ID   SYT_BORA1               Reviewed;         650 AA.
AC   Q2L2M5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=BAV1393;
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   -!- 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; AM167904; CAJ49002.1; -; Genomic_DNA.
DR   RefSeq; YP_785915.1; -.
DR   GeneID; 6265354; -.
DR   GenomeReviews; AM167904_GR; BAV1393.
DR   KEGG; bav:BAV1393; -.
DR   NMPDR; fig|521.1.peg.2288; -.
DR   HOGENOM; Q2L2M5; -.
DR   OMA; Q2L2M5; NTKIAIG.
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    650       Threonyl-tRNA synthetase.
FT                                /FTId=PRO_1000020345.
FT   REGION      247    538       Catalytic.
FT   METAL       338    338       Zinc; catalytic (By similarity).
FT   METAL       389    389       Zinc; catalytic (By similarity).
FT   METAL       515    515       Zinc; catalytic (By similarity).
SQ   SEQUENCE   650 AA;  73600 MW;  038AD8FF425350FD CRC64;
     MVQITLPDGS QRQYPGPVTV AEVAQSIGTG LAKAALAGRV TVNDAEPKLV DTSFRIDQDA
     KLAIVTAKDA DGLDLIRHST AHLLAYAVKS LYPDAQVTIG PVIDNGFYYD FSYKRPFTPE
     DLQAIEKKMA ELARKDEVVT REEWTRDDAV AYFKSIGENY KAEIIASIPS NEKISLYREG
     EFIDLCRGPH VPSTGKLKVF KLMKLAGAYW RGDSNNEMLQ RIYGTAWATK DEQDAYLHML
     EEAERRDHRK IGRDLDLFHF QDEGPGLIFW HPKGWTLWQQ VEQYMRAVYR DNGYQEVKAP
     QILDLSLWKK TGHWDNYREN MFTTESENRV YGLKPMNCPG HVQIFNAGLH SYRELPLRYG
     EFGQCHRNEP SGSLHGMMRV RGFTQDDGHI FCTEDQLQDE CADFTALLQK VYRDFGFTEV
     LYKVATRPEK RIGSDEIWDK AETALMESLR RTGCEFEISP GEGAFYGPKI EYTLKDAIGR
     HWQCGTIQVD FSMPVRLGAE YVDQNDQRRA PVMLHRAILG SLERFIGMLI ENHAGAMPPW
     LAPVQAVVCC ISEPSAEYAA KITQSLKKQG FRVQADLRGE KITRKIREHS LQKVPYILVV
     GDKEAQNGTV AVRGLGGLDL GAIPFDDFVA RLNEDVASRR NVVQPDSKAV
//