ID A0A195D5M2_9HYME Unreviewed; 1107 AA.
AC A0A195D5M2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform {ECO:0000313|EMBL:KYN07739.1};
GN ORFNames=ALC62_01250 {ECO:0000313|EMBL:KYN07739.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN07739.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYN07739.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYN07739.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN07739.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) 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; KQ976870; KYN07739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195D5M2; -.
DR STRING; 456900.A0A195D5M2; -.
DR Proteomes; UP000078542; 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:KYN07739.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078542};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 24..140
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 222..313
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 357..524
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 560..737
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 805..1089
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1107 AA; 127465 MW; ACBC65712F715444 CRC64;
MVHGNIPSVY KYNFWAERPG DAHEPSVVEL TCLMPNGVVI PFEINRNITL DQIKEAIDIL
DTRLEHKKYE RYDYICILGY ILDLWDEASK YPLHGTLKDA PSYVFSCINS NAEIEELRDE
TRRLCDIKPF CSVLKVIERE GIKSDRNLDS QIGVLIGKGL HEFTALKNSE VNDFRWKMRL
LGDDVALSRQ KRCWTEKVHY QFPSRIAPTS TVPKNIESRL KDGNIVLFTK FEKSEVTFTF
QIVHTTTPPE LIEAILNKRA NILKTRGEQP NDFTLKVCGQ EEYLIGDNIP LIQFGYIQDC
LAKDVMPTLV MLSRQSVPVD QDSAFDNLDV DTLQRTKPSS STLTLRKKGK HISAWKIEEP
FVFTVNGISR LNCDAAHRTV EIGLQAGLFH GGKSLCESQK TKEIIVSADG SCEWEETLKF
DIKVRDIPRM ARLCFVLYEI SKTAKGLKSR RLIRDSKQEF FINPLCWANT TIYDFKSQLK
TGAMTLYTWT YAEDIQNDDL LHPLGTVVSN PHIDRGAALM LTFPNYGKDQ CVLYPTPEKM
VEYAQTLREQ SNERLVKDEL NQESDVGSQQ LEQLRLLADR DPLHELHEQE KKTMWTLRHH
CLREIPTLLA KLLQCVEWND HREVAEATAL IQQWPKLPVE KALELLDYAY ADQNVRNFAV
RCLRDVTDDD LSLYLLQLAQ VLKHENYLAC PLTEFLLKRA LNNQRIGHFL FWHLRSEMQV
GAVSVRFGLI LEAYCRGSQQ HMLSLFKQMK CLEKLKSVSQ QVKLKKDRKA ALQGFQDIIL
EPHCQEAISD VLNPLDPSFR WNRIKIEKCR VMDSKMRPLW LVFENSDPFG DDIYLILKHG
DDLRQDMLTL QMLRIMDKLW KKEGLDLRMN PYGCISTENR VGMIEVVLNA ETIANIQKEK
GTFSATAAFR RGSLLAWLKD HNHTEAALNK AIEEFTLSCA GYCVATYVLG IADRHSDNIM
VKKTGQLFHV DFGHILGHFK EKFGFRRERV PFVLTNDFVH VINKGQTKKG HAAEFQRFQN
HCEQAFLVLR QHGGLILSLF AMMISTGLPE LSSEKDLNYL RDTLVLEMSE GEAQKHFRSK
FDEALCNSWK TSLNWASHNM SKNNKTT
//
