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Database: UniProt
Entry: L7FN90_ENTIV
LinkDB: L7FN90_ENTIV
Original site: L7FN90_ENTIV 
ID   L7FN90_ENTIV            Unreviewed;       843 AA.
AC   L7FN90;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=phosphatidylinositol-3-phosphatase {ECO:0000256|ARBA:ARBA00013038};
DE            EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
GN   ORFNames=EIN_129490 {ECO:0000313|EMBL:ELP91599.1};
OS   Entamoeba invadens IP1.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP91599.1, ECO:0000313|Proteomes:UP000014680};
RN   [1] {ECO:0000313|EMBL:ELP91599.1, ECO:0000313|Proteomes:UP000014680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP1 {ECO:0000313|EMBL:ELP91599.1,
RC   ECO:0000313|Proteomes:UP000014680};
RA   Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL   Submitted (OCT-2012) 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};
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; KB206458; ELP91599.1; -; Genomic_DNA.
DR   RefSeq; XP_004258370.1; XM_004258322.1.
DR   AlphaFoldDB; L7FN90; -.
DR   EnsemblProtists; ELP91599; ELP91599; EIN_129490.
DR   GeneID; 14890558; -.
DR   KEGG; eiv:EIN_129490; -.
DR   VEuPathDB; AmoebaDB:EIN_129490; -.
DR   OrthoDB; 7311at2759; -.
DR   Proteomes; UP000014680; 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   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; 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   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000014680}.
FT   DOMAIN          461..838
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          136..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        677
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         613..614
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         677..683
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   843 AA;  96964 MW;  89239007FD67F78E CRC64;
     MDKVVMNQEN GTLLIIEGQS GEEQKDVQPI DKQQIPENKE MNTIESIQNS HTQIPVQTTK
     PIILNTCEKI KVEKNDTISM QNNDTFIKTS PPLKTSEIKK VTCNIVIDQN EVTKDSQVTV
     MKIEETPINN QLNVETNESQ VSQQIKNKDE HSSCTPLSSD NSEEDKYQET EQLTHIEQQE
     EVDETPEILL KKEELRKILT ALRPQDFEPN RPPPQPPQYT EKKSDHPEAV FKVTAQSDGY
     TESHSKEVPT TPLPPTPTKK ESENSKQNED DDSGIMPISR KFLQTLFTKK TPENTKESDD
     FKRSESFTEI HVDHSTSEIE ISSPLSLDAT TKDVHVPFKK GEKTVLNTAI TLIARNDTSN
     YTEMVGTFVL TNYRVEFQTT AAVYSFTIPL TKIANFKKIN TSDKSRKRTF YLETKDNQCF
     TFSFSDNQRT RRVINTELIK RVFTTSPDVL FIFCSNEFKK KRSFYDFRGE FERQGISSEW
     KVFEGNARYK LASTYPSLVY VPKTADETTI KNTMKHRSKG RFPVLTWFSN KNKAALLRSA
     QPLPGFVTSV TGKNTSGDVE YLQKVEEVTG NKILHVLDSR PLLNAMTNKA AGGGYEDEDR
     YPFLQVDFEN IANIHVVRDA WRQLYYAVYN MPTRHFDTPF MKSKEVSKWV ALQETVVQSA
     VKASKLLGKG ISVLVHCSDG WDRTSQCCGI AEIILDGYYR TLNGFIVLIE KDWKSFGHRF
     MTRSGFGAES PFGQYAPIFF QFLDCVHIMM NTFSNFFEFN EDFLIELNDA IFCSEFGTFM
     FDTERERVES QIENKTPCFW EYVLENRAKF VNEKFNEETG QLDIENIVPT VVMWEKYFLK
     NKI
//
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