ID   CRK_DAUCA               Reviewed;         602 AA.
AC   P53681;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=CDPK-related protein kinase;
DE            EC=2.7.11.1;
DE   AltName: Full=PK421;
GN   Name=CRK;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Juwarot;
RX   PubMed=7640352; DOI=10.1007/bf00042065;
RA   Lindzen E., Choi J.H.;
RT   "A carrot cDNA encoding an atypical protein kinase homologous to plant
RT   calcium-dependent protein kinases.";
RL   Plant Mol. Biol. 28:785-797(1995).
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=2.7.11.1;
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=2.7.11.1;
CC   -!- DOMAIN: All EF-hand domains seem to be non-functional.
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; X83869; CAA58750.1; -; mRNA.
DR   PIR; S60052; S60052.
DR   AlphaFoldDB; P53681; -.
DR   SMR; P53681; -.
DR   BRENDA; 2.7.11.1; 1841.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-dom_pair.
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; SSF47473; SSF47473; 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; Kinase; Nucleotide-binding; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..602
FT                   /note="CDPK-related protein kinase"
FT                   /id="PRO_0000085880"
FT   REPEAT          20..26
FT                   /note="1"
FT   REPEAT          27..33
FT                   /note="2"
FT   REPEAT          34..40
FT                   /note="3"
FT   DOMAIN          148..410
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          451..486
FT                   /note="EF-hand 1"
FT   DOMAIN          487..527
FT                   /note="EF-hand 2"
FT   DOMAIN          528..563
FT                   /note="EF-hand 3"
FT   DOMAIN          564..602
FT                   /note="EF-hand 4"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          20..40
FT                   /note="3 X 7 AA tandem repeats of S-[LI]-P-X-X-D-X"
FT   COMPBIAS        19..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        276
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         154..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   602 AA;  67184 MW;  1D10BF68B37BF447 CRC64;
     MGICVSKPSP EPDLHNHHTS IPVNDTSLPP QDNSIPPKDI AIPAQDNNKP PGKKSPFLPF
     YSPSPAHFLF SKKSPAVGSP AAGSSNSTPK RLFPFPPPSP AKHIKAAWAR RHGSVKPNEA
     AIPENNEVDG GAGLDKSFGF SKKFGSKFEV GEEVGRGHFG YTCRAKFKKG EFKGQDVAVK
     VIPKAKMTTA IAIEDVRREV KILRALTGHN NLVQFYDAFE DHTNVYVVME LCEGGELLDR
     ILSRGGKYTE DDAKAVMIQI LNVVAFCHLQ GVVHRDLKPE NFLFKSKDED SQLKAIDFGL
     SDYVKPDERL NDIVGSAYYV APEVLHRSYS TEADVWSIGV ISYILLCGSR PFWARTESGI
     FRAVLKANLS FDEPPWPSVS SEAKDFVKRL LNKDPRKRMT AAQALCHSWI KNSNDIKFPL
     DILVFKLMKV YMRSSPLRKA ALRALSKTLT VDELFYLKEQ FVLLEPTKNG TISLENIKQA
     LMRNSTDAMK DSRVLDLLVS LNALQYRRMD FEEFCAAALS VHQLEALDRW EQHARCAYDL
     FEKDGNRAIM IEELASELGL GPSIPVHAVL HDWIRHTDGK LSFLGYVKLL HGVSTRAIAK
     AQ