CDPK5_ORYSJ
ID CDPK5_ORYSJ Reviewed; 549 AA.
AC Q0DYK7;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Calcium-dependent protein kinase 5 {ECO:0000305};
DE Short=OsCDPK5 {ECO:0000305};
DE Short=OsCPK5 {ECO:0000303|PubMed:15695435};
DE EC=2.7.11.1 {ECO:0000305};
GN Name=CPK5 {ECO:0000303|PubMed:15695435};
GN OrderedLocusNames=Os02g0685900 {ECO:0000312|EMBL:BAF09681.1},
GN LOC_Os02g46090 {ECO:0000305};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15695435; DOI=10.1093/pcp/pci035;
RA Asano T., Tanaka N., Yang G., Hayashi N., Komatsu S.;
RT "Genome-wide identification of the rice calcium-dependent protein kinase
RT and its closely related kinase gene families: comprehensive analysis of the
RT CDPKs gene family in rice.";
RL Plant Cell Physiol. 46:356-366(2005).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger. {ECO:0000250|UniProtKB:Q06850}.
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 Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Activated by calcium. Autophosphorylation may play
CC an important role in the regulation of the kinase activity.
CC {ECO:0000250|UniProtKB:Q06850}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- DOMAIN: There are 3 contiguous domains conserved in the CDPK subfamily:
CC a kinase domain, an autoinhibitory (junction) domain and a calmodulin-
CC like domain. The autoinhibitory domain (356-386) inactivates kinase
CC activity under calcium-free conditions. {ECO:0000250|UniProtKB:Q06850}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000305}.
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DR EMBL; AP004071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP008208; BAF09681.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80334.1; -; Genomic_DNA.
DR RefSeq; XP_015625261.1; XM_015769775.1.
DR AlphaFoldDB; Q0DYK7; -.
DR SMR; Q0DYK7; -.
DR STRING; 4530.OS02T0685900-00; -.
DR PaxDb; Q0DYK7; -.
DR PRIDE; Q0DYK7; -.
DR EnsemblPlants; Os02t0685900-00; Os02t0685900-00; Os02g0685900.
DR GeneID; 4330351; -.
DR Gramene; Os02t0685900-00; Os02t0685900-00; Os02g0685900.
DR KEGG; osa:4330351; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR InParanoid; Q0DYK7; -.
DR OMA; GKYFQGY; -.
DR OrthoDB; 330091at2759; -.
DR PlantReactome; R-ADU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-AHA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-AIP-9607185; Generation of superoxide radicals.
DR PlantReactome; R-ALY-9607185; Generation of superoxide radicals.
DR PlantReactome; R-ATA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-ATH-9607185; Generation of superoxide radicals.
DR PlantReactome; R-BDI-9607185; Generation of superoxide radicals.
DR PlantReactome; R-BNA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-BOL-9607185; Generation of superoxide radicals.
DR PlantReactome; R-BRA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-BVU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-CAN-9607185; Generation of superoxide radicals.
DR PlantReactome; R-CAR-9607185; Generation of superoxide radicals.
DR PlantReactome; R-CCA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-CCL-9607185; Generation of superoxide radicals.
DR PlantReactome; R-CCN-9607185; Generation of superoxide radicals.
DR PlantReactome; R-CCP-9607185; Generation of superoxide radicals.
DR PlantReactome; R-CLA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-COL-9607185; Generation of superoxide radicals.
DR PlantReactome; R-CRU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-CSA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-CSC-9607185; Generation of superoxide radicals.
DR PlantReactome; R-CSI-9607185; Generation of superoxide radicals.
DR PlantReactome; R-CSK-9607185; Generation of superoxide radicals.
DR PlantReactome; R-DCA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-ECU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-EGR-9607185; Generation of superoxide radicals.
DR PlantReactome; R-ETE-9607185; Generation of superoxide radicals.
DR PlantReactome; R-FVE-9607185; Generation of superoxide radicals.
DR PlantReactome; R-GMA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-GRA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-HLP-9607185; Generation of superoxide radicals.
DR PlantReactome; R-HVU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-ITR-9607185; Generation of superoxide radicals.
DR PlantReactome; R-JCU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-LAN-9607185; Generation of superoxide radicals.
DR PlantReactome; R-LPE-9607185; Generation of superoxide radicals.
