ID A0A2B7Z7S7_9EURO Unreviewed; 768 AA.
AC A0A2B7Z7S7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51339};
GN ORFNames=GX50_04754 {ECO:0000313|EMBL:PGH32454.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH32454.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH32454.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH32454.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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:PGH32454.1}.
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DR EMBL; PDND01000092; PGH32454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7Z7S7; -.
DR STRING; 73230.A0A2B7Z7S7; -.
DR VEuPathDB; FungiDB:EMCG_09477; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000226031; 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 CDD; cd17666; PTP-MTM-like_fungal; 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:UP000226031}.
FT DOMAIN 141..670
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 254..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
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 768 AA; 86007 MW; BA7EC84F3C55A8B7 CRC64;
MERTRIAKVD NVTLSRRGEQ VLGTLHLTPH HLIFSHTPPA TATTTDQPQG DNVVPKPREL
WITYPIISFC TFRPAPVSSR QPSSIRLRCR DFTFVCFYFP NESRARDAYE SIKSWTCRLG
RIEKLYAFTY QPPPPERGLN GWNIYDPREE WLRLGVGKPD TNCGWRISTI NQDYSFSPTY
PALLPVPLAM SDNTINYAGR YRSRARIPVL TYLHPVNNCS ITRSSQPLVG VRGKRSIQDE
KLLAAIFSTS RQERPLASYT PPSSLEAESL NSSQEEQPSA PADFELSNAE ELEDEVISAA
REEGTASQPQ IYGAQQHNLI VDARPTVNAF AMQAVGLGSE NMDNYKFATK AYLGIDNIHV
MRDSLNRVID ALKESDVTPL GPNRDQLARS GWLKHITGIL DGAALIARQV GLQHSHVLIH
CSDGWDRTAQ LSALSQLCLD PYYRTMEGFM VLVEKDWLSF GHMFRHRSGF LNSEKWFQVE
NDRMGGDANR TGFGDAGGAG KALENALLSA KGFFNRDNTS RDSLGESDGE VQALDADNSK
KPAARISTPA NGVEVTKVKE TSPVFHQFLD ATYQLLYQHP TRFEFNERFL RRLLYHLYSC
QYGTFLFNSE KERLDAKAKE KTRSVWDYFL ARREQFTNQQ YDPVIDDNKR GRERLLFPRP
GEVRWWSEAF GRSDAEMNTP RSGGVSLDKD YPSGSRTPVL TGVETSERSF GSSTSTQSAP
SNTTSTPSAG MAALAAGLSG LGLPTGRESS QGKRTEAVGN KEMEVEMQ
//
