ID   PPT1_SCHPO              Reviewed;         473 AA.
AC   O43049;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Serine/threonine-protein phosphatase T;
DE            Short=PPT;
DE            EC=3.1.3.16;
GN   Name=ppt1; ORFNames=SPBC3F6.01c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Protein phosphatase that specifically binds to and
CC       dephosphorylates the molecular chaperone Hsp90. Dephosphorylation
CC       positively regulates the Hsp90 chaperone machinery (By similarity).
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The TPR repeats mediate protein-protein interactions with
CC       substrate proteins, but also autoinhibit PPT phosphatase activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CU329671; CAA17690.2; -; Genomic_DNA.
DR   PIR; T40391; T40391.
DR   RefSeq; NP_596740.1; NM_001022666.2.
DR   AlphaFoldDB; O43049; -.
DR   SMR; O43049; -.
DR   BioGRID; 277519; 27.
DR   STRING; 284812.O43049; -.
DR   MaxQB; O43049; -.
DR   PaxDb; 4896-SPBC3F6-01c-1; -.
DR   EnsemblFungi; SPBC3F6.01c.1; SPBC3F6.01c.1:pep; SPBC3F6.01c.
DR   GeneID; 2541004; -.
DR   KEGG; spo:SPBC3F6.01c; -.
DR   PomBase; SPBC3F6.01c; -.
DR   VEuPathDB; FungiDB:SPBC3F6.01c; -.
DR   eggNOG; KOG0376; Eukaryota.
DR   HOGENOM; CLU_004962_5_2_1; -.
DR   InParanoid; O43049; -.
DR   OMA; NHFFMSR; -.
DR   PhylomeDB; O43049; -.
DR   PRO; PR:O43049; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; ISS:PomBase.
DR   CDD; cd07417; MPP_PP5_C; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041753; PP5_C.
DR   InterPro; IPR013235; PPP_dom.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF08321; PPP5; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   PIRSF; PIRSF033096; PPPtase_5; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   TPR repeat.
FT   CHAIN           1..473
FT                   /note="Serine/threonine-protein phosphatase T"
FT                   /id="PRO_0000363378"
FT   REPEAT          5..38
FT                   /note="TPR 1"
FT   REPEAT          40..72
FT                   /note="TPR 2"
FT   REPEAT          73..106
FT                   /note="TPR 3"
FT   REGION          159..472
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        279
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   473 AA;  53291 MW;  752AB4B13E1702FC CRC64;
     MAKEALELKN EANKFLKEGH IVQAIDLYTK AIELDSTNAI LYSNRSLAHL KSEDYGLAIN
     DASKAIECDP EYAKAYFRRA TAHIAIFQPK EAVGDFRKAL ALAPSDPAAR KKLRECEQLV
     KRIRFQEAIH NTEPPSPLAN INIEDMDIPS DYDGVILEKQ ITKEFVEDMK ERFCQGKKLP
     LKFAYSILRD LKELLEKTPS LIDIPVKGDE TLVICGDTHG QYFDLLNIFK LHGPPSPTNK
     YLFNGDFVDR GSWSTEVAFT LYAYKLLYPD AVFINRGNHE TDDMNKVYGF EGECRSKYNE
     RTFNIFSETF SLLPLGSLIS DSYLVVHGGL FSDDNVTLDQ LRNIDRFSKK QPGQSGLMME
     MLWTDPQPAP GRGPSKRGVG LQFGPDVSKR FCEANGLKAV IRSHEVRDQG YEVEHDGYCI
     TVFSAPNYCD STGNLGAVIK VKEDMELDFH QFEAVPHPNI RPMAYANGLL SGM
//