ID B0W579_CULQU Unreviewed; 1236 AA.
AC B0W579;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN Name=6033410 {ECO:0000313|EnsemblMetazoa:CPIJ002194-PA};
GN ORFNames=CpipJ_CPIJ002194 {ECO:0000313|EMBL:EDS34826.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS34826.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS34826.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ002194-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ002194-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000256|ARBA:ARBA00001786};
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; DS231841; EDS34826.1; -; Genomic_DNA.
DR RefSeq; XP_001843863.1; XM_001843811.1.
DR AlphaFoldDB; B0W579; -.
DR STRING; 7176.B0W579; -.
DR EnsemblMetazoa; CPIJ002194-RA; CPIJ002194-PA; CPIJ002194.
DR KEGG; cqu:CpipJ_CPIJ002194; -.
DR VEuPathDB; VectorBase:CPIJ002194; -.
DR VEuPathDB; VectorBase:CQUJHB005920; -.
DR eggNOG; KOG0566; Eukaryota.
DR HOGENOM; CLU_003016_5_0_1; -.
DR InParanoid; B0W579; -.
DR OMA; HPCHELR; -.
DR OrthoDB; 21647at2759; -.
DR Proteomes; UP000002320; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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 CDD; cd09089; INPP5c_Synj; 1.
DR Gene3D; 3.30.70.330; -; 1.
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; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR002013; SAC_dom.
DR InterPro; IPR015047; SYNJ1/2_RRM.
DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR PANTHER; PTHR11200:SF257; PHOSPHOINOSITIDE 5-PHOSPHATASE; 1.
DR Pfam; PF08952; DUF1866; 1.
DR Pfam; PF02383; Syja_N; 1.
DR SMART; SM01165; DUF1866; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50275; SAC; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320}.
FT DOMAIN 120..455
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1039
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1236
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1236 AA; 135908 MW; 34FF59790577D7FA CRC64;
MAMSKGFRVL EKSKPPSPHS VLLEHRNKSE TLLFESQAVA VLSAQETEIV RKQYTKVLDA
YGCLGVLQLN AGDSSLLYLV MVTGCFSVGK ILDNEIFRIT QTQFVSLQYQ PTNEDRISEI
RKVLNSGTFY FSFSNQPGGN GGGASFDITL SAQRRKRTMD TDNRFFWNRM LFIHMLRFGV
EYNFWLLKAM CGSVEIRTVY AGSKQARAAI ISRLSCERAG TRFNVRGTND EGCVANFVET
EQCIYLDGEV SSYIQTRGSV PLFWEQPGVQ VGSHKVKLSR GFEASRSAFD RHMTTMKARY
GKQAIVNLLG TSLIGSKEGE ASLSNEFQRH HKESNHVDVP HIVFDYHQEC RGGNTGALSK
LKAKIDAMCS DFGLFHAMGD SVFREQKGAI RTNCLDCLDR TNCVQTYIGL EILNEQISQM
SALSDKKQQI SSRFEEIFRQ MWINNGNEVS KIYAGTGAIQ GGSKLMDGAR SAARTIQNNL
LDSSKQEAID VLLVGSTLSS ELADRARILL PSNMLHAPTP VLREMCRRYE EFVLPSEIRV
ACGTYNVNGG KHFRSVAYKD VSLADWLLDC HRLARSRSLV DVSHPEDTNE PPIDIFAVGF
QEIVDLNASN IVAASSDNAK AWAEELQKVI SRDEEYVLLT YQQLVGVCLY IYIRPRHAAY
IRDVAIDCVK TGLGGATGNK GAAAIRFVIN GTSICFVCAH FAAGQSQVVE RNADYAEITR
KIAFPMGRSL KSHDYIFWCG DFNYRIDMDK EELKESLKQG DIESVLQYDQ LRIQQNTGSV
FNDFFEGEIS FPPTYKYDLF SDDYDTSEKA RAPAWTDRVL WRRRKQSPDA DKQPNWNPGR
LVHYGRAELK QSDHRPVIAI IDVEICKIDQ QRRTQVFGDV IRDLGPPDGT ILIQAANPSA
ESGDEDEGSI YDENLMSALI QELTQIGEVT LVRFVGDTMW VTFRDGQSAL TAAQKQSVQV
CGVNLTIKLK TENWIQTVEK EILLCTPNTV SFCDSQVGDY NSLGIPEVPS RPKSPPALNQ
PPLRPAPPGR PPLPKSPQAS PKHQPMQHHH PKAGVISLGA EVLMASKLHQ KPAVPPQPLV
PPQSASKTTP PIEEYASSSP ILGSPAHGSS GVSSPQQQQD TGAIYEEIND DIAVPEPRGP
PPPPPRCDVY DLDVVATSNN KPAPPPTTTT TKSSPPGGGN SGGSSGAGSP QGGGGSASAG
GPPKTNPPPL PVRRGVPPPI PNRSAGAPPL PARPNQ
//