ID   TRMB_CHLTA              Reviewed;         219 AA.
AC   Q3KKL0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   05-MAY-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=CTA_0903;
OS   Chlamydia trachomatis (strain A/HAR-13 / ATCC VR-571B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177312; DOI=10.1128/IAI.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
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; CP000051; AAX51112.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_328660.2; -.
DR   GeneID; 3688067; -.
DR   GenomeReviews; CP000051_GR; CTA_0903.
DR   KEGG; cta:CTA_0903; -.
DR   HOGENOM; Q3KKL0; -.
DR   BioCyc; CTRA315277-1:CTA_0903-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.
PE   3: Inferred from homology;
KW   Complete proteome; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN         1    219       tRNA (guanine-N(7)-)-methyltransferase.
FT                                /FTId=PRO_0000288134.
FT   BINDING      49     49       S-adenosyl-L-methionine (By similarity).
FT   BINDING      74     74       S-adenosyl-L-methionine (By similarity).
FT   BINDING     101    101       S-adenosyl-L-methionine (By similarity).
FT   BINDING     124    124       S-adenosyl-L-methionine (By similarity).
FT   BINDING     128    128       Substrate (By similarity).
FT   BINDING     160    160       Substrate (Potential).
SQ   SEQUENCE   219 AA;  25854 MW;  6A605C3022819F6A CRC64;
     MKLPYFWEER SPQIANHVFY VPNYYSRYEE FVMPTWQELF ANNGPICCEL CSGNGDWVVE
     QALKDASVNW IAVEKRFDRV RKIWSKMGNY RVNNLLIVCG EAQTFFSHYV SDASFQKIVV
     NFPDPWPKFR HRKHRLFQDL FVQDMMRTLV VGGQLTLATD DYNYLVNAIT VMLKYLSPGL
     KSPHYINVKD NYGGSWFENL WRSKGQEIFC TEFIKRVGI
//