ID W2XXP6_PHYPR Unreviewed; 1358 AA.
AC W2XXP6;
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=Protein-tyrosine-phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=F441_00217 {ECO:0000313|EMBL:ETP27282.1};
OS Phytophthora parasitica CJ01A1.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317063 {ECO:0000313|EMBL:ETP27282.1, ECO:0000313|Proteomes:UP000018958};
RN [1] {ECO:0000313|EMBL:ETP27282.1, ECO:0000313|Proteomes:UP000018958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ01A1 {ECO:0000313|EMBL:ETP27282.1,
RC ECO:0000313|Proteomes:UP000018958};
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., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ01A1.";
RL Submitted (NOV-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETP27282.1}.
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DR EMBL; ANIX01000040; ETP27282.1; -; Genomic_DNA.
DR EnsemblProtists; ETP27282; ETP27282; F441_00217.
DR Proteomes; UP000018958; 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 CDD; cd00030; C2; 1.
DR CDD; cd14507; PTP-MTM-like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
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 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; PF00168; C2; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 1..103
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 523..920
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 1295..1356
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 95..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 753
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 693..694
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 753..759
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1358 AA; 152639 MW; B3C8B716A252BFFB CRC64;
MLLKIIRAEA LASADLNGKS DPFVRVFYDG KEVGASHRVK RSLNPRWDFQ VTITLAHAGP
LDVELEVLDK DELSQNDLLG SLRVPFPEWR QLVDQYQKRK QRKEMPPTKH RGSKCVDVRQ
LRVNKIADTS NSANNSDSKL LQKGNSSQST DFQRRSRSLN SSGGYLQAET KGRASVASGE
VSMEPVSDVM DIKPVFIWCR LVKGSAAQGR ILCSVQYEER DLKYLVNHPY GTSIQEVFLP
QNPRFEQAYC HLPRSWHPDV AVRQDELTAM HQGTPKDCLF PWHEKLLHMV EEVTVTFHVN
ESNQGVLATL VLTNYRIWFV PYRRVRGLLH EDVHTLPVSK ILKASIQQQK RSNNNVITVL
ILDNMDAGHY HVTLSPISRL RDSVRDFSRE AELKRVKTLH NIVREIEWLR IENSFCSPTD
RNHTVATADE MQLEDDLLHY TPKHSSSSMP PPMARALTQN YSKYQKHTFT KESIGSLTLN
GSGGPMERPK VKHQLSESDA YPPLTQTMSV RKPPQQFQLA ARRRIRYDPE AEFARLGALD
HPRWRKCELN EQYQLCPTYP AFLMVPECLN DEIITAAAGF RSKSRFPALT WIHPRTGAPL
CRSSQPNTGV LRSTNPEDKK LIWAIRDAAI PADQAAKSKR ALPKKNSVVH IVDARPEINA
KSNALAGKGH ESVKQYDRDG VSTAAITFMG IDNIHVVRNS LAGLAQALYE VEDSNFFGAV
QKSRWLEHIC SILQGASEVA THLERGDAVL VHCSDGWDRT AQLSALAQIM LDPYYRTLEG
FAQLIEKDWC SFGHNFQRRC SHPTSDQTSP IFLQFIDAVY QLTLQFPTHF QFNELLLSSV
AEAVYSSWYG TFQKNSENER RLFLSTVPSV SVWDVIRATT DQFLNPLFAG REVHASSGSN
MEPMLPVCRV RVMQLWVSQY QKAIGHMRLQ QREFEMLQLI RQQEADLSRL YAALSSDQQL
ELRASQLRSD IAKLSRSMNL KYPDELATPS KELEKKRMAS SGEMLRNSGK RPTAASLDFH
DLASIVAMGT AGAAAKAGAV SSPPREHMTL AQMLQRGNLE ASSGPTPAGS AGVPTQSHNL
PNPRRRKSIT SRSRSNSLKN TLINVVAQMK GGSHDKEIDE PEEVGSATLP NPVRVSEGRR
NLRLSSPSRR DELKRDLHHL ESQLSKLNHQ VALKEDAAKQ TMRRFRCYNY NLPETALRNE
NDTLSPTSGK KVRLGCSNGN KPYPSPRTYS PPSSSSSPGS GATSASARVS GEPYDSSSLD
GDPRNFTPGS SPLLGTDKVI SGGNYLNSQP VWERDEDAPC CKRCKKKFKT LLRNRHHCRC
CGYVFCGRCT SHRMSLPDFG YYDVVRVCKV CYNSGEDG
//
