Q00771 · KCC1A_EMENI
- ProteinCalcium/calmodulin-dependent protein kinase cmkA
- GenecmkA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids414 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Calcium/calmodulin-dependent protein kinase (PubMed:2835766).
Required in nuclear division cycle for progression from G2 to mitosis. Required for hyphal growth (PubMed:8898358).
Required in nuclear division cycle for progression from G2 to mitosis. Required for hyphal growth (PubMed:8898358).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Activated by Ca2+/calmodulin (PubMed:8898358).
Binding of calmodulin may relieve intrasteric autoinhibition (Probable)
Binding of calmodulin may relieve intrasteric autoinhibition (Probable)
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | calmodulin binding | |
Molecular Function | calmodulin-dependent protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Biological Process | cell division | |
Biological Process | cellular response to oxidative stress | |
Biological Process | G2/M transition of mitotic cell cycle | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCalcium/calmodulin-dependent protein kinase cmkA
- EC number
- Short namesCMPK
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionQ00771
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Spores arrest with a single nucleus and fail to extend a germ tube.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 50 | Loss of kinase activity. | ||||
Sequence: K → M |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086087 | 1-414 | Calcium/calmodulin-dependent protein kinase cmkA | |||
Sequence: MSFANMFNKLSGQPESYEKKSLYRFGRTLGAGTYGIVREADCSSGKVAVKIILKRNVRGNERMVYDELDLLQKLNHPHIVHFVDWFESKDKFYIVTQLATGGELFDRICEYGKFTEKDASQTIRQVLDAVNYLHQRNIVHRDLKPENLLYLTRDLDSQLVLADFGIAKMLDNPAEVLTSMAGSFGYAAPEVMLKQGHGKAVDIWSLGVITYTLLCGYSPFRSENLTDLIEECRSGRVVFHERYWKDVSKDAKDFILSLLQVDPAQRPTSEEALKHPWLKGESASDRDLLPEIRAYIARSRLKRGIEIIKLANRIEALKMQEEDEEDIPSAVDVQASEASDKSGLSPFPALSTENSNTHPASTGNGESGGTKKRSLSKIARGAIFREVVLAKVREMKENEEREKVEREARERAHS |
Post-translational modification
Autophosphorylated in a calcium/calmodulin-dependent manner.
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 23-278 | Protein kinase | ||||
Sequence: YRFGRTLGAGTYGIVREADCSSGKVAVKIILKRNVRGNERMVYDELDLLQKLNHPHIVHFVDWFESKDKFYIVTQLATGGELFDRICEYGKFTEKDASQTIRQVLDAVNYLHQRNIVHRDLKPENLLYLTRDLDSQLVLADFGIAKMLDNPAEVLTSMAGSFGYAAPEVMLKQGHGKAVDIWSLGVITYTLLCGYSPFRSENLTDLIEECRSGRVVFHERYWKDVSKDAKDFILSLLQVDPAQRPTSEEALKHPWL | ||||||
Region | 278-314 | Autoinhibitory domain | ||||
Sequence: LKGESASDRDLLPEIRAYIARSRLKRGIEIIKLANRI | ||||||
Region | 293-315 | Calmodulin-binding | ||||
Sequence: RAYIARSRLKRGIEIIKLANRIE | ||||||
Region | 320-375 | Disordered | ||||
Sequence: QEEDEEDIPSAVDVQASEASDKSGLSPFPALSTENSNTHPASTGNGESGGTKKRSL | ||||||
Compositional bias | 335-371 | Polar residues | ||||
Sequence: ASEASDKSGLSPFPALSTENSNTHPASTGNGESGGTK | ||||||
Region | 394-414 | Disordered | ||||
Sequence: EMKENEEREKVEREARERAHS |
Domain
The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate.
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length414
- Mass (Da)46,804
- Last updated2009-05-26 v2
- Checksum1E8D58A1C0B2E85C
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 335-371 | Polar residues | ||||
Sequence: ASEASDKSGLSPFPALSTENSNTHPASTGNGESGGTK | ||||||
Sequence conflict | 408 | in Ref. 1; AAB97502 and 2; AAD22581 | ||||
Sequence: A → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M74120 EMBL· GenBank· DDBJ | AAB97502.1 EMBL· GenBank· DDBJ | mRNA | ||
AF054580 EMBL· GenBank· DDBJ | AAD22581.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AACD01000039 EMBL· GenBank· DDBJ | EAA64523.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BN001307 EMBL· GenBank· DDBJ | CBF86796.1 EMBL· GenBank· DDBJ | Genomic DNA |