A0A915CKU6 · A0A915CKU6_PARUN
- ProteinPeptidase metallopeptidase domain-containing protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids538 (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 | 81 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | |||
Binding site | 157 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 167 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 169 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 174 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 175 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 182 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 191 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 193 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 195 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 197 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 198 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 200 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 200 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 223 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Active site | 224 | ||||
Binding site | 227 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 233 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 241 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 324 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 326 | Ca2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 369 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 371 | Ca2+ 5 (UniProtKB | ChEBI) | |||
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 accessionA0A915CKU6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-18 | ||||
Chain | PRO_5041189962 | 19-538 | |||
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, repeat.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 102-267 | Peptidase metallopeptidase | |||
Region | 270-317 | Disordered | |||
Compositional bias | 286-302 | Pro residues | |||
Repeat | 320-364 | Hemopexin | |||
Repeat | 365-412 | Hemopexin | |||
Repeat | 460-504 | Hemopexin | |||
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length538
- Mass (Da)61,007
- Last updated2023-02-22 v1
- MD5 Checksum160D6046F84701421588B5E671542A24
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 286-302 | Pro residues | |||
Keywords
- Technical term