ID   SYT_BURTA               Reviewed;         635 AA.
AC   Q2SVD8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Threonyl-tRNA synthetase;
DE            EC=6.1.1.3;
DE   AltName: Full=Threonine--tRNA ligase;
DE            Short=ThrRS;
GN   Name=thrS; OrderedLocusNames=BTH_I2595;
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   -!- CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP +
CC       diphosphate + L-threonyl-tRNA(Thr).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000086; ABC37600.1; -; Genomic_DNA.
DR   RefSeq; YP_443111.1; -.
DR   GeneID; 3848822; -.
DR   GenomeReviews; CP000086_GR; BTH_I2595.
DR   KEGG; bte:BTH_I2595; -.
DR   TIGR; BTH_I2595; -.
DR   HOGENOM; Q2SVD8; -.
DR   OMA; Q2SVD8; QDEAPGM.
DR   BioCyc; BTHA271848:BTH_I2595-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00184; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004154; Anticodon_bd.
DR   InterPro; IPR012675; b-grasp_ferredoxin-like.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR002320; Thr-tRNA-synth_IIa.
DR   InterPro; IPR018158; Thr-tRNA-synth_IIa_cons-reg.
DR   InterPro; IPR012947; tRNA_SAD.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF02824; TGS; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR01047; TRNASYNTHTHR.
DR   TIGRFAMs; TIGR00418; thrS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 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    635       Threonyl-tRNA synthetase.
FT                                /FTId=PRO_1000020359.
FT   REGION      242    533       Catalytic.
FT   METAL       333    333       Zinc; catalytic (By similarity).
FT   METAL       384    384       Zinc; catalytic (By similarity).
FT   METAL       510    510       Zinc; catalytic (By similarity).
SQ   SEQUENCE   635 AA;  72297 MW;  9EA5167EB6CB586C CRC64;
     MVSIRLPDGS IRQYEHPVTV AEVAASIGPG LAKAALGGKL DGELVDTSAL IDRDASLAIV
     TDKDADGLDI IRHSTAHLLA YAVKELHPDA QVTIGPVIDN GFYYDFSYHR PFTPEDLEAI
     EKRMQELAKR DEPVTRRVVS RDEAVSYFRS IGEKYKAEII ESIPASDEIK LYSHGGFTDL
     CRGPHVPSTG KLKVFKLMKV AGAYWRGDSK NEQLQRIYGT AWTKKEDQDA YLHMLEEAEK
     RDHRKLGKQL DLFHIQEEAP GMVFWHPKGW TLWQRVEQYM RRRLDAAGYL EIKTPMIMDR
     SLWEASGHWQ NYRENMFTTE SEKRDYAIKP MNCPGHVQVF KHGLRSYRDL PLRYAEFGSC
     HRNEASGALH GLMRVRGFVQ DDAHIFCTED QINSEAIAFN KLAMSVYEDF GFDRIDIKLS
     LRPEQRMGSD ETWDHAEEGL RNALKACGLE WEELPGEGAF YGPKIEYHIK DALGRSWQCG
     TLQLDMMLPE RLGAEYVAED NSRRRPVMLH RAIVGSMERF LGILIEHHAG AMPAWLAPFH
     AVVLNIAESQ AEYAQTVVQS LQKQGLRVSA DLRNEKISYK IREHTLEKVP YLLVVGDKER
     EAQTVAVRAR GGVDLGVMPV EAFVERLRED IQAFK
//