ID   SYTC_SCHPO              Reviewed;         703 AA.
AC   P87144;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Threonine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.3;
DE   AltName: Full=Threonyl-tRNA synthetase;
DE            Short=ThrRS;
GN   Name=ths1; ORFNames=SPBC25H2.02;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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; CU329671; CAB08788.1; -; Genomic_DNA.
DR   PIR; T39997; T39997.
DR   RefSeq; NP_596364.1; NM_001022285.2.
DR   AlphaFoldDB; P87144; -.
DR   SMR; P87144; -.
DR   BioGRID; 277077; 7.
DR   STRING; 4896.SPBC25H2.02.1; -.
DR   iPTMnet; P87144; -.
DR   MaxQB; P87144; -.
DR   PaxDb; P87144; -.
DR   PRIDE; P87144; -.
DR   EnsemblFungi; SPBC25H2.02.1; SPBC25H2.02.1:pep; SPBC25H2.02.
DR   PomBase; SPBC25H2.02; -.
DR   VEuPathDB; FungiDB:SPBC25H2.02; -.
DR   eggNOG; KOG1637; Eukaryota.
DR   HOGENOM; CLU_008554_0_2_1; -.
DR   InParanoid; P87144; -.
DR   OMA; FYYDFAY; -.
DR   PhylomeDB; P87144; -.
DR   PRO; PR:P87144; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004829; F:threonine-tRNA ligase activity; ISS:PomBase.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR   GO; GO:0006435; P:threonyl-tRNA aminoacylation; ISS:PomBase.
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; PF02824; TGS; 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;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..703
FT                   /note="Threonine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000101124"
FT   DOMAIN          47..109
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
SQ   SEQUENCE   703 AA;  80138 MW;  518F29F100C73553 CRC64;
     MSAAAVKGVQ ASLDNLSLEI PFIQHRLDLF DKLQKEYKES LATKPREEID ITLPDGKVIK
     GTSWETTPIS IAASISKGLA DRVTVAIVNG EPWDLTRPLE ASCTLKLCDF NDPEGKRVFW
     HSSAHILGEA TELSFHCHLC IGPPTDEGFF YEMGIDNGRV ITNDDYSSIE SYAKQAIKQK
     QPFERLVISK EGLLEMFRYN KYKQYIIQTK IPDGASTTVY RCGPLIDLCT GPHVPHTGRI
     KSFAVTKNSS SYFLGDAKND SLQRVYGISF PDNKQMQEYK TFLAEAAKRD HRKIGRDQEL
     FFFNEISPGS CFFLPHGARI YNTLLKYMRY QYSKRGYQEV ITPNMYNVNL WKTSGHWNNY
     SENMFSFDIE KEKYALKPMN CPGHCVMFKS RDRSYRDLPW RVADFGVLHR NEFSGALSGL
     TRVRRFQQDD AHIFCTPDQV RSEIEGCFDF LKEVYGTFGF TFHLELSTRP EEKYLGDLAT
     WDKAEAQLKA ALDASGYKWE LNAGDGAFYG PKIDITVFDA LKRQHQCATI QLDFQLPERF
     QLEFHAPASA EEAKESGNNN KYTRPVMVHR AILGSLERMI AILTEHYAGK WPFWMSPRQV
     CIIPVSAAAY NYADKVHNIL SEADIFVDTD KSDNTLPKKI RNAQLAQYNF IFVVGAEEES
     TNSVNVRNRD DPKKQSKGST VAVEEVVKKL LKLKESKSLI NDL