ID A0A0M9AAE9_9HYME Unreviewed; 1095 AA.
AC A0A0M9AAE9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform {ECO:0000313|EMBL:KOX79243.1};
GN ORFNames=WN51_09044 {ECO:0000313|EMBL:KOX79243.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX79243.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX79243.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX79243.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX79243.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
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DR EMBL; KQ435713; KOX79243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9AAE9; -.
DR STRING; 166423.A0A0M9AAE9; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; cd08693; C2_PI3K_class_I_beta_delta; 1.
DR CDD; cd05165; PI3Kc_I; 1.
DR Gene3D; 3.10.20.770; -; 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 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; IPR003113; PI3K_ABD.
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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR PANTHER; PTHR10048:SF118; PI-3 KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF02192; PI3K_p85B; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00143; PI3K_p85B; 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; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51544; PI3K_ABD; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KOX79243.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..106
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 188..277
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 321..488
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 525..702
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 770..1054
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1095 AA; 125871 MW; F34BD0A0AE9EE885 CRC64;
MVHIPSAYTY NFWAKSPTEV VELTCLMPNG VVIPLETNRN ITLAEIKEDL WDEASKYPLH
GTLKDAPSYV FSCINSNAEA EELRDETRRL CDIKPFCSVL KVIEREGVKS DRNLDSQIGL
LIGKGLHEFT ALRNSEVNDF RWKMRVLGDE VAMARQKKSW MEKVRYQFPT RLAPTATIPK
NIECRLKDGN IVLVTKFENT ETAFTFQISH TTTPYQLLVS ILNKRANTLM SKGHPNDFTL
KVCGQEEYLI GDYPLIQFSY IQDCLAKDII PTLVTLSRDS VSVDQENTAE NVEPDTLQRT
RPSFSTLTLR KKGKHISAWK IEEPFVFTVN AISRLNCDAA HRTVEIGLQA GLFHGGKSLC
ESQKTKETIV SSDGSCEWEE PLRFDIKVRD IPRMARLCFV LYEISKTAKG LKSRRLVKDT
KQEFFINPLC WANTTIYDFK SQLKTGAMTL YTWTYAEDMQ NDDLLHPLGT VVSNPHIDRA
AALMLTFPNY GKDKSVLYPT PEKMVEYARK LRESSAERSI QEEPDKESDV GKLQQLEQLR
LLADRDPLHE LHEQERKIMW TLRHHCLLEI PTLLAKLLHC VEWNDHREVA EATALVQQWP
KLPVEKALEL LDYAYADQNV RSFAVRCLMD VSDEDLSLYL LQLVHAMKHE NYLSCDLTEF
LLRRALNNRR IGHFLFWHLR SEMQVGAVSV RFGLTLEAYC RGSQQHMRSL FKQMECLGKL
KSASEQIKQR KDRKAALQGF QEFIQEPHCQ DALSNVLNPL DPSFRWKRIK IEKCRVMDSK
MRPLWLVFEN DDPFGDDIYL ILKHGDDLRQ DMLTLQMLRI MDKLWKREGL DLRMNPYGCI
STENRVGMIE VVLNAETIAN IQKEKGTFSA TAAFRRGSLL AWLKDHNHTE AALNRAIEEF
TLSCAGYCVA TYVLGIADRH SDNIMVKKTG QLFHVDFGHI LGHFKEKFGF RRERVPFVLT
NDFVHVINKG QTKKGQAVEF QRFQSHCEQA FLVLRQHGGL ILSLFAMMIS TGLPELSSEK
DLNYLRDTLV LEMSESEAQK HFRIALPVSS WITGVTLHKL TQTTTNEDGT TTTETEDVKF
QRNKQTAYPV SNNQA
//
