PPS1_YEAST
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 03-AUG-2022, entry version 171.
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; 37.
DR DIP; DIP-6546N; -.
DR IntAct; P38148; 3.
DR MINT; P38148; -.
DR STRING; 4932.YBR276C; -.
DR iPTMnet; P38148; -.
DR MaxQB; P38148; -.
DR PaxDb; P38148; -.
DR PRIDE; P38148; -.
DR EnsemblFungi; YBR276C_mRNA; YBR276C; YBR276C.
DR GeneID; 852579; -.
DR KEGG; sce:YBR276C; -.
DR SGD; S000000480; PPS1.
DR VEuPathDB; FungiDB:YBR276C; -.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_365223_0_0_1; -.
DR InParanoid; P38148; -.
DR OMA; LVHCMVG; -.
DR BioCyc; YEAST:G3O-29197-MON; -.
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:0033260; P:nuclear DNA replication; IMP:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
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 Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 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
