ID A0A1M2V7G4_TRAPU Unreviewed; 967 AA.
AC A0A1M2V7G4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Phosphoinositide 3-phosphatase {ECO:0000313|EMBL:OJT03524.1};
GN ORFNames=TRAPUB_5803 {ECO:0000313|EMBL:OJT03524.1};
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT03524.1, ECO:0000313|Proteomes:UP000184267};
RN [1] {ECO:0000313|EMBL:OJT03524.1, ECO:0000313|Proteomes:UP000184267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC735 {ECO:0000313|EMBL:OJT03524.1,
RC ECO:0000313|Proteomes:UP000184267};
RA Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA Hilden K.;
RT "Genome sequence of the basidiomycete white-rot fungus Trametes
RT pubescens.";
RL Submitted (OCT-2016) 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:OJT03524.1}.
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DR EMBL; MNAD01001609; OJT03524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M2V7G4; -.
DR STRING; 154538.A0A1M2V7G4; -.
DR OMA; DPFYRTQ; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000184267; 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 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:UP000184267}.
FT DOMAIN 139..591
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 613..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 382
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 279..282
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 382..388
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 967 AA; 105438 MW; D655C92B4C5B7CBF CRC64;
MDALRVTKVC RRNLSTLQSV DRSLQVEGVL CTKGGSTSSG TLHLTAHHAI FHYDEEGREE
MWVPYPLISL VSRMPMTLQG QAPLTIHTRT FETTFLSFVT EKEAIDVFES VKELTVATSV
TQLYAFYYVP NPPFPVSNGW SIYSPREEFL RMGVGTRSKA WRFTDINKDY SLSPTYPARL
VVPTRISDTT IQYAAKFRSK CRIPVLTYLH WANYGSITRS SQPMVGLTNN RSIQDEKLIE
SIFQTHHNPE SRVSAGPVYG ATATNLIIDA RPTTNAMANT AKGAGTENMD HYKDAKKAYL
GIDHIHTMRE ALARVVEALR GTEVMLAATT PADDEPPSVA PVLDRQALRR SGWLRHIGAI
LEGTLLCVRN VHVNSSHVLI HCSDGWDRTA QLSSLTQLCL DPFYRTQRGF EILIEKDWVS
FGHKFLDRCG HLSSEKFFLA PVENSGGGGG AEAAQAFLAS VQNRFASQNH IKETSPVFHQ
FLESVRQIQR QFPERFEFNE RFLRQLHYHL YSCQFGTFLF NSERERRVGE SGPPPCDRTV
SVWDFFNSPP EVELNKNPLY DPSLDDVTRP KADMGVLMPN PKDVRFWHEL YGRTDEEMNG
RFVVKQAVEE SELSAPIDSA ESDPALPLNP EASVTGLPAP TPTGPQMALP SAQSIARFLQ
RGASPASQST PFGESPATPE AQRARTPSLR PYDTPSTSPG VLSSDPITPP RTPSPRMRTV
RTTSPRATTS SQAGAELFSS GGVRSFWGKF STNATAAFSV VQDAYGGLAK DLRGLSVGEG
GDPVRGGELK SREEIDAWGA NGDDSRASSP RGGPSSPRAH TVSSGSTLNP WLTGQARPTI
PSMYLDNPWS SVRASESEPR PTIPASLYAE LETQQSSLPL DPTVELPPSF PHSRGTTSGS
TPLGGARPPS IRANSDKATG LAGVGANSGG PLGQNDGLST HATPAAPAEP SADSSASSDP
LGVAVWS
//
