ID A0A5J5CQ67_9PERO Unreviewed; 734 AA.
AC A0A5J5CQ67;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 18-JUN-2025, entry version 22.
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};
GN ORFNames=FQN60_015065 {ECO:0000313|EMBL:KAA8583857.1};
OS Etheostoma spectabile (orangethroat darter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Etheostomatinae; Etheostoma.
OX NCBI_TaxID=54343 {ECO:0000313|EMBL:KAA8583857.1, ECO:0000313|Proteomes:UP000327493};
RN [1] {ECO:0000313|EMBL:KAA8583857.1, ECO:0000313|Proteomes:UP000327493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EspeVRDwgs_2016 {ECO:0000313|EMBL:KAA8583857.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAA8583857.1};
RA Moran R.L., Catchen J.M., Fuller R.C.;
RT "A chromosome-level genome assembly, high-density linkage maps, and genome
RT scans reveal the genomic architecture of hybrid incompatibilities
RT underlying speciation via character displacement in darters (Percidae:
RT Etheostominae).";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[I-kappa-B protein] + ATP = O-phospho-L-seryl-[I-
CC kappa-B protein] + ADP + H(+); 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:ARBA00048789};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA8583857.1}.
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DR EMBL; VOFY01000017; KAA8583857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5CQ67; -.
DR OrthoDB; 267381at2759; -.
DR Proteomes; UP000327493; Chromosome 17.
DR GO; GO:0008385; C:IkappaB kinase complex; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008384; F:IkappaB kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:TreeGrafter.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:TreeGrafter.
DR FunFam; 1.20.1270.250:FF:000001; Inhibitor of nuclear factor kappa-B kinase subunit alpha; 1.
DR FunFam; 1.10.510.10:FF:000147; Inhibitor of nuclear factor kappa-B kinase subunit beta; 1.
DR Gene3D; 1.20.1270.250; -; 1.
DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 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; IPR051180; IKK.
DR InterPro; IPR022007; IKKbetaNEMObind.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000327493};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..303
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 734 AA; 83851 MW; 05897D0C6A9E4402 CRC64;
MERSTLKQSQ LCGSWEMKEK LGTGGFGHVY LYQHLELGEK IALKLCRLEL NSKNKDRWGR
EIQIMKKLNH VNVVQAKDVP EELSSIALND LPLLAMEYCS RGDLRKVLNK PENCCGLKES
EVLSLLSDIG SGIQYLHENK IIHRDLKPEN IVLQEVGGKL VHKIIDLGYA KDLDQGSLCT
SFVGTLQYLA PELFESKPYT VTVDYWSFGT VIFECTCGFR PFLHHMQPVQ WTSKVKNKGL
KDIMAVEDMN GEVRFSPHLP YPNNLSRPLL EPVECLLQML LLWDAAMRGG GLDPDTNKPH
CYTALQNILN MKVIHVLDMT SAQLHSLVLG AEESLHSLQL RLETHTQTHI SPLSQELLLE
TGISLDPRRL PAHCLPEGLR GWDSSIVFLF DKSLTKYSGP LTARPLPDSV NFIVRETKTQ
LPLSALRKVW GEAVSYICGL KEDYIRLYQG QRAAMLSLLR YNTNLTRYKN LLFSQSQQLR
AKLAFFKTSI QHDLEQYTKQ RHIGISSEKM LKTWQENEDK ADGFTKVADV GYLDEEIVAL
HSEIVELQRS PFARRQGDVM EQLEEKAIDL FKQLKAKCKS PDPPHGYSDS SDMVKMILQT
VQNQDRVLKD LYTHLSTILV CKRRIVDLFP KLERAVENIK TAEAAVMQMQ MKRQKEFWYL
LKIACAQSNS PSQSLMQQST DSETVHQLLD ENQRHLSQLT SLLQDATQEM EHSVMDQDWS
WTQYGAVKAQ PQKL
//
