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Database: UniProt
Entry: A5E0D1_LODEL
LinkDB: A5E0D1_LODEL
Original site: A5E0D1_LODEL 
ID   A5E0D1_LODEL            Unreviewed;       333 AA.
AC   A5E0D1;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   13-NOV-2019, entry version 84.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=LELG_03068 {ECO:0000313|EMBL:EDK44889.1};
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 /
OS   NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Candida/Lodderomyces clade; Lodderomyces.
OX   NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK44889.1, ECO:0000313|Proteomes:UP000001996};
RN   [1] {ECO:0000313|EMBL:EDK44889.1, ECO:0000313|Proteomes:UP000001996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239
RC   {ECO:0000313|Proteomes:UP000001996};
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).
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; CH981527; EDK44889.1; -; Genomic_DNA.
DR   RefSeq; XP_001525140.1; XM_001525090.1.
DR   STRING; 36914.XP_001525140.1; -.
DR   EnsemblFungi; EDK44889; EDK44889; LELG_03068.
DR   GeneID; 5232775; -.
DR   KEGG; lel:LELG_03068; -.
DR   eggNOG; KOG0374; Eukaryota.
DR   eggNOG; COG0639; LUCA.
DR   InParanoid; A5E0D1; -.
DR   KO; K06269; -.
DR   OMA; EEHEIRY; -.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
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:UP000001996};
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:UP000001996}.
FT   DOMAIN      123    128       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION      301    333       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   333 AA;  37984 MW;  227343664FB9E45D CRC64;
     MSTDHQEAAD IDSIVDRLLE VRGSRPGKQV TLQEHEIRYL CTKAREIFIQ QPILLELEAP
     IKICGDIHGQ YYDLLRLFEY GGFPPEANYL FLGDYVDRGK QSLETICLLL AYKIKYPENF
     FILRGNHECA SINRIYGFYD ECKRRYNIKL WKTFTDCFNC LPIAAIIDEK IFCMHGGLSP
     DLNSMEQIRR VMRPTDIPDV GLLCDLLWSD PDKDITGWSE NDRGVSFTFG PDVVSRFLQK
     HDMDLICRAH QVVEDGYEFF SKRQLVTLFS APNYCGEFDN AGAMMSVDES LLCSFQILKP
     ADKKPRYPTG GANVGNRSSG ANTPGRKQKK AGK
//
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