ID A0A165TEX0_9AGAM Unreviewed; 904 AA.
AC A0A165TEX0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Phosphatases II {ECO:0000313|EMBL:KZT26565.1};
GN ORFNames=NEOLEDRAFT_1132087 {ECO:0000313|EMBL:KZT26565.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT26565.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT26565.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT26565.1,
RC ECO:0000313|Proteomes:UP000076761};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV425566; KZT26565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165TEX0; -.
DR STRING; 1314782.A0A165TEX0; -.
DR InParanoid; A0A165TEX0; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000076761; 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:UP000076761}.
FT DOMAIN 121..569
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 604..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..697
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 358
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 261..264
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 358..364
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 904 AA; 98801 MW; 7F236D141C46F97D CRC64;
MDAIRVTKVE NVLCSKGGKT GLGTLHLTAH HLIFHYQDGE KEMWVPYPLI SLVTRLPQTL
QGQCPITVRC RTFEMFSLVF AQESVAIDVF ESVKELTVIT SVQQLYAFFY TPNPPFPTST
GWSLYSPREE FGRMGVGVRT KAWRFTDLNK DYTFCPTYPA RLVVPTKISD TTLQYAGKYR
SKARIPTLTY LHWANFGTIT RSSQPMVGLT QSRSVQDEKL VEATFQSHWA PDARAVSGPI
YGATSTNLIV DARPTTNAMA NTAKGAGSEN MDHYKDARKA YLGIDHIHVM RDSLGRVVEA
LREADAVAVG GDPPGEAILD RGALRRSGWL RHISAIMEGT VLIVRNVHVN SSHVLIHCSD
GWDRTSQLSA LAQLCLDPFY RTMRGFMVLV EKDWVSFGHK FLDRCGHLSS EKFFVAPAEN
AAAGGSAEAA QAFFASVQKR FASQADIKET SPVFHQFLES VRQVQRQFPE RFEFNERFLR
QLHYHLYACQ FGTFLFNTER ERRVGDGGPP PCERTVSVWD FFNSPDEREK NLNPDYDPSL
DDPTSRLSKA DMGVLFPNPR DVRFWYQLYS RTDEEMNGRV ITSQARGVEM LGPIEGVDED
PTIITSSAAS TPPSPAGTPV ALPSSPQPSG SSASLISQPP PQVTASSGLS SSLPELSQMT
LNDTSANSGS SSEFSLRTPS GPQRTPSPAP GRGPSSPRRP PDWAGGVKSI WGKLSSNAST
AFSAVQGAYD GVARDLSKSL AASTDDGESG VNAGELKSRD QLSSAWGEDS SSATSRAQPS
YTVSSSNPWE TMRERPTIPS LFLDNPWNTA RAPLPSHAPL LNEIPFAGTS SLPHDPTVSY
PKPIAPVRSS TLGRPRDVIS PAPVIQLSSG SHSPSGATQV KNSQPTSVSD RPSENVDPLG
VGFM
//
