SYTC_YEAST
ID SYTC_YEAST Reviewed; 734 AA.
AC P04801; D6VVK6;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 198.
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; OrderedLocusNames=YIL078W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2995918; DOI=10.1093/nar/13.17.6171;
RA Pape L.K., Tzagoloff A.;
RT "Cloning and characterization of the gene for the yeast cytoplasmic
RT threonyl-tRNA synthetase.";
RL Nucleic Acids Res. 13:6171-6183(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; THR-381; SER-453;
RP SER-457; THR-460 AND SER-605, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-289; THR-297;
RP SER-453 AND SER-457, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 -!- MISCELLANEOUS: Present with 42600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; Z37997; CAA86092.1; -; Genomic_DNA.
DR EMBL; X02906; CAA26666.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08472.1; -; Genomic_DNA.
DR PIR; S48366; YSBYTC.
DR RefSeq; NP_116578.3; NM_001179428.3.
DR AlphaFoldDB; P04801; -.
DR SMR; P04801; -.
DR BioGRID; 34914; 302.
DR DIP; DIP-5307N; -.
DR IntAct; P04801; 17.
DR MINT; P04801; -.
DR STRING; 4932.YIL078W; -.
DR iPTMnet; P04801; -.
DR MaxQB; P04801; -.
DR PaxDb; P04801; -.
DR PRIDE; P04801; -.
DR EnsemblFungi; YIL078W_mRNA; YIL078W; YIL078W.
DR GeneID; 854732; -.
DR KEGG; sce:YIL078W; -.
DR SGD; S000001340; THS1.
DR VEuPathDB; FungiDB:YIL078W; -.
DR eggNOG; KOG1637; Eukaryota.
DR GeneTree; ENSGT00940000170409; -.
DR HOGENOM; CLU_008554_0_1_1; -.
DR InParanoid; P04801; -.
DR OMA; FYYDFAY; -.
DR BioCyc; YEAST:G3O-31343-MON; -.
DR PRO; PR:P04801; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P04801; protein.
DR GO; GO:0005737; C:cytoplasm; IMP:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IDA:SGD.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IDA:SGD.
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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..734
FT /note="Threonine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000101125"
FT DOMAIN 69..135
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 297
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 381
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 460
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 9
FT /note="T -> A (in Ref. 1; CAA26666)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="K -> N (in Ref. 1; CAA26666)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="K -> E (in Ref. 1; CAA26666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 734 AA; 84520 MW; EA328F8EC08417C3 CRC64;
MSASEAGVTE QVKKLSVKDS SNDAVKPNKK ENKKSKQQSL YLDPEPTFIE ERIEMFDRLQ
KEYNDKVASM PRVPLKIVLK DGAVKEATSW ETTPMDIAKG ISKSLADRLC ISKVNGQLWD
LDRPFEGEAN EEIKLELLDF ESDEGKKVFW HSSAHVLGES CECHLGAHIC LGPPTDDGFF
YEMAVRDSMK DISESPERTV SQADFPGLEG VAKNVIKQKQ KFERLVMSKE DLLKMFHYSK
YKTYLVQTKV PDGGATTVYR CGKLIDLCVG PHIPHTGRIK AFKLLKNSSC YFLGDATNDS
LQRVYGISFP DKKLMDAHLK FLAEASMRDH RKIGKEQELF LFNEMSPGSC FWLPHGTRIY
NTLVDLLRTE YRKRGYEEVI TPNMYNSKLW ETSGHWANYK ENMFTFEVEK ETFGLKPMNC
PGHCLMFKSR ERSYRELPWR VADFGVIHRN EFSGALSGLT RVRRFQQDDA HIFCTHDQIE
SEIENIFNFL QYIYGVFGFE FKMELSTRPE KYVGKIETWD AAESKLESAL KKWGGNWEIN
AGDGAFYGPK IDIMISDALR RWHQCATIQL DFQLPNRFEL EFKSKDQDSE SYERPVMIHR
AILGSVERMT AILTEHFAGK WPFWLSPRQV LVVPVGVKYQ GYAEDVRNKL HDAGFYADVD
LTGNTLQKKV RNGQMLKYNF IFIVGEQEMN EKSVNIRNRD VMEQQGKNAT VSVEEVLKQL
RNLKDEKRGD NVLA
