ID SYTC_METS5 Reviewed; 541 AA.
AC A4YH38;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=Msed_1585;
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=18083856; DOI=10.1128/aem.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP95740.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YH38; -.
DR SMR; A4YH38; -.
DR STRING; 399549.Msed_1585; -.
DR KEGG; mse:Msed_1585; -.
DR eggNOG; arCOG00401; Archaea.
DR HOGENOM; CLU_008554_2_2_2; -.
DR Proteomes; UP000000242; 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; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..541
FT /note="Threonine--tRNA ligase catalytic subunit"
FT /id="PRO_1000071677"
FT REGION 135..429
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 541 AA; 62755 MW; EF92F08E2D389842 CRC64;
MESYRGLWLK GAIVMALNMY EAGLTPVEIG LGERDFYIDV QSDSALSLQE SEKFAQWKDH
KYEIKDGKVT YNGKQILLQG DVTPSGEPRY FKVLNISVHH PSANVQLVRI RGIAFETKEQ
MDDYLQWLEK ASETDHRIIG ERMDLFSFHE ESGPGLVLFH PKGQLIRNEM INYMREINAS
MGYQEVYTSH VFRTVLWKIS GHYDTYRDKM LIFQKDDDEL GIKPMNCPAH ILIYKSRVRS
YRDLPIRFSE FGNVYRWEKK GELYGLLRTR GFTQDDGHIF LREDQLKDEV KNLVRKTLDV
LGKFGFKGED VRINLSTRPD ESIGSDEQWE KATKALLDVL KELNVPYVVK EKEGAFYGPK
IDFDIRDSLN RWWQLSTIQV DFNLPERFKL EYVDEDGSKK RPVMVHRAIY GSLDRMIAIL
LEHFRGKLPT WLSPVQVRVL PISEDNLDYA KRVMDVLVQR GIRTEIDPSG ETLSKRIKRG
YDDGVPYLVI VGRKEASEEK VTIRARGNVE IKGVPLSRFV DELSLEIGNR DAENTLIKRI
G
//
