ID   A0A091QTX9_MERNU        Unreviewed;       607 AA.
AC   A0A091QTX9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
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};
DE   Flags: Fragment;
GN   ORFNames=N331_05989 {ECO:0000313|EMBL:KFQ30379.1};
OS   Merops nubicus (Northern carmine bee-eater).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX   NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ30379.1, ECO:0000313|Proteomes:UP000052967};
RN   [1] {ECO:0000313|EMBL:KFQ30379.1, ECO:0000313|Proteomes:UP000052967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ30379.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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; KK706066; KFQ30379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091QTX9; -.
DR   Proteomes; UP000052967; 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   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd14586; PTP-MTMR3; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR046352; MTMR3_PTP.
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   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF66; MYOTUBULARIN-RELATED PROTEIN 3; 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:UP000052967}.
FT   DOMAIN          155..576
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          585..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        413
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         326..329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         351..352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         413..419
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ30379.1"
FT   NON_TER         607
FT                   /evidence="ECO:0000313|EMBL:KFQ30379.1"
SQ   SEQUENCE   607 AA;  69147 MW;  50B5345C3E952590 CRC64;
     QDEETQHSLE CIQANQIFPR KQLIREDENL QVPFIELHGE STEYVGRAED AIIALSNYRL
     HIKFKESVVN VPLQLIESVE CRDIFQLHLT CKDCKVIRCQ FSTFEQCQDW LKRLNNAIRP
     PSKIEDLFSF AYHAWCMEVY ASEKEQHGDL CRPGEHVTSR FKNEVERMGF DMNNAWRISN
     INEKYKLCGS YPQEIIVPAW ITDKELESVA SFRSWKRIPA VVYRHQSNGA VISRCGQPEV
     SWWGWRNADD EHLVQSVAKA CASDSRSNSN KLMNGNCSRD FSNGGDLSDV EFDSSISNAS
     GAESLAIQPQ KLLILDARSY AAAVANRAKG GGCECPEYYP NCEVVFMGMA NIHSIRKSFQ
     SLRLLCTQMP DPGNWLSALE STKWLQHLSV LLKSALLVVH AVDRDQRPVL VHCSDGWDRT
     PQIVALAKLL LDPYYRTTEG FQVLVETEWL DFGHKFADRC GHGENSDDLN ERCPVFLQWL
     DCVHQLQRQF PCSFEFNEAF LVKLVQHTYS CLFGTFLCNN AKERGEKHTQ ERTCSVWSLL
     RAANKAFKNL LYSSQSESVL YPVCHVRNLM LWSAVYLPCS SPSTPTDDTC APYPVPGSSP
     EDQPLGR
//