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
//