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Database: UniProt
Entry: A0A3Q1FGW7_9TELE
LinkDB: A0A3Q1FGW7_9TELE
Original site: A0A3Q1FGW7_9TELE 
ID   A0A3Q1FGW7_9TELE        Unreviewed;       703 AA.
AC   A0A3Q1FGW7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
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   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000017086.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000017086.1}
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A3Q1FGW7; -.
DR   STRING; 80966.ENSAPOP00000017086; -.
DR   Ensembl; ENSAPOT00000033916.1; ENSAPOP00000017086.1; ENSAPOG00000020305.1.
DR   GeneTree; ENSGT00950000182937; -.
DR   InParanoid; A0A3Q1FGW7; -.
DR   Proteomes; UP000257200; 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-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; 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   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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..250
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          625..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   703 AA;  80289 MW;  26C76D64D8F69C2D CRC64;
     MFTSTSIRLN HINVVTAQDV PEEIEYIALN DLPLLAMEYC SRGDLRKMLG KPENCCGLKE
     SEVLSLLNDV GSGIQYLHEN KIIHRDLKPE NIVLQDINGK LVHKIIDLGY AKDLDQGSLC
     TSFVGTLQYL APELFENKPY TVTVDYWSFG TMIFECSCGF RPFLDNLQPV QWASEVKNKG
     PKDIMATEEL NGEVRFSTHL PYPNNLSRTL LEPMEELLQL MLKWDPVQRG GRINSETRKP
     QCFEKLEQIL SMKVVHILNM TTAQVHSFQL TPDESLHSLQ RRIEAETKIE VVNQELLQET
     GVSLDPRKPA AQCVLDGVRG WDSYIVYLFD KSITTYSGPF SARRLSEKVN TIVQDAKTQL
     PLVVLKKVWG EAVSYICGLK DDYSRLFQGQ RAAMLSLLRY NTNLTRCKNC MFGFSQQLKA
     KLDFFKSSIQ YDLEKYSDQM HYGISSEKML KAWQENEERA AAFAQVAEVS HLDDEIMALH
     SEIVELQRSP YARRQGEKME QLEEKAIELY RQLKMKCKVP DSDVSSDSSE MVKAIIQTVQ
     NQDKVLKDLF THLSKILISK QKIIDLFPRI EKTLESIKDA DNTVMQMQIK RQREFWHLLK
     IACAQNSSRN SMAASPESSN LLQVSQWSQS AQPVSSPHPL TSLPGPNDSD AAPRLLQENQ
     KYLSQLTSLM QEAADDQANS IVDQDWSWTK YETLTTKLKK RNA
//
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