ID A0A093IXD9_EURHL Unreviewed; 434 AA.
AC A0A093IXD9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phosphatidylinositol 3-kinase regulatory subunit gamma {ECO:0000313|EMBL:KFW04302.1};
DE Flags: Fragment;
GN ORFNames=N326_04795 {ECO:0000313|EMBL:KFW04302.1};
OS Eurypyga helias (Sunbittern) (Ardea helias).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Eurypygiformes;
OC Eurypygidae; Eurypyga.
OX NCBI_TaxID=54383 {ECO:0000313|EMBL:KFW04302.1, ECO:0000313|Proteomes:UP000054232};
RN [1] {ECO:0000313|EMBL:KFW04302.1, ECO:0000313|Proteomes:UP000054232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N326 {ECO:0000313|EMBL:KFW04302.1};
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 PI3K p85 subunit family.
CC {ECO:0000256|ARBA:ARBA00009442}.
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DR EMBL; KK565922; KFW04302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093IXD9; -.
DR Proteomes; UP000054232; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd09930; SH2_cSH2_p85_like; 1.
DR CDD; cd09942; SH2_nSH2_p85_like; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR InterPro; IPR032498; PI3K_P85_iSH2.
DR InterPro; IPR035020; PI3kinase_P85_cSH2.
DR InterPro; IPR035022; PI3kinase_P85_nSH2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR PANTHER; PTHR10155; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10155:SF10; PI3K21B, ISOFORM B; 1.
DR Pfam; PF16454; PI3K_P85_iSH2; 1.
DR Pfam; PF00017; SH2; 2.
DR PRINTS; PR00678; PI3KINASEP85.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR PROSITE; PS50001; SH2; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KFW04302.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054232};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Transferase {ECO:0000313|EMBL:KFW04302.1}.
FT DOMAIN 37..132
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 330..424
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..180
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW04302.1"
FT NON_TER 434
FT /evidence="ECO:0000313|EMBL:KFW04302.1"
SQ SEQUENCE 434 AA; 51030 MW; 5EA2DFFF69DE035D CRC64;
IEMDPPALPP KPPKPMTPVN TNGIKDSSSF SLQEAEWYWG DISREEVNDK LRDMPDGTFL
VRDASTKMQG DYTLTLRKGG NNKLIKIYHR DGKYGFSDPL TFNSVVELIN HYRNESLAQY
NPKLDVKLMY PVSRYQQDQL VKEDNIDAVG KKLQEYHAQY QEKSKEYDKL YEEYTRTSQE
IQMKRTAIEA FNETIKIFEE QCHSQERYSK EYIERFRREG NDKEIERIMM NYEKLKSRLG
EIHDSKMRLE QDLKKQALDN RETDKKMNSI KPDLIQLRKI RDQYLVWLNH KGVRQKRIND
WLGIKNENID DTYFVNEEDE NLPHHDEKTW FVGDLNRIQA EDLLCGKPDG AFLIRESSKK
GCYACSVVAD GEVKHCVIYS TPRGYGFAEP YNLYSTLKDL VLHYQQTSLV QHNDSLNVRL
AYPVYAQMPP SLCR
//
