C3XSA5 · C3XSA5_BRAFL
- ProteinPeptidase metallopeptidase domain-containing protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids494 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 86 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | |||
Binding site | 149 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 159 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 161 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 166 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 167 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 174 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 183 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 185 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 187 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 189 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 192 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 192 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 210 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Active site | 211 | ||||
Binding site | 214 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 220 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 228 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 314 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 316 | Ca2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 359 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 451 | Ca2+ 4 (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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePeptidase metallopeptidase domain-containing protein
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Cephalochordata > Leptocardii > Amphioxiformes > Branchiostomatidae > Branchiostoma
Accessions
- Primary accessionC3XSA5
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-21 | ||||
Chain | PRO_5002934714 | 22-494 | Peptidase metallopeptidase domain-containing protein | ||
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, repeat.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 97-255 | Peptidase metallopeptidase | |||
Region | 283-308 | Disordered | |||
Repeat | 310-351 | Hemopexin | |||
Repeat | 398-446 | Hemopexin | |||
Repeat | 447-494 | Hemopexin | |||
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length494
- Mass (Da)56,248
- Last updated2009-07-28 v1
- MD5 ChecksumD4612558ACCC8C9C09D67609AD44E834
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 494 | ||||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GG666458 EMBL· GenBank· DDBJ | EEN69033.1 EMBL· GenBank· DDBJ | Genomic DNA |