ID   A0A1S3WKE2_ERIEU        Unreviewed;       719 AA.
AC   A0A1S3WKE2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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   Name=CHUK {ECO:0000313|RefSeq:XP_016046848.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016046848.1};
RN   [1] {ECO:0000313|RefSeq:XP_016046848.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_016046848.1; XM_016191362.1.
DR   AlphaFoldDB; A0A1S3WKE2; -.
DR   GeneID; 103119930; -.
DR   CTD; 1147; -.
DR   OrthoDB; 3949542at2759; -.
DR   Proteomes; UP000079721; Unplaced.
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-UniRule.
DR   GO; GO:0008384; F:IkappaB kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:UniProt.
DR   CDD; cd14039; STKc_IKK_alpha; 1.
DR   CDD; cd17046; Ubl_IKKA_like; 1.
DR   Gene3D; 1.20.1270.250; -; 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; 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; PF00069; Pkinase; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_016046848.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          15..302
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   719 AA;  82124 MW;  667983B88B8867E6 CRC64;
     MERPPGLRPG AGGPWEMRER LGTGGFGNVC LYQHRELDLK IAIKSCRLEL STKNRERWCH
     EIQIMKKLDH ANVVKACDVP EELNFLINDV PLLAMEYCSG GDLRKLLNKP ENCCGLKESQ
     ILSLLNDIGS GIRYLHENKI IHRDLKPENI VLQDVGGKIM HKIIDLGYAK DVDQGSLCTS
     FVGTLQYLAP ELFENKPYTA TVDYWSFGTM VFECIAGYRP FLHHLQPFTW HEKIKKKDPK
     CIFACEEMTG EVRFSSHLPQ PNSLCSLIVE PMENWLQLML SWDPQQRGGP VDVTLKQPRC
     FVLMDYILNL KIVHILNMTS AKIISFLLPS DESLHSLQSR IERETGINTG SQELLSETGI
     SLDPRKPASQ CVLDGVRGCD SYMVYLFDKS KTVYEGPFAS RSLSECVNYI VQDSKIQLPI
     IQLRKVWAEA VNYVSGLKED YSRLFQGQRA AMLSLLRYNA NLTKMKNTLI SASQQLKAKL
     EFFHKSIQLD LERYSEQMTY GISSEKMLKA WKEMEEKAIH YAEVGVIGYL EDQIMSLHTE
     IMELQKSPYG RRQGDLMESL EQRAIDLYKQ LKHRPPDHSY SDSTDMVKII VHTVQSQDRV
     LKELFGHLSK LLGCKQKIID LLPKVEMALS NIKEADNTVM FMQGKRQKEI WHLLKIACTQ
     SSARSLVGSS LEGAVTPQTS AWQPPTSAER EIPLSCVGNF DTNDRRKYEL SWSLRHNYS
//