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Database: UniProt
Entry: S9XJZ4_SCHCR
LinkDB: S9XJZ4_SCHCR
Original site: S9XJZ4_SCHCR 
ID   S9XJZ4_SCHCR            Unreviewed;       328 AA.
AC   S9XJZ4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   13-NOV-2019, entry version 41.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=SPOG_02756 {ECO:0000313|EMBL:EPY54021.1};
OS   Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS
OS   11777 / NBRC 106824 / NRRL Y48691) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY54021.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY54021.1, ECO:0000313|Proteomes:UP000015464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC   {ECO:0000313|Proteomes:UP000015464};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K.,
RA   Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.,
RA   Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L.,
RA   FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D.,
RA   Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M.,
RA   Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M.,
RA   Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D.,
RA   Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H.,
RA   Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
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,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|SAAS:SAAS01116782};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
CC         [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
CC         COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
CC         EC=3.1.3.16; Evidence={ECO:0000256|RuleBase:RU004273,
CC         ECO:0000256|SAAS:SAAS01116780};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017257}.
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DR   EMBL; KE546988; EPY54021.1; -; Genomic_DNA.
DR   RefSeq; XP_013020872.1; XM_013165418.1.
DR   STRING; 866546.EPY54021; -.
DR   EnsemblFungi; EPY54021; EPY54021; SPOG_02756.
DR   GeneID; 25037078; -.
DR   OMA; EEHEIRY; -.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:1902716; C:cell cortex of growing cell tip; IEA:EnsemblFungi.
DR   GO; GO:0032153; C:cell division site; IEA:EnsemblFungi.
DR   GO; GO:0061638; C:CENP-A containing chromatin; IEA:EnsemblFungi.
DR   GO; GO:1990567; C:DPS complex; IEA:EnsemblFungi.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:EnsemblFungi.
DR   GO; GO:0035839; C:non-growing cell tip; IEA:EnsemblFungi.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:EnsemblFungi.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:EnsemblFungi.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IEA:EnsemblFungi.
DR   GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; IEA:EnsemblFungi.
DR   GO; GO:0032091; P:negative regulation of protein binding; IEA:EnsemblFungi.
DR   GO; GO:1904595; P:positive regulation of termination of RNA polymerase II transcription; IEA:EnsemblFungi.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000015464};
KW   Hydrolase {ECO:0000256|RuleBase:RU004273,
KW   ECO:0000256|SAAS:SAAS01017252};
KW   Manganese {ECO:0000256|SAAS:SAAS01017251};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01017255};
KW   Protein phosphatase {ECO:0000256|SAAS:SAAS01017274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015464}.
FT   DOMAIN      120    125       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
SQ   SEQUENCE   328 AA;  37689 MW;  263ECABF5FA35A09 CRC64;
     MSNQDVDLDS IIDRLLEVRG NRPGKQVQLA ENEIRFLCNK AREIFISQPI LLELEAPLKI
     CGDIHGQYYD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL EVICLLLAYK IKYPENFFIL
     RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPI AAIIDEKIFT MHGGLSPDLN
     SMDQIQRIMR PTDVPDTGLL CDLLWSDPDK DLTGWGDNDR GVSFTFGPDV VSRFLHKHDM
     DLVCRAHQVV EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAEK
     KQRYGGYQGM GQNWHINTPR KNKAGNSK
//
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