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Database: UniProt
Entry: A0A3B4WZ67_SERLL
LinkDB: A0A3B4WZ67_SERLL
Original site: A0A3B4WZ67_SERLL 
ID   A0A3B4WZ67_SERLL        Unreviewed;       536 AA.
AC   A0A3B4WZ67;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Acetyl-CoA carboxylase kinase {ECO:0000256|ARBA:ARBA00032270};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.31 {ECO:0000256|ARBA:ARBA00012403};
DE   AltName: Full=Hydroxymethylglutaryl-CoA reductase kinase {ECO:0000256|ARBA:ARBA00032865};
GN   Name=PRKAA2 {ECO:0000313|Ensembl:ENSSLDP00000009230.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000009230.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000009230.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A
CC         reductase] = ADP + H(+) + O-phospho-L-seryl-[3-hydroxy-3-
CC         methylglutaryl-coenzyme A reductase]; Xref=Rhea:RHEA:23172,
CC         Rhea:RHEA-COMP:13692, Rhea:RHEA-COMP:13693, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; EC=2.7.11.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00023941};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[acetyl-CoA carboxylase] = ADP + H(+) + O-
CC         phospho-L-seryl-[acetyl-CoA carboxylase]; Xref=Rhea:RHEA:20333,
CC         Rhea:RHEA-COMP:13722, Rhea:RHEA-COMP:13723, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036863};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}.
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DR   AlphaFoldDB; A0A3B4WZ67; -.
DR   Ensembl; ENSSLDT00000009549.1; ENSSLDP00000009230.1; ENSSLDG00000007304.1.
DR   GeneTree; ENSGT00940000156945; -.
DR   Proteomes; UP000261360; Unplaced.
DR   GO; GO:0050405; F:[acetyl-CoA carboxylase] kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047322; F:[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0031331; P:positive regulation of cellular catabolic process; IEA:UniProt.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd14079; STKc_AMPK_alpha; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR032270; AMPK_C.
DR   InterPro; IPR028375; KA1/Ssp2_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR049020; PRKAA1/2_AID.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR   PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR   Pfam; PF16579; AdenylateSensor; 1.
DR   Pfam; PF21147; AMPK_alpha_AID; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF103243; KA1-like; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW   Cholesterol biosynthesis {ECO:0000256|ARBA:ARBA00022778};
KW   Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022778};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022955};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023011};
KW   Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023011};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT   DOMAIN          1..249
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   536 AA;  60693 MW;  434B330623D1B2B1 CRC64;
     MSKYINDKKS WYIGEHQLTG HKVAVKILNR QKIRSLDVVG KIKREIQNLK LFRHPHIIKL
     YQVISTPTDF FMVMEYVSGG ELFDYICKHG RVEDTEARRL FQQIISAVDY CHRHMVVHRD
     LKPENVLLDA SKNAKIADFG LSNMMSDGEF LRTSCGSPNY AAPEVISGRL YAGPEVDIWS
     CGVILYALLC GTLPFDDEHV PTLFKKIRGG VFYIPEYLTR SVASLLMLML QVDPLKRATI
     KDIREHEWFK QDLPGYLFPE DPSYDATVLD EEAVREVCEK FECMESEVMS SLYSGDPQDQ
     LAVAYHLIID NRRIMTQASE FYLASSPPQG SFIEEGMPLP PGVKPHPERM PPLLADSPKS
     RCPLDALNTT RPKPLAVKKA KWHLGIRSQS RPYDIMAEVY RAMKQLNFDW KVVNPYHLRV
     RRKNPVTGNL VKMSLQLYQV DSRSYLLDFK SIDDDIIEAV GFKSGSSTPQ RSGSTAGLHR
     PRLSIDSASP AFDLPQLSSS LPGSLSGSNP LLTPRQGSHT MDFFEMCASL ITTLAR
//
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