ID A0A1S3Q498_SALSA Unreviewed; 684 AA.
AC A0A1S3Q498;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=cGMP-dependent protein kinase {ECO:0000256|ARBA:ARBA00012428, ECO:0000256|PIRNR:PIRNR000559};
DE EC=2.7.11.12 {ECO:0000256|ARBA:ARBA00012428, ECO:0000256|PIRNR:PIRNR000559};
GN Name=LOC106589397 {ECO:0000313|RefSeq:XP_014034785.1};
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_014034785.1};
RN [1] {ECO:0000313|RefSeq:XP_014034785.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014034785.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000962};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.12; Evidence={ECO:0000256|ARBA:ARBA00000555,
CC ECO:0000256|PIRNR:PIRNR000559};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cGMP subfamily. {ECO:0000256|ARBA:ARBA00006352,
CC ECO:0000256|PIRNR:PIRNR000559}.
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DR RefSeq; XP_014034785.1; XM_014179310.1.
DR AlphaFoldDB; A0A1S3Q498; -.
DR GeneID; 106589397; -.
DR CTD; 566430; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000087266; Chromosome ssa28.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd12086; DD_cGKI-beta; 1.
DR CDD; cd05572; STKc_cGK; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR002374; cGMP_dep_kinase.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031831; PKcGMP_CC.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR035014; STKc_cGK.
DR PANTHER; PTHR24353:SF151; -; 1.
DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF16808; PKcGMP_CC; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000559; cGMP-dep_kinase; 1.
DR PRINTS; PR00104; CGMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PIRNR:PIRNR000559};
KW cGMP {ECO:0000256|ARBA:ARBA00022535, ECO:0000256|PIRNR:PIRNR000559};
KW cGMP-binding {ECO:0000256|ARBA:ARBA00022992,
KW ECO:0000256|PIRNR:PIRNR000559}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000559};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000559};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000559};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000559}.
FT DOMAIN 116..231
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 234..355
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 373..632
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 633..684
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 648..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 11..59
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 649..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 497
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-1"
FT BINDING 379..387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2"
FT BINDING 403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 684 AA; 77860 MW; 4E6B33CDD6662B49 CRC64;
MGTLRDLQYA LQEKIEELRQ RDALIDELEL ELDQKDELIQ KLQNELDKYR SVIKPATQQV
HKASVLQEQH RTKRQAISGE PTAFDIHELS HVTLPFYPKS PQSKDLIKEA ILDNDFMKNL
ELSQIQEIVD SMYPVEYGKD SCIIKEGDVG SLVYVMEDGK VEVTKESMKL CTMGPGKVFG
ELAILYNCTR TATVKTLTNV KLWAIDRQCF QTIMMRTGLI KHAEYMEFLK SVPTFQGLSE
EILSKLADVM EETHYGDGEY IIRQGARGDT FFIISKGKVN VTREDLPNDM PVYLRALGKG
DWFGEKALQG EDIRTANVIA ADAVTCLVID RDSFKHLIGG LEDVSNKGYE DAGAKAKYEA
ENAFFCNLKL VDFNIIDTLG VGGFGRVELV QLKSDEIKTF AMKILKKRHI VDTRQQEHIR
SEKQIMQEAH SDFIVRLYRT FKDAKYLYML MEACLGGELW TILRDRGSFE DSTTRFYTAC
VVEAFAYLHS KGIIYRDLKP ENLILDHRGY AKLVDFGFAK KIGFGKKTWT FCGTPEYVAP
EIILNKGHDI SADYWSLGIL MYELLTGSPP FSGPDPMKTY NIILRGIDMI EFPKKITKNA
ANLIKKLCRD NPSERLGNLK NGVKDIQKHK WFEGFNWEGL RKGTLTPPII PEVSSSTDTS
NFDSFPEDNN DPPPDDMSGW DTDF
//
