ID A0A0L0VV11_9BASI Unreviewed; 1491 AA.
AC A0A0L0VV11;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN ORFNames=PSTG_03616 {ECO:0000313|EMBL:KNF03022.1};
OS Puccinia striiformis f. sp. tritici PST-78.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNF03022.1, ECO:0000313|Proteomes:UP000054564};
RN [1] {ECO:0000313|Proteomes:UP000054564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78.";
RL Submitted (MAR-2014) 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 -!- 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:KNF03022.1}.
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DR EMBL; AJIL01000019; KNF03022.1; -; Genomic_DNA.
DR STRING; 1165861.A0A0L0VV11; -.
DR OrthoDB; 996872at2759; -.
DR Proteomes; UP000054564; 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:UP000054564}.
FT DOMAIN 142..527
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT REGION 1021..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1491 AA; 163635 MW; 98EF929D40B730CD CRC64;
MRRPELSLGL TTKPRTLVIS SASHALILRA SPSKQLSVEF LGIDKRTQTA IKIAPCWGAL
GLLEIEREIF LVIVTHATPI GVLQPSQEQI HRVVSVDLFC LTSTNFDYQQ ATRGNLNQSI
GNGSNHDAEE PIGPDHPTLN GIKKILSNGQ FYFSSTTSDL SSRTEYRLAP NEDDCSSTRR
FSWNSFMLVG LTGFQNGLPI PNRLEFDRQN FLVSIIQGYV ATYELKLPPP LSSSSVPSTK
DEDNNEPISF SISLFSRLGS LRAGTRFNTR GIDDDGNVAN FVESETLILT NNKLFSFVQI
RGSVPLFFEQ SGTGMTNVIG GLSGNGHPTQ LTRTGIATQP AFDRHFNDLL SNYHSVQILN
LLSSSRDSES NLTNAYQQRL KSFINDHKEY PEDIVNFVNF DLHHRSKSSG LDGVRQLLIN
DKLIGGQIEN IGAFFACLKS SEQDRNQDQQ DQQEPIEIIT KQMGVFRVNC LDCLDRTNVI
QEMLSRMAVE SFLESTYPHL LRSDYLWNCH RSLWADNGDV LSKIYAGTGA LNTTFTRGGK
QTFSGILSNA SKSVGRMYNS NFIDKSKQAH IDLMLGNLSG QKPVKVFDPL NDTIKRMLHE
RLSDYSKTIS ISIWVGTYNL NGRTPPMANN DELMAWLCPT PNFDPDIMAV SFQEIVKLSP
QQIMITDPEK KSRWERIILK SLENRADKKS SYAVIRSDQL VGAALIILAK TELVPAVRSV
EAKTKKTGLK GIAGNKGAVA IRLDIHDTSF CFVTAHFAAG LSNVEERNHD YETIEDGLKF
LRGKTIAGHE NVIWAGDFNY RIDGGLPNNA VRQAVADENY AELLAADQLL EHMASQAVFH
KYTEGTINFP PTYKYDVGTD RYDTSEKMRI PAWTDRILYQ GSDLNLKAYS RAEIKTSDHR
PVYATLETKV RMVDRTKKEI IKQEILESSE VGSLRDALMM PLKTGDSSNV EVAVLDEWWT
NPEDPNGEYE ANPSELAQAI GSSSNPFKPQ IGAVRPGRHS FHPEVNPAMN NRFVNGKLDR
QISSSVPSSP PPPVGKGVPP AIPARSTSRS PSETRRPVAE KTGALPKAQP PAPPPRPTSK
ILVNIDNTSM EASLKGPPPP RPINFGPLLT AQLPPDSAET LSPRSRSLSG RKSVPSGLRL
SVPPPPSHPA SKLAPRPEPV KSPLLSASTS KLLSSRQSTP VWLEHNAPIP PPRPVSRGFV
NKSDAPIGVI DPNHSPLFSP RSSFKLSQRR DTIPADPDSA SNPPLPPRPM SRLSTGESAD
SKGFQSLNIL SGKGVDPSEF DRKNPTPPPR PLSRIISGKE TPSAGITGSD ITTLPARPIS
SLLTTTGSES LRSSTRVVEV RGSSTATPLP RPISLLEKET KSVRSFSSSP SPTRSIYQLS
STTQPPPPPS RKASKLSLNN LDPPIIDTRL PATPPRPSLE HVSSTASFTQ VVDPPDDTTT
FTTVNTTTSS PPPIPPKPKP PKPALKPKPQ TLRKSASHES KPFLTSESSN Q
//
