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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 23129: Aspartic protease pep1

There are 9 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
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...)
Rhizopuspepsin. [EC: 3.4.23.21]
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of insulin.
  • From the zygomycete fungi Rhizopus chinensis and R.niveus.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.17, EC 3.4.23.6, EC 3.4.23.9 and EC 3.4.99.25.
 23 A0A0C7AWS4 A0A1D8PV96 B8YJG1 B8YJG2 B8YJG3 B8YJG4 B8YJG5 B8YJG6 B8YJG7 I1BK02
(13 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
Transferred entry: 3.4.21.103, 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30. [EC: 3.4.23.6]
    		1 Q02017
    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
    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 K4F4I1
    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.
    		 1 G3XWX0
    Gly-Xaa carboxypeptidase. [EC: 3.4.17.4]
    Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly-|-Leu.
    • Belongs to peptidase family M20A.
    • Formerly EC 3.4.2.3, EC 3.4.12.8 and EC 3.4.17.9.
    		 1 U5HT00