ID A0A1E3PKZ6_9ASCO Unreviewed; 814 AA.
AC A0A1E3PKZ6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Phosphatases II {ECO:0000313|EMBL:ODQ66103.1};
GN ORFNames=NADFUDRAFT_51371 {ECO:0000313|EMBL:ODQ66103.1};
OS Nadsonia fulvescens var. elongata DSM 6958.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Nadsonia.
OX NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ66103.1, ECO:0000313|Proteomes:UP000095009};
RN [1] {ECO:0000313|EMBL:ODQ66103.1, ECO:0000313|Proteomes:UP000095009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ66103.1,
RC ECO:0000313|Proteomes:UP000095009};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(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; KV454409; ODQ66103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3PKZ6; -.
DR STRING; 857566.A0A1E3PKZ6; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000095009; 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 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:UP000095009}.
FT DOMAIN 186..615
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 626..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 411
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 347..348
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 411..417
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 814 AA; 92677 MW; B8A2421F1412FF73 CRC64;
MEYIKVANVP DVLLFRHGSS AKATLHLTTH HMILTIDKGV NENPNLPNRE VWICYPMLQN
VTLHVSLANI PYNESINAMI SAPKNQITDV KEDLTLASNE DMTGIIEGHS TKALFYPNLN
QIDVSNSPAV MRIRCRDFTM MGLCFQDHRI ARDVYDSIMK LTCVPNIDRL YGFMFTPSKQ
ELMFNGWKIY DKKREWERMG LNFFKDSSWR ITNLNTDYKL CPSYPSYIVV PSAISDTVII
HAAKFRSKAR LPALSYFHGF NSCTITRCAQ PLVGLKQNRS AQDEKLVYSI FISSQPTQEG
VRGSTQDNLI VDARPTANAV AQTALGAGSE NIDNYKGSRK IYLGIDNIHV MRDSLGRVIE
ALKDTDITSN PVNRELLVKS NWLKHINIVL EGAIQTSDTI HFNFSHVLIH CSDGWDRTSQ
ISSLAQVFLD PYYRTMEGFA VLVEKEWLSF GHRFFERCGH LSSEKQFNFN RYEGGSGSIN
TVSSQASQVF SSVSSKLVKQ SHVKYTSPVF HQFLDCMYQC VRQFPERFEY NERFLRRLLY
HTYSCQYGTF LFNSEKERKE YNIENKSASV WGYFLARRSM FTHSKYDKAK ELNYNEKDRY
LVPNTADTKW WFECFGRSDE EMNGSLKIPD LLEKKTKPAE EDIERKHHSR PRSSRDHFEP
TSNQVPTFVN PVSTLHLTSS PDVSTFSPIG SVSSSISSLP ILLPLEGKDM KLRLDDEKSP
NLSGAQNGEV TSKLPSEPKL SEPESLINSL SLSSSEFPST GFSRTAYPKS FINNQNIESH
GKPLISVSNQ DSQTVEERVR ANLKSNSPII ESIK
//
