ID   A0A3Q1JN72_ANATE        Unreviewed;       688 AA.
AC   A0A3Q1JN72;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 25.
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};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000032094.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000032094.2}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; A0A3Q1JN72; -.
DR   Ensembl; ENSATET00000032564.2; ENSATEP00000032094.2; ENSATEG00000022062.2.
DR   GeneTree; ENSGT00950000182937; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        646..669
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..302
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   688 AA;  78890 MW;  B1F4F344968F4DD3 CRC64;
     MERTAQLCGS WEMKEKLGMG GFGHVYLYQH LESGEKIAVK LCRLELNSKN KDRWSREIQI
     MKKLNHVNVV QAREVPEELS SIALNDLPLL SMEYCSRGDL RKVLNKPENC CGLKESEVLS
     LLNDIGSGIQ YLHENKIIHR DLKPENIVLQ DIDGKLVHKI IDLGYAKDLD QGSLCTSFVG
     TLQYLAPELF ESKPYTVTVD YWSFGTVIFE CTCGFRPFLH HMQPVTSKVK NKGPKDIMAV
     EDMNGEVRFS THLPYPNNLS RPLLEPVESL LQMLLLWDPA TRGGGLDPGT TKQGKHCAHL
     FLQVIHVLDM TSAQLHSLVL GGEESLHSLQ LRLEIQTQTH ISPLSQELLL ETGISLDPRR
     PPAHCLPEGL RGWDTSIVFL FDKSLTKYCG PLTARPLPDS VNFIVRETKT QLPLTALRKV
     WGEAVSYICG LKEDYLRLYQ GQRAAMLSLL RYNTTLTRYK NMLFSQSQQL RAKLAFFKTS
     IQHDLEQYIK QRHSGISSEK MLKTWQENEK KADEFTKVAD VGYLDEEIVA LHSEIVELQR
     SPFARRQEDV MEQLEEKAIE LYKQLKAKCP DPPHGYSDSS DMVKTILQTV QNQDRVLKDL
     YTHLSTILVC KRRIVDLFPK LEGAVENIKT AEATVMQMQM KRQKEFWYLL KIACVTSCLS
     VKPFINYWMR ITTPPKRWST VSWYDMKV
//