ID   A0A3P8RZS3_AMPPE        Unreviewed;       742 AA.
AC   A0A3P8RZS3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
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   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000005357.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000005357.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000005357.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A3P8RZS3; -.
DR   Ensembl; ENSAPET00000005497.1; ENSAPEP00000005357.1; ENSAPEG00000003851.1.
DR   GeneTree; ENSGT00950000182937; -.
DR   OMA; MQPFTWH; -.
DR   Proteomes; UP000265080; Chromosome 19.
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   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; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          15..309
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          685..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   742 AA;  84878 MW;  FF7927CEE3E5D374 CRC64;
     MEKPPFRQNH NCGDWELKER LGMGGFAHVY LFQHQETNEK LAVKMCRLEL TPRNKDRWSR
     EIQIMKKLNH INVVTARDVP EEIEYIALND LPLLAMEYCS RGDLRKMLGK PENCCGLKES
     EVLSLLNDVG SGIQYLHENK IIHRDLKPEN IVLQDINGKL VHKIIDLGYA KDLDQGSLCT
     SFVGTLQYLA PELFETKPYT VTVDYWSFGT MIFECSCGFR PFLDNLQPVQ WASEVKNKGP
     KDIMATAELN GEVRFSKHLP YPNNLSRTLL EPMEELLQLM LKWDPSLRGG RVNSETKKPQ
     CFEKLEQILS MKVVHILNMT TAQVHSFQLT PDESLHSLQK RIEIETKIEV VNQELLQETG
     VSLDPRKPAA QCVLDGVRGW DSYIVYLFDK SITTYSGPFS ARRLSEKVNT IVQDAKTQLP
     LAMLKKVWGE AVSYICGLKE DYSRLFQGQR AAMLSLLRYN TNLTRCKNCM FGFSQQLKAK
     LDFFKSSIQY DLEKYSDQMH YGISSEKMLK AWQENEERAA AFAQVAEVGH LDDEIMALHS
     EIVELQRSPY ARRQGDKMEQ LEEKAIELYR QLKMKCKIPD SDVSSDSSEM VKAIIQTVQN
     QDKVLKDLFT HLSKILISKQ KIIDLFPRIE KTLESIKDAD NAVMQMQIKR QREFWHLLKI
     ACAQNSSRNS IAASPESSNL LQVSQWSQSA QPVSSPHPLT SLPGPNDSDA APRLLQENQK
     YLSQLTSLMQ EAADDQAKSI VL
//