ID A0A484B5K5_DRONA Unreviewed; 1680 AA.
AC A0A484B5K5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phosphatidylinositol-4-phosphate 3-kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AWZ03_009613 {ECO:0000313|EMBL:TDG43978.1};
OS Drosophila navojoa (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG43978.1, ECO:0000313|Proteomes:UP000295192};
RN [1] {ECO:0000313|EMBL:TDG43978.1, ECO:0000313|Proteomes:UP000295192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG43978.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:TDG43978.1};
RX PubMed=30423125; DOI=.1093/jhered/esy059;
RA Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT the mojavensis Cluster.";
RL J. Hered. 110:118-123(2019).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
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:TDG43978.1}.
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DR EMBL; LSRL02000123; TDG43978.1; -; Genomic_DNA.
DR STRING; 7232.A0A484B5K5; -.
DR OMA; HQWPALY; -.
DR Proteomes; UP000295192; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
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; cd00869; PI3Ka_II; 1.
DR CDD; cd05166; PI3Kc_II; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
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; 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; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 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:UP000295192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 565..671
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 857..1029
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 1037..1215
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1304..1579
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1617..1680
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 50..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1680 AA; 187210 MW; ABF630280B45FD56 CRC64;
MSNQAQIDYD RQFQEDLAKA TALSLEQQAL DDYRRNKKYG TGYQTVSADY YSQQQQQQQQ
QQRSHGAVQR RHSEVHQASS SYSSSAGRAN TPPAQTNNGN GDNDLICFAS PTTKQPTSES
GSSFERLIED LQRLQTNSPQ TALVPVGPVA AATPMPVQYA APPYGVPPLG EAGGVGMQLV
PYQAPPQQPQ QRPLNNEELQ RLYSMPNHLA LQPVVPVRPA GFVYYPTFSA PVVPGSAAYL
PPQYPSQAYG YGYALSNGGS SHVDFVRPHS SPATAGIPTP VPAPSSSHSV PHSGATTPAA
FNVQRATPPV GSCPSVGPAL PAQRSGNDLI DLNKDDYSRV SVLEAFDPLL NENSGNDGAS
DCTSYYADYD PFDFLYSGDN GTQYSDPMYE AVNRWDKSAV NSGSVSSIGW RQDYLTQPSH
SHSPPLSLQA SAAAVASAAS TSAQADSRSN TGSVSPPPPL PPRNQQLYET GATTSTISQT
SSKPHQLAPF TDSYTNSIPA HVVLDRRKNF TRLYQLISEQ RSDDSELLEF YHMVRELRAS
YRHDDKKTNV GHIIAAEFNY HYMMDTSIKV IVHPAVNTLQ PHALSSSLAG EQVKGYGTPV
TFTCDIDSVV AQVVAQALAS LEGQVQGTVT DYAVKPIGLL EWLAPTSKLS QLECVHNSFQ
LEKDVHLGLC LRTAANMEAI ARTEQDDEND ADLQPEQVLP NEVVPIVTYD NMMILIETLE
TEIDKLESSA DGAPSGRSIV SCSGVVQAVK AICALLGSID TLEIARCISD LRRICEEAQT
KYAPLAGSNN PEIISDYGEY AQVTLRPRSM LEQIKLKCNS LRDAVQELIE LYANVFRVAF
SVKTPDYTTT PIPVSCVSKP IVVSINCLHR PPPNWKYDDY SLCVQLVYGT RLLSNPNVLS
CSNDTSGGLF PRLNFSAWLT FDQHPICTLP REARLTFVLY GKQAASENEP NAEPNGERRQ
VTTELGWCSI QLFDFKRTMI CGPYLLSVWP PTTDKMLGPA PARGCHPHPD FCPVLSIEVP
PYGGRIEFPE HQEAPKPAPH YDFASLDANL QEELLNTAEL GYSGATERRE VFWEKRLYLQ
NYPNALPKVL HAAHSWDYAN LIDLHSLLHS WAPLSPLQAL ELLLPRYPDA KVREKAVEWI
SHMPNDQLVD FLPQLVQSLK HDTYEASALS RFLLAKCLES PRFAHHMYWL LVHSLPDDPL
NSIGASLVDQ EYDESQITQA RYYRRNKMML RALMAICGEK LLKRFMYQHR MCQNLSKIAE
SVKEAKESMR QKSLVAGMDE VHQDLLEKPT CLPLGPELEV SGVNVRNCSY FNSNTLPLKI
TFVGPDAEPL PAIFKCGDDL QQDMLTIQLI RIMNKMWLAE RLDLKMVTFN CVPTGYKRGM
IELVSEAETL RKIQVECGLT GSFKDRPIAE WLGKQNPSPL EYQSAVRNFT LSCAGYSVAT
YVLGICDRHN DNIMLKTSGH LFHIDFGKFL GDAQMFGNFK RDRTPFVLTS DMAYVINGGD
KPSTDFHYFV DLCCRAFNIV RKNADLLLHT LAHMATAGMP GVNSNAVTYV RRALLPSQSN
PEAAATFAKM IQSSLKSWFT QFNFFLHNLA QMRFNNDEGS GELLSFVPRK YTMQQDGRLK
IVKVVRFQKH YSMEKYYMYI LQVTRHGQLD PTHLFRSYRE FTEFHQKLCM HFPLVKLHRR
//
