P78968 · PPZ_SCHPO
- ProteinSerine/threonine-protein phosphatase PP-Z
- Genepzh1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids515 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Catalytic activity
- O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
Cofactor
Note: Binds 2 manganese ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 248 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 250 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 276 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 276 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 308 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Active site | 309 | Proton donor | |||
Binding site | 357 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 432 | Mn2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | fungal-type vacuole | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | phosphatase activity | |
Molecular Function | protein serine/threonine phosphatase activity | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein phosphatase PP-Z
- EC number
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionP78968
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-32 | Polar residues | |||
Region | 1-186 | Disordered | |||
Compositional bias | 39-60 | Basic and acidic residues | |||
Compositional bias | 63-77 | Pro residues | |||
Compositional bias | 82-185 | Polar residues | |||
Sequence similarities
Belongs to the PPP phosphatase family. PP-Z subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length515
- Mass (Da)57,131
- Last updated1997-05-01 v1
- ChecksumB9F14C0FE3F93B97
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-32 | Polar residues | |||
Compositional bias | 39-60 | Basic and acidic residues | |||
Compositional bias | 63-77 | Pro residues | |||
Compositional bias | 82-185 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U73689 EMBL· GenBank· DDBJ | AAB96332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CU329670 EMBL· GenBank· DDBJ | CAB08766.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB027801 EMBL· GenBank· DDBJ | BAA87105.1 EMBL· GenBank· DDBJ | Genomic DNA |