ID T0PZ19_SAPDV Unreviewed; 978 AA.
AC T0PZ19;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Phosphatidylinositol-3-phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SDRG_15827 {ECO:0000313|EMBL:EQC26340.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC26340.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC26340.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC26340.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-
CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934;
CC Evidence={ECO:0000256|ARBA:ARBA00023732};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC Evidence={ECO:0000256|ARBA:ARBA00001291};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR EMBL; JH767234; EQC26339.1; -; Genomic_DNA.
DR EMBL; JH767234; EQC26340.1; -; Genomic_DNA.
DR RefSeq; XP_008620232.1; XM_008622010.1.
DR RefSeq; XP_008620233.1; XM_008622011.1.
DR AlphaFoldDB; T0PZ19; -.
DR STRING; 1156394.T0PZ19; -.
DR EnsemblProtists; EQC26339; EQC26339; SDRG_15827.
DR EnsemblProtists; EQC26340; EQC26340; SDRG_15827.
DR GeneID; 19956554; -.
DR VEuPathDB; FungiDB:SDRG_15827; -.
DR eggNOG; KOG4471; Eukaryota.
DR InParanoid; T0PZ19; -.
DR OMA; CSSARMP; -.
DR OrthoDB; 66964at2759; -.
DR Proteomes; UP000030762; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR022587; MTMR12-like_C.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF8; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF12578; 3-PAP; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030762};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 61..121
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 345..894
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 15..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 591
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 522..523
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 591..597
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 978 AA; 109192 MW; 35E09649745891C4 CRC64;
MTSLSKSLQV VIPSVPTDER RTSPERTSTA VGRESPAESI RQVILNEVSR ITQKSVAWVP
DSLADKCYQC QATFSLVLRR HHCRRCGNIF CDACSLSRMP LVSAGFFTPV RVCDKCCEAA
KRSHRHMVNE RRRQSLTQSL PASSMTTMHA DLHHHLPIDD DCDDSSLYDV SASQSPMTAS
LADAVCIQTI PGEVVVVRGP DVYLRTPDYK DNEPGTLYIT NYRVVFTSLH KPLANEVATP
LRRRSSKSQS GLSIHSAPML APPLYHAIPL RSIDRIKRQE LPESDTGVLD LICKDIRRLQ
LIFPGLVQRQ TYSFFDKCDQ LLRHPMPYFA KVSTETFPTA TIGDGWNVYD PVAEFNRLGV
GVTTTWRITS VNHNYTFCPT YSAAIAVPAI ISDAVLLVAG AFRSKSRIPA LSWRDVQTGA
TICRSSQPLV GLGQKQCAED IALIQAIAAA NPSSSTLVIV DARPWANAVA QKTVGRAGYE
LTAHYEAKPS SDDDADEPAV ATSSSMHLGL TDCRLVFMGI ENIHIMRKSF QKLVDLCVAK
EQRPATSGSI GKWNEHVAAT KWLDHISCIL HAAVEIVRLV KTEKASVLVH CSDGWDRTSQ
LTALAELMLD PHYRTLRGFA LLVEKDWCSF GHKFSERTGH PPPSDTINAS EVSVVFLQWI
ECVWQLMRQF PCSFEFNTRY LILVLDHLYA CRFGTFLYDS ENARVCEEKS APTISLWTYL
SSLEVSLISN PFYEPRKYSR QNWHARMKER RQANEVPMPP WTDAHTVVGL EESKDDDLVF
VHNDAAPVRT PMASTAPASP PTNEASAKTK LVHSIVQDLD TGLMFPHVTE ETVVPPRPPR
HVRDALVASF VSNAADESDE SSDGNARCVD AVDDTDVLIP SVSVKSLRLW TEYYLRWDAT
CSIERNADLE REAKLRDVLA EMEALQKDKD DDDASSSSPA WVDVVVEEAV DDGASRFRRE
MDRMCMAYED QLSLWLRG
//
