ID   A0A3R7F801_9EURO        Unreviewed;      1197 AA.
AC   A0A3R7F801;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Inositol polyphosphate-related phosphatase domain-containing protein {ECO:0000259|SMART:SM00128};
GN   ORFNames=CFD26_104725 {ECO:0000313|EMBL:RLL97592.1};
OS   Aspergillus turcosus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL97592.1, ECO:0000313|Proteomes:UP000215289};
RN   [1] {ECO:0000313|EMBL:RLL97592.1, ECO:0000313|Proteomes:UP000215289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL97592.1};
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 sequences of two Aspergillus turcosus clinical strains
RT   isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT   other azole-resistant.";
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:RLL97592.1}.
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DR   EMBL; NIDN02000073; RLL97592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R7F801; -.
DR   STRING; 1245748.A0A3R7F801; -.
DR   Proteomes; UP000215289; 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   PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR   PANTHER; PTHR11200:SF240; INOSITOL POLYPHOSPHATE 5-PHOSPHATASE C9G1.10C-RELATED; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000215289}.
FT   DOMAIN          807..1145
FT                   /note="Inositol polyphosphate-related phosphatase"
FT                   /evidence="ECO:0000259|SMART:SM00128"
FT   REGION          34..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..285
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1197 AA;  133523 MW;  951B1127B50A1FDF CRC64;
     MEGSGKDKDG TDNAPIRPVS SLLSHFENLS HRRLPSAFTT TSPHDSTPFL RTPEPVDEVR
     SARASLDLPR SQSPWNATAK SQNGQRYDRA NGGFSRRNGS PGRSPGRRQS RPMSMNFHSS
     PQLAPTLTVN SPRSPPRGFG SQDRAEHTVD SRISRSPPDL SRGSLPPPTN RPTTPNTSTS
     QQRPGHLSPA HSHSGGFIGE SPPDRKQKSS SLPPPFDRAE KPKVPAKPAA LASHESGTLA
     PRPERAVSED RVSPFSTPPS SPEKPSVKPS PSGRPQLPRS PSRPMTEPPS RQSFDDRTPV
     PSVQALRDAR ELGFSRRRPI PEPTRDMKPL MVQVPPYPLK QTEPLSAVPS SARRLQATDT
     PTEPPSLPPR HSSLARRGGA SPSRPSLHLD SPSHPEPSPR PQSFQLPPRE IQTPTQIHRQ
     PSFSRDAKPG QAHSGPERQL ARADTFGEDP VEEPQISRTD YPDASTTNRR PPLLKNGLRE
     IHTRYDTRLM DVCGKHVCTT GYITRVWDLT NGEQIMSLSH GETVKSLSIA FKPGTGLEDE
     GQRLWLGMST GEIHEVDIST RSIVATRSYP SRREVIKILR HKKEMWTLDD EGRLLVWPPD
     ESGTPNLQYS YHSPYDRVAR GHTFSLVVGD TLWLATGKEV HVYRPHARED VSFKVLKKPL
     GSQHTGDVTS GTYTTRDGGR VYLGHADGKV TVYSSTDYAC LAVVNVSVYK ISCLGVVGDY
     LWAAYKTGMI YVYDTSTNPW MVKKDWRAHD GPVSSFLLDS SSVWTMNRLQ VTSLGDDNCI
     RLWDGMLEDD WLETRMQSRD VEFCKFREIS AVIVTWNAGA STPGSVRSSN FIQEAIHPEN
     PPEILVFGFQ ELVDLENKKI TAKSLLLGSK KKESGEKEHM SRQYRVWMEH LTRCINDCMP
     LEESYVLLHS ANLIGLFTCV FVKHKERQRI TNIGAAEVKR GMGGLHGNKG ALILRFILDD
     SSFCFVNCHL AAGQSQTAHR NNDIAAILES EVLPMESSLT TRANHFVSGG DGTMIMDHEI
     CILNGDLNYR IDSIPRNVII EDIRNNNLAK LLERDQLLAS KRKNPGFRLR SFTEAPITFA
     PTYKYDVGTD EYDSSEKKRS PAWCDRVLYR GLGRIKQLEY RRHEVRASDH RPVSASFKLR
     VKTVLPQERA AVWEACQQEF QKEKRRLASE ASIEYLISVL GTDPQQARAL ILGPGSQ
//