ID   A0A1B8FSD6_9PEZI        Unreviewed;       765 AA.
AC   A0A1B8FSD6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51339};
GN   ORFNames=VE02_05346 {ECO:0000313|EMBL:OBT86443.1};
OS   Pseudogymnoascus sp. 03VT05.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1622148 {ECO:0000313|EMBL:OBT86443.1};
RN   [1] {ECO:0000313|EMBL:OBT86443.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03VT05 {ECO:0000313|EMBL:OBT86443.1};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) 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; KV459422; OBT86443.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8FSD6; -.
DR   Proteomes; UP000091872; 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   Pfam; PF21098; PH-GRAM_MTMR6-like; 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;
FT   DOMAIN          136..657
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          508..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        412
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         348..349
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         412..418
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   765 AA;  85705 MW;  D586709A361E5ECB CRC64;
     MEKIRIPKVE GVQALSNGGQ QFKGTLHLTN HHLIYSCKRI NLKEGNPLAQ KTSEFWITYH
     IISRCTFRPT APGSAIPSNI RIRGRDFSSI TFNFDDPVQA KDVFESIRGL TCRLKRINKL
     YAYRYKGNPK EDPIKGWEIY DAKAEWKRQG ISEKGIDQGW RISTINSDYA FSPTYPALLV
     VPTSISDNVL NYAAKFRSKA RIPALTYLHP VNNCSITRSA QPGVGIRSAR SVQDEKLVGA
     CFSASDNISA CSTPDKRSSP TASQLDIVEI SPEDANMAET DIEKLEDIMI ATADDDGEQP
     RIYGAQRRNL IVDARPTVNA LAQHAAGFGS ENMDNYKFAA KAYLGIDNIH VMRNSLRKVV
     EALKDGDLTP LPPNRDLLAK SNWLKHIANI LDGSALIARQ VGIHHSHVLI HCSDGWDRTS
     QLSALSQIML DPYYRTLDGF IVLIEKDWLA FGHMFQHRNG YLNSEKWFTT EYDGLAGSSV
     QPGLNDAPRN ETIENALAKT KRFFTKRTPT DEVDSDGEPI YEETPGLFRA PAKGTPEEEE
     ATKENETSPV FHQFLDAVYQ LIRQHPKRFE FNQHFLRRLL YHTYSCQYGT FLHNNEKARL
     DAQVSKLTRS VWDYILADRA KFLNPDWDGG EIDDHVRGKE RLLFPRLEEV KWWFELFGKT
     DEEMNGPSIP PVEQFHQKSA SRDASTGVLT EVETANSDVV SGDLKPDTAV NASPRQLNSG
     NAVGLSGLRS TLSNLSIGGI AQSQGGLGSR TPASRNAEES EVEMQ
//