ID   SYT_BURMS               Reviewed;         635 AA.
AC   A1V3R3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
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=BMASAVP1_A1539;
OS   Burkholderia mallei (strain SAVP1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320388;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (DEC-2006) 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; CP000526; ABM52129.1; -; Genomic_DNA.
DR   RefSeq; YP_992866.1; -.
DR   GeneID; 4681248; -.
DR   GenomeReviews; CP000526_GR; BMASAVP1_A1539.
DR   KEGG; bmv:BMASAVP1_A1539; -.
DR   TIGR; BMASAVP1_A1539; -.
DR   OMA; A1V3R3; QDEAPGM.
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_1000020354.
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;  72265 MW;  6AA2BEB8B94C0344 CRC64;
     MVSIRLPDGS VRQYEHPVTV AEVAASIGPG LAKAALGGKL DGELVDTSAL IDRDASLAIV
     TDKDADGLDI IRHSTAHLLA YAVKELHPDA QVTIGPVIDN GFYYDFSYHR PFTPEDLEAI
     EKRMQELAKR DEPVTRRVVS RDEAVSYFRS IGEKYKAEII ESIPASDEIK LYSHGSFTDL
     CRGPHVPSTG KLKVFKLMKV AGAYWRGDSK NEQLQRIYGT AWTRKEDQDA YLHMLEEAEK
     RDHRKLGKQL DLFHIQEEAP GMVFWHPKGW TLWQQVEQYM 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 AMPVWLAPAH
     AVVLNIAESQ AEYARTVAQS LQKQGLRVSA DLRNEKISYK IREHTLEKVP YLLVVGDKER
     EAQTVAVRAR GGVDLGVMPV EAFVERLRED IQAFK
//