ID   SYT_WOLWR               Reviewed;         633 AA.
AC   C0R403;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   05-DEC-2018, entry version 70.
DE   RecName: Full=Threonine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00184};
DE            EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184};
DE   AltName: Full=Threonyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00184};
DE            Short=ThrRS {ECO:0000255|HAMAP-Rule:MF_00184};
GN   Name=thrS {ECO:0000255|HAMAP-Rule:MF_00184};
GN   OrderedLocusNames=WRi_009280;
OS   Wolbachia sp. subsp. Drosophila simulans (strain wRi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=66084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wRi;
RX   PubMed=19307581; DOI=10.1073/pnas.0810753106;
RA   Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y.,
RA   Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K.,
RA   Andersson S.G.;
RT   "The mosaic genome structure of the Wolbachia wRi strain infecting
RT   Drosophila simulans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(2009).
CC   -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a
CC       two-step reaction: L-threonine is first activated by ATP to form
CC       Thr-AMP and then transferred to the acceptor end of tRNA(Thr).
CC       Also edits incorrectly charged L-seryl-tRNA(Thr).
CC       {ECO:0000255|HAMAP-Rule:MF_00184}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+)
CC         + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-
CC         COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215;
CC         EC=6.1.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00184};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00184}.
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DR   EMBL; CP001391; ACN95645.1; -; Genomic_DNA.
DR   RefSeq; WP_012673323.1; NZ_MKIF01000064.1.
DR   ProteinModelPortal; C0R403; -.
DR   SMR; C0R403; -.
DR   EnsemblBacteria; ACN95645; ACN95645; WRi_009280.
DR   KEGG; wri:WRi_009280; -.
DR   HOGENOM; HOG000003880; -.
DR   KO; K01868; -.
DR   OMA; FYYDFAY; -.
DR   BioCyc; WSP66084:WRI_RS04655-MONOMER; -.
DR   Proteomes; UP000001293; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00771; ThrRS_core; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR033728; ThrRS_core.
DR   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR11451; PTHR11451; 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   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
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;
KW   RNA-binding; tRNA-binding; Zinc.
FT   CHAIN         1    633       Threonine--tRNA ligase.
FT                                /FTId=PRO_1000199577.
FT   REGION      240    532       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00184}.
FT   METAL       332    332       Zinc. {ECO:0000255|HAMAP-Rule:MF_00184}.
FT   METAL       383    383       Zinc; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00184}.
FT   METAL       509    509       Zinc; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00184}.
SQ   SEQUENCE   633 AA;  72338 MW;  94B8F15EEF64B56F CRC64;
     MIRITFSAEQ KVKEYSGKVT GFDILQPDVL KEAIAFKVNG ELHDLSREIE ADAEIEVIQL
     SDEAGLDIIR HDAAHIMAQA VKELFPNTQI TIGPTIQDGF YYDFATGRTF TTDDLTAIEK
     KMKEIVKSNH RFVREVWTRK QAIDFFSDIG EKYKVDIISS IPEGENLTVY RQGDFIDLCR
     GPHSPSTGRV KAFKLMKVAG AYWRGDAKGP MLQRIYGTAW RNKDELNAYL ECLKEAEKRD
     HRKIAKDMDL FHIQEEAVGQ VFWHEQGYIL YNVLESYIRK KLINNGYFEV KTPILVSKEL
     WEKSGHWDKF RENMFIVDES ESKKLAIKPM NCPCHVQIFN SHTRSYRDLP IRMAEFGTCH
     RNESSGSLHG LMRVRGFTQD DAHIFCMEEQ VNSETIKFCD LLKEVYSELG FNEISVKFSD
     RPDVRAGDDE VWDRAEKALL EAVKEAGLSY ELSPGEGAFY GPKLEFVLKD AIGRSWQCGT
     LQVDFILPER LGAFYIGADG HKHHPVMLHR AILGTFERFI GILIENYAGK FPVWLAPTQL
     AILTITNEAD GYATKISNVL KEQGVRVKTD LTNEKISYKI RLHSLNKVPI LWIVGKNEVT
     SKTVSVRNLG SERQESFSLE KAIELLLKSI NLN
//