DR PlantReactome; R-MAC-9607185; Generation of superoxide radicals.
DR PlantReactome; R-MES-9607185; Generation of superoxide radicals.
DR PlantReactome; R-MGU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-MTR-9607185; Generation of superoxide radicals.
DR PlantReactome; R-NAT-9607185; Generation of superoxide radicals.
DR PlantReactome; R-NNU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OAU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OBA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OBR-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OGL-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OGR-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OGU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OLO-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OME-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OMI-9607185; Generation of superoxide radicals.
DR PlantReactome; R-ONI-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OOF-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OPU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-ORU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling.
DR PlantReactome; R-OSA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-OSI-9607185; Generation of superoxide radicals.
DR PlantReactome; R-PAB-9607185; Generation of superoxide radicals.
DR PlantReactome; R-PAV-9607185; Generation of superoxide radicals.
DR PlantReactome; R-PDA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-PED-9607185; Generation of superoxide radicals.
DR PlantReactome; R-PHA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-PHH-9607185; Generation of superoxide radicals.
DR PlantReactome; R-PPE-9607185; Generation of superoxide radicals.
DR PlantReactome; R-PTA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-PTI-9607185; Generation of superoxide radicals.
DR PlantReactome; R-PVE-9607185; Generation of superoxide radicals.
DR PlantReactome; R-PVU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-SBI-9607185; Generation of superoxide radicals.
DR PlantReactome; R-SHI-9607185; Generation of superoxide radicals.
DR PlantReactome; R-SIT-9607185; Generation of superoxide radicals.
DR PlantReactome; R-SLY-9607185; Generation of superoxide radicals.
DR PlantReactome; R-STU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-TAE-9607185; Generation of superoxide radicals.
DR PlantReactome; R-TCA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-TDI-9607185; Generation of superoxide radicals.
DR PlantReactome; R-TPR-9607185; Generation of superoxide radicals.
DR PlantReactome; R-TTU-9607185; Generation of superoxide radicals.
DR PlantReactome; R-TUR-9607185; Generation of superoxide radicals.
DR PlantReactome; R-VAN-9607185; Generation of superoxide radicals.
DR PlantReactome; R-VRA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-VVN-9607185; Generation of superoxide radicals.
DR PlantReactome; R-ZJA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-ZMA-9607185; Generation of superoxide radicals.
DR PlantReactome; R-ZMY-9607185; Generation of superoxide radicals.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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; PF13499; EF-hand_7; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
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; Calcium; Kinase; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..549
FT /note="Calcium-dependent protein kinase 5"
FT /id="PRO_0000437550"
FT DOMAIN 92..350
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 393..428
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 429..464
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 465..500
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 501..534
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 43..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..386
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:Q06850"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 98..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 448
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 480
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 482
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 484
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 512
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 514
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 518
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 523
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 549 AA; 60388 MW; 9E8AAB2F5926489A CRC64;
MGNTCGVTLR SKYFASFRGA SQRHDEAGYA PVATSAAAAA AADEPAGKKA PRGSAAAADA
PHAASMKRGA PAPAELTANV LGHPTPSLSE HYALGRKLGQ GQFGTTYLCT DLATGVDYAC
KSIAKRKLIT KEDVEDVRRE IQIMHHLAGH RNVVAIKGAY EDPQYVHIVM ELCAGGELFD
RIIERGQFSE RKAAELTRII VGVIEACHSL GVIHRDLKPE NFLLANKDDD LSLKAIDFGL
SVFFKPGQVF TDVVGSPYYV APEVLRKCYG PEADVWTAGV ILYILLSGVP PFWAETQQGI
FDAVLKGVID FDSDPWPVIS DSAKDLIRRM LNPRPKERLT AHEVLCHPWI CDHGVAPDRP
LDPAVLSRIK QFSAMNKLKK MALRVIAESL SEEEIAGLKE MFKAMDTDNS GAITYDELKE
GMRKYGSTLK DTEIRDLMEA ADVDNSGTID YIEFIAATLH LNKLEREEHL VAAFSYFDKD
GSGYITVDEL QQACKEHNMP DAFLDDVIKE ADQDNDGRID YGEFVAMMTK GNMGVGRRTM
RNSLNISMR
