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
//