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Database: UniProt
Entry: A0A0A1U1W3_ENTIV
LinkDB: A0A0A1U1W3_ENTIV
Original site: A0A0A1U1W3_ENTIV 
ID   A0A0A1U1W3_ENTIV        Unreviewed;       909 AA.
AC   A0A0A1U1W3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   08-NOV-2023, entry version 37.
DE   RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51339};
GN   ORFNames=EIN_162560 {ECO:0000313|EMBL:ELP86612.1};
OS   Entamoeba invadens IP1.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP86612.1, ECO:0000313|Proteomes:UP000014680};
RN   [1] {ECO:0000313|EMBL:ELP86612.1, ECO:0000313|Proteomes:UP000014680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP1 {ECO:0000313|EMBL:ELP86612.1,
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};
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DR   EMBL; KB206960; ELP86612.1; -; Genomic_DNA.
DR   RefSeq; XP_004185958.1; XM_004185910.1.
DR   AlphaFoldDB; A0A0A1U1W3; -.
DR   EnsemblProtists; ELP86612; ELP86612; EIN_162560.
DR   GeneID; 14885519; -.
DR   KEGG; eiv:EIN_162560; -.
DR   VEuPathDB; AmoebaDB:EIN_162560; -.
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   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   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF8; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR   Pfam; PF06602; Myotub-related; 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   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000014680}.
FT   DOMAIN          528..900
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   ACT_SITE        740
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         650..653
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         675..676
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         740..746
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   909 AA;  104787 MW;  C3FBB636478076EE CRC64;
     MSLEVFPDEA ENFYTLRILS TEVVDGIALL KVSVSSIELM WTIYRRWDEY VKYLISLQRI
     TPVRLIVFKE QNQSVALSSK TSLESSISFL QNSTHQILAF DQVQAEIEKS SYLFDSFEPS
     YITLKVIHQG FLEVKSSLSR YEDPFTKAFA VLSESNIFYM YHSPSEYSLP LFQATLPFLS
     CVTVPENSNY IFVQISHKEI LMLKTPNYIE TEWWSKFFMR SVSKSHVPGI IKDAFKAISN
     ESQSTFEHCC HEYNPHKKKV LRNEVKKQMQ SQNVSEAITK LKKKNIIKNV GEFVELSVQA
     LTGATLPNIQ SALNSFVCLT VNDVVVTNSS NIKDVALTSA DVVRIQPINK EMQMLFDSTV
     QNEAKFLTLK NANETPKTPG NLPLVYFPNE QLVMVYSNIV HIHTKYDCGP PTCCTGLDPI
     PGTILITSAR LIFRVQRQSG TSESDGLFSS FHGKCKEEGF EIPIPLFYQI RKEKIALPTV
     GIFSCVIVKC KNFHSFVLAF FDGEKADELE QIVIKAVSRR TMTEVFYFKG VYEGPNYLKD
     FERMNYRKAG LSLYESGVKS YPSRIALPSQ MTPEDILQIV NFRSKGRIPA MSWWNYEKKM
     YLLRSAQPLV GLTTTRNFAD EKLVEIARGM SESQKMTFVD CRPKLSASAN MIKGMGYEDS
     RYYEGSDVVF LDIDNIHKMR ESYNQLFSAM RRISYAHVSM TEGMKIVANS KWLYHISKIL
     KGTVIAINRM IQGSTLLVHC SDGWDRTSQI ASLIEIVVDP FYRTIEGFQV LIDKEWIAFG
     HKFKDRCRHL VSTQSMNEYS PVFLQFIDCV FQIMRVAPKE FEYNENFLME IAQQSFSCYF
     ANFLCNSQEE MNCKAESLWN VINKENIRFR FVNPTYKKSE KMLNVNDIEK SAPVLWRKFY
     QSYFRFHSM
//
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