ID   KCCS_MALDO              Reviewed;         415 AA.
AC   Q07250;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Calcium/calmodulin-dependent serine/threonine-protein kinase;
DE            EC=2.7.11.17;
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wijcik;
RX   PubMed=8310066; DOI=10.1104/pp.101.4.1381;
RA   Watillon B., Kettmann R., Boxus P., Burny A.;
RT   "A calcium/calmodulin-binding serine/threonine protein kinase homologous to
RT   the mammalian type II calcium/calmodulin-dependent protein kinase is
RT   expressed in plant cells.";
RL   Plant Physiol. 101:1381-1384(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7610182; DOI=10.1104/pp.108.2.847;
RA   Watillon B., Kettmann R., Boxus P., Burny A.;
RT   "Structure of a calmodulin-binding protein kinase gene from apple.";
RL   Plant Physiol. 108:847-848(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 266-391.
RC   STRAIN=cv. Wijcik;
RA   Watillon B., Kettmann R., Boxus P., Burny A.;
RT   "Cloning and characterization of an apple (Malus domestica [L.] Borkh) cDNA
RT   encoding a calmodulin-binding protein domain similar to the calmodulin-
RT   binding region of mammalian CaM kinase II.";
RL   Plant Sci. 81:227-235(1992).
CC   -!- FUNCTION: May be involved in signal transduction processes.
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   -!- 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;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR   EMBL; Z17313; CAA78961.1; -; mRNA.
DR   EMBL; Z38126; CAA86286.1; -; Genomic_DNA.
DR   PIR; JQ2251; JQ2251.
DR   AlphaFoldDB; Q07250; -.
DR   SMR; Q07250; -.
DR   STRING; 3750.XP_008364745.1; -.
DR   PRIDE; Q07250; -.
DR   BRENDA; 2.7.11.17; 3164.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calcium; Calmodulin-binding; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..415
FT                   /note="Calcium/calmodulin-dependent serine/threonine-
FT                   protein kinase"
FT                   /id="PRO_0000086110"
FT   DOMAIN          12..308
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          318..328
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        173
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         18..26
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   415 AA;  46492 MW;  8DF34A4418A9A363 CRC64;
     MIQETRRLAD EYEISEILGR GGFSVVRKGI SRKSSSSSDK TDVAIKTLKR PFAPSNPPPL
     PPHARRNDQN SFAAAAFQTR KQVSISNVLL TNEILVMRKI VENVSPHPNV IDLYDVYEDE
     NGVHLVLELC SGGELFDRIV KQERYSEVGA AAVVRQIAQG LAALHRSNIV HRDLKPENCL
     FLDNTVDSPL KIMDFGLSSV EEFTDPVVGL FGSIDYVSPE ALSQGQVTSK SDMWALGVIL
     YILLSGYPPF IAQSNRQKQQ MIMAGEFSFY EKTWKGFLCQ PKQLISSLLK VDPDKRPSAQ
     ELLDHPWVVG LSAREDQMDA EIVSRLQSFN ARRKLRAAAI ASVWTSSIFL RTKKLKSLLG
     SYDLKPDEIK NLSSHFKKIC VKGDNATLSE FRLSCKRLIQ LRLVSMSLRA EPARL