ID   TRMB_BORA1              Reviewed;         256 AA.
AC   Q2KYW5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase;
DE            EC=2.1.1.33;
DE   AltName: Full=tRNA(m7G46)-methyltransferase;
GN   Name=trmB; OrderedLocusNames=BAV0455;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ48060.1; -; Genomic_DNA.
DR   RefSeq; YP_784989.1; -.
DR   GeneID; 6267538; -.
DR   GenomeReviews; AM167904_GR; BAV0455.
DR   KEGG; bav:BAV0455; -.
DR   NMPDR; fig|521.1.peg.2611; -.
DR   HOGENOM; Q2KYW5; -.
DR   OMA; Q2KYW5; TKFENRG.
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    256       tRNA (guanine-N(7)-)-methyltransferase.
FT                                /FTId=PRO_0000288126.
FT   REGION      234    237       Substrate binding (Potential).
FT   BINDING      88     88       S-adenosyl-L-methionine (By similarity).
FT   BINDING     113    113       S-adenosyl-L-methionine (By similarity).
FT   BINDING     140    140       S-adenosyl-L-methionine (By similarity).
FT   BINDING     163    163       S-adenosyl-L-methionine (By similarity).
FT   BINDING     167    167       Substrate (By similarity).
FT   BINDING     199    199       Substrate (Potential).
SQ   SEQUENCE   256 AA;  28553 MW;  D79ADFA612E3C52D CRC64;
     MNANTPTPID GQPTELTPST QAALEPANHA PASPGATHIR SFVHRRGHIT QRQRDALEQL
     MGKWAIPYAP RPLNPATAFG REAPTILEIG FGMGETTEKI ALARPEDNFL GVEVFNAGVG
     SMLHRIETSQ IPNVRIIQHD AVEVVRDMIA PDSLAGVHVY FPDPWPKKRH HKRRLLQPAF
     VQLLASRIKP GGYLHCATDW QDYAVQMLEV LGGEALLENT AQDYAERPAY RPQTKFETRG
     LRLGHGVWDL IFKRKA
//