ID N4UWH7_FUSC1 Unreviewed; 774 AA.
AC N4UWH7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Phosphoinositide 3-phosphatase {ECO:0000313|EMBL:ENH73106.1};
GN ORFNames=FOC1_g10008602 {ECO:0000313|EMBL:ENH73106.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH73106.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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; KB730086; ENH73106.1; -; Genomic_DNA.
DR AlphaFoldDB; N4UWH7; -.
DR STRING; 1229664.N4UWH7; -.
DR VEuPathDB; FungiDB:FOC1_g10008602; -.
DR HOGENOM; CLU_001839_5_1_1; -.
DR OMA; RTMEGFM; -.
DR Proteomes; UP000016928; 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:UP000016928}.
FT DOMAIN 136..640
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 249..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 409
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 345..346
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 409..415
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 774 AA; 87087 MW; B00A75CDA511789A CRC64;
MEARKIIESV QGIYGGQTTH GTLRLTDFHL VFCAPIDQSA KPLESSSHKP KVRERWIPYP
MLCYCALRPV PPGSRQAPSI RLRCRDFTFV TFNFTDSEIA REAFDFIKSR TCKLGTVEKL
YAFSHKPLKH EREVGGWSVY DPKAEFRRQG ISEKLPDKGW RITHINKDYT FCDTYPAFLV
VPSKISDNVL KYAKEFRSRN RVPALSYIHP VNNCTITRSS QPLSGITRKT NVQDEKLVAA
SFNALLPPGS EESTPLSSQP DVSLGNSSLE TELSETERYE DELISRSVAV YDSSGKRQVY
GAQQSNLIVD ARPTINAMVN QVQGMGSENM DKYKFARKIF LSIENIHVMR SSLNKVIDAL
KDADISPLPP NRELLHQSGW LRHIHDVLDG SAIIARQIGI NHSHVLIHCS DGWDRTSQLS
ALAQIMLDPY YRTIEGFIVL VEKDWLSFGH MFRLRSGHLN HEDWFTVQKD AFAGSKVQPG
ENDGRGDAFQ NVLSGAKRFF NQNKDDPDLA AVSETAPGKV VDDEATSPKM VSPVFHQFLD
CTYQLLRQNK TRFEYNERFL RRLLYHLYSC QYGTFLFNSE KQRKDARAAE RTSSVWDYFL
CRRAEFTNPD FDASIDDHVK GQERILLPRL KEIRWWHQVF GRTEDEMNGG LNAAAAAETD
RQTAISNLQY PSVIQADADP RSSTSSSKSG PPSVLTGVET AHETLTPESR HTPIERSAST
EPSGNAFAAI RDGIAGLNLG KGMLGQFTNT GESASSSSSA PVPARSDQEL REMI
//