ID   TRMB_BARHE              Reviewed;         233 AA.
AC   Q6G4W3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase;
DE            EC=2.1.1.33;
DE   AltName: Full=tRNA(m7G46)-methyltransferase;
GN   Name=trmB; OrderedLocusNames=BH02190;
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=38323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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.
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; BX897699; CAF27031.1; -; Genomic_DNA.
DR   RefSeq; YP_033072.1; -.
DR   GeneID; 2864622; -.
DR   GenomeReviews; BX897699_GR; BH02190.
DR   KEGG; bhe:BH02190; -.
DR   NMPDR; fig|283166.1.peg.200; -.
DR   HOGENOM; Q6G4W3; -.
DR   OMA; Q6G4W3; YPDPWPK.
DR   BioCyc; BHEN283166:BH02190-MON; -.
DR   BRENDA; 2.1.1.33; 277357.
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    233       tRNA (guanine-N(7)-)-methyltransferase.
FT                                /FTId=PRO_0000171297.
FT   REGION      212    215       Substrate binding (Potential).
FT   BINDING      62     62       S-adenosyl-L-methionine (By similarity).
FT   BINDING      87     87       S-adenosyl-L-methionine (By similarity).
FT   BINDING     116    116       S-adenosyl-L-methionine (By similarity).
FT   BINDING     138    138       S-adenosyl-L-methionine (By similarity).
FT   BINDING     142    142       Substrate (By similarity).
FT   BINDING     174    174       Substrate (Potential).
SQ   SEQUENCE   233 AA;  27515 MW;  778154B3E04E820F CRC64;
     MIDHNIRTGK AFFGRRKGKR LRNSQLVLIK KLFPTLDINL NNSVPLNLTS LFSRKVKEVR
     LEIGFGGGEH LLHEMKHFPQ TGFIGIEPFI NGMAKMLMSL EEHKQYQNQL RLYNDDATGL
     LDWLPNASLD GIDLFYPDPW PKKKHWKRRF INMKNLNRFA RVLKTGKKFR FASDIESYVN
     WTLYHCSNHH SFEWEAKNPK DWKTPYTLWS GTRYEAKALR EGRAPTYLTF IKK
//