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Serine/threonine-protein phosphatase PPQ (EC 3.1.3.16)

 PPQ1_YEAST              Reviewed;         549 AA.
P32945; D6W3I9;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
18-JUL-2018, entry version 166.
RecName: Full=Serine/threonine-protein phosphatase PPQ;
EC=3.1.3.16;
Name=PPQ1; Synonyms=SAL6; OrderedLocusNames=YPL179W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8269960; DOI=10.1111/j.1432-1033.1993.tb18423.x;
Chen M.X., Chen Y.H., Cohen P.T.W.;
"PPQ, a novel protein phosphatase containing a Ser + Asn-rich amino-
terminal domain, is involved in the regulation of protein synthesis.";
Eur. J. Biochem. 218:689-699(1993).
[2]
ERRATUM.
Chen M.X., Chen Y.H., Cohen P.T.W.;
Eur. J. Biochem. 221:1133-1133(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=S288c / GRF88;
PubMed=7851758;
Vincent A., Newnam G.P., Liebman S.W.;
"The yeast translational allosuppressor, SAL6: a new member of the
PP1-like phosphatase family with a long serine-rich N-terminal
extension.";
Genetics 138:597-607(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-328.
PubMed=1321058; DOI=10.1016/0014-5793(92)80836-6;
Chen M.X., Chen Y.H., Cohen P.T.W.;
"Polymerase chain reactions using Saccharomyces, Drosophila and human
DNA predict a large family of protein serine/threonine phosphatases.";
FEBS Lett. 306:54-58(1992).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Phosphatase involved in the regulation of protein
synthesis. Affects translational accuracy.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- INTERACTION:
P36047:SDS22; NbExp=3; IntAct=EBI-13787, EBI-16783;
-!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
{ECO:0000305}.
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EMBL; X75485; CAA53214.1; -; Genomic_DNA.
EMBL; U00795; AAC48924.1; -; Genomic_DNA.
EMBL; Z73535; CAA97886.1; -; Genomic_DNA.
EMBL; S39958; AAB22461.1; -; Genomic_DNA.
EMBL; BK006949; DAA11255.1; -; Genomic_DNA.
PIR; S39533; S39533.
RefSeq; NP_015146.1; NM_001183993.1.
ProteinModelPortal; P32945; -.
SMR; P32945; -.
BioGrid; 36003; 166.
DIP; DIP-5504N; -.
IntAct; P32945; 7.
MINT; P32945; -.
STRING; 4932.YPL179W; -.
iPTMnet; P32945; -.
MaxQB; P32945; -.
PaxDb; P32945; -.
PRIDE; P32945; -.
EnsemblFungi; YPL179W; YPL179W; YPL179W.
GeneID; 855923; -.
KEGG; sce:YPL179W; -.
EuPathDB; FungiDB:YPL179W; -.
SGD; S000006100; PPQ1.
GeneTree; ENSGT00920000149824; -.
HOGENOM; HOG000172697; -.
InParanoid; P32945; -.
KO; K06269; -.
OrthoDB; EOG092C37EX; -.
BioCyc; YEAST:G3O-34074-MONOMER; -.
PRO; PR:P32945; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0048037; F:cofactor binding; IEA:InterPro.
GO; GO:0004724; F:magnesium-dependent protein serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:SGD.
GO; GO:0090029; P:negative regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:SGD.
GO; GO:0006470; P:protein dephosphorylation; IDA:SGD.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR011159; PPPtase_PPZ/Ppq1.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
InterPro; IPR031675; STPPase_N.
Pfam; PF00149; Metallophos; 1.
Pfam; PF16891; STPPase_N; 1.
PIRSF; PIRSF000909; PPPtase_PPZ; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
Complete proteome; Hydrolase; Manganese; Metal-binding;
Protein phosphatase; Reference proteome.
CHAIN 1 549 Serine/threonine-protein phosphatase PPQ.
/FTId=PRO_0000058893.
COMPBIAS 113 219 Ser-rich.
ACT_SITE 362 362 Proton donor. {ECO:0000250}.
METAL 301 301 Manganese 1. {ECO:0000250}.
METAL 303 303 Manganese 1. {ECO:0000250}.
METAL 329 329 Manganese 1. {ECO:0000250}.
METAL 329 329 Manganese 2. {ECO:0000250}.
METAL 361 361 Manganese 2. {ECO:0000250}.
METAL 410 410 Manganese 2. {ECO:0000250}.
METAL 485 485 Manganese 2. {ECO:0000250}.
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


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