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CATH Superfamily 2.40.70.10

Acid Proteases

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Acid Proteases
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 23148: Aspartic protease pep1

There are 10 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Candidapepsin. [EC: 3.4.23.24]
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.
  • This endopeptidase from the imperfect yeast Candida albicans is inhibited by pepstatin, but not by methyl 2-diazoacetamido-hexanoate or 1,2-epoxy-3-(p-nitrophenoxy)propane.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.17 and EC 3.4.23.6.
 34 B8YPM3 B9WDL8 B9WDY9 B9WEB2 B9WJ11 B9WMH7 C4YMJ3 C4YNQ5 C4YQ21 C4YSF6
(24 more...)
Aspergillopepsin I. [EC: 3.4.23.18]
Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.
  • Found in a variety of Aspergillus species (imperfect fungi): A.awamori, A.foetidus, A.fumigatus, A.kawachii, A.niger, A.oryzae, A.saitoi, and A.sojae.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.23.6.
 27 A0A0D9MQK0 A0A0F4YKI8 A0A0F4YZQ0 A0A0F4Z587 A0A0J5Q5Z0 A0A100IK58 A0A146F0J0 A1CBR4 A1DDK1 A2Q7E3
(17 more...)
Yapsin 1. [EC: 3.4.23.41]
Hydrolyzes various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favorable in both non- prime and prime positions.
  • Weakly inhibited by pepstatin.
  • Can partially substitute for kexin in a deficient strain of Saccharomyces cerevisiae.
  • The homologous product of the MKC7 gene (S.cerevisiae) has similar catalytic activity and has been termed yapsin 2.
  • Belongs to peptidase family A1.
 13 A0A0L8VKP1 A7A122 C8ZD89 E7KFJ3 E7KRP3 G2WIW2 H0GK81 K0KD48 N1NZA6 P32329
(3 more...)
Barrierpepsin. [EC: 3.4.23.35]
Selective cleavage of 6-Leu-|-Lys-7 bond in the pheromone alpha-mating factor.
  • Belongs to peptidase family A1.
 12 B5VKS5 C7GSF7 C8ZAN5 E2PT33 E7KDW4 E7KPY2 E7LVU2 E7QG71 H0GI10 K0KA43
(2 more...)
Penicillopepsin. [EC: 3.4.23.20]
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.
  • From the imperfect fungus Penicillium janthinellum.
  • Closely related enzymes have been isolated from P.roqueforti and P.duponti.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.17, EC 3.4.23.6 and EC 3.4.23.7.
 7 A0A167TDZ1 B6HL60 B8MF81 P00798 P78735 Q01972 Q9HEZ3
Pepsin A. [EC: 3.4.23.1]
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
  • The predominant endopeptidase in the gastric juice of vertebrates, formed from pepsinogen A by limited proteolysis.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.1.
 4 G3XWX0 G3YDG9 K0KTE5 K0KVH4
Endothiapepsin. [EC: 3.4.23.22]
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.
  • From the ascomycete Endothia parasitica.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.17, EC 3.4.23.6 and EC 3.4.23.10.
 1 P11838
Dolichyl-diphosphooligosaccharide--protein glycotransferase. [EC: 2.4.99.18]
Dolichyl diphosphooligosaccharide + [protein]-L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
  • Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains.
  • The basic oligosaccharide is the tetradecasaccharide Glc(3)Man(9)GlcNAc(2).
  • However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved.
  • Man(3)GlcNAc(2) seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-asparagine.
  • Occurs on the cytosolic face of the endoplasmic reticulum.
  • The dolichol involved normally has 14-21 isoprenoid units with two trans double-bonds at the omega end, and the rest of the double-bonds in cis form.
  • Formerly EC 2.4.1.119.
 1 A0A139HNZ0
Cathepsin D. [EC: 3.4.23.5]
Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.
  • Occurs intracellularly, in lysosomes.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.23.
 1 M5CH21
Mucorpepsin. [EC: 3.4.23.23]
Hydrolysis of proteins, favoring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen.
  • Isolated from the zygomycete fungi Mucor pusillus and M.miehei.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.17 and EC 3.4.23.6.
 1 P00799