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Database: UniProt
Entry: H0EYW9_GLAL7
LinkDB: H0EYW9_GLAL7
Original site: H0EYW9_GLAL7 
ID   H0EYW9_GLAL7            Unreviewed;       678 AA.
AC   H0EYW9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Putative Phosphoinositide 3-phosphatase {ECO:0000313|EMBL:EHK96272.1};
GN   ORFNames=M7I_8030 {ECO:0000313|EMBL:EHK96272.1};
OS   Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK96272.1, ECO:0000313|Proteomes:UP000005446};
RN   [1] {ECO:0000313|EMBL:EHK96272.1, ECO:0000313|Proteomes:UP000005446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX   PubMed=22302591; DOI=10.1128/EC.05302-11;
RA   Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT   "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT   of a species from the Helotiaceae family.";
RL   Eukaryot. Cell 11:250-250(2012).
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:EHK96272.1}.
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DR   EMBL; AGUE01000262; EHK96272.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0EYW9; -.
DR   HOGENOM; CLU_001839_5_1_1; -.
DR   InParanoid; H0EYW9; -.
DR   Proteomes; UP000005446; 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   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   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005446}.
FT   DOMAIN          108..554
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          412..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..662
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        316
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         252..253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         316..322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   678 AA;  75152 MW;  31D98AFAC4549978 CRC64;
     MTDNLKTPKV NTRKSAEINP PKDLLQVEDV QLLAEGITTV VTLHLKAHHL ICYSSPSTPP
     QGTSTPSKPA KSRSVVFAYA LFSSVIYRPT PPTSSHQSSI RIRTRDFRFA RLIFNQDKQA
     RDVFETLKSW NRSIQDEKLV AACFSASAPL AERDVNSSIS SRASPASSQV DLDLEKVEGE
     LSDTEKLEDQ MISASSKIEI QDAPHIYGAQ QNNLIVDARP TVNALAMQAA GKGSENMEHY
     KFAKKAYLGI DNIHVMRKSL DVVIEAIKDS DVSKLPPNRD LLAKSGWLKH ITGVLDGSAL
     IARQVGIQHS HVLIHCSDGW DRTSQLSALS QLMLDPYYRT IEGFVVLVEK DWLSYGHMFQ
     LRGGYLNSEK WFKIDKDAMA GSAINPGDRG EGRSDTFETL FQGTKRLFAK TQTSAQDHAD
     RESGDLLEDA KSANSAKEAT DLENISPIFH QFLDATYQLL HQHPTRFEFN ERFLKRMLYH
     LYSCQYGTFL YNNEKSRLDA RVHERTNSVW GYFLANKVQF LNPQYNGEIN DNVRGQERLL
     FPKLDKVRWW NDVFNRSDAD MNGPSNAVTE RYLGGDMTPD RGRSSPSPRP NPNNLGINQG
     VLTGVETAHA ALTVNRTSSP TRVVSNGAVA GFATLRDGIA GLGLGKGKSA SGSSSGANGG
     NSPASWKGKG REMEVEMQ
//
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