GenomeNet

Database: UniProt
Entry: B0W579_CULQU
LinkDB: B0W579_CULQU
Original site: B0W579_CULQU 
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
//
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