ID A0A1S3PEH4_SALSA Unreviewed; 532 AA.
AC A0A1S3PEH4;
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=calcium/calmodulin-dependent protein kinase {ECO:0000256|ARBA:ARBA00012434};
DE EC=2.7.11.17 {ECO:0000256|ARBA:ARBA00012434};
GN Name=LOC106584897 {ECO:0000313|RefSeq:XP_014026017.1};
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_014026017.1};
RN [1] {ECO:0000313|RefSeq:XP_014026017.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014026017.1};
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=2.7.11.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000902};
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=2.7.11.17; Evidence={ECO:0000256|ARBA:ARBA00000517};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000256|ARBA:ARBA00005354}.
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DR RefSeq; XP_014026017.1; XM_014170542.1.
DR AlphaFoldDB; A0A1S3PEH4; -.
DR GeneID; 106584897; -.
DR OrthoDB; 1121238at2759; -.
DR Proteomes; UP000087266; Chromosome ssa24.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14086; STKc_CaMKII; 1.
DR Gene3D; 3.10.450.50; -; 1.
DR Gene3D; 6.10.140.620; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032710; NTF2-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; PTHR24347:SF403; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT BETA; 1.
DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08332; CaMKII_AD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54427; NTF2-like; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Kinase {ECO:0000313|RefSeq:XP_014026017.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000313|RefSeq:XP_014026017.1}.
FT DOMAIN 13..285
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 373..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 532 AA; 59505 MW; 0B4366BCFA92C1F5 CRC64;
MAVTTCTRFT DEFQLYEELG KGAFSVVRRC VKLCTGQEYA AKIINTKKLS ARDHQKLERE
ARICRLLKHS NIVPWRRKAQ VPGSGLVRLH DSISEEGFHY LLFDLVTGGE LFEDIVAREY
YSEADASHCI TQILDSVHHI HQHDIVHRDL KPENLLLASK CKNAAVKLAD FGLAIEVQGD
QQAWFGFAGT PGYLSPEVLR KEAYGKPVDI WACGVILYIL LVGYPPFWDE DQHKLYQQIK
AGAYDFPSPE WDTVTPEAKN LINQMLTINP AKRITAQEAL KHPWVCQRST VASMMHRQET
VECLKKFNAR RKLKGAVLTA MLVSRNFSVG CRSTAPISIT AAAAAASAAA GSTTGLVEQA
AKSLLNKKAD VKKRKSSSAV RHMESSDSSN TVEDEDVKAR KQEIIKITEQ LIEAVNNGDF
EAYAKICDPG LTSFEPEALG NLVEGMDFHR FYFENLLSKN SKPIHTTILN PHVHLIGEDA
ACIAYIRLTQ FVDGQGHPRS SQSEETRVWH RRDAKWQNVH FHCSGAPAAP LQ
//
