ID   SYT_BORAP               Reviewed;         581 AA.
AC   Q0SMD6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=BAPKO_0764;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(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; CP000395; ABH01992.1; -; Genomic_DNA.
DR   RefSeq; YP_710168.1; -.
DR   GeneID; 4227063; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0764.
DR   KEGG; baf:BAPKO_0764; -.
DR   NMPDR; fig|390236.5.peg.774; -.
DR   HOGENOM; Q0SMD6; -.
DR   OMA; Q0SMD6; NTKIAIG.
DR   BioCyc; BAFZ390236:BAPKO_0764-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; 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   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    581       Threonyl-tRNA synthetase.
FT                                /FTId=PRO_1000020346.
FT   REGION      185    478       Catalytic.
FT   METAL       278    278       Zinc; catalytic (By similarity).
FT   METAL       329    329       Zinc; catalytic (By similarity).
FT   METAL       455    455       Zinc; catalytic (By similarity).
SQ   SEQUENCE   581 AA;  68138 MW;  3A206764A2BBEFAB CRC64;
     MSKDLDKEDV LYKKRHSIAH VMAEAVRDLF PNTKIAIGPP IKDGFYYDFE FKKQITEDSL
     LDIENRMREI LKTGSSFEKE LISVEQALEI FKDEPYKIDL IKNFDLQNEI SIYKSHNFID
     LCRGPHVDNM NKIDPKAFKL TSIAGAYWRG NEKNTMLTRI YGTLWNNEKE LRSYLNLREE
     IKKRDHRKLG KELDLFSIHE EIGPGLVFFH PNGAKIRALI EDFWREEHSK NGYDILFTPH
     IGKSWLWQTS GHLDFYKDSM FEKMEMDKSD YYLKPMNCPF HIAIYNTGKH SYRDLPFRWA
     ELGTVYRYEK IGALHGIMRA RGFTQDDAHI ICTHSQVLDE IKEVLRFAIY MWSKFGFNSL
     KAYLSTKPDK FVGNDSDWEM SLKVLEEALS GFEVPYEIDK GGGAFYGPKI DLKIVDSLER
     EWQMSTIQFD FNLPERFNMT YTAEDGKEKR PFMIHRALLG SIERFFGILI EHYGGAFPLW
     LSPIQAVIIP VNNAVEDYAI KVFNKFKNEG MRIKLDNTSS RMNAKIREYQ AKKIPYMFII
     GEREAKEEKI SIRTRTNEQI NGLELDEALK LILLKIRDKE I
//