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Database: UniProt
Entry: A0A2K5U5T6_MACFA
LinkDB: A0A2K5U5T6_MACFA
Original site: A0A2K5U5T6_MACFA 
ID   A0A2K5U5T6_MACFA        Unreviewed;       775 AA.
AC   A0A2K5U5T6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=calcium/calmodulin-dependent protein kinase {ECO:0000256|ARBA:ARBA00012434};
DE            EC=2.7.11.17 {ECO:0000256|ARBA:ARBA00012434};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000007685.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000007685.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000007685.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A2K5U5T6; -.
DR   Ensembl; ENSMFAT00000026379.2; ENSMFAP00000007685.2; ENSMFAG00000040802.2.
DR   VEuPathDB; HostDB:ENSMFAG00000040802; -.
DR   GeneTree; ENSGT00940000159769; -.
DR   OrthoDB; 1121238at2759; -.
DR   Proteomes; UP000233100; Chromosome 5.
DR   Bgee; ENSMFAG00000040802; Expressed in heart and 13 other cell types or tissues.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24347:SF436; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT   DOMAIN          245..523
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   775 AA;  86590 MW;  7FD62561FBF8296E CRC64;
     REIHEGTHLE SLEGGVGPAR RGLRQGGGAG WRRERREEAP GEETEAWGRQ TRLRPSRALF
     LSLRRLEAAR AREQREAVKV PRFAGSAAAR WREAGPGRAR SPEPRARSAP EPADSCRWAL
     AVRSGLRGLG SAALHLRPLG LPPLCFYPSC LQCGSFRNCL PLAPCPAVFP FPGPLFLNTL
     PPVFGDRDWK RGGWSVQWRR RKRGPQEEED RRTVGRRPHA TVSGHLPSRP APAHTPSRAS
     YFRTRKVRAA LGDSAAGPIP GLAARLLASR PSRSQPGHSP DQGWLRPQPA PGSRTSISFS
     RSLENHQKLE REARICRLLK HPNIVRLHDS ISEEGFHYLV FDLVTGGELF EDIVAREYYS
     EADASHCIQQ ILESVNHCHL NGIVHRDLKP ENLLLASKSK GAAVKLADFG LAIEVQGDQQ
     AWFGFAGTPG YLSPEVLRKD PYGKPVDMWA CGVILYILLV GYPPFWDEDQ HRLYQQIKAG
     AYDFPSPEWD TVTPEAKDLI NKMLTINPAK RITASEALKH PWICQRSTVA SMMHRQETVD
     CLKKFNARRK LKGAILTTML ATRNFSAAKS LLKKPDGVKK RKSSSSVQMM EPQTTVIHNP
     DGNKESTESS NTTIEDEDVK ARKQEIIKVT EQLIEAINNG DFEAYTKICD PGLTAFEPEA
     LGNLVEGMDF HRFYFENALS KSNKPIHTII LNPHVHLVGD DAACIAYIRL TQYMDGSGMP
     KTMQSEETRV WHRRDGKWQN VHFHRSGSPT VPIKPPCIPN GKENFSGGTS LWQNI
//
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