ID   TRMB_ALCBS              Reviewed;         239 AA.
AC   Q0VLC7;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase;
DE            EC=2.1.1.33;
DE   AltName: Full=tRNA(m7G46)-methyltransferase;
GN   Name=trmB; OrderedLocusNames=ABO_2573;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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; AM286690; CAL18021.1; -; Genomic_DNA.
DR   RefSeq; YP_694293.1; -.
DR   GeneID; 4213307; -.
DR   GenomeReviews; AM286690_GR; ABO_2573.
DR   KEGG; abo:ABO_2573; -.
DR   NMPDR; fig|393595.12.peg.2580; -.
DR   HOGENOM; Q0VLC7; -.
DR   OMA; Q0VLC7; TKFENRG.
DR   BioCyc; ABOR393595:ABO_2573-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    239       tRNA (guanine-N(7)-)-methyltransferase.
FT                                /FTId=PRO_0000288115.
FT   REGION      217    220       Substrate binding (Potential).
FT   BINDING      69     69       S-adenosyl-L-methionine (By similarity).
FT   BINDING      94     94       S-adenosyl-L-methionine (By similarity).
FT   BINDING     121    121       S-adenosyl-L-methionine (By similarity).
FT   BINDING     144    144       S-adenosyl-L-methionine (By similarity).
FT   BINDING     148    148       Substrate (By similarity).
FT   BINDING     180    180       Substrate (Potential).
SQ   SEQUENCE   239 AA;  27171 MW;  83740B9F34ED94AC CRC64;
     MLDFINHDKD PETGKVMRKV RSFVLREGRL TAGQRNALDT LWPRFGLERD QGMLNPESVF
     GRDAPRVLEI GYGMGQSLAQ MAAADPDKDF IGIEVHRPGV GALLMEIEQQ GLSNLRSYCD
     DAVEILELCI PDNSLARVQL YFPDPWHKKK HHKRRIVQPA WVALVQRKLQ PGGILHMATD
     WENYAEHMME VMDAAAGFSN LAGPSAFSPR PSWRPETKFE RRGEKLGHGV WDLLFEKRA
//