ID U7Q4J5_SPOS1 Unreviewed; 991 AA.
AC U7Q4J5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51339};
GN ORFNames=HMPREF1624_02888 {ECO:0000313|EMBL:ERT01636.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERT01636.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(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; KI440843; ERT01636.1; -; Genomic_DNA.
DR AlphaFoldDB; U7Q4J5; -.
DR STRING; 1391915.U7Q4J5; -.
DR eggNOG; KOG1089; Eukaryota.
DR HOGENOM; CLU_001839_5_1_1; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000018087; 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:UP000018087}.
FT DOMAIN 176..725
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 43..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 478
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 414..415
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 478..484
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 991 AA; 106806 MW; 7968F593E5E49BFA CRC64;
MDPKLTIENV SVLSAGTSTR GTLKLTNFHI VFCAPIPTPP LARAASSTAS SAATPPPPPP
KDSPTHTSND SSTPSDSSKQ KPQPPTTAPA RQRESWITYP IIAHCTFRPT PSSSGVPSSI
RIRCRDFNIV CFSFTDEKQA REVFEFIRSR TCRLGSIEKL YAFSYAPARQ EKDLCGWDVY
DARAEFRRQG INEKLPDRGW RISHINKDYT FSPTYPSLLV VPSKISDNVL KYAGQFRSRA
RIPALTYYHP ITQCSITRSS QPLVGVRNNR SIQDERLVSA CFYKSTAVFS GDATHSNSNI
RNNGSNTATS DSSTPSGESG SGSGDTMIVT YDGVAEAVTI VDKMGGSGGD DSATEADDGS
DDNPASRVFG ARRDNLIVDA RPAINSLAMQ VVGKGSENMD HYKSATKMFL SIDNIHVMRE
SLNKVIEAVK DADISPLPPS QDLLAKSGWL KHIRGILTGS QTIARQVGVS AAHVLIHCSD
GWDRTSQLSG LAQIMLDPYF RTIDGFIVLV EKDWLSFGHM FQQRSGHLNS EKWFVTQNDA
MAGTKIEPGE SDGRNEVFDN AVASARRFFK KSLSQDKEES DGDGAAEDAG SRSAPVEESQ
ATRPREISPV FHQFLDATYQ LLRQYPTRFE FNERFLRRLL YHLYSCQYGT FLYNNERQRL
EAKVRERTSS VWDYFLSRRA EFTNPQYDAS AMAAATNGSN EGNGRQDDRL LFPKLDEIRW
WHQAFNRTDQ DMNSALNAAA AAAVERHVNY HATMTATAAA PATVIVTPGD DDPAAPSGLT
ARSARSSRSV SPRRGASPAS PPSFQTSQSA GAELATTATT ATTTATTINV PNAATARALL
ASPVDDNVDS IPSFQRSGSS TNEPSAFAAL RDGFAGLGLG QKVGGVLGTL SAVGSSIGSG
NGNGSTTGNA TNTVHESSGS VSGTRSGTPA SNINGRESLF GLADADGDKD NATSSGGSGS
GGVFDSFVGG SGSRRSRQMN RSSGEQELRD M
//
