Q53P85 · CDPKO_ORYSJ
- ProteinCalcium-dependent protein kinase 24
- GeneCPK24
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids513 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May play a role in signal transduction pathways that involve calcium as a second messenger (By similarity).
Possesses calcium-dependent protein kinase activity in vitro (PubMed:16255173).
Possesses calcium-dependent protein kinase activity in vitro (PubMed:16255173).
Catalytic activity
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
Activity regulation
Activated by calcium. Autophosphorylation may play an important role in the regulation of the kinase activity.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 53-61 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LGQGQFGTT | ||||||
Binding site | 76 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 171 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 361 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 363 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 365 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 367 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 372 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 397 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 399 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 401 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 403 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 408 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 433 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 435 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 437 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 444 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 467 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 469 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 471 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 473 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 478 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent protein serine/threonine kinase activity | |
Molecular Function | calcium/calmodulin-dependent protein kinase activity | |
Molecular Function | calmodulin binding | |
Molecular Function | histone H2AS1 kinase activity | |
Molecular Function | protein serine kinase activity | |
Biological Process | intracellular signal transduction | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCalcium-dependent protein kinase 24
- EC number
- Short namesOsCDPK24 ; OsCPK24
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ53P85
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000437566 | 1-513 | UniProt | Calcium-dependent protein kinase 24 | |||
Sequence: MQPDPSGSGGDGNANAKAKLAPPPVTAAGGRPVSVLPHKTANVRDHYRIGKKLGQGQFGTTYLCVDKASGGEFACKSIPKRKLLCREDYEDVWREIQIMHHLSEHPNVVRIRGAYEDALFVHIVMELCAGGELFDRIVAKGHYTERAAAQLIRTIVAVVEGCHSLGVMHRDLKPENFLFASAAEDAPLKATDFGLSMFYKPGDKFSDVVGSPYYVAPEVLQKCYGPESDVWSAGVILYILLCGVPPFWAETEAGIFRQILRGKLDFESEPWPSISDSAKDLVRNMLCRDPTKRLTAHEVLCHPWIVDDAVAPDKPIDSAVLSRLKHFSAMNKLKKMALRVIAESLSEEEIGGLKELFKMIDTDDSGTITFDELKEGLKRVGSELTEHEIQALMEAADIDNSGTIDYGEFIAATLHMNKLEREENLVSAFSFFDKDGSGFITIDELSQACREFGLDDLHLEDMIKDVDQNNDGQIDYSEFTAMMRKGNAGGAGRRTMRNSLQLNLGEILNPSNS | |||||||
Modified residue (large scale data) | 211 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 430 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 495 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 499 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-33 | Disordered | ||||
Sequence: MQPDPSGSGGDGNANAKAKLAPPPVTAAGGRPV | ||||||
Domain | 47-305 | Protein kinase | ||||
Sequence: YRIGKKLGQGQFGTTYLCVDKASGGEFACKSIPKRKLLCREDYEDVWREIQIMHHLSEHPNVVRIRGAYEDALFVHIVMELCAGGELFDRIVAKGHYTERAAAQLIRTIVAVVEGCHSLGVMHRDLKPENFLFASAAEDAPLKATDFGLSMFYKPGDKFSDVVGSPYYVAPEVLQKCYGPESDVWSAGVILYILLCGVPPFWAETEAGIFRQILRGKLDFESEPWPSISDSAKDLVRNMLCRDPTKRLTAHEVLCHPWI | ||||||
Region | 311-341 | Autoinhibitory domain | ||||
Sequence: APDKPIDSAVLSRLKHFSAMNKLKKMALRVI | ||||||
Domain | 348-383 | EF-hand 1 | ||||
Sequence: EEIGGLKELFKMIDTDDSGTITFDELKEGLKRVGSE | ||||||
Domain | 384-419 | EF-hand 2 | ||||
Sequence: LTEHEIQALMEAADIDNSGTIDYGEFIAATLHMNKL | ||||||
Domain | 420-455 | EF-hand 3 | ||||
Sequence: EREENLVSAFSFFDKDGSGFITIDELSQACREFGLD | ||||||
Domain | 458-489 | EF-hand 4 | ||||
Sequence: HLEDMIKDVDQNNDGQIDYSEFTAMMRKGNAG |
Domain
There are 3 contiguous domains conserved in the CDPK subfamily: a kinase domain, an autoinhibitory (junction) domain and a calmodulin-like domain. The autoinhibitory domain (311-341) inactivates kinase activity under calcium-free conditions.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length513
- Mass (Da)56,672
- Last updated2005-05-24 v1
- Checksum63EF52BB256FE0E3
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 52 | in Ref. 1; AAN41657 | ||||
Sequence: K → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY144497 EMBL· GenBank· DDBJ | AAN41657.1 EMBL· GenBank· DDBJ | mRNA | ||
AC128643 EMBL· GenBank· DDBJ | AAX95085.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DP000010 EMBL· GenBank· DDBJ | ABA91635.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP008217 EMBL· GenBank· DDBJ | BAF27709.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014967 EMBL· GenBank· DDBJ | BAT12871.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM000148 EMBL· GenBank· DDBJ | EAZ17585.1 EMBL· GenBank· DDBJ | Genomic DNA |