ID A0A0D7A9I5_9AGAR Unreviewed; 1017 AA.
AC A0A0D7A9I5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN ORFNames=FISHEDRAFT_45168 {ECO:0000313|EMBL:KIY47483.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY47483.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY47483.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY47483.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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}.
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DR EMBL; KN881933; KIY47483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7A9I5; -.
DR OrthoDB; 996872at2759; -.
DR Proteomes; UP000054144; 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 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:UP000054144}.
FT DOMAIN 155..502
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT REGION 905..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1017
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 114115 MW; 6FEC5EBD1A4764DC CRC64;
MYLYLGNGFR VLYLVTSPSE EKQGRPKRVL VFRAREDNPT QAIVEFLPKD EVDLSTAIRL
TSRVIHGLLG LINIENEIFL AVVTSATEVG NTRPSAKYPE NAARLHEASF YSLNSSTWDE
FAAAGSGDPL QNPDLDPTIL GSVTPPTFEH PCLPLIKILC SGSFYYATNA QWDLSSRLAV
RLSRGEYDPA TFDGRFVWNE YIVRSLLDFR DRLEAFERDE FDRCHYIALT IQGYVGTATL
ALPAPPTNGA PSIATLSLIS RLGWKRAGTR FNTRGVDDDG NCANFVETEV ILATDQHCVS
YVQVRGSVPL FWEQQGLQTF GQRIQITRPH ASQPAFERHF RQLIEEYGGG VHAVNLLGSK
ENEAILTSAY ARHIQTVGAS LGETVDITHF DFHNVVKMGG HEYLARELRR CETLVNYVDK
FGFTMCDASN DEVVTKQSGV FRTNCLDCLD RTNFVQDIIS RLITEQYLFM TRREWLHAHA
LWSHHRELWA ENGDALSRIY AGTGALNTSF TRTGKRTLAG VLSDATKSVS RAYINNFQDR
SKQIAIDTFL GNLSDQRQVT IFDPIHDYVR AALEQRLAEY STTKHCTIFA GTWNVNGRAP
SESLLPWLFP RDSIPDIFVL AFQEIVPLTA SQILQTDPEK RHVWETAIMK TLDQRPHKKC
DYVLLRSEQL VGTALFVLVK AELTAVIRNV EAATRKTGLR GMSGNKGAVG VRLDYHDTSF
CFLTAHLAAG HVNVFERNAD YRTIASGLHF QKGKTIDGHE NVVWAADTNY RIDLENDNVR
IMADKDELDA LLGADQLRNA IDLGHAFVGY EEGPLLFRPT YRYDLGTQYY DTSEKMRIPA
WTDRILYKGN QLDLSVYSRA ELMGSDHRPV FAIFRAAVRI IDAAKRTTLS KSLLDTVTST
ASGEKLDDKL TSMMRSPDYP ELPPPSSDER AWWDTPEYPN GKLPVAELQA LSMSQRPNQT
NPFDSPVESP LSSSPSSLDE ELYTDALTLH RPPSVVQATT PLPVQRRPPP PLPARSS
//