ID W2NU99_PHYPR Unreviewed; 1522 AA.
AC W2NU99;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=L914_04166 {ECO:0000313|EMBL:ETM52237.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETM52237.1};
RN [1] {ECO:0000313|EMBL:ETM52237.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAC_01/95 {ECO:0000313|EMBL:ETM52237.1};
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 IAC_01/95.";
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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR EMBL; KI691664; ETM52237.1; -; Genomic_DNA.
DR EnsemblProtists; ETM52237; ETM52237; L914_04166.
DR VEuPathDB; FungiDB:PPTG_08336; -.
DR VEuPathDB; FungiDB:PPTG_10736; -.
DR Proteomes; UP000054532; 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:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd00065; FYVE_like_SF; 1.
DR CDD; cd14507; PTP-MTM-like; 1.
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; 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; 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; PF01363; FYVE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00064; FYVE; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 182..244
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 998..1392
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 39..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..116
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1229
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 1229..1235
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1522 AA; 168928 MW; 8B43B21EE490321E CRC64;
MLSSAKSMDD EAARLAVLRD PKRMAALLVR AFSSSILDES VNGAARRGST HAQEEEDEEV
EETQEEFQEL ERRASAGTAT EAAPLRVVIR PVAEDDEDDA GEEYEDEDDD DEKPLDEEEL
EAAATALQTA TRIVEELRLK MLLKAGQQME RQRQDNSEPP IVVEDTPSST GGPGVPVPHA
QVRSNSTCSG CGKSFNPFHR SKNCAACGFA FCPKCSSKNF VLPTCFGYRD ESVRTCDLCA
KWFQKAMDRY FDAMELAKEQ EQESSIHRGS MGEITIEEKP RSLSSFNSVP VSTPSTNDGI
LSVITRRSSV SSLDPAPSCP SDDVADESVE NEDQITPSTS TSSTSRRRHR RSSIASAPSP
SINKNKPWFS GHLRAMHVND RLPRKKKTRG ESEGGETENN SPELRSRRSR LSSVASSKSR
HTNEDAGEKQ HENSAGSSPI DIQDGEDASK SSGTGRGSSL TISVKPANDS DDSNRPRRKT
RRSKFSRSAS FDLANLQSSV SPDSSPEMRR CNTFGPDDGR KLASDVVSSG GSDRSNSMLS
LKAFDDSDIV DERAQLDSAD VKMKSEAKLA AAVLRFAVYE MGGKEGAGLR RTFGFTKANP
VLDRYTLELD CRQRIVRAKS VFMHRFWSFH CDSVQSFVSG SSDGMARLVV FNGGQGNQTL
ELKFANDDER EQFRQAMDSC RSTNLDRMRK FASRTAMSLP ARPELPASPV LENFRSPVPL
EPSTTFSADT STSIESELGL THDTGCSISA DSAVVQSIHV PLLPGEVVVK DTELQATLLI
GPVSETNEST LVWGRIRGKI AVTNYRVIFT PFERVQVQAR CGGQGGIAYI PLFAITHVQL
LYPGGRRPKS GRTYYAGMAG SASIISINCK DVRVMRFQLD SHASVSDDHA HKLRATIAKL
ADASQRYTVV ERGSPMRTSP GLGPLSSSAS DSDTLPDREG DNFLHESKEP FFQNSSRTPA
YAASPVLRPD RMLTLPREIS GSFAFSYSIS NVPPDQNGWN LFVDEREFKR QIGGDPAVSP
FLKYYKNDRG NICKSYPSKL LLPASMNSAT LAKVADFRAK NRLPVITYYH RRNRCVLTRS
SQPLLGNLLS GTSNVSDQLL LGVYRRLPDI IKNQSQSSQS SRPIYIFDAR KPKASTGNRL
MGKGGVETPQ DYPGAVIHHL NIANMYRMQS SFMGLMKLFL PGGVEDTDRT WLSSVESTRW
LDHVRLVLDG ALKIARVLEL EGASALVHCS DGWDRTAQLC ALAQLIIDPY YRTIRGFATL
VEKDWLAFGH KYAERCGSDR NRDPQRNKSS PIMFQFIDAV WQMQRQYPRS FEFNERFLLH
LANALTSGLY GTFMYDSRLQ RDVNEVKYNS VSVWTPVLMK PELYSNSNYE MHDGPIWPWV
SCKMMRLWEN YFFQWHPKFY KCQWACSLVY HGLSSSRGST SNGDKDRENA QQQTPHRDAS
HVKDPPALDL LATPITSSIA EENGDLDVPI ISLSSEDEDS SKRVRTASGT YTQKAPKRNI
FGLTRGSRQR AQSEENGSQE VC
//
