ID   SYT_AYWBP               Reviewed;         641 AA.
AC   Q2NIG3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-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=AYWB_663;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma;
OC   Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A.,
RA   Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W.,
RA   Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to
RT   diverse environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(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; CP000061; ABC65780.1; -; Genomic_DNA.
DR   RefSeq; YP_456859.1; -.
DR   GeneID; 3865656; -.
DR   GenomeReviews; CP000061_GR; AYWB_663.
DR   KEGG; ayw:AYWB_663; -.
DR   HOGENOM; Q2NIG3; -.
DR   OMA; Q2NIG3; IQLDFML.
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    641       Threonyl-tRNA synthetase.
FT                                /FTId=PRO_1000020339.
FT   REGION      240    538       Catalytic.
FT   METAL       334    334       Zinc; catalytic (By similarity).
FT   METAL       385    385       Zinc; catalytic (By similarity).
FT   METAL       515    515       Zinc; catalytic (By similarity).
SQ   SEQUENCE   641 AA;  74950 MW;  C94278E10EB71C31 CRC64;
     MIKISFFDNQ IQEFISGTTP LAIWKEHLSE HFKKPVAALF NNQPIELDFP LKKNGNLEIL
     TESDPKSLEV LNHSTAHLMA QAVARLYPDA LFTVGPAIKE GFYYDIDFQK HTISEKDFLT
     IEKVMHQISL ENHKITREEI SFEKAKKLFA YNPYKQVLLE KFRDQTISIY RQGEFFDLCR
     GVHVIKTNLI KHFKILKISG AYFQGDAKNK TLTRIYGTSF FKKQALADYL QLLEERKERD
     HKKINKELDL FMFNKEVGLG LPFWLPKGAT VRRIVERYIV DKELSYDYHH VYTPIMANTE
     LYRISGHLDH YASNMFPIMS LENGEKLVLR PMNCPHHMMI YKKNPHSYKE LPLRIAELGM
     MHRFEKSGAV SGLQRVREMT LNDAHIFARP DQIKEEIKKI INLILEVYCD FNIKNYELRL
     SYRNPNNTEK YFNDDQMWYN AEKTLKETIK ELGLPFKEAI GEAAFYGPKL DVQVFNALGN
     EETLSTVQLD FLLPQKFDLT FIGEDNKHHR PVVIHRAVVS TMERFLAHLV EETKGVFPLW
     LAPVQVLLIP VSAPLHFEFS QKIKETLQLQ NFRVEINSKD NTLGYKIREA QKLKIPYQVV
     IGDHEMINNL ITFRKYGSHL QTTIKVDEFV SLLKDKVLQK K
//