ID   SYM_BAUCH               Reviewed;         547 AA.
AC   Q1LT75;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Methionyl-tRNA synthetase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionine--tRNA ligase;
DE            Short=MetRS;
GN   Name=metG; OrderedLocusNames=BCI_0396;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
CC   -!- FUNCTION: Is required not only for elongation of protein synthesis
CC       but also for the initiation of all mRNA translation through
CC       initiator tRNA(fMet) aminoacylation (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP +
CC       diphosphate + L-methionyl-tRNA(Met).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. MetG type 1 subfamily.
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DR   EMBL; CP000238; ABF14300.1; -; Genomic_DNA.
DR   RefSeq; YP_588839.1; -.
DR   SMR; Q1LT75; 5-546.
DR   GeneID; 4056275; -.
DR   GenomeReviews; CP000238_GR; BCI_0396.
DR   KEGG; bci:BCI_0396; -.
DR   HOGENOM; Q1LT75; -.
DR   OMA; Q1LT75; DFSWREF.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00098; -; 1.
DR   InterPro; IPR015413; aa-tRNA-synt_I.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002304; Met-tRNA-synth_Ia.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR014758; tRNA-synt_met_N.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN         1    547       Methionyl-tRNA synthetase.
FT                                /FTId=PRO_1000075579.
FT   MOTIF        15     25       "HIGH" region.
FT   MOTIF       332    336       "KMSKS" region.
FT   METAL       146    146       Zinc (By similarity).
FT   METAL       149    149       Zinc (By similarity).
FT   METAL       159    159       Zinc (By similarity).
FT   METAL       162    162       Zinc (By similarity).
FT   BINDING     335    335       ATP (By similarity).
SQ   SEQUENCE   547 AA;  62987 MW;  8BE3640077799B5B CRC64;
     MIQVASKILV TCALPYANGS LHLGHMLEHI QADIWVRYQR IRGKQVYFIC ADDAHGTPIM
     LKAKQSGITP EAMINKINQE HQTDLAQFEI SYDNYYSTHS DENRELVISI YNTLKENGLI
     KKRMISQLYD PIHNIFLPDR FVKGYCPRCK LPDQYGDNCE ICGATYHPTD LIDPKSTLSG
     VTPVISKSKH LFFDLPVFSE VLRAWTRSGA LQEQVANKMQ EWFDMGLQQW DISRDAPYFG
     FEVPDTPGKY FYVWLDAPIG YIGAFKNLCN KRNDIIFDEF WHLSSKADLY HFIGKDITYF
     HGIFWPAILE GSKLRKPTNL FVHGYVTING AKMSKSRGTL IKASTYLAHL DASYLRYYYA
     TKLSSDINDI DLNFNDFVNR VNADIINKVI NLAARNASFI QKYFDNKLSA TIEDQYLYDY
     FVTASVSIGE AFNNRETSRA IREIMILADR ANVYIHKKEP WVVAKNKYYQ QDLHNICSMG
     INLFRLLMTY LQPVLPNLAI QAEAFLNTKL NWDSMVIPLT NHKISPFKTL LQRITLSQVK
     AMIDATH
//