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Database: UniProt
Entry: A0A135LQX4_PENPA
LinkDB: A0A135LQX4_PENPA
Original site: A0A135LQX4_PENPA 
ID   A0A135LQX4_PENPA        Unreviewed;      1105 AA.
AC   A0A135LQX4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE            EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN   ORFNames=PGRI_093900 {ECO:0000313|EMBL:KXG51378.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG51378.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG51378.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG51378.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest pathogen
RT   Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(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:KXG51378.1}.
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DR   EMBL; LHQR01000031; KXG51378.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135LQX4; -.
DR   STRING; 5078.A0A135LQX4; -.
DR   OMA; HPCHELR; -.
DR   OrthoDB; 996872at2759; -.
DR   Proteomes; UP000070168; 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:KXG51378.1};
KW   Exonuclease {ECO:0000313|EMBL:KXG51378.1};
KW   Hydrolase {ECO:0000313|EMBL:KXG51378.1};
KW   Nuclease {ECO:0000313|EMBL:KXG51378.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070168}.
FT   DOMAIN          146..517
FT                   /note="SAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50275"
FT   REGION          934..958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          972..1105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1077
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1105 AA;  123119 MW;  5B2909E3BA4345F9 CRC64;
     MSNLRVLCRD QPQRTIALVS SDHALVFHYT STDTSAKDSP RCQVEFSDLE EVDLQGYRPL
     GYGYGTLGLV TLNEDVFVCV VTSSSQAATV RPGETVSRID NVGFYCLNRS EYEYGLEHET
     ASQFAAEERL GTDGKDVVTD HPFLALKKLL GDGSFYYSLD FNLTDRLQDR ANKLVAFDID
     TLDEDMLWNS YMISPLLFFR SHLPPSDKAK LDASQMLTCV IRGFASTLKV PATISILPHV
     RTNFPSMLTI ISRQSSRRAG TRFNSRGIDD DGHVANFVET ETILWISPGI VFSYAQVRGS
     VPIFWEQAPG LIPGQQKIEV TRSSDATQHA FNKHFESLEL EYGAVHVVNL LSELKPGEAE
     LSCKFRQHIN KSSTRQKEGD GTSPHRSLLR MTEYDFLAET RGPSGYEASS QIKHELINSL
     DEFSYFLSED SGRPNKTSYD GADAVNNSSV ILQQEGVFRT NCLDCLDRTN LVQTIISSMA
     FETFLSQQGG SLSSDLQVRH STIWADNGDA LSKIYAGTGA LKSSFTRHGK MSLAGALADA
     RKSATRLYVN NFTDKAKQKT IDLLLGRLTN QLPVYLYDPI NDLVIEELSH RTPEYSSRKQ
     VRFWVGTFNV NGRDEGPGTD LTPWLFPGSD ESDEDPAIFV VGFQEIVALS PQQIMSTDPS
     TRKVWERAVY DCLNAHSKMK GTGKYVHLRS GQLVGAAVLL YVKEDSLKYI KNVEGSTGLS
     GIAGNKGGCA VRFDFSNTSV CFVTAHLAAG FANYDERNRD YEIIDRGLRF QKNRSIADHD
     AVIWLGDFNY RIGLGNPSVR ELILQRDYRR LYDNDQLNLQ MVAGRVFQFY SEGPIEFPPT
     YKYDVGRDSY DTSEKARIPA WCDRILWRGS SLRQTNYQTA DLKVSDHRPV WATFDCVIDI
     VNYTLKESLR RSIYEEKQGH GHTSLADSVS LLDLDDDDET TPHVSIAPGL PPASSDRSRW
     WLDNGASVKA TVQPPKQGYI PNPQRKSNPF SADVDWVLSP DSIENKNAEP IPVTKKSMLP
     PRRDTSESFT ESLLPQADGT KKVRPAVPRK PLSLSSQGKV GTVSPSSQHT SRQDSPGDGV
     TAGMGSTDLL SDSGSEQIEW KPLFQ
//
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