ID   A0A3B6SCU8_WHEAT        Unreviewed;       798 AA.
AC   A0A3B6SCU8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51339};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS7B02G175000.2};
RN   [1] {ECO:0000313|EnsemblPlants:TraesCS7B02G175000.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS7B02G175000.2};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS7B02G175000.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) 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; A0A3B6SCU8; -.
DR   EnsemblPlants; TraesCS7B02G175000.2; TraesCS7B02G175000.2; TraesCS7B02G175000.
DR   Gramene; TraesCS7B02G175000.2; TraesCS7B02G175000.2; TraesCS7B02G175000.
DR   Gramene; TraesCS7B03G0469100.2; TraesCS7B03G0469100.2.CDS; TraesCS7B03G0469100.
DR   Proteomes; UP000019116; Chromosome 7B.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14507; PTP-MTM-like; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000019116}.
FT   DOMAIN          139..605
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          466..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..644
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        395
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         280..283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         305..306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         395..401
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   798 AA;  89548 MW;  93AF22011730DF67 CRC64;
     MEASGSWDAI DWNQIEDPRS RRSSQGMEEF LLEDEEVYAQ GHGVVLLNTD EAGIVSVTNF
     RLLFVDVKLQ SVPRQYDKKQ PRELLQVIGK DMRVIVFAFR PRTKQKNEVF DALRRYAKPS
     QLWELYAFSC DPSTVDKKSD PKMRLMKEYH RLLSEGSEFE VEKYYFRNNW RLTTVNSSYS
     LCSTYPSQLI VPKSISDEDL WQASTFRAGR RLPIISWCNP VSGAVLARSS QPLVGLMMNF
     RNNADEKLVS ALCIQNVDAN LPPRKLYIVD ARPRANALAN GAKGGGSESS SNYPKSEVLF
     LGIQNIHTMR DSLSRLRDYV DAHGSISSNG SSSAVSLVGD RRNRGSTWGG GSLNSMTQFS
     SMLGEWLNHI QNILVGASWI AAQIAQESAS VLVHCSDGWD RTTQLIALAC LLLDPYYRTF
     DGFQALVEKD WLAFGHPFAE RLGIPTVSEN GGSQYELLRQ PSVGNLTSSP SRGSLGTPGS
     SSNTSVQSQT SNNSSPILLQ WLDCIAQLLR LYPAAFQFSS KFLVDFMDCV LSCRFGNFLC
     NSEREREQSG VTSSCHCMWT YLADLRASGG SFHEHINPFY DRERYWLPLV PPAAALAPTL
     WPQFYLRWTC PPESQGGGLE SHGHSMRKKY EASVKSKEMA ESRSRDIKMK MESMLTDLQR
     ERRASSSALA MAQRARRENV AIKRAIQTIG CTVNFSTNEN QVDKPEEMSY SFRREADTVS
     QQDDNADMSV SISAIEDSLV SETPSNQVCE SLCPFRSREG CRWPHAACAQ LGSQFVGLKA
     NFDAFDRLSV KDCYFPKE
//