ID   A0A3M7QVZ5_BRAPC        Unreviewed;       547 AA.
AC   A0A3M7QVZ5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=phosphatidylinositol-3-phosphatase {ECO:0000256|ARBA:ARBA00013038};
DE            EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
DE   AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
GN   ORFNames=BpHYR1_044850 {ECO:0000313|EMBL:RNA15125.1};
OS   Brachionus plicatilis (Marine rotifer) (Brachionus muelleri).
OC   Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC   Monogononta; Pseudotrocha; Ploima; Brachionidae; Brachionus.
OX   NCBI_TaxID=10195 {ECO:0000313|EMBL:RNA15125.1, ECO:0000313|Proteomes:UP000276133};
RN   [1] {ECO:0000313|EMBL:RNA15125.1, ECO:0000313|Proteomes:UP000276133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HYR1 {ECO:0000313|EMBL:RNA15125.1};
RX   PubMed=30375419; DOI=10.1038/s41598-018-34188-y;
RA   Franch-Gras L., Hahn C., Garcia-Roger E.M., Carmona M.J., Serra M.,
RA   Gomez A.;
RT   "Genomic signatures of local adaptation to the degree of environmental
RT   predictability in rotifers.";
RL   Sci. Rep. 8:16051-16051(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RNA15125.1}.
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DR   EMBL; REGN01005038; RNA15125.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M7QVZ5; -.
DR   STRING; 10195.A0A3M7QVZ5; -.
DR   Proteomes; UP000276133; 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   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:SF130; PHOSPHATIDYLINOSITOL-3,5-BISPHOSPHATE 3-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   Hydrolase {ECO:0000313|EMBL:RNA15125.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276133}.
FT   DOMAIN          142..498
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   ACT_SITE        338
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         291..292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         338..344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   547 AA;  63467 MW;  17EC4A2BF991D607 CRC64;
     MSNEVSGSDQ EPNLVRLLDG EQYLNTNTDC FLSAFDTRIR GHLTITNFRF FFSSQPLTVD
     VPLGFILKID KLYATSTSTP DEIIGLTVIC KNGRYYQFTK LENDPNFELL VHDQLVKHTF
     YLSSSIDCFA FVHKPSLSDS TGWSVYDPDR EYTRMGIGDQ WRMSNANQNF ELCETYPRKL
     CVPSFVTDEE LRLVAQFRSK NRLPVLSWTS ESKHFGGILR SSQPLCGMSG KRSLYDEDYL
     KKIAQMVAAP KGFIYDARPY LNALANCTNG GGYENEKHYD FFKIEFLRIE NIHTMRDCLG
     VVSFNLDSKW LEHLKLILDG CVKICDRVNT GHVVLVHCSD GWDRTPQLTS LSVILMDDYY
     RTLQGFQVLI EKEWLSFGHK FSTRVGHGCH KYFDQDRSPI FVQFIDCVWQ IMSQNKVFFE
     FNEQLLHDIL QSLYSNQYGT FLMDSEKERD KNELKAKTVS LWSYVNSNKE KYTNENYMVY
     EGDLKIETDK LKLWESYYFK EIDRKLLGDE ANRQELDSVG ILKSNQSSFN NLFASGLRLL
     NTMLDKS
//