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Database: UniProt
Entry: A0A3Q1BP27_AMPOC
LinkDB: A0A3Q1BP27_AMPOC
Original site: A0A3Q1BP27_AMPOC 
ID   A0A3Q1BP27_AMPOC        Unreviewed;       478 AA.
AC   A0A3Q1BP27;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=calcium/calmodulin-dependent protein kinase {ECO:0000256|ARBA:ARBA00012434};
DE            EC=2.7.11.17 {ECO:0000256|ARBA:ARBA00012434};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000014609.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000014609.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; A0A3Q1BP27; -.
DR   STRING; 80972.ENSAOCP00000014609; -.
DR   Ensembl; ENSAOCT00000031511.1; ENSAOCP00000014609.1; ENSAOCG00000019343.1.
DR   GeneTree; ENSGT00940000155150; -.
DR   OrthoDB; 1121238at2759; -.
DR   Proteomes; UP000257160; Unplaced.
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   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:SF384; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT ALPHA; 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:0000256|RuleBase:RU000304};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|RuleBase:RU000304}.
FT   DOMAIN          13..271
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          315..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..341
FT                   /note="Basic and acidic residues"
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   478 AA;  53973 MW;  8BE2E15438E5E93D CRC64;
     MATVICTRFT EEYQLYEELG KGAFSVVRRC VKVLSGQEYA AKIINTKKLS ARDHQKLDRE
     ARICRLLKHP NIVRLHDSIS EEAHHYLIFD LVTGGELFED IVAREYYSEA DASHCIQQIL
     EAVLHCHQMG VVHRDLKPEN LLLASKSKGA AVKLADFGLA IEVEGDQQAW FGFAGTPGYL
     SPEVLRKDPY GKAVDLWACG VILYILLVGY PPFWDEDQHR LYQQIKAGAY DFPSPEWDTV
     TPEAKDLINK MLTINPAKRI TAAEALKHPW ISHRSTVASC MHRQETVECL KKFNARRKLK
     GAILTTMLAT RNFSGGKSGS NKKADGVKES SESTNTTIED EDTRVRKQDI IKVTEQLIEA
     ISNGDFESYT KMCDPAVTAF EPEALGNLVE GLDFHRFYFE NLWSKNSKPV HTTILNPHIH
     LVGDEAACIA YIRVTQYIDA NGTPRTAQSE ETRVWHRRDG KWQIVHFHRS GSASTLSN
//
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