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Database: UniProt
Entry: G8ZWJ6_TORDC
LinkDB: G8ZWJ6_TORDC
Original site: G8ZWJ6_TORDC 
ID   G8ZWJ6_TORDC            Unreviewed;       559 AA.
AC   G8ZWJ6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   26-FEB-2020, entry version 44.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
GN   Name=TDEL0F01790 {ECO:0000313|EMBL:CCE92990.1};
GN   ORFNames=TDEL_0F01790 {ECO:0000313|EMBL:CCE92990.1};
OS   Torulaspora delbrueckii (strain ATCC 10662 / CBS 1146 / NBRC 0425 / NCYC
OS   2629 / NRRL Y-866) (Yeast) (Candida colliculosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Torulaspora.
OX   NCBI_TaxID=1076872 {ECO:0000313|Proteomes:UP000005627};
RN   [1] {ECO:0000313|EMBL:CCE92990.1, ECO:0000313|Proteomes:UP000005627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10662 / CBS 1146 / NBRC 0425 / NCYC 2629 / NRRL Y-866
RC   {ECO:0000313|Proteomes:UP000005627};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(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, ChEBI:CHEBI:43474,
CC         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-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000909,
CC         ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01116780};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000909};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
CC       {ECO:0000256|PIRNR:PIRNR000909}.
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DR   EMBL; HE616747; CCE92990.1; -; Genomic_DNA.
DR   RefSeq; XP_003682201.1; XM_003682153.1.
DR   STRING; 4950.XP_003682201.1; -.
DR   EnsemblFungi; CCE92990; CCE92990; TDEL_0F01790.
DR   GeneID; 11501450; -.
DR   KEGG; tdl:TDEL_0F01790; -.
DR   HOGENOM; CLU_004962_4_1_1; -.
DR   InParanoid; G8ZWJ6; -.
DR   KO; K06269; -.
DR   Proteomes; UP000005627; Chromosome 6.
DR   GO; GO:0048037; F:cofactor binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004724; F:magnesium-dependent protein serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0090029; P:negative regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; 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; IPR011159; PPPtase_PPZ/Ppq1.
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   PIRSF; PIRSF000909; PPPtase_PPZ; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273,
KW   ECO:0000256|SAAS:SAAS01017252};
KW   Manganese {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|SAAS:SAAS01017251};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|SAAS:SAAS01017255};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|SAAS:SAAS01017274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005627}.
FT   DOMAIN          357..362
FT                   /note="SER_THR_PHOSPHATASE"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..72
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..110
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  62236 MW;  F1FD62CDD1B1DB20 CRC64;
     MGNSPSKSNN TNFAVPNSST SQQLTTPSDD LNANEPNDPD DSRLLPTISN NDHSTTKNID
     ITAKTTGSAA GKLKSGKNLK RYSPPVTASA DSDLTMVHQT PPSMRKGRKS SFTFDVDIST
     AKAFASDQAN GHSGSDSSYS SQDSSGSSSN TLFSPSPSTT TTSTCANNIT SSFNDSVSNN
     FAYLKPTARS PQGNLRKQIV HKGVENNSLV KSGTSIPNYR DLEKRVFLKR HPHDTTSNDG
     LDIDDAIEKL LKIGETRYYK SRDFPFNSWE VQLICYHARE IFMSQPSLLR LQAPIKVVGD
     IHGQFTDLLR ILKLSGVPAE TNYLFLGDYV DRGKQSLETI LLLFCYKIKY RDNFFMLRGN
     HESANVTKMY GFFDECKRRT SSKTWKMFID VFNTLPFAAI IQDRIFCVHG GISPELKSLK
     QIENIVRPTD IPDEGLVTDI LWSDPDSQVS DWSLNDRGVS YTFGKKNVID FCSSFNFDLI
     IRGHMVVEDG YEFFAKKKFV TVFSAPNYCG EFNNWGAVMS VTTGLMCSFE LLKPHAAEKS
     NQKKTISTNV KTKPKSTKK
//
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