ID A0A091RG62_9GRUI Unreviewed; 589 AA.
AC A0A091RG62;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3 {ECO:0000313|EMBL:KFQ38262.1};
DE Flags: Fragment;
GN ORFNames=N332_03483 {ECO:0000313|EMBL:KFQ38262.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ38262.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ38262.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ38262.1};
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. {ECO:0000256|PROSITE-
CC ProRule:PRU00880}.
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DR EMBL; KK816010; KFQ38262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RG62; -.
DR Proteomes; UP000053369; 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 CDD; cd08397; C2_PI3K_class_III; 1.
DR CDD; cd00870; PI3Ka_III; 1.
DR Gene3D; 2.60.40.150; C2 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; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KFQ38262.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053369};
KW Transferase {ECO:0000313|EMBL:KFQ38262.1}.
FT DOMAIN 12..163
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 260..496
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT REGION 127..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ38262.1"
FT NON_TER 589
FT /evidence="ECO:0000313|EMBL:KFQ38262.1"
SQ SEQUENCE 589 AA; 67536 MW; A345090EAD273069 CRC64;
GSLEGKREQK SYKALLEDPM LKFSGLYQET CSDLYVTCQV FAEGKPLALP VRTSYKAFST
RWNWNEWLKL PVKYPDLPRN AQVALTIWDV YGPGKAVPVG GTTVSLFGKY GMFRQGMHDL
KVWPNVEADG SEPTRTPGRT SSTVSEDQMS RLAKLTKSHR QGHMVKVDWL DRLTFREIEM
INEREKRSSN FMYLMIEFRC VKCDDKEYGI VYYEKDGDES SSILTSSEIV KIPDPQMSME
NLVESKHHKL ARSLRSGPSD HDLKPNAATR DQLNIIVSYP PTKQLTYEEQ DLVWKFRYYL
TNQEKALTKF LKCVNWDLPQ EAKQALELLG KWKPMDVEDS LELLSSHFTN PTVRRYAVAR
LQQADDEDLL MYLLQLVQAL KYENFDDIKN GLEPSKRDSQ GSMSESMATS GTNGAEIDSS
QIMTPVPPVS SPPLTSKTKE LADNENLDQD LCTFLISRAC KNSTLANYLY WYVIVECEDQ
DTQQRDPKTH EMYLNVMRRF SQALLKGDKS VRVMRSLLAA QQTFVDRLVH VMKAVQRESG
NRKKKNERLQ ALLADNEKMN LADMELIPLP LEPQVKIKGI IPEKATLFK
//
