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Database: UniProt
Entry: G8BKA4_CANPC
LinkDB: G8BKA4_CANPC
Original site: G8BKA4_CANPC 
ID   G8BKA4_CANPC            Unreviewed;       342 AA.
AC   G8BKA4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, 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   Name=GLC7 {ECO:0000313|CGD:CAL0000148265};
GN   OrderedLocusNames=CPAR2_701810 {ECO:0000313|CGD:CAL0000148265,
GN   ECO:0000313|EMBL:CCE45169.1};
OS   Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS   parapsilosis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=578454 {ECO:0000313|Proteomes:UP000005221};
RN   [1] {ECO:0000313|Proteomes:UP000005221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L.,
RA   Agrafioti I., Arnaud M.B., Bates S., Brown A.J., Brunke S.,
RA   Costanzo M.C., Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L.,
RA   Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R.,
RA   Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C.,
RA   Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.,
RA   Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.,
RA   Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M.,
RA   Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0000313|Proteomes:UP000005221}
RP   GENOME REANNOTATION.
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA   Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G.,
RA   Corton N.J., Berriman M., Butler G.;
RT   "Using RNA-seq to determine the transcriptional landscape and the
RT   hypoxic response of the pathogenic yeast Candida parapsilosis.";
RL   BMC Genomics 12:628-628(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; HE605209; CCE45169.1; -; Genomic_DNA.
DR   STRING; 5480.G8BKA4; -.
DR   EnsemblFungi; CCE45169; CCE45169; CPAR2_701810.
DR   CGD; CAL0000148265; GLC7.
DR   Proteomes; UP000005221; Chromosome 7.
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; 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:UP000005221};
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:UP000005221}.
FT   DOMAIN      123    128       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION      302    342       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   342 AA;  38548 MW;  69CA05646C7169E5 CRC64;
     MSTADHQEAD IDSIVDRLLE VRGSRPGKQV TLAEHEIRYL CTKAREIFIQ QPILLELEAP
     IKICGDIHGQ YYDLLRLFEY GGFPPEANYL FLGDYVDRGK QSLETICLLL AYKIKYPENF
     FILRGNHECA SINRIYGFYD ECKRRYNIKL WKTFTDCFNC LPIAAIIDEK IFTMHGGLSP
     DLNSMEQIRR VMRPTDIPDV GLLCDLLWSD PDKDITGWSE NDRGVSFTFG PDVVSRFLQK
     HDMDLICRAH QVVEDGYEFF SKRQLVTLFS APNYCGEFDN AGAMMSVDES LLCSFQILKP
     ADKKPRYPSS AGSSIGGGAG GAGGAGGNRP NPNTKKPKKP TK
//
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