
     GLLEGPAYTK PAVWRGLEVP EVLLSGNHAA IARWRREQAI RRTAVRRPEL LDALPPGSLT
     PHEEALAAEA RLHAGRSAET PPPAGAAGSQ AEGPPGTSPS DAAVAH