ID   TRMD_ANAPZ              Reviewed;         232 AA.
AC   Q2GIL5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-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=APH_1267;
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(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; CP000235; ABD43497.1; -; Genomic_DNA.
DR   RefSeq; YP_505786.1; -.
DR   GeneID; 3930029; -.
DR   GenomeReviews; CP000235_GR; APH_1267.
DR   KEGG; aph:APH_1267; -.
DR   NMPDR; fig|212042.5.peg.1214; -.
DR   TIGR; APH_1267; -.
DR   HOGENOM; Q2GIL5; -.
DR   OMA; Q2GIL5; HRSVDDT.
DR   BioCyc; APHA212042:APH_1267-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    232       tRNA (guanine-N(1)-)-methyltransferase.
FT                                /FTId=PRO_0000257389.
FT   REGION      132    137       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   BINDING     112    112       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity).
SQ   SEQUENCE   232 AA;  25761 MW;  413D471EE118F339 CRC64;
     MIFNVLTIFP QMFPGPLGVS NLGSALKKGL WTLNVFDIRA FANNKHNTVD DTPYGGGPGM
     LLRADVLGRC IDEVLSLHPN TKLMFTSPRG VSFTQDIARQ TMNFDNITLL CGRFEGIDER
     VVDFYKLQEV SIGDYVLSGG ELAAMVIIDT CVRMVPGVIG NAESLKQESM EGSLEYPQYT
     RPASWKGMEV PEVLLTGNHG EIEKWRRNAS LSITAARRPD LLKDRYGEND VE
//