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Database: UniProt
Entry: A0A2S7R2K5_9HELO
LinkDB: A0A2S7R2K5_9HELO
Original site: A0A2S7R2K5_9HELO 
ID   A0A2S7R2K5_9HELO        Unreviewed;       768 AA.
AC   A0A2S7R2K5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Phosphatase protein {ECO:0000313|EMBL:PQE33039.1};
GN   ORFNames=CJF32_00011176 {ECO:0000313|EMBL:PQE33039.1};
OS   Rutstroemia sp. NJR-2017a WRK4.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Rutstroemiaceae; Rutstroemia.
OX   NCBI_TaxID=2070412 {ECO:0000313|EMBL:PQE33039.1, ECO:0000313|Proteomes:UP000238813};
RN   [1] {ECO:0000313|EMBL:PQE33039.1, ECO:0000313|Proteomes:UP000238813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJR-2017a WRK4 {ECO:0000313|EMBL:PQE33039.1,
RC   ECO:0000313|Proteomes:UP000238813};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) 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}.
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:PQE33039.1}.
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DR   EMBL; NJPR01000020; PQE33039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S7R2K5; -.
DR   STRING; 2070412.A0A2S7R2K5; -.
DR   InParanoid; A0A2S7R2K5; -.
DR   OrthoDB; 5474662at2759; -.
DR   Proteomes; UP000238813; 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:UP000238813}.
FT   DOMAIN          136..657
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          245..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..768
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        414
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         350..351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         414..420
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   768 AA;  84716 MW;  0E78796A95153B4C CRC64;
     MAEKLQETKV HNVQVVARGQ ASNVTLLLTA HHLVVIQAAP SPDETPAAPV KQRQSWIAYP
     MIAHCTFRPT PPGSGIASSI RLRGRDFTFY TLNFDDDKSA RETFEYIKTA TCKVGSIEKL
     YAFSYKAHGP EKHINGWDIY DPKTEWKRLG ISEKGVDRGW RISKLNQDYA FSPTYPALLP
     VPSSISDITI KHAGQHRSRA RIPVLTYLHP VNNCAITRCS QPRTGMRGAR SIQDEKLVSA
     CFSATTQTDG GDSVSPAMSR TSPESSSADL STPNNGELID PEQFEDELIS SGSNIEIPAE
     KPHVYGAQQN NIIVDARPPV NAYANQVNGF GTENMDHYPL AKKVYLNIAN IHVMRDSLGK
     VVDAIKDADI SILPPNRDQL AKSGWLKHIG GILDGAAIIA RQVGIQHSHV LIHCSDGWDR
     TSQLSALSQL MLDPYYRTIE GFIVLVEKDW LSFGHMFQHR SGFLNSEKWF VTQNDALAGS
     AIQPGGNSDG RGDAIENAIL SAKRFFNKNN ASQEALNDPD IDEIMTVNVP TKLEALPQSE
     ATKPKETSPV FHQFLDATYQ LLRQHPTRFE FNERFLRRLL YHLYSCQYGT FLYNNEKSRV
     DARVKERTKS VWAYFLAKKE EFTNKEYDGG EIDDHVRGKE RLILPILDDV KWWHQAFGRT
     DLEMNGPHNP ATERYLALSN NGSSGYTVVG GATMPARTVL TGVESAGSPT KQVLNGPAAG
     LASLREGIAG LGIGRAKGSG LGSRSPAAAN GSTGANSNGK QEMEVEMQ
//
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