ID   TRMD_BORA1              Reviewed;         270 AA.
AC   Q2KY83;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=BAV2349;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ49959.1; -; Genomic_DNA.
DR   RefSeq; YP_786863.1; -.
DR   GeneID; 6267926; -.
DR   GenomeReviews; AM167904_GR; BAV2349.
DR   KEGG; bav:BAV2349; -.
DR   NMPDR; fig|521.1.peg.105; -.
DR   HOGENOM; Q2KY83; -.
DR   OMA; Q2KY83; HRSVDDT.
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    270       tRNA (guanine-N(1)-)-methyltransferase.
FT                                /FTId=PRO_0000257393.
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   270 AA;  29382 MW;  140ABD2B98A8B3FF CRC64;
     MRIDVITLFP EMFGVVRDLG VTGRAHAQGL WSLHAWNPRD FTTDVHRTVD DRPYGGGPGM
     VMMAAPLEAA VKAAQAARAA QHLPPAPVAL LSPVGRRYDQ GAAQQLASSD GLVLICGRYE
     GLDQRFIDRC VTLEISLGDF VLSGGEIAAL AVIDAAVRLL PGALGDGDSA LQDSFNDTLS
     GLLDSPHYTR PEVYEDQAVP AELLSGHHAR IARWRRDQSL RLTLARRPEL IDRARTQGWL
     SYADECVLAE LQGVVAPPDP RKKRRRKPAA
//