ID Q0IGF6_AEDAE Unreviewed; 1922 AA.
AC Q0IGF6;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:AAEL000386-PA};
GN Name=5576326 {ECO:0000313|EnsemblMetazoa:AAEL000386-PA};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EnsemblMetazoa:AAEL000386-PA, ECO:0000313|Proteomes:UP000008820};
RN [1] {ECO:0000313|EnsemblMetazoa:AAEL000386-PA, ECO:0000313|Proteomes:UP000008820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL000386-PA,
RC ECO:0000313|Proteomes:UP000008820};
RG Aedes aegypti Genome Working Group (AGWG);
RA Matthews B.J.;
RT "Aedes aegypti genome working group (AGWG) sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AAEL000386-PA}
RP IDENTIFICATION.
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL000386-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
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DR RefSeq; XP_001656061.1; XM_001656011.1.
DR STRING; 7159.Q0IGF6; -.
DR PaxDb; 7159-AAEL000386-PA; -.
DR EnsemblMetazoa; AAEL000386-RA; AAEL000386-PA; AAEL000386.
DR GeneID; 5576326; -.
DR KEGG; aag:5576326; -.
DR VEuPathDB; VectorBase:AAEL000386; -.
DR eggNOG; KOG0905; Eukaryota.
DR HOGENOM; CLU_002191_0_1_1; -.
DR InParanoid; Q0IGF6; -.
DR OMA; QMAAGFR; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000008820; Chromosome 3.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04012; C2A_PI3K_class_II; 1.
DR CDD; cd08381; C2B_PI3K_class_II; 1.
DR CDD; cd05166; PI3Kc_II; 1.
DR CDD; cd06884; PX_PI3K_C2_68D; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF14; LD28067P; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000008820};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 1922 AA; 215702 MW; E3DB7FB3AFD42C80 CRC64;
MASRNEVEME KQFLAELEKA KALSLETFEL EKIRQQRYSQ PESLNKSDTR TLAEYKTYLE
RRAKLHQGAP SGSNDGPKSA SNVNLPNVSR FNSEPRTDAQ GSQLPRGKGE ADLISFIAPP
APPNPQDEAH NNLKELVDQM HRLNTQNPYE QSFKTQRSLS MSSATSYGGY SPAYLQQQVV
QNCNPAAMQL VPYNQQTAKP KPLTPDELNR LYNMPTYGTM PAGPPPQAGF IAQPQYAPVN
YPQTSTTFPL QQVHPVSVPT NFIPQPVAPV APAAASGFIP QTPQTIYATS TVPVANPNSA
LVHVPKAVNP KLTLNTRSAS QPQQPFPPAI PGPSNSNPFS RNSLGSNPTN NRTTNSNHNV
TSGSSGNNGS SSNGDVVLRP KSDPSKLGGG DNLIDFGGFE DNSRVSVLEA FDPLLCGNRT
SSGDGSDDDK DDTASTYYED YDPFDYIYSG GTQYSDPVYE AVNRSDKTPL SPNSSGSGPP
PIGWNVSSAY GFGEPEFQEG EPPPLPPRNS DLYHPMIGGG GGLGPAITSS NYEIMQTPAA
QRRSVPTKLY ENVVVRKSYD KELIAFYNMV KQLRAQFRYD DLKTNVGHVV ASEFNNHYPD
GTSIKLLVHP SLDCFTSFDS QNKGQIDGYG PPIPFTCDIT TSVEHVIAQV FCALEGQIMN
SVGDYVLKSI GMQEILSTSS RLNQLQCVHN SIKLEHDVQL GLVPKSPRIM RTIARTAQDD
HRDAEIRLEH ILPKEATSAV GYDQLMILLE TLEAEIDKLQ STADDHSPHS ILSCSGVTQA
VKAICAMLGK IDTLEITKAV DDLKTCCDSG QTIYSYNDSS DYNNGSLSIV SESGDYAEVK
LRPRTISQQI RYRCNEVRNA IQSLLEIYSH AFRVTFMVNV PEWNTNPIPI NMISQSIMVN
VMCLHRIPEL WRHDEYNLGV QIYHGARYIS EPLVTYCSNE RTGTYPRLTF NSWLTFRNAV
VTLPRESRLI FVLYGVTREP VEGDKQDGSS NADQNTQEGR VTKIELGWSA IQFFDFERKM
IQGSYLLPLW PPTAEKYFGP APAKGTHPMG DAYPILGIEI PSYGGSVVFP EPIKNMPPAV
KLDFNSLDRN LQQELIDTAE QGYSADKLEK REVLWEKRHY LHSLPHALPK VLHAAHSWDY
ACLEDLHAFL KSWPALTPVQ ALELLLPRYP DLEVRRQAVE WISHMPNDEF VDYLPQLLQA
LKHDTYEASP LAQLLLSKSL ESPRIAHHLY WLLLHSLPGD APQNMIEMGQ YDETLVIQAR
YHRRNQLMLR ALMATCGEKL TARFLSQNMM CKKLGEVAQS VKMTKESQRL QILKQGLESV
NQMLIDNPTV LPLGPGNEVT GVVVRSCNYF NSNTLPLKVN FMGPDKVIVP AIFKSGDDLQ
QDMLTIQMVR IMDKLWLREG LDLKMVTFNC VPTSYKKGMI EMVSDSETLR KIQVEWGLTG
SFKDKSIAEW LAKQNPSQLE YQRAVENFTR SCAGYSVATY ILGICDRHND NIMLKTSGHL
FHIDFGKFLG DAQMFGNFKR DRTPFVLTSD MAYVINGGDK PSAKFHKFVD LCCTAFNIVR
KHGDLILHMF ALMTTSGIPG VTVEAVNYVR NALLPGQSNP EAAASFAKMI GISLKSWFTQ
FNFFLHNIAQ MKFSAENDDG ELLSFVPRVY TMAQDGRLKS VTVHGFQKRY DLEKYYTYIL
KVTRQNQPDP AYLFRSYKEF CEFHQKLCIH FPLAKLHSLP SGIHVGRSNV KTVAERRLPE
IRQFLISLFN SADEIAHSDL VYTFFHPLLR DQQEADIHAT KVKGNRAIAD EYQQLRGEIK
FSLQYHRDAL IVMIQHARSL PSTPNNPEPN TYVKVYLRPD QSKATKRKTK VVRKNCNPSF
METLEYRLPL EFIQKKTLEV TVWSHDSLQE NAFLGGHRLA LAELDLRYEI NEWFPLGYLP
RS
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