ID   TRMD_ALCBS              Reviewed;         265 AA.
AC   Q0VRF0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-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=ABO_0800;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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; AM286690; CAL16248.1; -; Genomic_DNA.
DR   RefSeq; YP_692520.1; -.
DR   GeneID; 4211924; -.
DR   GenomeReviews; AM286690_GR; ABO_0800.
DR   KEGG; abo:ABO_0800; -.
DR   NMPDR; fig|393595.12.peg.801; -.
DR   HOGENOM; Q0VRF0; -.
DR   OMA; Q0VRF0; LYTRPEV.
DR   BioCyc; ABOR393595:ABO_0800-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    265       tRNA (guanine-N(1)-)-methyltransferase.
FT                                /FTId=PRO_0000257386.
FT   REGION      139    144       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   BINDING     119    119       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity).
SQ   SEQUENCE   265 AA;  29160 MW;  E8A396872951D4B7 CRC64;
     MMTTKPTFAV TLVTLFPEMA QAITGFGVTR RAVDNGQLQV ETVNPRDFTE DRHRTVDDRP
     FGGGPGMVMK VEPLAKALQA ARVANPAAKV IYLSPQGQPL TQAKATALAE QPGLILLAGR
     YEGVDERLLD AEVDEQISIG DYVLSGGELP ALVLIDAVSR LIPGVLGHQD SAEQDSFSGE
     FENLLDCPHY TRPEVYGEQA VPPVLLSGNH ELIRRWRLKQ ALGRTWQQRP DLLEARRARG
     LSKEEQQLLD EYIAEQPSHT AKTTD
//