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Database: UniProt
Entry: B2WAU0_PYRTR
LinkDB: B2WAU0_PYRTR
Original site: B2WAU0_PYRTR 
ID   B2WAU0_PYRTR            Unreviewed;       321 AA.
AC   B2WAU0;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   26-FEB-2020, entry version 66.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=PTRG_07403 {ECO:0000313|EMBL:EDU50322.1};
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU50322.1, ECO:0000313|Proteomes:UP000001471};
RN   [1] {ECO:0000313|Proteomes:UP000001471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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|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; DS231621; EDU50322.1; -; Genomic_DNA.
DR   RefSeq; XP_001937735.1; XM_001937700.1.
DR   STRING; 45151.EDU50322; -.
DR   EnsemblFungi; EDU50322; EDU50322; PTRG_07403.
DR   GeneID; 6345676; -.
DR   eggNOG; ENOG410IN85; Eukaryota.
DR   eggNOG; ENOG410XPVF; LUCA.
DR   HOGENOM; CLU_004962_0_0_1; -.
DR   InParanoid; B2WAU0; -.
DR   OMA; EEHEIRY; -.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:InterPro.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR037979; PPP1CA.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668:SF377; PTHR11668:SF377; 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   Hydrolase {ECO:0000256|RuleBase:RU004273, 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:UP000001471}.
FT   DOMAIN          120..125
FT                   /note="SER_THR_PHOSPHATASE"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
SQ   SEQUENCE   321 AA;  36868 MW;  437031F902AB036E CRC64;
     MAENEVDLDS IIDRLLEVRG SRPGKQVQLL ETEIRFLCTK AREIFISQPI LLELEAPIKI
     CGDIHGQYYD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFVL
     RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPI AAIIDEKIFT MHGGLSPDLN
     SMEQIRRVMR PTDIPDCGLL CDLLWSDPDK DITGWSENDR GVSFTFGPDV VSRFLQKHDM
     DLICRAHQVV EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAEK
     KQKYVPNLGS GRLASPRTKK T
//
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