ID   SYT_BAUCH               Reviewed;         642 AA.
AC   Q1LT04;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=BCI_0472;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(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; CP000238; ABF13851.1; -; Genomic_DNA.
DR   RefSeq; YP_588910.1; -.
DR   SMR; Q1LT04; 242-642.
DR   GeneID; 4056409; -.
DR   GenomeReviews; CP000238_GR; BCI_0472.
DR   KEGG; bci:BCI_0472; -.
DR   HOGENOM; Q1LT04; -.
DR   OMA; Q1LT04; 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; 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; 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    642       Threonyl-tRNA synthetase.
FT                                /FTId=PRO_1000020344.
FT   REGION      243    534       Catalytic.
FT   METAL       334    334       Zinc; catalytic (By similarity).
FT   METAL       385    385       Zinc; catalytic (By similarity).
FT   METAL       511    511       Zinc; catalytic (By similarity).
SQ   SEQUENCE   642 AA;  75086 MW;  B6B1324B5BB2914E CRC64;
     MPVITITNGL QLTFQKPVSS LEIAKYISSN CEQNCIASYL NNRLVDAVDL IMQDSKLDII
     TAEDKAGLDI LRCSCNHLLG HAIKQLWPEA KMTIGKIIDK GFYYDIDLEH KLQPEDIDAL
     EKCMHTLANK NYNIVKKYVS WQQAREIFQA NGEIYKVAIL DDNINQHTLV ALYYYEEYVD
     MCRGPHAPNI RFCHHFKLQK TSITYWRNND KNKKLQRIYG TAWGTDMQLK CYLQSLQEVK
     KRDHRKIGQQ LDLYHIQEEA PGMVFWHVDG WIIFRELETF IRSKLQTYKY QEVKSPVMID
     RTLWEQTGHW SNYAEHIFTT SSENREYCIK PMNCPGHVQI FNQQINSYRD LPLRMAEFGS
     CYRNEPSGSL HGLMRVRNFT QDDAHIFCTE EQVCDEINNN IKMLYEVYHT FGFKKILVNL
     STRPAHRIGN DKIWDKAEQD LATTLTNNGI LFKYNVGAGA FYGPKIEFTL LDSFDRAWQC
     GTIQLDFSLP SRLKAFYINK NNQRLVPVMI HRAILGSLER FIGILIEEYA GFFPTWLAPT
     QVVLMNISDN QSNYVIQLMQ KLSTANIRAK IDLRNEKIGF KIREHTLRRV PYMLICGDQE
     IKMGKVTIRT RYGKNLGMFE MNNFIEKLQH EINHRNLSQI EK
//