ID   SYM_BURTA               Reviewed;         718 AA.
AC   Q2T087;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
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=BTH_I0856;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) 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; CP000086; ABC38961.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_441412.2; -.
DR   GeneID; 3848452; -.
DR   GenomeReviews; CP000086_GR; BTH_I0856.
DR   KEGG; bte:BTH_I0856; -.
DR   TIGR; BTH_I0856; -.
DR   HOGENOM; Q2T087; -.
DR   BioCyc; BTHA271848:BTH_I0856-MON; -.
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    718       Methionyl-tRNA synthetase.
FT                                /FTId=PRO_0000331797.
FT   DOMAIN      612    718       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   718 AA;  79413 MW;  4DC90AD0ECA7ED19 CRC64;
     MSASDLHPVQ AGAPQGRRQI LVTSALPYAN GQIHIGHLVE YIQTDIWART MRMHGHEIYY
     IGADDTHGTP VMLRAEQEGV SPKQLIERVW REHKRDFDSF GVSFDNFYTT DSDENRVLSE
     KIYLALKEAG FIAEREIEQA YDPVKQMFLP DRFIKGECPK CHAKDQYGDS CEVCGTTYQP
     TDLVNPYSVV SGATPVRKTS THHFFRLSDP RCEAFLREWV SGLAQPEATN KMREWLGDAG
     EAKLADWDIS RDAPYFGFEI PGAPGKYFYV WLDAPVGYYA SFKNLCERRG LDFDAWISKD
     STTEQYHFIG KDILYFHTLF WPAMLEFSGH RTPTNVFAHG FLTVDGAKMS KSRGTFITAQ
     SYIDAGLNPE WLRYYFAAKL NATMEDIDLN LEDFQARVNS DLVGKYVNIA SRAAGFLIKR
     FDGRVQASAT NHPLLVTLRD AIPQIAAHYE AREYGRALRQ TMELADAVNG YVDTAKPWEL
     AKDPANAVAL HETCTVSLEA FRLLSLALKP VLPRVAEGVE AFLGIAPLTW ADANKPLSSE
     QPIRAYQHLM TRVDPKQIDA LLAANRSSLQ GAAAADAAGA TNGNGAKAAK SAKAANAASA
     DDEASPFISI DDFAKIDLRI AKIVACQAVE GSDKLLQLTL DVGEEKTRNV FSGIKSAYQP
     EQLVGKLTVM VANLAPRKMK FGLSEGMVLA ASAADEKAEP GLYILEPHSG AKPGMRVK
//