Q9SCS2 · CAMK5_ARATH
- ProteinCDPK-related kinase 5
- GeneCRK5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids601 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
May play a role in signal transduction pathways that involve calcium as a second messenger.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Activated by calcium and calmodulin. Autophosphorylation may play an important role in the regulation of the kinase activity (By similarity).
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 154-162 | ATP (UniProtKB | ChEBI) | ||||
Sequence: VGRGHFGYT | ||||||
Binding site | 180 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 276 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 467 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 469 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 471 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 476 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 508 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 513 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 546 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 553 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 578 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 580 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCDPK-related kinase 5
- EC number
- Short namesAtCRK5
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9SCS2
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine | ||||
Sequence: G | ||||||
Chain | PRO_0000420532 | 2-601 | CDPK-related kinase 5 | |||
Sequence: GLCTSKPNSSNSDQTPARNSPLPASESVKPSSSSVNGEDQCVTTTNNEGKKSPFFPFYSPSPAHYFFSKKTPARSPATNSTNSTPKRFFKRPFPPPSPAKHIRAVLARRHGSVKPNSSAIPEGSEAEGGGVGLDKSFGFSKSFASKYELGDEVGRGHFGYTCAAKFKKGDNKGQQVAVKVIPKAKMTTAIAIEDVRREVKILRALSGHNNLPHFYDAYEDHDNVYIVMELCEGGELLDRILSRGGKYTEEDAKTVMIQILNVVAFCHLQGVVHRDLKPENFLFTSKEDTSQLKAIDFGLSDYVRPDERLNDIVGSAYYVAPEVLHRSYSTEADIWSVGVIVYILLCGSRPFWARTESGIFRAVLKADPSFDDPPWPLLSSEARDFVKRLLNKDPRKRLTAAQALSHPWIKDSNDAKVPMDILVFKLMRAYLRSSSLRKAALRALSKTLTVDELFYLREQFALLEPSKNGTISLENIKSALMKMATDAMKDSRIPEFLGQLSALQYRRMDFEEFCAAALSVHQLEALDRWEQHARCAYELFEKEGNRPIMIDELASELGLGPSVPVHAVLHDWLRHTDGKLSFLGFVKLLHGVSSRTIKAH | ||||||
Modified residue | 316 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 582 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Binds calmodulin (CaM) in a calcium-dependent manner.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-53 | Polar residues | ||||
Sequence: MGLCTSKPNSSNSDQTPARNSPLPASESVKPSSSSVNGEDQCVTTTNNEGKKS | ||||||
Region | 1-55 | Disordered | ||||
Sequence: MGLCTSKPNSSNSDQTPARNSPLPASESVKPSSSSVNGEDQCVTTTNNEGKKSPF | ||||||
Region | 70-98 | Disordered | ||||
Sequence: KKTPARSPATNSTNSTPKRFFKRPFPPPS | ||||||
Compositional bias | 73-88 | Polar residues | ||||
Sequence: PARSPATNSTNSTPKR | ||||||
Domain | 148-410 | Protein kinase | ||||
Sequence: YELGDEVGRGHFGYTCAAKFKKGDNKGQQVAVKVIPKAKMTTAIAIEDVRREVKILRALSGHNNLPHFYDAYEDHDNVYIVMELCEGGELLDRILSRGGKYTEEDAKTVMIQILNVVAFCHLQGVVHRDLKPENFLFTSKEDTSQLKAIDFGLSDYVRPDERLNDIVGSAYYVAPEVLHRSYSTEADIWSVGVIVYILLCGSRPFWARTESGIFRAVLKADPSFDDPPWPLLSSEARDFVKRLLNKDPRKRLTAAQALSHPWI | ||||||
Region | 415-445 | Autoinhibitory domain | ||||
Sequence: DAKVPMDILVFKLMRAYLRSSSLRKAALRAL | ||||||
Region | 434-454 | Calmodulin binding (CaMBD) | ||||
Sequence: SSSLRKAALRALSKTLTVDEL | ||||||
Domain | 452-488 | EF-hand 1 | ||||
Sequence: DELFYLREQFALLEPSKNGTISLENIKSALMKMATDA | ||||||
Domain | 489-524 | EF-hand 2 | ||||
Sequence: MKDSRIPEFLGQLSALQYRRMDFEEFCAAALSVHQL | ||||||
Domain | 525-564 | EF-hand 3 | ||||
Sequence: EALDRWEQHARCAYELFEKEGNRPIMIDELASELGLGPSV | ||||||
Domain | 567-596 | EF-hand 4 | ||||
Sequence: HAVLHDWLRHTDGKLSFLGFVKLLHGVSSR |
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 (415-445) inactivates kinase activity under calcium-free conditions (By similarity).
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9SCS2-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length601
- Mass (Da)66,991
- Last updated2000-05-01 v1
- Checksum61B4502B53C25DBF
Q9SCS2-2
- Name2
- Differences from canonical
- 306-306: P → PGKALRLYAICKLRFQNLETSICLYALTIAFA
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-53 | Polar residues | ||||
Sequence: MGLCTSKPNSSNSDQTPARNSPLPASESVKPSSSSVNGEDQCVTTTNNEGKKS | ||||||
Sequence conflict | 72 | in Ref. 5; BAF00328 | ||||
Sequence: T → S | ||||||
Compositional bias | 73-88 | Polar residues | ||||
Sequence: PARSPATNSTNSTPKR | ||||||
Alternative sequence | VSP_044531 | 306 | in isoform 2 | |||
Sequence: P → PGKALRLYAICKLRFQNLETSICLYALTIAFA | ||||||
Sequence conflict | 342 | in Ref. 5; BAF00328 | ||||
Sequence: V → I | ||||||
Sequence conflict | 590 | in Ref. 1; AAL30814 and 2; CAA70572 | ||||
Sequence: L → Q |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF435446 EMBL· GenBank· DDBJ | AAL30814.1 EMBL· GenBank· DDBJ | mRNA | ||
Y09418 EMBL· GenBank· DDBJ | CAA70572.1 EMBL· GenBank· DDBJ | mRNA | ||
AL133363 EMBL· GenBank· DDBJ | CAB62482.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE78676.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE78677.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK228391 EMBL· GenBank· DDBJ | BAF00328.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |