ID   A0A178EBE8_9PLEO        Unreviewed;      1271 AA.
AC   A0A178EBE8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-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=IQ07DRAFT_356859 {ECO:0000313|EMBL:OAL53308.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL53308.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL53308.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL53308.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KV441640; OAL53308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178EBE8; -.
DR   STRING; 765867.A0A178EBE8; -.
DR   InParanoid; A0A178EBE8; -.
DR   OrthoDB; 996872at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000077535}.
FT   DOMAIN          169..538
FT                   /note="SAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50275"
FT   REGION          944..1021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1051..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1089..1271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1017
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1051..1072
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1096..1135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1247..1263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1271 AA;  140847 MW;  95653ED6FC5956C5 CRC64;
     MSIRVLIKEY PHRAIALATA THALVLRHSA SSIENNGNAN ASSTSLGSNG SSAARCMVEF
     ARRDDVDLND YRALQSVNAH GTLGLITING DVFLAVVNGA SKVATVRPGE TVQRIHSVGF
     YCLTSSNYDS LLNDEVNPYP TDTIDDEGYE MGYGGRKEQS PLEHPCLALK KLLSSGSFYY
     SSDFDLTRRL QDRTSDVATV SIDTLNGGFL WNSYMIQPLV DFRSRLAPRE KEALDASGIL
     TSAIRGFALT ITVPTSSAPI KVPGSGMPSA MTLISRLSCR RAGTRFNARG IDDDGNVANF
     VETETIYWAP SGACFSYVQV RGSVPIFWEQ QSGLLPGQQK ITITRSPEAT QPAFDKHFDN
     LELSYGGIHV VNLLSNEKPN EIELTDRYRG HIRNSPLNYG SEKSDREHEL IKLTEYDFHA
     ETRGPGGYEM ASMIARWIQE SAEGFNYYLC EEVEEDARVN GQHQIIRRAM TILQQEGIFR
     TNCLDCLDRT NLVQTIISKM ALEIFFNHKT LKATNDFWAR HSSMWADNGD ALSRIYAGTG
     ALKSSFTRHG KMSLAGALAD ARKSATRMYI NNFADKGRQN TIDVLLGRLM GQVPVHLYDP
     INDFVVAELS RRAAEYSESE VINILVGTFN LNGKTHGIKE DLSRWLCPDV DPSQQCPEIV
     AVGFQEIVDL SPQQIMSTDP ARRELWENAV RNCLNRNAEK HDKDEYVILR GGQLVGASLS
     VFVRSDCLKH IKNVEGSLKK TGMSGMAGNK GAVAIRFEYA NTSICLVTAH LAAGFANYEE
     RNRDYKTISH GLRFQRNRSI EDHETVIWLG DFNYRIGLSN DKVQRLCHVG DLETLYENDQ
     LNLQMVAGLT FPYYSEARIT FAPTYKYDLN SDQFDTSEKA RIPAWCDRIL RKGDNIRQIH
     YDSAPLRFSD HRPVYATFQA LVQRVDEKRK DLLKEALYRQ RREAVGETRA GGRLGDEESD
     DEDIIGYDSI EPGLPPASSD RRKWWLDNGL PAKARVQPPS NDHIPNPKRP SNPFTPSPEP
     EWVDVRKLQN NGKPEPPPAR GSQRTRAAEF NGLSASSSKS SSTTSLQQAP AHALPSHTAR
     KMNVPLYPGH ASQILNTDGP RDSYTDLQRT TSNASTNSLP ALPYRPSSMH SAPSSNPRVL
     RKPGPPPIPT KKPSLSTHTS STPFSRNTAS PPHQTLHDEP LSEPERGRPQ PPPPRRSMAT
     SSTGGLVKKP VPNLIDGDER PPLPPRTGTG LSAGSTGSNG RGRMGGGRSL MDEEPEEMAG
     LRDWEVLRPA G
//