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Protease Sapp1p from Candida parapsilosis in complex with KB74

Source organisms:
Biochemical function: aspartic-type endopeptidase activity
Biological process: proteolysis
Cellular component: extracellular region

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EC 3.4.23.24: Candidapepsin

Reaction catalysed:
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.
Systematic name:
-
Alternative Name(s):
  • Candida albicans aspartic proteinase
  • Candida albicans carboxyl proteinase
  • Candida albicans secretory acid proteinase
  • Candida aspartic proteinase
  • Candida olea acid proteinase
  • Candida olea aspartic proteinase

GO terms

Biochemical function:
Biological process:
Cellular component:

Sequence family

Pfam Protein family (Pfam)
PF00026
Domain description: Eukaryotic aspartyl protease
Occurring in:
  1. Candidapepsin-1
The deposited structure of PDB entry 7agc contains 4 copies of Pfam domain PF00026 (Eukaryotic aspartyl protease) in Candidapepsin-1. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR001461
Domain description: Aspartic peptidase A1
Occurring in:
  1. Candidapepsin-1
IPR021109
Domain description: Aspartic peptidase domain superfamily
Occurring in:
  1. Candidapepsin-1
IPR001969
Domain description: Aspartic peptidase, active site
Occurring in:
  1. Candidapepsin-1
IPR033121
Domain description: Peptidase family A1 domain
Occurring in:
  1. Candidapepsin-1
IPR033876
Domain description: Secreted aspartic endopeptidase
Occurring in:
  1. Candidapepsin-1

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