ID   TRMD_BAUCH              Reviewed;         252 AA.
AC   Q1LTR1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=BCI_0196;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000238; ABF13796.1; -; Genomic_DNA.
DR   RefSeq; YP_588653.1; -.
DR   SMR; Q1LTR1; 1-247.
DR   GeneID; 4056378; -.
DR   GenomeReviews; CP000238_GR; BCI_0196.
DR   KEGG; bci:BCI_0196; -.
DR   HOGENOM; Q1LTR1; -.
DR   OMA; Q1LTR1; 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    252       tRNA (guanine-N(1)-)-methyltransferase.
FT                                /FTId=PRO_0000257391.
FT   REGION      133    138       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   BINDING     113    113       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity).
SQ   SEQUENCE   252 AA;  28777 MW;  0DC81399F6657346 CRC64;
     MWIGLISIFP DMFRAVMDYG VTGRAVKKGL LQVHCWNPRA FSHNRHQTVD DRPYGGGPGM
     LLMMQPLRDA IHEAKNHTET GVKVIYLSPQ GRKLDQQGVY ELAANKKLIL ICGRYKGIDE
     RLITTEIDEE WSIGDYVLSG GELAAMILID SMTRLIPGAL SHESSAVEDS FAQGLLDCPH
     YTRPEVLYGI KVPPVLLSGH HANIRRWRLK QSLGRTWLRR PELLNNLYLT HEQVRLLKEF
     QYEYNNLIES QV
//