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Database: UniProt
Entry: A0A091FRH0_9AVES
LinkDB: A0A091FRH0_9AVES
Original site: A0A091FRH0_9AVES 
ID   A0A091FRH0_9AVES        Unreviewed;       690 AA.
AC   A0A091FRH0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=IkappaB kinase {ECO:0000256|ARBA:ARBA00012442};
DE            EC=2.7.11.10 {ECO:0000256|ARBA:ARBA00012442};
DE   Flags: Fragment;
GN   ORFNames=N303_05453 {ECO:0000313|EMBL:KFO71576.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO71576.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO71576.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO71576.1};
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; KL447267; KFO71576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091FRH0; -.
DR   STRING; 55661.A0A091FRH0; -.
DR   Proteomes; UP000053760; 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   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR22969; IKB KINASE; 1.
DR   PANTHER; PTHR22969:SF7; INHIBITOR OF NUCLEAR FACTOR KAPPA-B KINASE SUBUNIT BETA; 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   SUPFAM; SSF54236; Ubiquitin-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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFO71576.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..233
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   COILED          463..513
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO71576.1"
FT   NON_TER         690
FT                   /evidence="ECO:0000313|EMBL:KFO71576.1"
SQ   SEQUENCE   690 AA;  79389 MW;  169EBCDE6F350884 CRC64;
     RLNHPNVVAA RDVPEGMQKL APNDLPLLAM EYCQGGDLRK YLNQLENCCG LREEAILILL
     SDIASALRYL HENRIIHRDL KPENIVLQQG EQRLIHKIID LGYAKELDQG SLCTSFVGTL
     QYAPELLEQQ KYTVTVDYWS FGTLAFECIT GFRPFLPNWQ PVQWHTKVRQ KSELDIVVSE
     DLSGEVKFSS SLPCPNNLNS VLAGRLEKWL QLMLMWHPRQ RGTDPTYGPY GCFKALDDIL
     NLKLLHVLNM VTGTVHTYPV TEEDTLQTLK ARIQSDTGIP EQDQELLQEA GLELFSQKLA
     TKHIADSKVN DTAAADTDLL FLFDNQKVAY EAQVALRPHP ESVDCILQDP KKNLHFFQLR
     KVWGQIWHTI RMLKEDCNRL QQGQRAAMMN LLRYNSTLSK MKNSMASLSQ QLKAKLDFFK
     TSIQIDLEKY KEQIEFGITS EKLLFAWKEM EQAVELCGRE DDVDQLVKRM MALQTDIVDL
     QRSPLGRKQG GTLEDLEEQA RELYRRLREK PRDQRTSGDS QEIVRLLLQA IQAFEKKVRV
     IYAQLSKTVV CKQKALELFP RVEKVMNLMN EDEETVVRLQ EKRQKELWNL LKIACSKVRG
     PVTGSPESMN TSRLGSPGHL MLQVPSGTYN LSESVRKSEE LLLESQKLCS QLENVMRDTM
     KDQEQSFMAL DWSWLQLHTE EPNSPEQTQM
//
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