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Endothiapepsin in complex with fragment 181

Source organism: Cryphonectria parasitica
Biochemical function: aspartic-type endopeptidase activity
Biological process: proteolysis
Cellular component: not assigned

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EC 3.4.23.22: Endothiapepsin

Reaction catalysed:
Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.
Systematic name:
-
Alternative Name(s):
  • Endothia acid proteinase
  • Endothia aspartic proteinase
  • Endothia parasitica acid proteinase
  • Endothia parasitica aspartic proteinase

GO terms

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF00026
Domain description: Eukaryotic aspartyl protease
Occurring in:
  1. Endothiapepsin
The deposited structure of PDB entry 4y3a contains 1 copy of Pfam domain PF00026 (Eukaryotic aspartyl protease) in Endothiapepsin. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR001461
Domain description: Aspartic peptidase A1 family
Occurring in:
  1. Endothiapepsin
IPR021109
Domain description: Aspartic peptidase domain superfamily
Occurring in:
  1. Endothiapepsin
IPR033121
Domain description: Peptidase family A1 domain
Occurring in:
  1. Endothiapepsin
IPR001969
Domain description: Aspartic peptidase, active site
Occurring in:
  1. Endothiapepsin
IPR034163
Domain description: Aspergillopepsin-like catalytic domain
Occurring in:
  1. Endothiapepsin

Structure domain

CATH CATH domain
2.40.70.10
Class: Mainly Beta
Architecture: Beta Barrel
Topology: Cathepsin D, subunit A; domain 1
Homology: Acid Proteases
Occurring in:
  1. Endothiapepsin
The deposited structure of PDB entry 4y3a contains 2 copies of CATH domain 2.40.70.10 (Cathepsin D, subunit A; domain 1) in Endothiapepsin. Showing 2 copies in chain A.

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