ID W2LHA1_PHYPR Unreviewed; 989 AA.
AC W2LHA1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=phosphatidylinositol-3-phosphatase {ECO:0000256|ARBA:ARBA00013038};
DE EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
GN ORFNames=L917_05767 {ECO:0000313|EMBL:ETL96833.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL96833.1};
RN [1] {ECO:0000313|EMBL:ETL96833.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL96833.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; KI678838; ETL96833.1; -; Genomic_DNA.
DR AlphaFoldDB; W2LHA1; -.
DR EnsemblProtists; ETL96833; ETL96833; L917_05767.
DR VEuPathDB; FungiDB:PPTG_02208; -.
DR Proteomes; UP000054423; Unassembled WGS sequence.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14507; PTP-MTM-like; 1.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF8; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 4: Predicted;
FT DOMAIN 592..989
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 15..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 808
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 745..746
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 808..814
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 989 AA; 109237 MW; 29BA35F69797DBE1 CRC64;
MASARDSDFY VNVTSDGCRD EADERLSTHS ARHQDDAEYT SVLYARPEEV MSPTSSSSNG
SGSEFFSTGH QLKNGTAGDI RATNAAAPTS ATATETETDS DLEESRSDAD KEKEHVIRAM
NVAEDKSDAD AEATDDEECK GLGETGTAEE KDQDRFKLAI ALDFETDTNA AMSIGPPSVT
RQTSSSFSDL GDYEDFSFSD AITIPNGGGP GSVESSSNSG TPTTFYPIYE NEAFRFTHAS
VSNCGYGSYD AIEKIPGVYT NSPARSARSA NSPTMLRLDN YGYNGGRITP TFQLTQPADE
SQPLIGDIYP VSGEVVRLRV DNAAYIIFYK SDDSGEEQNT KNEMLAMSSS SEDDVDTSEW
NEEGSGRAPP PRSYASLGAA GHKVQTDNCF TRDYNHPTRS LGRGLFRAST SVGSAFLKGA
AGLVNKTYQG GANGGVFGFA KGLGMGMLGL GTHTVKGAFR GVGQVTHLVG EMVLGTAPHF
SIDGTLVLTN YRIIWQALST KDAMEIPLAS ILSAESSTTA PHVANIEGKH LLRASLAFQD
ETTCSDFLGC IWELYSTGGS PPHYLFAHLH YQALRHKDEL KTPDGSGLET PNDSLYDAEE
DYRRLKLLDE DSWMRLYDNS DYTMFPSYPD TFVIPSVLDE DDLRELSAYR SASRIPAVVW
RHPHTGALVC RCAQPCTGLS GYVVEADQKM VSALQHATSA YGDARFHFFD ARSQMAAAAN
SAQGKGTEDP RNYPNSELHF CDIANIHAVR SSYASLASVC QPGQERESSG WLFQLRNTFW
FLHISNILST SQEICRYLSQ GNSVMIHCSD GWDRTPQLTA MVQLLLDPYY RTVRGLLCLI
EKEWCSFGHL FRYRYGHGEG PGQQELEEQS PVFIQWLDAL WQIWRQQPWA FEFNEALLSA
LYESIFSGLY GNFLYNNERQ RKQEEATAPT RSLWFVLLEQ MEKYLNVEYD SAKNFNSIGL
VLPFSSEEND LVMWANHLVY ADPVCRKYE
//