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Database: UniProt
Entry: A0A0D2GKM9_9EURO
LinkDB: A0A0D2GKM9_9EURO
Original site: A0A0D2GKM9_9EURO 
ID   A0A0D2GKM9_9EURO        Unreviewed;       973 AA.
AC   A0A0D2GKM9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51339};
GN   ORFNames=Z517_08880 {ECO:0000313|EMBL:KIW79040.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW79040.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW79040.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW79040.1,
RC   ECO:0000313|Proteomes:UP000053029};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; KN846973; KIW79040.1; -; Genomic_DNA.
DR   RefSeq; XP_013282848.1; XM_013427394.1.
DR   AlphaFoldDB; A0A0D2GKM9; -.
DR   STRING; 1442368.A0A0D2GKM9; -.
DR   GeneID; 25308370; -.
DR   VEuPathDB; FungiDB:Z517_08880; -.
DR   HOGENOM; CLU_001839_5_1_1; -.
DR   OrthoDB; 5474662at2759; -.
DR   Proteomes; UP000053029; 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:SF128; PHOSPHATIDYLINOSITOL-3,5-BISPHOSPHATE 3-PHOSPHATASE; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   Pfam; PF21098; PH-GRAM_MTMR6-like; 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:UP000053029}.
FT   DOMAIN          137..680
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          250..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          748..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          948..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..820
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..848
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        903..935
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        424
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         360..361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         424..430
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   973 AA;  109245 MW;  7000BC3A6F2EF0B8 CRC64;
     MAMERTRIAK VDDVTLSRRG IQVNGTLHLT PHHLIFVHAA PPAADGKPTR PRENWITYPI
     IQFCTFRPSP TASRQPSSIR LRCRDFTFYC FYFNDDRKAR DVYDSVKAWT CKLSGIEKLY
     AFSYHPTGPE KDVGGKGWAL YDPMREWRRM GLGDESRKTN WRISTINKDY SFSPTYPAVL
     AVPATISDNT LNYAGRYRSR ARIPVLTYLH PVNDCTITRS SQPLVGVRGN RSIQDEKLVA
     AIFNTTRAER PLSAYNSPPP EREDSGSSKE STCAVVLDSE ISQADAEAVE DAIIARFRGD
     DDAQDGAEDR RPLVYGAQQR NMIVDARPTI NALVMQTQGM GSEDMSNYKF ATKAYLGIDN
     IHVMRDSLQK VIDAFKDSDL TPLGPNQELL QKSNWLKHIG LILDGSGLIA RQVGLQHSHV
     LIHCSDGWDR TSQLSSLSQI CLDPYYRTME GFMVLVEKDW LSFGHMFKHR SGFLSSEKWF
     QIENERISRG SEDVDGKEEK SGAMATFENA FLTAKGFFSN TKNNESRESI NVDSDADTPN
     NYDSESQPGR RIVSGAAKKE KEKPVTRVKE TSPVFHQFLD ATYQLLYQYP TRFEFTERFL
     RRLLFHLYSC QYGTFLGDNE RERKEARLSD RTRSVWDYFL ARKQEFLNPK YDPVIDDNIR
     GKERLIFPRP DEVRWWNELF GRTDDEMNAK PQPSIKTQTN GAIEGGGAEL WTSVSDAGGS
     QLDYSSSASA PTSRARTPVL VGLETSEASI GLTTSPPPKL HSKVHEPVAD RSKVPVVSGS
     VLSPSRTASR TASPMPRESF SRSRTPIPTA SSTKQELEGI QGQPNEPIMK KDRDDDVKTS
     DRLRAVKDDS AASNILSTSD QSTVMIHHFP HGQQAQAAPL PASPSLSPLI KPQPGQGSRP
     QIEEPQRQDD SSAVSREAEK DNSTGEIKEP VETLVDDLDP LGIGEAKDIP MAQQSLSMSM
     RAKRREQMEL LMK
//
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