A0A915AFX0 · A0A915AFX0_PARUN
- ProteinPeptidase metallopeptidase domain-containing protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids559 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Cofactor
Protein has several cofactor binding sites:
Note: Can bind about 5 Ca2+ ions per subunit.
Note: Binds 2 Zn2+ ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 100 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | |||
Binding site | 132 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 165 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 175 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 177 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 182 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 183 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 190 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 200 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 202 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 205 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 205 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 229 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Active site | 230 | ||||
Binding site | 233 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 239 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 247 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular matrix | |
Cellular Component | extracellular space | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | collagen catabolic process | |
Biological Process | extracellular matrix organization | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Spirurina > Ascaridomorpha > Ascaridoidea > Ascarididae > Parascaris
Accessions
- Primary accessionA0A915AFX0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-22 | ||||
Chain | PRO_5037150704 | 23-559 | |||
Structure
Family & Domains
Features
Showing features for motif, domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Motif | 98-105 | Cysteine switch | |||
Domain | 113-280 | Peptidase metallopeptidase | |||
Region | 284-309 | Disordered | |||
Compositional bias | 325-365 | Polar residues | |||
Region | 325-379 | Disordered | |||
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length559
- Mass (Da)62,239
- Last updated2023-02-22 v1
- MD5 Checksum4DA4A778367D626FD64C3B4BAC8608B8
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 325-365 | Polar residues | |||
Keywords
- Technical term