SYT_WOLWR
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 03-AUG-2022, entry version 84.
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; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified 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}.
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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 EnsemblBacteria; ACN95645; ACN95645; 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; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.930.10; -; 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; 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; 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; SSF55681; SSF55681; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00418; thrS; 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
