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   16-JUN-2009, entry version 59.
DE   RecName: Full=tRNA (guanine-N(1)-)-methyltransferase;
DE            EC=2.1.1.31;
DE   AltName: Full=M1G-methyltransferase;
DE   AltName: Full=tRNA [GM37] methyltransferase;
GN   Name=trmD; OrderedLocusNames=ACIAD3311;
OS   Acinetobacter sp. (strain ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA   Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA   Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp.
RT   ADP1, 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   MEDLINE=95286514; PubMed=7768830;
RA   Kok R.G., Thor J.J., Nugteren-Roodzant I.M., Vosman B.,
RA   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       (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-
CC       homocysteine + tRNA containing N(1)-methylguanine.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase trmD family.
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DR   EMBL; CR543861; CAG69984.1; -; Genomic_DNA.
DR   EMBL; X80800; CAA56781.1; -; Genomic_DNA.
DR   PIR; S61928; S61928.
DR   RefSeq; YP_047806.1; -.
DR   HSSP; P43912; 1UAJ.
DR   GeneID; 2880730; -.
DR   GenomeReviews; CR543861_GR; ACIAD3311.
DR   KEGG; aci:ACIAD3311; -.
DR   NMPDR; fig|62977.3.peg.2999; -.
DR   HOGENOM; Q43963; -.
DR   OMA; Q43963; HRSVDDT.
DR   BioCyc; ASP62977:ACIAD3311-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IEA:HAMAP.
DR   GO; GO:0006400; P:tRNA modification; IEA:HAMAP.
DR   HAMAP; MF_00605; -; 1.
DR   InterPro; IPR016009; tRNA_m1G_MeTrfase.
DR   InterPro; IPR002649; tRNA_m1G_MeTrfase_bac.
DR   Pfam; PF01746; tRNA_m1G_MT; 1.
DR   PIRSF; PIRSF000386; tRNA_mtase; 1.
DR   ProDom; PD004978; tRNA_m1G_mtfrase; 1.
DR   TIGRFAMs; TIGR00088; trmD; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN         1    249       tRNA (guanine-N(1)-)-methyltransferase.
FT                                /FTId=PRO_0000060313.
FT   REGION      137    142       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   BINDING     117    117       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity).
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
//