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CATH Superfamily 2.130.10.120

Prolyl oligopeptidase, N-terminal domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Prolyl oligopeptidase, N-terminal domain
".

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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 2 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
Prolyl oligopeptidase. [EC: 3.4.21.26]
Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.
  • Found in vertebrates, plants and Flavobacterium.
  • Generally cytosolic, commonly activated by thiol compounds.
  • Belongs to peptidase family S9A.
  • Formerly EC 3.4.22.18.
 16 A0A1T3I693 A0A480WGK4 E2JFG1 E2JFG2 H2E7Q7 H2E7Q8 O70196 P23687 P27028 P27195
(6 more...)
Oligopeptidase B. [EC: 3.4.21.83]
Hydrolysis of -Arg-|-Xaa- and -Lys-|-Xaa- bonds in oligopeptides, even when P1' residue is proline.
  • Inhibited by Tos-Lys-CH(2)Cl.
  • Belongs to peptidase family S9A.
 9 A0A069XG02 A0A094VLH0 A0A0B4ZN40 A0A0M7PG80 A0A1X3JGT4 G0F6W3 I2XCD4 P24555 Q59536