ID   SYM_BURCM               Reviewed;         720 AA.
AC   Q0BCT3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=Bamb_2484;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000440; ABI88040.1; -; Genomic_DNA.
DR   RefSeq; YP_774374.1; -.
DR   GeneID; 4308871; -.
DR   GenomeReviews; CP000440_GR; Bamb_2484.
DR   KEGG; bam:Bamb_2484; -.
DR   OMA; Q0BCT3; 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    720       Methionyl-tRNA synthetase.
FT                                /FTId=PRO_0000331789.
FT   DOMAIN      614    720       tRNA-binding.
FT   MOTIF        27     37       "HIGH" region.
FT   MOTIF       348    352       "KMSKS" region.
FT   METAL       158    158       Zinc (By similarity).
FT   METAL       161    161       Zinc (By similarity).
FT   METAL       171    171       Zinc (By similarity).
FT   METAL       174    174       Zinc (By similarity).
FT   BINDING     351    351       ATP (By similarity).
SQ   SEQUENCE   720 AA;  79328 MW;  0985FD04AC94F32F CRC64;
     MSASDLTSVQ ATAPQGRRQI LVTSALPYAN GQIHIGHLVE YIQTDIWVRT LRMHGHEVYY
     IGADDTHGTP VMLRAEKEGL TPKQLIDRVW TEHKRDFDSF GVSFDNFYST DSDENRVLSE
     SIYLALKENG LIAERAIEQA YDPVKEMFLP DRFIKGECPK CHAKDQYGDN CEVCGSTYLP
     TELLNPYSVV SGATPVRKTS THYFFRLSDP RCESFLREWV SGLAQPEATN KMREWLGDAG
     EAKLADWDIS RDAPYFGFEI PGAPGKYFYV WLDAPVGYYA SFKNLCDREG IDFDAWIRAG
     STAEQYHFIG KDILYFHTLF WPAMLEFSGH RTPTNVFAHG FLTVDGAKMS KSRGTFITAQ
     SYIDTGLNPE WLRYYFAAKL NATMEDIDLN LDDFQARVNS DLVGKYVNIA SRAAGFLIKR
     FDGRVQDSAM NHPLVAKLRD AIASIAAHYE GREYSRALRH TMELADEVNA YVDGAKPWEL
     AKDPANAVAL HETCSVSLEA FRLLSLALKP VMPRVAEAVE AFFGVAPLAW ADAAKPLSSA
     QPIKAYQHLM TRVDPKQIDA LLAANRDSLQ ADAAGAAAAG ATAANAAKDA KNAKANAKAV
     AANGADDAPI SIDDFAKVDL RIAKIVACQA VEGSDKLLQL TLDIGEEKTR NVFSGIKSAY
     QPEQLVGKLT VMVANLAPRK MKFGLSEGMV LAASAADEKA EPGLYILEPH SGAKPGMRVK
//