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 24-JAN-2024, entry version 89. 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}; OrderedLocusNames=WRi_009280; OS Wolbachia sp. subsp. Drosophila simulans (strain wRi). OC Bacteria; Pseudomonadota; 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 two- CC step reaction: L-threonine is first activated by ATP to form Thr-AMP CC and then transferred to the acceptor end of tRNA(Thr). Also edits CC incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP- CC Rule:MF_00184}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L- CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; CC 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-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 family. CC {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; NZ_MKIF01000064.1. DR AlphaFoldDB; C0R403; -. DR SMR; C0R403; -. DR STRING; 66084.WRi_009280; -. DR KEGG; wri:WRi_009280; -. DR HOGENOM; CLU_008554_0_1_5; -. 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-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; cd01667; TGS_ThrRS; 1. DR CDD; cd00860; ThrRS_anticodon; 1. DR CDD; cd00771; ThrRS_core; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.30.54.20; -; 1. DR Gene3D; 3.40.50.800; Anticodon-binding domain; 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; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR036621; Anticodon-bd_dom_sf. DR InterPro; IPR012675; Beta-grasp_dom_sf. DR InterPro; IPR004095; TGS. DR InterPro; IPR012676; TGS-like. DR InterPro; IPR002320; Thr-tRNA-ligase_IIa. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR047246; ThrRS_anticodon. DR InterPro; IPR033728; ThrRS_core. DR InterPro; IPR012947; tRNA_SAD. DR NCBIfam; TIGR00418; thrS; 1. DR PANTHER; PTHR11451:SF44; THREONINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2; 1. DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 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; SSF52954; Class II aaRS ABD-related; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF81271; TGS-like; 1. DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. DR PROSITE; PS51880; TGS; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding; KW Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc. FT CHAIN 1..633 FT /note="Threonine--tRNA ligase" FT /id="PRO_1000199577" FT DOMAIN 1..59 FT /note="TGS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228" FT REGION 240..532 FT /note="Catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184" FT BINDING 332 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184" FT BINDING 383 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184" FT BINDING 509 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="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 //