ID A0A8M9Q199_DANRE Unreviewed; 582 AA. AC A0A8M9Q199; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 28-JUN-2023, entry version 6. DE RecName: Full=calcium/calmodulin-dependent protein kinase {ECO:0000256|ARBA:ARBA00012434}; DE EC=2.7.11.17 {ECO:0000256|ARBA:ARBA00012434}; GN Name=camk2g2 {ECO:0000313|RefSeq:XP_021328391.1, GN ECO:0000313|RefSeq:XP_021336476.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_021328391.1}; RN [1] {ECO:0000313|RefSeq:XP_021328391.1, ECO:0000313|RefSeq:XP_021336476.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_021328391.1, RC ECO:0000313|RefSeq:XP_021336476.1}; RG RefSeq; RL Submitted (MAR-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_021328391.1; XM_021472716.1. DR RefSeq; XP_021336476.1; XM_021480801.1. DR Proteomes; UP000000437; Alternate scaffold 13. 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:InterPro. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. 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:SF398; CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT GAMMA; 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 1: Evidence at protein level; 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_021328391.1, KW ECO:0000313|RefSeq:XP_021336476.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A8M9Q199}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transferase {ECO:0000313|RefSeq:XP_021328391.1, KW ECO:0000313|RefSeq:XP_021336476.1}. FT DOMAIN 14..272 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 345..450 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 372..392 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 393..407 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 436..450 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 582 AA; 64468 MW; CDE0F71D67332572 CRC64; MATIVTCTRF TDEYQLYEEL GKGAFSVVRR CVKKSTGQEY AAKIINTKKL SARDHQKLER EARICRLLKH PNIVRLHDSI AEEGFHYLVF DLVTGGELFE DIVAREYYSE SDASHCINQI LESVSHIHQH DIVHRDLKPE NLLLASKMKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY LSPEVLRKDP YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT VTPEAKNLIN QMLTINPAKR ITADQALKHP WVCQRSTVAS MMHRQETVEC LRKFNARRKL KGAILTTMLV SRNFSVGRQH TSPATPTTST AALAQEACKS LLNKKSDGVK GSTESCNTTE EEDMKVSVGG VSSDSAVVSQ CSGSEEPSPA PQAQTEASPP CPPASDPPHD VKNVAWSSSG QSSCPDLEPA VPAPASTTAG GSSVNRQQSR KQEIIKITEQ LIEAINNGDF EAYTRICDPG LTSFEPEALG NLVEGMDFHK FYFENLLSKN SKPVHTTILN PHVHLIGEDA ACIAYIRLTQ YIDGQGRPRS SQSEETRVWH RRDAKWLNIH FHCSGAPAAP LQ //