ID   PPS1_YEAST              Reviewed;         807 AA.
AC   P38148; D6VQS2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Dual specificity protein phosphatase PPS1;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
GN   Name=PPS1; OrderedLocusNames=YBR276C; ORFNames=YBR2013;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091861; DOI=10.1002/yea.320100007;
RA   Holmstroem K., Brandt T., Kallesoe T.;
RT   "The sequence of a 32,420 bp segment located on the right arm of chromosome
RT   II from Saccharomyces cerevisiae.";
RL   Yeast 10:S47-S62(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
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   FUNCTION.
RX   PubMed=9083070; DOI=10.1074/jbc.272.14.9332;
RA   Ernsting B.R., Dixon J.E.;
RT   "The PPS1 gene of Saccharomyces cerevisiae codes for a dual specificity
RT   protein phosphatase with a role in the DNA synthesis phase of the cell
RT   cycle.";
RL   J. Biol. Chem. 272:9332-9343(1997).
CC   -!- FUNCTION: Protein phosphatase with specificity for serine, threonine,
CC       and tyrosine residues; has a role in the DNA synthesis phase of the
CC       cell cycle. {ECO:0000269|PubMed:9083070}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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DR   EMBL; X76053; CAA53639.1; -; Genomic_DNA.
DR   EMBL; Z36145; CAA85239.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07392.1; -; Genomic_DNA.
DR   PIR; S44538; S44538.
DR   RefSeq; NP_009835.3; NM_001178624.3.
DR   AlphaFoldDB; P38148; -.
DR   SMR; P38148; -.
DR   BioGRID; 32971; 39.
DR   DIP; DIP-6546N; -.
DR   IntAct; P38148; 3.
DR   MINT; P38148; -.
DR   STRING; 4932.YBR276C; -.
DR   iPTMnet; P38148; -.
DR   MaxQB; P38148; -.
DR   PaxDb; 4932-YBR276C; -.
DR   PeptideAtlas; P38148; -.
DR   EnsemblFungi; YBR276C_mRNA; YBR276C; YBR276C.
DR   GeneID; 852579; -.
DR   KEGG; sce:YBR276C; -.
DR   AGR; SGD:S000000480; -.
DR   SGD; S000000480; PPS1.
DR   VEuPathDB; FungiDB:YBR276C; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   HOGENOM; CLU_365223_0_0_1; -.
DR   InParanoid; P38148; -.
DR   OMA; TVCIAEC; -.
DR   OrthoDB; 2045814at2759; -.
DR   BioCyc; YEAST:G3O-29197-MONOMER; -.
DR   BioGRID-ORCS; 852579; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38148; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38148; Protein.
DR   GO; GO:0005634; C:nucleus; IEA:GOC.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:SGD.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0033260; P:nuclear DNA replication; IMP:SGD.
DR   CDD; cd14516; DSP_fungal_PPS1; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR047949; PPS1_DSP.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR47550; DUAL SPECIFICITY PROTEIN PHOSPHATASE PPS1; 1.
DR   PANTHER; PTHR47550:SF1; DUAL SPECIFICITY PROTEIN PHOSPHATASE PPS1; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..807
FT                   /note="Dual specificity protein phosphatase PPS1"
FT                   /id="PRO_0000094921"
FT   DOMAIN          585..783
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          593..807
FT                   /note="Catalytic"
FT   ACT_SITE        725
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   807 AA;  91685 MW;  17840CF7256EF785 CRC64;
     MVLEVPSITP GELHDLMRLH QDAEWPECKK MFPWAHDISF GQPPDFPHSL AIVKSQSDAN
     NSALLRNSLE VNDIFQSWKV RTSFHREGDT CETGNDSNGF QYPNNTKELL NLLKFQIRQL
     ELQVDDVALE NAATYCHNHS ILPFLKVDPR GLSLELKRYS RNKVGSNTTL KRSGQDVWGR
     RGLFRRFDLQ CAKMIEMVDN IVIYCSRTGG STDMQTESAP ACSHEGNCPN CTTLALLLQI
     CLMFVQKGYV GSGGSLYKTN LFICTYQNFN TDIPQTLIGT PLLDNEFFKN NTPLNLCSSP
     SEIVCFNNVD KNMVLCEKLE LNKLTSATRL EETGLICGNT TDWHNYQIIK KNNISLTHRF
     EENTSIVNLK SLNYDTDNPT TSISQLYNIP NTKEVWKLII KCTSNSQMPS LTKIRTYLDL
     LLDDDASKSQ EHLHLTFPAS GSIGLGNLNI QSVEILLNVC YLIFQVSQVQ ELLTFMYCED
     GYTETSLLLT AYIIFHFNIP LQDALLRIHP RPFFLFPSDL QILGHLQPVL REFSPQNGSN
     LKLYANALKF RDKSFQLHIS SELFSSIFFM KIPLESNFVN LKGPLPSRIL RHLYLGSLDH
     AQNPALLKSL GITHIVSVGE VVSWTLNKDK IAHPVRPHRA ITMTNTNEVA GNTTCNKSRN
     RADTVVSDKQ ENGSNVVISE NSGFQICQIE NLDDNGKDPL FHQIDKVLDF ISNSEATGGK
     VLVHCMVGVS RSATVCIAEC MRYLQCDLAS AYLFVRVRRL NVIIQPNLFF VYELFKWWKK
     HYNREKDKTM DWHIICRGIA EVNMKYT
//