PPT1_SCHPO
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 03-AUG-2022, entry version 157.
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; 4896.SPBC3F6.01c.1; -.
DR MaxQB; O43049; -.
DR PaxDb; O43049; -.
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 Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR PRO; PR:O43049; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
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; ISO:PomBase.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; ISS:PomBase.
DR CDD; cd07417; MPP_PP5_C; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.60.21.10; -; 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; IPR011236; Ser/Thr_PPase_5.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45668:SF5; PTHR45668:SF5; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08321; PPP5; 1.
DR Pfam; PF13181; TPR_8; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF56300; SSF56300; 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
