ID   TRMB_BURTA              Reviewed;         265 AA.
AC   Q2SYE0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase;
DE            EC=2.1.1.33;
DE   AltName: Full=tRNA(m7G46)-methyltransferase;
GN   Name=trmB; OrderedLocusNames=BTH_I1513;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at
CC       position 46 (m7G46) in tRNA (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-
CC       homocysteine + tRNA containing N(7)-methylguanine.
CC   -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. TrmB
CC       family.
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DR   EMBL; CP000086; ABC36287.1; -; Genomic_DNA.
DR   RefSeq; YP_442059.1; -.
DR   GeneID; 3846934; -.
DR   GenomeReviews; CP000086_GR; BTH_I1513.
DR   KEGG; bte:BTH_I1513; -.
DR   TIGR; BTH_I1513; -.
DR   HOGENOM; Q2SYE0; -.
DR   OMA; Q2SYE0; TKFENRG.
DR   BioCyc; BTHA271848:BTH_I1513-MON; -.
DR   GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:HAMAP.
DR   GO; GO:0006400; P:tRNA modification; IEA:HAMAP.
DR   HAMAP; MF_01057; -; 1.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase.
DR   PANTHER; PTHR23417:SF1; Methyltransf_4; 1.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   TIGRFAMs; TIGR00091; CHP91; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN         1    265       tRNA (guanine-N(7)-)-methyltransferase.
FT                                /FTId=PRO_0000288130.
FT   REGION      241    244       Substrate binding (Potential).
FT   BINDING      95     95       S-adenosyl-L-methionine (By similarity).
FT   BINDING     120    120       S-adenosyl-L-methionine (By similarity).
FT   BINDING     147    147       S-adenosyl-L-methionine (By similarity).
FT   BINDING     170    170       S-adenosyl-L-methionine (By similarity).
FT   BINDING     174    174       Substrate (By similarity).
FT   BINDING     206    206       Substrate (Potential).
SQ   SEQUENCE   265 AA;  29365 MW;  346228F881714D97 CRC64;
     MNHDDPNASG VPHDDANDAA PASASDAARA TGHADDESSP LHLRRIRSFV TRAGRVSTGQ
     RRAIDELGPR FVVPYDNAQP DWDTVFGRRA PRVLEIGFGM GASTAEIAAH RPGDDFIGVE
     VHEPGVGALL KLIGEQQLSN IRIIQHDAVE VLEHMIAPDS LDGAHIFFPD PWHKARHHKR
     RLIQPPFVAQ LAARLKPGAY LHCATDWQNY AEQMLEVLGA DPSLENTAQD YAPRPDYRPV
     TKFERRGLRL GHGVWDLVFR KKRAG
//