ID   A0A091J2P0_EGRGA        Unreviewed;       679 AA.
AC   A0A091J2P0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Inhibitor of nuclear factor kappa-B kinase subunit alpha {ECO:0000256|ARBA:ARBA00021841};
DE            EC=2.7.11.10 {ECO:0000256|ARBA:ARBA00012442};
DE   AltName: Full=Nuclear factor NF-kappa-B inhibitor kinase alpha {ECO:0000256|ARBA:ARBA00032095};
DE   Flags: Fragment;
GN   ORFNames=Z169_05164 {ECO:0000313|EMBL:KFP14872.1};
OS   Egretta garzetta (Little egret).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX   NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP14872.1, ECO:0000313|Proteomes:UP000053119};
RN   [1] {ECO:0000313|EMBL:KFP14872.1, ECO:0000313|Proteomes:UP000053119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP14872.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-
CC         seryl-[I-kappa-B protein]; Xref=Rhea:RHEA:19073, Rhea:RHEA-
CC         COMP:13698, Rhea:RHEA-COMP:13699, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; EC=2.7.11.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00023939};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KK501441; KFP14872.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091J2P0; -.
DR   STRING; 188379.A0A091J2P0; -.
DR   Proteomes; UP000053119; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008384; F:IkappaB kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd17046; Ubl_IKKA_like; 1.
DR   Gene3D; 1.20.1270.250; -; 1.
DR   Gene3D; 6.10.250.2110; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041185; IKBKB_SDD.
DR   InterPro; IPR046375; IKBKB_SDD_sf.
DR   InterPro; IPR022007; IKKbetaNEMObind.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22969; IKB KINASE; 1.
DR   PANTHER; PTHR22969:SF13; INHIBITOR OF NUCLEAR FACTOR KAPPA-B KINASE SUBUNIT ALPHA; 1.
DR   Pfam; PF18397; IKBKB_SDD; 1.
DR   Pfam; PF12179; IKKbetaNEMObind; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM01239; IKKbetaNEMObind; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFP14872.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..236
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          612..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP14872.1"
FT   NON_TER         679
FT                   /evidence="ECO:0000313|EMBL:KFP14872.1"
SQ   SEQUENCE   679 AA;  77348 MW;  9965D516781DC96B CRC64;
     RLNHPNVVRA CDVPEEMNFL VNDVPLLAME YCSGGDLRKL LNKPENCCGL KESQILSLLS
     DIGSGIQYLH ENRIIHRDLK PENIVLQDEG GKIVHKIIDL GYAKDLDQGS LCTSFVGTLQ
     YLAPELFENK SYSVTVDYWS FGTMVFECIA GFRPFLHNLQ PFTWHEKIKK KDPKHIFASE
     EMNGEVRFST HLPQPHSLCG LIVEPIENWL QLMLNWDPQQ RGGGLDPETS RPKCFLIMDH
     ILNLKVVHIL NMTSAKIVSF LLHPEDSLHS LQIRIEFETG ISTGNQELLL ETGICLDPRK
     PASQCVIDGV RGWDSYMVYL FDKSKTVYDG PFASRSLSDC VNYIVQDSKI QLPIPQLRKV
     WAEAVHYVIG LKEDYSRLFQ GQRAAMLSLL RYNANLIKMK NNMVSASQQL KAKLEFFQQS
     IRLDLERYSD QMAYGISSEK MLKAWKEMEE KASQCAQAED IGYLDEQIMA LHTEIVELQK
     SPYARRQGEV MESLEQRAID LYKQLKTRPP DHAYSDSTDM VKIIVQTVQS QDRVLKELFG
     HLSKLLGCKQ KIIDLLPKIE VALNNIKEAD NSVMQMQGKR QREIWHLLKI ACTQSSSRSL
     VSSSLEGTAS TPAATWLPQS SSGNVPHPLS SMATPEDGEN FVHVIEENLT YLELFSSILQ
     EARQEQNSSM MSFDWSWLK
//