ID A0A091RKR8_MERNU Unreviewed; 1064 AA.
AC A0A091RKR8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma {ECO:0000313|EMBL:KFQ29132.1};
DE Flags: Fragment;
GN ORFNames=N331_04210 {ECO:0000313|EMBL:KFQ29132.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ29132.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ29132.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ29132.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK704029; KFQ29132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RKR8; -.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05177; PI3Kc_C2_gamma; 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; IPR037707; PI3K-C2-gamma_dom.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
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 Pfam; PF00787; PX; 1.
DR SMART; SM00239; 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 PROSITE; PS50004; C2; 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; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFQ29132.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 97..261
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 261..437
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 506..784
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 818..930
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 947..1064
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ29132.1"
FT NON_TER 1064
FT /evidence="ECO:0000313|EMBL:KFQ29132.1"
SQ SEQUENCE 1064 AA; 121420 MW; 9E2A4ED6AAE930F3 CRC64;
DDQRRFSVNQ LLQDTCAWRL TGQNLTSLIM KYRGQVEYLL QNEHAVDNVI EVTKAICSVL
GFVETRDITD AVKKLRAVPL VKVQVKDESY VLFFSLIEAA VTELSMAISC LIHVYSSSFD
VNFQLASIPK IPSCADISLD SQLSFTVYAA HNIPEAWVNR INFPLRIKAL PRETMLTIKL
LGVNSASKNT EVLAWTCSPL YPKERLIHGT VLLSMTLCST LTKTMVAPGI CSTDTPTSVT
LQIDFPETNL EFIKPEPEER RDELEEPTKD CLKHIARLSQ MHSLLLLSEQ QRRILWFYRY
YCNNQNCSLP LVLGSAPSWD RTTIAEMYTM LRRWEFSNPL EALGLLTFSF PDQDIRRTAV
QQIEYMSNDE LLEYLPQLVQ VLKFEWSLES PLVKLLLNRS LQSLQVAHQF YWLLKNAQNE
VHFKIWYRKL LAALQFCAGE TLNNEFSKEG KLIRILEDIA EKVKAAGDPK RKEVLKVELN
RLQQFFQEVK ACRLPLNPAL VVQGIEADSC SYFTSNAFPL KISFINANAP GRNINVIFKI
GDDLRQDMLV LQIIRVMDSI WLQEGLDMQM IIYRCLSTGK GQGLVQMVPD AITLAKIHRE
SGLIGPLKEN TIKKWFHHHH PLESSYQEAI RNFFYSCAGW CVVTFILGVC DRHSDNIMLT
NAGHMFHIDF GRFLGHAQTF GSIRRDRAPF IFTSEMEYFI TEGGKNPQRF QDFVELSCRA
YNIVRKHSRL VLNLLEMMLH AGLPELNSIQ DLKYVYDNLR PQDSDLQATS YFTRKVKESL
ECFPVKLNNL IHTLVQMSVA GPAKPPAPET VPQEWMMLDA DKSIARATIL GFNKKPNSLY
LVQVVQTCNV VSFVEKSFDQ FAKLHSHLQK QFPSHALPEF PHSWNLSSTY LEHKRVKDLN
LYLKQLLSGS RKLANNEHVL SFFLNGYKNT LAEDSSSVTL GPQSTAHKPG VQLVISYESA
CLTIMLKHMR NIRLPDGSAP SAHAEFYLLP DPYEVSRRKT RTAPKSSDPT YNEIIVYDKV
TELRGHVLKL VVKSKGTFVG AVNIQLSSVQ LNEEKWYPLG NSVI
//
