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Database: UniProt
Entry: A0A1S3LVS0_SALSA
LinkDB: A0A1S3LVS0_SALSA
Original site: A0A1S3LVS0_SALSA 
ID   A0A1S3LVS0_SALSA        Unreviewed;       563 AA.
AC   A0A1S3LVS0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=LOC106568674 {ECO:0000313|RefSeq:XP_013994674.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013994674.1};
RN   [1] {ECO:0000313|RefSeq:XP_013994674.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013994674.1};
RG   RefSeq;
RL   Submitted (NOV-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   RefSeq; XP_013994674.1; XM_014139199.1.
DR   AlphaFoldDB; A0A1S3LVS0; -.
DR   STRING; 8030.ENSSSAP00000111808; -.
DR   PaxDb; 8030-ENSSSAP00000111808; -.
DR   KEGG; sasa:106568674; -.
DR   OrthoDB; 5475340at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa01.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   CDD; cd14403; UBA_AID_AAPK1; 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; IPR028797; PRKAA1_UBA.
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   Kinase {ECO:0000313|RefSeq:XP_013994674.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000087266};
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   Transferase {ECO:0000313|RefSeq:XP_013994674.1};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT   DOMAIN          1..244
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          484..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  63597 MW;  53434D26BB891C75 CRC64;
     MLSLSLVVGQ HELTKHQVAV KILNRQKIRS LDVVGKIRRE IQNLKLFRHP HIIKLYQVIS
     TPTDIFMVME YVSGGELFDY ICKNGKLDEK ESRRLFQQII SAVDYCHRHM VVHRDLKPEN
     VLLDAQMNAK IADFGLSNMM SDGEFLRTSC GSPNYAAPEV ISGRLYAGPE VDIWSSGVIL
     YALLCGTLPF DDDHVPTLFK KICDGIFFTP QYLNPSVASL LKHMLQVDPM KRATIKEIRE
     DEWFKEELPK YLFPEDPSYS NNMIDDEALK EVCEKFECTE EEILTCLYSR NHHDPLAVAY
     HLIIDNRRIM SEAKDFYLAS SPPDSFLDDQ HLTASAAAAA GLKPHPERMQ PFLAVETPPR
     PRHTLDELNP QKSKHQGVRR AKWHLGIRSQ SRPNDIMSEV CRAMKQLDYE WKVANPYYLR
     VKRKNPVTGM QTKMSLQLYQ VDSRTYLLDF RSIDNDMLEA KSGTATPHRS GSVGNYRMAL
     KNDTAAEGGS QTEGAKEDAT PTPATSIPPT PTKASESSLA SSLTSSVDST GGDLALTTVY
     PRPGSHTIEF FEMCANLIKL LAR
//
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