ID A0A2T3B1H0_AMORE Unreviewed; 761 AA.
AC A0A2T3B1H0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51339};
GN ORFNames=M430DRAFT_27864 {ECO:0000313|EMBL:PSS18406.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS18406.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS18406.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS18406.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(2018).
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; KZ679011; PSS18406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3B1H0; -.
DR STRING; 857342.A0A2T3B1H0; -.
DR InParanoid; A0A2T3B1H0; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000241818; 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:UP000241818}.
FT DOMAIN 143..670
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 259..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 421
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 357..358
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 421..427
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 761 AA; 84608 MW; E31B98D659D64264 CRC64;
MADKLRITKV EDVQVLSRGE ISVVTLHLTP HHLVLVQTLG PPSARQAPSP NHRPTPVRTR
ESWIAYPMIA FCTFRPTPPG SALSSSIRLR CRDFKFLTLN FGDDRQARDV FESIKGATCR
LGSIEKLYAF SYKPQPPEKR ISGWEIYDAK AEWKRQGISD KGVDRGWRIS KINIDYSFSP
TYPALLAVPS TISDNTLNYA GRYRSRVRIP VLTYLHPVNN CSITRSSQPL AGLRGNRSIQ
DEKLVSACFS ACATVDDGDT ATSSTSRSSP ASSQADLGPS SADGELSEAE RLEDEMISSS
TLEVVSEKPH VYGAQQHNLI VDARPTVNAL AMQAVGLGSE NMDHYKFATK AYLGIDNIHV
MRESLAKVIE AIKDSDVSNL PPNRELLAKS GWLKHIAGLL DGAALIARQV GIQHSNVLIH
CSDGWDRTSQ LSALAQLLLD PYYRTIEGFI VLVEKDWLAF GHMFQHRSGF LNSEKWFSVQ
NDALAGSAIQ PGGNGDGRGD AIENALLSAK RFFNKSNHSQ DNIADPDGEL LPFDDSPKGK
KTSISKDSSA DSEATKPKET SPVFHQFLDA TYQLLRQFPT RFEFNERFLR RLLYHLYSCQ
YGTFLYNNEK SRKDARVQER TVSVWAYFLS NKEGFTNNDY DGGVIDDHVK GKERLIFPNL
DKVRWWHEVF NRTDEEMNGP TNTVTERYLG NHTPRSGSPH SVLTGVETSG TATTTRQVSN
GNTGGFASLR EGMAGLGFGG KGIQGNKRSR DTKKEMEVEM Q
//
