ID   TRMD_AYWBP              Reviewed;         242 AA.
AC   Q2NJG9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-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=AYWB_307;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma;
OC   Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A.,
RA   Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W.,
RA   Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to
RT   diverse environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(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; CP000061; ABC65424.1; -; Genomic_DNA.
DR   RefSeq; YP_456503.1; -.
DR   GeneID; 3865901; -.
DR   GenomeReviews; CP000061_GR; AYWB_307.
DR   KEGG; ayw:AYWB_307; -.
DR   HOGENOM; Q2NJG9; -.
DR   OMA; Q2NJG9; 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    242       tRNA (guanine-N(1)-)-methyltransferase.
FT                                /FTId=PRO_0000257390.
FT   REGION      130    135       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   BINDING     111    111       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity).
SQ   SEQUENCE   242 AA;  27695 MW;  7B99E5D53F50C403 CRC64;
     MIIEIITIFP SFFKSFCETS IIKRALEQKK VQIKIHDLRI YSSNKHNQVD DSVYGGGVGM
     LLSFPPFFDC LQKIKTPQSK VILLSPQGQI FNQIHATNFA QKETHLIILC GNYEGVDARI
     LQYIDAEISI GDYVLTGGEI AATVLVDAIT RLIPGVIKEQ SYLEDSHQQG LLKYPQYTRP
     QNYFNHVVPT ILLSGNHAKI RSWRQKESLK KTLQKRPDLL ENKKLTLEQT KLLKEIKQEL
     QK
//