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 15-FEB-2017, entry version 58. 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 -!- CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP + CC diphosphate + L-threonyl-tRNA(Thr). {ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001391; ACN95645.1; -; Genomic_DNA. DR RefSeq; WP_012673323.1; NC_012416.1. DR ProteinModelPortal; C0R403; -. DR EnsemblBacteria; ACN95645; ACN95645; WRi_009280. DR KEGG; wri:WRi_009280; -. DR PATRIC; 24036133; VBIWolSp98304_1063. DR HOGENOM; HOG000003880; -. DR KO; K01868; -. DR OMA; FYYDFAY; -. DR Proteomes; UP000001293; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-EC. DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:InterPro. 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; IPR012675; Beta-grasp_dom. 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 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; SSF52954; SSF52954; 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; Zinc. FT CHAIN 1 633 Threonine--tRNA ligase. FT /FTId=PRO_1000199577. FT REGION 240 532 Catalytic. FT METAL 332 332 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00184}. FT METAL 383 383 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00184}. FT METAL 509 509 Zinc; catalytic. {ECO:0000255|HAMAP- FT 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 //