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A0A915AFX0 · A0A915AFX0_PARUN

Function

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Can bind about 5 Ca2+ ions per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Features

Showing features for binding site, active site.

155950100150200250300350400450500550
Type
IDPosition(s)Description
Binding site100Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site132Ca2+ 1 (UniProtKB | ChEBI)
Binding site165Ca2+ 2 (UniProtKB | ChEBI)
Binding site175Zn2+ 1 (UniProtKB | ChEBI)
Binding site177Zn2+ 1 (UniProtKB | ChEBI)
Binding site182Ca2+ 3 (UniProtKB | ChEBI)
Binding site183Ca2+ 3 (UniProtKB | ChEBI)
Binding site190Zn2+ 1 (UniProtKB | ChEBI)
Binding site200Zn2+ 1 (UniProtKB | ChEBI)
Binding site202Ca2+ 3 (UniProtKB | ChEBI)
Binding site205Ca2+ 3 (UniProtKB | ChEBI)
Binding site205Ca2+ 1 (UniProtKB | ChEBI)
Binding site229Zn2+ 2 (UniProtKB | ChEBI); catalytic
Active site230
Binding site233Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site239Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site247Zn2+ 2 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentextracellular matrix
Cellular Componentextracellular space
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processcollagen catabolic process
Biological Processextracellular matrix organization
Biological Processproteolysis

Keywords

Names & Taxonomy

Protein names

  • Submitted names
    • Peptidase metallopeptidase domain-containing protein

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Spirurina > Ascaridomorpha > Ascaridoidea > Ascarididae > Parascaris

Accessions

  • Primary accession
    A0A915AFX0

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-22
ChainPRO_503715070423-559

Family & Domains

Features

Showing features for motif, domain, region, compositional bias.

Type
IDPosition(s)Description
Motif98-105Cysteine switch
Domain113-280Peptidase metallopeptidase
Region284-309Disordered
Compositional bias325-365Polar residues
Region325-379Disordered

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    559
  • Mass (Da)
    62,239
  • Last updated
    2023-02-22 v1
  • MD5 Checksum
    4DA4A778367D626FD64C3B4BAC8608B8
MALYRQLCLVALLLSLFRSFHCRRNLKPLSDAQATKYLSDYGYVSTSNVLSSAPSGVGLDREDTFSSLKNAIRKFQEFARLRQTGELDDATRRKMAQPRCGVTDVLAITKGGPAFKWNKKDLTYSIESFSPDLPQDDIRRAMAKAFATWSAVAPLNFEEVRTGGDIKIRFASRFHGDPWPFDGEGGVLAHATMPPSGLLHFDEDEHWVYMDPKKIFAYDYMDLLAVAIHESGHTLGLDHSRDESSIMAPFYQETVDAHGNYIMPKLNTDDITKIQNIYGPRRRVSLESDGIEPTARPSTGASRKESSGGSFLDRIKSFFGFGGDRSSSSIDSNVPSHGSDSTDSGFHSSGTESFSGSNSGSRRGSDSSPHSKECPKDVDGITTANGITYLFSGSKVYQLASGRVENVHSLRQLFPKSPAYVQGALTEPRSGVTLLFQHGQVYSYTYDRSEGAFRLDSSYPKRLSSDIKFNPMGAFMWIDGREVLVNAHDFAIYDHYWNKGTLQNKISNYFDNFPNEPIRGAIIDGNTVIFFANDNVYRYDVNQRRVVGGSIPLYSYLNC

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias325-365Polar residues

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

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