ID SYTC_SULIY Reviewed; 545 AA.
AC C3N9B3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Threonine--tRNA ligase catalytic subunit;
DE EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184};
DE AltName: Full=Threonyl-tRNA synthetase catalytic subunit;
DE Short=ThrRS-cat;
GN Name=thrS-cat {ECO:0000305};
GN Synonyms=thrS {ECO:0000255|HAMAP-Rule:MF_00184};
GN OrderedLocusNames=YG5714_0281;
OS Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=439386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.G.57.14 / Yellowstone #1;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(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 activates
CC L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly
CC charged amino acid; unlike most archaea the editing function is found
CC in a freestanding protein. {ECO:0000250|UniProtKB:Q97VW8}.
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 (By similarity). Probably interacts with its editing
CC subunit (By similarity). {ECO:0000250|UniProtKB:Q97VW8,
CC ECO:0000250|UniProtKB:Q9YDW0}.
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; CP001403; ACP44575.1; -; Genomic_DNA.
DR RefSeq; WP_010923890.1; NC_012622.1.
DR AlphaFoldDB; C3N9B3; -.
DR SMR; C3N9B3; -.
DR GeneID; 7808880; -.
DR KEGG; siy:YG5714_0281; -.
DR HOGENOM; CLU_008554_0_1_2; -.
DR Proteomes; UP000002308; 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; cd00860; ThrRS_anticodon; 1.
DR CDD; cd00771; ThrRS_core; 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; 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 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 PRINTS; PR01047; TRNASYNTHTHR.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 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..545
FT /note="Threonine--tRNA ligase catalytic subunit"
FT /id="PRO_1000203925"
FT REGION 139..433
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 545 AA; 63231 MW; D9CEA476A1A192B1 CRC64;
MESYKPVWLK GAVILAINLI DKGYKPVAVG LGERDFYIDV KSDTSITLDE VKKAINENVL
ANVSIENNQI VYKGNKVSII EDKVSISTNL NPKYFEILNI STHHPNPNEQ YVRIRGVAFE
TEEQLKDYLS WLEKAEETDH RLIGEKLDLF SFHEEAGSGL VLFHPKGQTI RNELIAFMRE
INDSMGYQEV YTSHVFKTDI WKISGHYTLY RDKLIVFNME GDEYGVKPMN CPAHILIYKS
KPRTYRDLPI RFSEFGHVYR WEKKGELYGL LRVRGFVQDD GHIFLREDQL REEIKMLISK
TVEVWHKFGF KDDDIKPYLS TRPDESIGSD ELWEKATNAL ISALQESGLK FGIKEKEGAF
YGPKIDFEIR DSLGRWWQLS TIQVDFNLPE RFKLEYIDKD GIKKRPVMVH RAIYGSIDRF
VAILLEHFKG KLPTWLSSVQ VRVLPITDEV NEYAEKVLND MRKRRIRAEI DYAGETLSKR
IKNAYDQGVP YILIVGKKEA SEGTVTVRAR GNIEVRNVKF EKFLELLITE IAQRDVEQTT
VKALK
//
