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Database: UniProt
Entry: G8JQ75_ERECY
LinkDB: G8JQ75_ERECY
Original site: G8JQ75_ERECY 
ID   G8JQ75_ERECY            Unreviewed;       312 AA.
AC   G8JQ75;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   13-NOV-2019, entry version 42.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   OrderedLocusNames=Ecym_2341 {ECO:0000313|EMBL:AET38077.1};
OS   Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166
OS   / NRRL Y-17582) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=931890 {ECO:0000313|EMBL:AET38077.1, ECO:0000313|Proteomes:UP000006790};
RN   [1] {ECO:0000313|Proteomes:UP000006790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC   {ECO:0000313|Proteomes:UP000006790};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M.,
RA   Mallet S., Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J.,
RA   Seret M.L., Talla E., Samson G., Jubin C., Poulain J., Vacherie B.,
RA   Barbe V., Pelletier E., Sherman D.J., Westhof E., Weissenbach J.,
RA   Baret P.V., Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps
RT   of genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(2012).
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; CP002498; AET38077.1; -; Genomic_DNA.
DR   RefSeq; XP_003644894.1; XM_003644846.1.
DR   STRING; 45285.XP_003644894.1; -.
DR   EnsemblFungi; AET38077; AET38077; Ecym_2341.
DR   GeneID; 11471846; -.
DR   KEGG; erc:Ecym_2341; -.
DR   eggNOG; KOG0374; Eukaryota.
DR   eggNOG; COG0639; LUCA.
DR   InParanoid; G8JQ75; -.
DR   KO; K06269; -.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000006790; Chromosome 2.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0032153; C:cell division site; IEA:EnsemblFungi.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0000778; C:condensed nuclear chromosome kinetochore; IEA:EnsemblFungi.
DR   GO; GO:0001400; C:mating projection base; IEA:EnsemblFungi.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:EnsemblFungi.
DR   GO; GO:0005816; C:spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR   GO; GO:0006873; P:cellular ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0007059; P:chromosome segregation; IEA:EnsemblFungi.
DR   GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IEA:EnsemblFungi.
DR   GO; GO:0000077; P:DNA damage checkpoint; IEA:EnsemblFungi.
DR   GO; GO:0000076; P:DNA replication checkpoint; IEA:EnsemblFungi.
DR   GO; GO:0016576; P:histone dephosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint; IEA:EnsemblFungi.
DR   GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IEA:EnsemblFungi.
DR   GO; GO:1903501; P:positive regulation of mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR   GO; GO:0035307; P:positive regulation of protein dephosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0034501; P:protein localization to kinetochore; IEA:EnsemblFungi.
DR   GO; GO:0007116; P:regulation of cell budding; IEA:EnsemblFungi.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:EnsemblFungi.
DR   GO; GO:0070873; P:regulation of glycogen metabolic process; IEA:EnsemblFungi.
DR   GO; GO:1901901; P:regulation of protein localization to cell division site involved in cytokinesis; IEA:EnsemblFungi.
DR   GO; GO:0031297; P:replication fork processing; IEA:EnsemblFungi.
DR   GO; GO:0009408; P:response to heat; IEA:EnsemblFungi.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:EnsemblFungi.
DR   GO; GO:0000723; P:telomere maintenance; IEA:EnsemblFungi.
DR   GO; GO:0061587; P:transfer RNA gene-mediated silencing; 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; IPR037981; PPP1CC.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668:SF204; PTHR11668:SF204; 1.
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:UP000006790};
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:UP000006790}.
FT   DOMAIN      120    125       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
SQ   SEQUENCE   312 AA;  35855 MW;  83DD0A82F0E15733 CRC64;
     METPPVDIDN IIDRLLEVRG SKPGQQVDLE EHEIRYLCSK ARSIFIKQPI LLELEAPIKI
     CGDIHGQYYD LLRLFEYGGF PPESNYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFIL
     RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPI AAIIDEKIFC MHGGLSPDLN
     TMEQIRRVMR PTDIPDVGLL CDLLWSDPDK DIVGWSENDR GVSFTFGPDV VSRFLQKQDM
     ELICRAHQVV EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAVK
     PSAGRGKPKK KK
//
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