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Database: UniProt
Entry: L5KKX9_PTEAL
LinkDB: L5KKX9_PTEAL
Original site: L5KKX9_PTEAL 
ID   L5KKX9_PTEAL            Unreviewed;       819 AA.
AC   L5KKX9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing gamma polypeptide {ECO:0000313|EMBL:ELK11977.1};
GN   ORFNames=PAL_GLEAN10015653 {ECO:0000313|EMBL:ELK11977.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK11977.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR   EMBL; KB030666; ELK11977.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5KKX9; -.
DR   STRING; 9402.L5KKX9; -.
DR   eggNOG; KOG0905; Eukaryota.
DR   InParanoid; L5KKX9; -.
DR   Proteomes; UP000010552; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048:SF29; PHOSPHATIDYLINOSITOL 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT GAMMA; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   SMART; SM00239; C2; 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   PROSITE; PS50004; C2; 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; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ELK11977.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          291..494
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          527..818
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          702..819
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
SQ   SEQUENCE   819 AA;  93190 MW;  BE4A3E5CABF2903D CRC64;
     MAYCWKTDLN PGESDEELHK HQELYSENQP LFPSQVSLGF DQVVDEISNK IPLYQSEIEE
     NAIFVPSAPN RNSKKHSLDA TQQISLNEFT SKTSELSHHQ VRKTPVIGFR RSVLTNAQNM
     NKESSCGNPT GKCHGADDYR FNILASSSTG LEKTNSQKEL ENENHNYHIG FESSFPSIYP
     SFSTDFMPRE ENKRSTNINV VEPSLMLFKG SFLPRMSEST WPKNIEQIGS SIQLVEMPQG
     SNMSLASFCN KVKSDHTLGS HKIFQKDKSV IQLNLQKNRE APGKLSRKKN VNDIIEEVKN
     ICSVLGCVET KQITDAVNEL NQILQRKAEN FHQNSETSAK GLIEKVTTEL STSIYQLIDV
     YCSSFYADFH PLNTPDSVSF VNPGLHSHLS FTVYAAHNIP EIWVHSFPDQ EIRKVAVQQL
     DNLLNDELLE YLPQLVQAVK FEWNLESPLV QLLLHRSLQS IQIAHRLYWL LKDAQNEAYF
     KSWYQKLLAA LQFCAGKALS DEFAKEMKLI KILGDIGEKV KSASDPQRQA CSYFISNAFP
     LKITFFNANP MGKNISIIFK VGDDLRQDML VLQIIQVMDN IWLQEGLDMQ MIIYRCLATG
     KGQGLVQMVP DAVTLAKIHQ HSGLIGPLKE NTIKKWFSQH NHLRADYEKA LKNFFYSCAG
     WCVVTFILGV CDRHNDNIML TKSGHMFHID FGKFLGEKFL DNRPKVQLVI SYEDVKLTIL
     VKHMKNIHLP DGSAPSAHVE FYLLPYPSEV RRRKTKSVPK CTDPTYNEIV VYDEVTELQG
     HVLMLIVKSK NTFVGAINIQ LCSVLLNEEK WYPLGNSII
//
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