ID   A0A397G1B8_9EURO        Unreviewed;      1196 AA.
AC   A0A397G1B8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Inositol polyphosphate-related phosphatase domain-containing protein {ECO:0000259|SMART:SM00128};
GN   ORFNames=CDV56_100394 {ECO:0000313|EMBL:RHZ43096.1};
OS   Aspergillus thermomutatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ43096.1, ECO:0000313|Proteomes:UP000215305};
RN   [1] {ECO:0000313|EMBL:RHZ43096.1, ECO:0000313|Proteomes:UP000215305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ43096.1,
RC   ECO:0000313|Proteomes:UP000215305};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT   (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT   aspirate.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RHZ43096.1}.
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DR   EMBL; NKHU02000525; RHZ43096.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397G1B8; -.
DR   STRING; 41047.A0A397G1B8; -.
DR   VEuPathDB; FungiDB:CDV56_100394; -.
DR   OrthoDB; 996872at2759; -.
DR   Proteomes; UP000215305; Unassembled WGS sequence.
DR   GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProt.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR046985; IP5.
DR   InterPro; IPR000300; IPPc.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR   PANTHER; PTHR11200:SF240; INOSITOL POLYPHOSPHATE 5-PHOSPHATASE C9G1.10C-RELATED; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000215305}.
FT   DOMAIN          806..1144
FT                   /note="Inositol polyphosphate-related phosphatase"
FT                   /evidence="ECO:0000259|SMART:SM00128"
FT   REGION          1..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1196 AA;  133151 MW;  C485C9FCDD0B851D CRC64;
     MEGSGKDKDG TDNAPIRPVS SLLSHFENLS HRRSPSAFTT TSPHDSSPFL RTPEPVDEVR
     SARASLDLPR PQSPWTVTAN SQNGQRYDRA NGGFSRHGGS PGSPGRRHSR PMSMNFHSSP
     QLAPTLTVDS PRSPPRGFAS QDHTEHSVDS RMSRSPPDPS RGSLPPPTNR PTTPNFSTSQ
     QRLGHLSPAH SHSGSFIGES PPDRKQKSAS LPPPVHRAEK PKVPAKPAAL TSHDSATLAP
     QPEGTTSEDR ISPFSTPPSS PEKSSLKPSS TGRPQIPRSP SRPVTEPPSR QSFDDRNPVP
     SAHALRDARE LGFSRRRPIP EPTRDMKPLM VQIPPHPLKQ TEALSAVPLS ARRLQVTDTP
     TEPPSLPPRH SSLARKGGVS PSRPSLHLDS PLHPEPSPRP QSIQFPPRES HTPTQIHRQP
     SFSRDAKPGQ ATSVPERQSA RADACGEDPV DEPTISRTDY PDASSTNRRP PLLRNGPREI
     HTRYDTRLMD VCGKHVCTTG YITRVWDLTN GEQIMSLSHG ETVKSLSIAF KPGTGLEDEG
     QRLWLGMSTG EIHEVDISTR SIIATRSYPS RREVVKILRH KKEMWTLDDE GRLLVWPPDE
     SGTPNLQYSY HNPYDRVARG HTCSLVVGDT LWLATGKEVH VYRPNAPDDI SFKVLKKPLG
     SQHSGDVTSG TYTTRDGGRV YLGHADGKVT VYSSTDYTCL AVVNVSVYKI NCLGVVGDYL
     WAAYKTGMIY VYDTRTNPWM VKKDWRAHDG PVSSFLLDSS SVWTMNRLQV TSLGDDNCIR
     LWDGMLEDDW LETCMQSKDV EFCKFREISA AIVTWNAGAS TPGSVRSSNF IQEAIHPENP
     PEILVFGFQE LVDLENKKIT AKSLLLGSKK KESGEKEHMS RQYRVWMEHL TRCINDCMPL
     EESYVLLHSA NLIGLFTCVF VKHKERQRIK NISAAEVKRG MGGLHGNKGA LILRFILDDS
     SFCFVNCHLA AGQSQTAHRN NDIAAILESE CLPIESSLTT RANHFVSGGD GSMIMDHEIC
     ILNGDLNYRI DSIPRNVIIE DIRNNNLAKL LERDQLLASR RKNPGFRLRS FTEAPITFAP
     TYKYDVGTDE YDSSEKKRSP AWCDRVLYRG LGRIKQLEYR RHEVRASDHR PVSASFKLRV
     KTVLPQERAT VWEACQQEFQ KEKRRLASEA SIEYLISVLG TDPQQARALI LGTGTQ
//