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Database: UniProt
Entry: Q978W0
LinkDB: Q978W0
Original site: Q978W0 
ID   SYT_THEVO               Reviewed;         660 AA.
AC   Q978W0;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=TV1305;
GN   ORFNames=TVG1345067;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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).
CC       {ECO:0000255|HAMAP-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; BA000011; BAB60447.1; -; Genomic_DNA.
DR   RefSeq; WP_010917540.1; NC_002689.2.
DR   AlphaFoldDB; Q978W0; -.
DR   SMR; Q978W0; -.
DR   STRING; 273116.gene:9382112; -.
DR   PaxDb; 273116-14325544; -.
DR   GeneID; 1441422; -.
DR   KEGG; tvo:TVG1345067; -.
DR   eggNOG; arCOG00401; Archaea.
DR   HOGENOM; CLU_008554_0_1_2; -.
DR   OrthoDB; 372136at2157; -.
DR   PhylomeDB; Q978W0; -.
DR   Proteomes; UP000001017; 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; 3.30.54.20; -; 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; IPR004095; TGS.
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   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; 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..660
FT                   /note="Threonine--tRNA ligase"
FT                   /id="PRO_0000101116"
FT   DOMAIN          1..49
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   REGION          225..554
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         531
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ   SEQUENCE   660 AA;  75603 MW;  070FE6E1F4DE2A56 CRC64;
     MPINEIRVQK GQRYRDAIND KKVIAVKKGD KFLDLDEIAG EDEAVQPVYL DSEDGLYILR
     HSAAHLLANA VTNLFPEALP NTGPVVENGF YYDFDMKPIT EEDLSKIEEE MKRIVKENVP
     IRRMIYSKDE LLKIFSKNPY KIRIINENVE GKSSVYQQGN FVDLCLGPHV PSTGYIKAFK
     LLSIASAVYK YDESKNLVRI YGTAFPDEKS LRRYLENLEE AKKRDHRKII AEMDLAVFNS
     EWAPGFPMYT PNGQIIRKEL IKYMDYVNGK NGWTDVWTPH VFKDTIWKQS GHYAKYKPNM
     YLFVLPDGDS YGIKPMNCPG HIAIFARRKY SYRDLPVKYS EPGTVYRYEK SGEVGGLTRP
     RAFTQDDGHE FIRMDQIVGE IKTLLGMVRE TFTTVFGNIE MAFDLSVIDK EHPENYLLSY
     VCKDCGNRVE GLRGTDIECP VCHSHNMDPD FSTWDNATEQ LRQAMDSMGI TYKEYPGEAA
     FYGPKIDVHV KDALGRMWQL STIQVDFFMP INFGLTYTNS EGKEERVVII HRAIYGSYER
     FMAILLEHFA GKLPTWLTPI QTYVIPVGTA NAEYARKVNK SLLDAGIRSV VDDGPDTVSK
     KIKMIHDQRP SYIVVVGAKE EQDNTVTVRN RAGKSKTYGM NEFLEIIKNE IEKRSVGQAF
//
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