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
//
