ID   SYM_BORA1               Reviewed;         691 AA.
AC   Q2KYS4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=BAV0472;
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: 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: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. MetG type 1 subfamily.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain.
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DR   EMBL; AM167904; CAJ48077.1; -; Genomic_DNA.
DR   RefSeq; YP_785005.1; -.
DR   GeneID; 6264767; -.
DR   GenomeReviews; AM167904_GR; BAV0472.
DR   KEGG; bav:BAV0472; -.
DR   HOGENOM; Q2KYS4; -.
DR   OMA; Q2KYS4; SAYQPEQ.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
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; IPR004495; Met-tRNA-synth_Ia_bsu_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR014758; tRNA-synt_met_N.
DR   InterPro; IPR002547; tRNA_bd.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   TIGRFAMs; TIGR00399; metG_C_term; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   RNA-binding; tRNA-binding; Zinc.
FT   CHAIN         1    691       Methionyl-tRNA synthetase.
FT                                /FTId=PRO_0000331785.
FT   DOMAIN      585    691       tRNA-binding.
FT   MOTIF        12     22       "HIGH" region.
FT   MOTIF       341    345       "KMSKS" region.
FT   METAL       143    143       Zinc (By similarity).
FT   METAL       146    146       Zinc (By similarity).
FT   METAL       156    156       Zinc (By similarity).
FT   METAL       159    159       Zinc (By similarity).
FT   BINDING     344    344       ATP (By similarity).
SQ   SEQUENCE   691 AA;  76712 MW;  53FDD38E678D7941 CRC64;
     MSRTLFVTTA LPYANGSFHI GHIMEYIQAD IWVRSMRMAG HTVHFVGADD AHGAPIMLKA
     EKEGITPQAL VARYAAERPR YLDGFHIRFD HWHSTDSAEN VALSHEIYRA LKAAGLIETR
     SIEQFFDPVK GMFLADRYIK GECPRCHAKD QYGDSCEVCG AVYAPTELIQ PYSALTGATP
     VLKRSDHFFF KLSDPRCVEF LQQWTTGSNR NGIKHLQSEV QAKTREWLGG EEGEAKLGDW
     DISRDAPYFG IEIPDAPGKY FYVWLDAPVG YLASLKSYCD KIGLDFDALL DPSSATEQVH
     FIGKDIIYFH ALFWPAMLKF AGRKTPDALN VHGFITVSGE KMSKSRGTGI SPLRYLEVGM
     DPEWLRYYMA AKLNARVEDM DFNPEDFIAR VNSDLVGKYV NIASRAANFI TRHFEGKLAY
     LGDTAALSAE FAQQTESIRA ALEAREFNRA IREIMAYADG INQAFDAAQP WVLAKGFAEA
     DEARRAQLQD ICSRALAGFK ALSVMLAPVL PALTSRVARD LFGAQRDFIW SDAADLPAQV
     APFKHLMQRV DPQMLDALFE PPAELAAPAP TPGGEALADT ISIDDFVKVD LRIAKIINCE
     EVEGSTKLLR LTLDAGEGRH RNVFSGIKSF YKPQDLIGKL TVLVANLAPR KMKFGVSEGM
     VLAASHADEK VDAGIYVLEP WPGAQPGMRI H
//