ID   TRMD_ACIAD              Reviewed;         249 AA.
AC   Q43963; Q6F7I1;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=tRNA (guanine-N(1)-)-methyltransferase;
DE            EC=2.1.1.228;
DE   AltName: Full=M1G-methyltransferase;
DE   AltName: Full=tRNA [GM37] methyltransferase;
GN   Name=trmD; OrderedLocusNames=ACIAD3311;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-249.
RX   PubMed=7768830; DOI=10.1128/jb.177.11.3295-3307.1995;
RA   Kok R.G., Thor J.J., Nugteren-Roodzant I.M., Vosman B., Hellingwerf K.J.;
RT   "Characterization of lipase-deficient mutants of Acinetobacter
RT   calcoaceticus BD413: identification of a periplasmic lipase chaperone
RT   essential for the production of extracellular lipase.";
RL   J. Bacteriol. 177:3295-3307(1995).
CC   -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC       {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC       {ECO:0000305}.
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DR   EMBL; CR543861; CAG69984.1; -; Genomic_DNA.
DR   EMBL; X80800; CAA56781.1; -; Genomic_DNA.
DR   PIR; S61928; S61928.
DR   RefSeq; WP_004923847.1; NC_005966.1.
DR   AlphaFoldDB; Q43963; -.
DR   SMR; Q43963; -.
DR   STRING; 62977.ACIAD3311; -.
DR   EnsemblBacteria; CAG69984; CAG69984; ACIAD3311.
DR   GeneID; 45235512; -.
DR   KEGG; aci:ACIAD3311; -.
DR   eggNOG; COG0336; Bacteria.
DR   HOGENOM; CLU_047363_0_1_6; -.
DR   OMA; ILCGHYK; -.
DR   OrthoDB; 525632at2; -.
DR   BioCyc; ASP62977:ACIAD_RS14985-MON; -.
DR   Proteomes; UP000000430; 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..249
FT                   /note="tRNA (guanine-N(1)-)-methyltransferase"
FT                   /id="PRO_0000060313"
FT   BINDING         117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         137..142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   249 AA;  28287 MW;  215139F2B65A195C CRC64;
     MFFAVITLFP EMFEAITAYG ISGRATKRQI ATVSCINPRD FAEGNYKRVD ERPFGGGPGM
     VMMAEPLAKA IIHAKQLAEQ AGCVHAPVVY MSPQGKTLNE HAVQQFVDYD GLIVLCGRYE
     GVDERLIQHY VDQEWSIGDY VLSGGELPAM VLLDSIIRRL PDAMSDEQSH IQDSFVDGLL
     DCPQYTKPDH FEGLDVPEVL KSGHHANIEK WRFLQRYQRT LDRRPELVEK VTLTKQQRKW
     LTFLDDSKN