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Database: UniProt
Entry: A0A0E0QMA2_ORYRU
LinkDB: A0A0E0QMA2_ORYRU
Original site: A0A0E0QMA2_ORYRU 
ID   A0A0E0QMA2_ORYRU        Unreviewed;       748 AA.
AC   A0A0E0QMA2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51339};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI08G25820.2, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI08G25820.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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   AlphaFoldDB; A0A0E0QMA2; -.
DR   EnsemblPlants; ORUFI08G25820.2; ORUFI08G25820.2; ORUFI08G25820.
DR   Gramene; ORUFI08G25820.2; ORUFI08G25820.2; ORUFI08G25820.
DR   Proteomes; UP000008022; 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; 2.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008022}.
FT   DOMAIN          163..555
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          587..614
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        297..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        363
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         292..295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         363..369
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   748 AA;  84047 MW;  C721446AE4457974 CRC64;
     MDGSGSWDAI DWNQIKEPRP PRSSSRGMED FLLEDEEVYA QGHGVVLLNT DEAGILSVTN
     FRLLFVSQAT KGVIELGTIP LTAIEKINDD VKLQPLPRQH DKKQPRELLQ VIGKDMRVIV
     FDFLPKTKQK NEVFDALRRY SKPTHLWDLY AFSCDPSTVY QKSDPKMRLL KEYHRLFRKW
     FPHSGSEFEK DLRNEWWRVS KVNSTYSLCS TYPSALIVPR SIRFIASFFF PIRQTLACYF
     VGLELFWQGH LSHCNTDEKL VSALCTQIID ATGSLRKLYI VDARPRANAL ANGAKGGGSE
     SASNYPRSER NRGSTWGGGN LNSMTQFSSM LGEWLNHIQS IMVGASWIAA QIVQESASVL
     VHCSDGWDRT TQLVALACLL LDPYYRTFNG FQALVEKDWL AFGHPFAERM GVPTITDNNS
     GSQFELLRQP SLGTLSNSPN RGALGSSVST SNTTSGQSQT SNNSSPILLQ KFLVDFMDCV
     LSCRFGNFLC NSEREREQSG AVSSCHCMWT YLADLRASGG SFHKHRNPFY DPLKHNGPLV
     PPAAALAPTL WPQFYLRWTC PIESQGGDLE SQWHAMNKKY TEAMKAKDTA ESRVKDIKTK
     MESMQLELQR EKRASSSALA MAQRAQRESV AIRKAVRSLG CTVNFGTNES QVEKTEGLTY
     SFRRDTDFES QHEKSSDFSV SITAIEDSLV SETPSNHICE SLCPFRTREG CRWPDAACAQ
     LGSQFVGLKA NFDAFDRLSV QDSYFGSE
//
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