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Database: UniProt
Entry: G5AF59_PHYSP
LinkDB: G5AF59_PHYSP
Original site: G5AF59_PHYSP 
ID   G5AF59_PHYSP            Unreviewed;       423 AA.
AC   G5AF59;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHYSODRAFT_319997 {ECO:0000313|EMBL:EGZ05849.1};
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ05849.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ05849.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ05849.1,
RC   ECO:0000313|Proteomes:UP000002640};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
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DR   EMBL; JH159165; EGZ05849.1; -; Genomic_DNA.
DR   RefSeq; XP_009538710.1; XM_009540415.1.
DR   AlphaFoldDB; G5AF59; -.
DR   STRING; 1094619.G5AF59; -.
DR   EnsemblProtists; EGZ05849; EGZ05849; PHYSODRAFT_319997.
DR   GeneID; 20644394; -.
DR   KEGG; psoj:PHYSODRAFT_319997; -.
DR   InParanoid; G5AF59; -.
DR   OMA; LGHFWFH; -.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
DR   GO; GO:0052866; F:phosphatidylinositol phosphate phosphatase activity; IEA:UniProt.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd14509; PTP_PTEN; 1.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR045101; PTP_PTEN.
DR   InterPro; IPR014020; Tensin_C2-dom.
DR   InterPro; IPR029023; Tensin_phosphatase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR12305; PHOSPHATASE WITH HOMOLOGY TO TENSIN; 1.
DR   PANTHER; PTHR12305:SF60; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 3-PHOSPHATASE TPTE2-RELATED; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   4: Predicted;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT   DOMAIN          34..206
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          123..194
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          241..409
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   423 AA;  47664 MW;  3C71E5DF7B7C230B CRC64;
     MSSSSSPSSS PTSSRRHTGG LANRLKHLVS KEKRRFSSDG FDLDLTYVTQ KLVALGYPAE
     KIEGIYRNHY RDVFRFFEHR HPGQYRVYNL CVERRYAPDE KFHGRVAEFG FEDHTPPPLS
     MVLPFCRDVH AWLQANSDNV VAVHCKAGKG RTGVMLCAYM LYARMWRSAR GALEFFAAAR
     SMKLQGVTIL SQRRFVGYFA EMCRRSESVE DVEVLGPYED EAARERAITL TEYHAQWLQE
     TQATSPRSSI IGSTPRPHAE PVLPARVHLV LVAVVLCGVA GHKKTNSSAA DWRVRVECGA
     IRPRAAVYEL PGGFQRQQRP NGTEGEEVVE LELRCNRVLV WDEVKVELRG RAGGTLGHFW
     FHTAFVPQVG DYFELTLAKN EIDKVAKDAK HGHKKFAPEF AVRLQFEVAT PQDLARSTSD
     AAA
//
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