ID   A0A166H3H8_9AGAM        Unreviewed;       898 AA.
AC   A0A166H3H8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Phosphatases II {ECO:0000313|EMBL:KZV71863.1};
GN   ORFNames=PENSPDRAFT_742984 {ECO:0000313|EMBL:KZV71863.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV71863.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV71863.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV71863.1,
RC   ECO:0000313|Proteomes:UP000077086};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV424507; KZV71863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166H3H8; -.
DR   STRING; 1314672.A0A166H3H8; -.
DR   InParanoid; A0A166H3H8; -.
DR   OrthoDB; 5474662at2759; -.
DR   Proteomes; UP000077086; 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; cd17666; PTP-MTM-like_fungal; 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   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF8; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   Pfam; PF21098; PH-GRAM_MTMR6-like; 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:UP000077086}.
FT   DOMAIN          129..577
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          597..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          733..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        371
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         273..276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         298..299
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         371..377
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   898 AA;  98259 MW;  431848442056728B CRC64;
     MDAIRVSKVP GVTLQKAGKS FLGALHLTAH HLIFSFEDAS APEMWASLLH SYIPYPIINL
     VTRLPQNLRG ECPVNFRCRT FETFALNFGN EGMAIDVFES VKELTVAADV KQLYAFFYTP
     NPPLTHNDGW LIFNPREEFG RMGVGTRSKA WRFTDINKDY TFCPTYPARM VVPTRISDAT
     LQYAVKYRSK GRIPALTYLH WANYGSITRS SQPLVGLTNA RSVQDEKLVE AVFQSHLSPE
     SRAGATAPPA AIYGATPTNL IIDARPTTNA MANTAKGAGT ENMDYYKECR KAYLGIDNIH
     TMRDSLNKVV EALRETEILA SSMTGGASML PVDRQTLRRS GWLKHLASIV EGTLVIVRNV
     HVNSSHVLIH CSDGWDRTSQ LSALSQICLD PYYRTLRGFQ VLVEKDWLAF GHRFLDRCGH
     LSSDKFFLAP TEGTTDGAGG GAGAFFASVQ NRFVGNHHIK ETSPVFHQFL ESVRNVQRQF
     PERFEFNESF LRELYFHLYS CQFGTFLLNS EKERREMQPP LSERTVAVWD FLNSRRDTYI
     NADFKPELDA ADRREAGADQ GVLLPDPKDL RFWNELYGRG DEEMNGRFVQ AQVQAHSELS
     GPIESAEEDP AIPSMGAGDS GRSPVTALAS LPVASGTGVD STRVSGSMLE LGSPPRRDIA
     LPISRSQTLS PSRSSAPYPA PSPRNAPAAD LFSSAGLGAR SVWGRLSSNA TSAFTSLQGA
     YDGLAKDLRV MNVAPPSPDR AADSVPATPG GGELRGRDEL GAWGSGAERF ETPRVEEAVR
     PSTFSASSSF GGNPWATTKE PTSSLSQKAS GHQPRLPSGL FDDPWGSVKP ATSRPSAASP
     WERMNDGALP ADPSVTVVQP TPRRAASTTV PEPPRTDVTP SAPQPTDADL DPLGVWKT
//