ID   PPQ1_YEAST              Reviewed;         549 AA.
AC   P32945; D6W3I9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 201.
DE   RecName: Full=Serine/threonine-protein phosphatase PPQ;
DE            EC=3.1.3.16;
GN   Name=PPQ1; Synonyms=SAL6; OrderedLocusNames=YPL179W;
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=8269960; DOI=10.1111/j.1432-1033.1993.tb18423.x;
RA   Chen M.X., Chen Y.H., Cohen P.T.W.;
RT   "PPQ, a novel protein phosphatase containing a Ser + Asn-rich amino-
RT   terminal domain, is involved in the regulation of protein synthesis.";
RL   Eur. J. Biochem. 218:689-699(1993).
RN   [2]
RP   ERRATUM OF PUBMED:8269960.
RA   Chen M.X., Chen Y.H., Cohen P.T.W.;
RL   Eur. J. Biochem. 221:1133-1133(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S288c / GRF88;
RX   PubMed=7851758; DOI=10.1093/genetics/138.3.597;
RA   Vincent A., Newnam G.P., Liebman S.W.;
RT   "The yeast translational allosuppressor, SAL6: a new member of the PP1-like
RT   phosphatase family with a long serine-rich N-terminal extension.";
RL   Genetics 138:597-607(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875; DOI=10.1038/387s103;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-328.
RX   PubMed=1321058; DOI=10.1016/0014-5793(92)80836-6;
RA   Chen M.X., Chen Y.H., Cohen P.T.W.;
RT   "Polymerase chain reactions using Saccharomyces, Drosophila and human DNA
RT   predict a large family of protein serine/threonine phosphatases.";
RL   FEBS Lett. 306:54-58(1992).
RN   [7]
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   -!- FUNCTION: Phosphatase involved in the regulation of protein synthesis.
CC       Affects translational accuracy.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = 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=O-phospho-L-threonyl-[protein] + H2O = 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- INTERACTION:
CC       P32945; P36047: SDS22; NbExp=4; IntAct=EBI-13787, EBI-16783;
CC   -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X75485; CAA53214.1; -; Genomic_DNA.
DR   EMBL; U00795; AAC48924.1; -; Genomic_DNA.
DR   EMBL; Z73535; CAA97886.1; -; Genomic_DNA.
DR   EMBL; S39958; AAB22461.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11255.1; -; Genomic_DNA.
DR   PIR; S39533; S39533.
DR   RefSeq; NP_015146.1; NM_001183993.1.
DR   AlphaFoldDB; P32945; -.
DR   SMR; P32945; -.
DR   BioGRID; 36003; 172.
DR   DIP; DIP-5504N; -.
DR   FunCoup; P32945; 228.
DR   IntAct; P32945; 4.
DR   MINT; P32945; -.
DR   STRING; 4932.YPL179W; -.
DR   iPTMnet; P32945; -.
DR   PaxDb; 4932-YPL179W; -.
DR   PeptideAtlas; P32945; -.
DR   EnsemblFungi; YPL179W_mRNA; YPL179W; YPL179W.
DR   GeneID; 855923; -.
DR   KEGG; sce:YPL179W; -.
DR   AGR; SGD:S000006100; -.
DR   SGD; S000006100; PPQ1.
DR   VEuPathDB; FungiDB:YPL179W; -.
DR   eggNOG; KOG0374; Eukaryota.
DR   HOGENOM; CLU_004962_4_1_1; -.
DR   InParanoid; P32945; -.
DR   OMA; EVQLICA; -.
DR   OrthoDB; 1930084at2759; -.
DR   BioCyc; YEAST:G3O-34074-MONOMER; -.
DR   BioGRID-ORCS; 855923; 5 hits in 10 CRISPR screens.
DR   PRO; PR:P32945; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P32945; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:SGD.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
DR   FunFam; 3.60.21.10:FF:000026; Serine/threonine-protein phosphatase; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR050341; PP1_catalytic_subunit.
DR   InterPro; IPR011159; PPPtase_PPZ/Ppq1.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF423; SERINE_THREONINE-PROTEIN PHOSPHATASE PPQ; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PIRSF; PIRSF000909; PPPtase_PPZ; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..549
FT                   /note="Serine/threonine-protein phosphatase PPQ"
FT                   /id="PRO_0000058893"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..13
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..32
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..83
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        362
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         361
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         410
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         485
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   549 AA;  61420 MW;  1E26D05E2865A8C1 CRC64;
     MRRSPSRSNN NFAVPNCSTN SNSSQQQLTT PSDDLNSNEP NDPDDSRSLP TIKKFNNKHS
     INNYNTLASA GKNNNNKRAS NDNLLIPGEN AHKQKIYTKD ENLKSLYLDI DVSVAKALSS
     SATAPKLINT ARTSSTTTAT TSNNILTSPS YRESNYSSPS SYSFSSYYSS ATSASSSTSS
     FLKSSGLSSR VKSPSSSVKA GSFGAPSSPT SGIPNPKSSK KPIFLRRYSH DTSSNEGLDI
     DVAIEKLLQV GESREITKTS KKKNFPFHSW EIQLICYHAR EIFLNQPTLL RLQAPIKVVG
     DVHGQFNDLL RILKLSGVPS DTNYLFLGDY VDRGKNSLET ILLLLCYKIK YKDNFFMLRG
     NHESANVTKM YGFYDECKRR LSSKVWKMFV DVFNTLPLAA IIQDKIFCVH GGISPDLHDM
     KQIEKVARPT DIPESGLVTD LLWSDPDPQV TDWSENDRGV SYTFSKRNVL DFCAKFKFDL
     ILRGHMVVED GYEFFARKKF VTIFSAPNYC GEFHNWGAVM SVTTGMMCSF ELLKPRALKN
     KKKLYKTKV
//