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Database: UniProt
Entry: A0A100ISZ4_ASPNG
LinkDB: A0A100ISZ4_ASPNG
Original site: A0A100ISZ4_ASPNG 
ID   A0A100ISZ4_ASPNG        Unreviewed;      1090 AA.
AC   A0A100ISZ4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE            EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN   ORFNames=ABL_09428 {ECO:0000313|EMBL:GAQ46767.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ46767.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
CC   -!- SIMILARITY: Belongs to the synaptojanin family.
CC       {ECO:0000256|ARBA:ARBA00008943}.
CC   -!- SIMILARITY: In the central section; belongs to the inositol 1,4,5-
CC       trisphosphate 5-phosphatase family. {ECO:0000256|ARBA:ARBA00009678}.
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:GAQ46767.1}.
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DR   EMBL; BCMY01000023; GAQ46767.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100ISZ4; -.
DR   PaxDb; 5061-CADANGAP00010327; -.
DR   VEuPathDB; FungiDB:An13g00020; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1081814; -.
DR   VEuPathDB; FungiDB:ATCC64974_23560; -.
DR   VEuPathDB; FungiDB:M747DRAFT_292612; -.
DR   OMA; HPCHELR; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR046985; IP5.
DR   InterPro; IPR000300; IPPc.
DR   InterPro; IPR002013; SAC_dom.
DR   PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR   PANTHER; PTHR11200:SF257; PHOSPHOINOSITIDE 5-PHOSPHATASE; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF02383; Syja_N; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   PROSITE; PS50275; SAC; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000313|EMBL:GAQ46767.1};
KW   Exonuclease {ECO:0000313|EMBL:GAQ46767.1};
KW   Hydrolase {ECO:0000313|EMBL:GAQ46767.1};
KW   Nuclease {ECO:0000313|EMBL:GAQ46767.1}.
FT   DOMAIN          155..520
FT                   /note="SAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50275"
FT   REGION          1048..1090
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1060..1074
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1090 AA;  122855 MW;  9EDDD437FCF5F75C CRC64;
     MSGLRIYTQN YPYRTIALAT SEYVLIFRHS LAGADVNTAS HLKTTPRCLV EFAPLSSVDL
     KGYRVIGDGH GTLGLVTLDN EVFLCVVTGS SKAASIRPGE TVLRIHSVDF FCLNHSKYDD
     RVDYELESSI AGQDPDHDFN FESKETNPDF PFLALKKLLS DGSFYYSCEF NLTDRLQDRS
     DETGIFDIES LDRDMLWNSY MIHPLLLFRN QLSSVEKQHL DSSQILTCVI RGYCGTLTVP
     ASTQLLPGTR KTHLPSSLTI ISRQSSRRAG TRFNSRGIDD DGHVANFVET ETILWIPPDI
     VFSYVQVRGS VPIFWEQATG FLPGQQKIEI TRSVEATKHA FDKHFRSLEL DYGAIHVVNL
     LSELKSGEYS LTARFRNHLQ NSPLNKHSSD HTLLQVTEFD FHAEARGPLG YGASSQIRQE
     IFDSLQGFAY FQSGEIGPVA LYDKHHASRN APVILQQEGV FRTNCLDCLD RTNLVQTIIS
     SMALEIFFSQ QGGTISPDLQ LRHSTLWADN GDALSKMYAG TGALKSSFTR HGKMSIAGAL
     ADARKTATRI YVNNFADKAR QNTIDLLLGR LTDQVPVHLY DPINDLVLEE LSQRSEEFSY
     SRSVTVWTGT FNVNGRHEGP DGDLRAWLFP KYDSQAEDPL IYAVGFQEIV TLSPQQIMST
     DPTTRKAWEI AVHTCLNKRA EAMGTPKYVL LRSGQLVGSA LMIYAREDAL SDIKNVEGNV
     KKTGLSGMAG NKGGCAIRFE YSNTRLCFVT AHLAAGFANY DERNRDYETI LRGLRFLRNR
     SIEDHDAVIW LGDFNYRIGL SNQKARELVQ EKDFQTLYDN DQMVAGRAFQ FYTEGPISFP
     PTYKYNIGRN DYDNSEKARI PAWCDRILWR GTNLRQINYG SADLRISDHR PVWAVFTCII
     NVVDEARKSK IQQSLYKERQ NNLRLGDMTT QVQKVDGELI AFDHIASELP PASSEQYKWW
     LNQGIPVKSQ LAPPAKDYVL NIHRDSNPFL CDGPANWCPT PLLAESNSNT NAENPRLPPR
     TVSKSFLRNR DASTETWLTD DQCVFEQKRR DLDSPSVSIE SPERGPNTNT KDLLGEAISD
     DLNWRPLTPE
//
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