A8P5N3 · A8P5N3_COPC7
- ProteinSerine/threonine-protein phosphatase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids646 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
Cofactor
Protein has several cofactor binding sites:
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | calcineurin complex | |
Cellular Component | cytoplasm | |
Molecular Function | calmodulin binding | |
Molecular Function | calmodulin-dependent protein phosphatase activity | |
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity | |
Biological Process | calcineurin-mediated signaling | |
Biological Process | fungal-type cell wall organization |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein phosphatase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Agaricineae > Psathyrellaceae > Coprinopsis
Accessions
- Primary accessionA8P5N3
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 174-179 | Serine/threonine specific protein phosphatases | |||
Compositional bias | 490-508 | Basic and acidic residues | |||
Region | 490-602 | Disordered | |||
Compositional bias | 511-535 | Polar residues | |||
Compositional bias | 551-571 | Polar residues | |||
Compositional bias | 584-602 | Polar residues | |||
Region | 614-646 | Disordered | |||
Sequence similarities
Belongs to the PPP phosphatase family. PP-2B subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length646
- Mass (Da)72,301
- Last updated2008-01-15 v1
- ChecksumF0C17DD9D2003007
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 490-508 | Basic and acidic residues | |||
Compositional bias | 511-535 | Polar residues | |||
Compositional bias | 551-571 | Polar residues | |||
Compositional bias | 584-602 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AACS02000011 EMBL· GenBank· DDBJ | EAU82917.1 EMBL· GenBank· DDBJ | Genomic DNA |