ID D0NY05_PHYIT Unreviewed; 1388 AA.
AC D0NY05;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Myotubularin-like protein {ECO:0000313|EMBL:EEY67956.1};
GN ORFNames=PITG_18372 {ECO:0000313|EMBL:EEY67956.1};
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY67956.1, ECO:0000313|Proteomes:UP000006643};
RN [1] {ECO:0000313|Proteomes:UP000006643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
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}.
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DR EMBL; DS028184; EEY67956.1; -; Genomic_DNA.
DR RefSeq; XP_002997818.1; XM_002997772.1.
DR STRING; 403677.D0NY05; -.
DR EnsemblProtists; PITG_18372T0; PITG_18372T0; PITG_18372.
DR GeneID; 9463523; -.
DR KEGG; pif:PITG_18372; -.
DR VEuPathDB; FungiDB:PITG_18372; -.
DR eggNOG; KOG1012; Eukaryota.
DR eggNOG; KOG1819; Eukaryota.
DR eggNOG; KOG4471; Eukaryota.
DR HOGENOM; CLU_257014_0_0_1; -.
DR InParanoid; D0NY05; -.
DR OMA; HCRCCGY; -.
DR OrthoDB; 91018at2759; -.
DR Proteomes; UP000006643; Partially assembled 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW Signal {ECO:0000256|SAM:SignalP}; 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 SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1388
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003012486"
FT DOMAIN 22..143
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 563..960
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 1325..1386
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 137..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 793
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 733..734
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 793..799
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1388 AA; 155789 MW; F783D4238942B8E0 CRC64;
MSLQIGVAFL KLLTSVQSLR NPKLTSFGDH HSVPAFPHLV MLLKIIRAEA LASADLNGKS
DPFVRVFYDG KEVGASHRVK RSLNPRWDFQ VTITLAHAGP LDVVLEVLDK DELSQNDLLG
SLRVLFPEWR QLVDEYQKRK QRKEIPPTNH RGSKCVDVRQ LGAHNTVEVN SNGNGSDSKQ
LQTGNSSHAT DFQRRSRSLN SSGGYLQAES KGRASVAAGE LSVEQVNDAM DIKPVFIWCR
LVKGSAAQGR ILCCVQYEER DLKYLVNHPY GTSIQEVFLP QNPRFEHAYC HLPRSWHPDV
AVRQDELTAM HQGTPKDCLF PWHEKLLHMV EEVTVTFHVN ESNQGVLATL VLTNYRIWFV
PYRRVRGLLH EDVHTLPVSK ILKASIQQQK RSNNNVITVL ILDNMDAGHY HVTLSPISRL
RDSVRDFSRE AELKRVKTLH NIVREIEWLR IENSFCSPTD RNHTVATADE MQLEDDLLHY
TPKHSSSSMP PPMARALTQN YSKYQKHTFT KESIGSLTLN GSGGPMERPK FRHQQSESAV
YPPLTQTMSV RKPPQQFQLA ARRRVRYDPE AEFARQGALE HPRWRRCELN EQYQLCPSYP
AFLMVPECLN DEIITAAAGF RSKSRFPALT WIHPRTGAPL CRSSQPNTGV LRSTNSEDKK
LIWAIRDAAI PADQAAKSKR TVPKKNSLVH IVDARPEINA KSNALAGKGH ESVKQYDRDG
VSTAAITFMG IDNIHVVRNS LAGLAQALYE VEDSNFFGAV QKSRWLEHIC SILQGASEVA
THLERGDAVL VHCSDGWDRT AQLSALAQIM LDPYYRTLEG FALLIEKDWC SFGHNFQKRC
SHPTSDQTSP IFLQFIDAVY QLTLQFPTHF QFNELLLSSV AEAVYSSWYG TFQKNSENER
RLFLSTVPSV SVWDVIRATT DQFLNPLFAG GEIHGSGGSN MEPMLPVCRV RVMQLWVSQY
QKAIGHMRLQ QREFEMLQLI RQQEADLSRL YAALSSDQQL ELRSSQLRSD IAKLSRSMNL
KYPDEPGTPS RDLERKRMAS SSTGDTLRNS GKRPTAASLD FHDLASIVAM GTAGATANAA
ASPPREHMTL AQMLQRANLE ASSGPPPPPS HNLPNPRRRK SLTSRSRSNS LKNTIINVVA
QMKGGSHDKE ADEPEDVGST TLPNPVRVSE GRRNLRLSSP SRRDDLKRDL RYLESQLSKL
NHQVAIKEDA AKQTMRRFRC YNYNLPETAL RNENDTLSPG SGKKVRLGGS NGSKPYPSPR
TLSPPSSSSS PGSGTASASA RELCESSSMD GDPRNFTPGS SPLLGTDKVI SGGNYLNSQP
VWERDEDAPC CKRCKKKFKT LLRNRHHCRC CGYVFCGRCT SHRMSLPDFG YYDVVRVCKV
CYTSGEDG
//
