Q9SCS2 · CAMK5_ARATH

Function

function

May play a role in signal transduction pathways that involve calcium as a second messenger.

Catalytic activity

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.

TypeIDPosition(s)Description
Binding site154-162ATP (UniProtKB | ChEBI)
Binding site180ATP (UniProtKB | ChEBI)
Active site276Proton acceptor
Binding site467Ca2+ 1 (UniProtKB | ChEBI)
Binding site469Ca2+ 1 (UniProtKB | ChEBI)
Binding site471Ca2+ 1 (UniProtKB | ChEBI)
Binding site476Ca2+ 1 (UniProtKB | ChEBI)
Binding site508Ca2+ 2 (UniProtKB | ChEBI)
Binding site513Ca2+ 2 (UniProtKB | ChEBI)
Binding site546Ca2+ 3 (UniProtKB | ChEBI)
Binding site553Ca2+ 3 (UniProtKB | ChEBI)
Binding site578Ca2+ 4 (UniProtKB | ChEBI)
Binding site580Ca2+ 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmembrane
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    CDPK-related kinase 5
  • EC number
  • Short names
    AtCRK5
  • Alternative names
    • Calcium/calmodulin-dependent protein kinase 1

Gene names

    • Name
      CRK5
    • Synonyms
      CaMK1
    • ORF names
      T20E23.130
    • Ordered locus names
      At3g50530

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9SCS2
  • Secondary accessions
    • F4J0N4
    • O04290
    • Q0WRC1

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Membrane
; Lipid-anchor

Keywords

PTM/Processing

Features

Showing features for initiator methionine, lipidation, chain, modified residue.

TypeIDPosition(s)Description
Initiator methionine1Removed
Lipidation2N-myristoyl glycine
ChainPRO_00004205322-601
Modified residue316Phosphoserine
Modified residue582Phosphoserine

Keywords

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.

TypeIDPosition(s)Description
Compositional bias1-53Polar residues
Region1-55Disordered
Region70-98Disordered
Compositional bias73-88Polar residues
Domain148-410Protein kinase
Region415-445Autoinhibitory domain
Region434-454Calmodulin binding (CaMBD)
Domain452-488EF-hand 1
Domain489-524EF-hand 2
Domain525-564EF-hand 3
Domain567-596EF-hand 4

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

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    601
  • Mass (Da)
    66,991
  • Last updated
    2000-05-01 v1
  • Checksum
    61B4502B53C25DBF
MGLCTSKPNSSNSDQTPARNSPLPASESVKPSSSSVNGEDQCVTTTNNEGKKSPFFPFYSPSPAHYFFSKKTPARSPATNSTNSTPKRFFKRPFPPPSPAKHIRAVLARRHGSVKPNSSAIPEGSEAEGGGVGLDKSFGFSKSFASKYELGDEVGRGHFGYTCAAKFKKGDNKGQQVAVKVIPKAKMTTAIAIEDVRREVKILRALSGHNNLPHFYDAYEDHDNVYIVMELCEGGELLDRILSRGGKYTEEDAKTVMIQILNVVAFCHLQGVVHRDLKPENFLFTSKEDTSQLKAIDFGLSDYVRPDERLNDIVGSAYYVAPEVLHRSYSTEADIWSVGVIVYILLCGSRPFWARTESGIFRAVLKADPSFDDPPWPLLSSEARDFVKRLLNKDPRKRLTAAQALSHPWIKDSNDAKVPMDILVFKLMRAYLRSSSLRKAALRALSKTLTVDELFYLREQFALLEPSKNGTISLENIKSALMKMATDAMKDSRIPEFLGQLSALQYRRMDFEEFCAAALSVHQLEALDRWEQHARCAYELFEKEGNRPIMIDELASELGLGPSVPVHAVLHDWLRHTDGKLSFLGFVKLLHGVSSRTIKAH

Q9SCS2-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 306-306: P → PGKALRLYAICKLRFQNLETSICLYALTIAFA

Sequence caution

The sequence BAF00328.1 differs from that shown. Reason: Frameshift

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Compositional bias1-53Polar residues
Sequence conflict72in Ref. 5; BAF00328
Compositional bias73-88Polar residues
Alternative sequenceVSP_044531306in isoform 2
Sequence conflict342in Ref. 5; BAF00328
Sequence conflict590in Ref. 1; AAL30814 and 2; CAA70572

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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