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CATH Superfamily 2.30.42.10

PDZ domain

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: waiting to be named.

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 23938: Probable periplasmic serine endoprotease DegP-like

There are 3 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
Peptidase Do. [EC: 3.4.21.107]
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.
  • This serine endopeptidase is essential for the clearance of denatured or aggregated proteins from the inner-membrane and periplasmic space in Escherichia coli.
  • Natural substrates of the enzyme include colicin A lysis protein, pilin subunits and MalS from E.coli.
  • The enzyme has weak peptidase activity with casein and other non- native substrates.
  • The peptidase acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures.
  • Molecular chaperones and peptidases control the folded state of proteins by recognizing hydrophobic stretches of polypeptide that become exposed by misfolding or unfolding.
  • They then bind these hydrophobic substrates to prevent aggregation or assist in protein refolding.
  • If attempts at refolding fail, then irreversibly damaged proteins are degraded by peptidases such as this enzyme.
  • Belongs to peptidase family S1B.
 35 A0A060I4V5 A0A072CKB3 A0A090GKF3 A0A0A8GA68 A0A0B4X064 A0A0E1XBU5 A0A0F6APV5 A0A0H3AQ96 A0A0M1WEA5 A0A192LTY7
(25 more...)
HtrA2 peptidase. [EC: 3.4.21.108]
Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues.
  • Up-regulated in mammalian cells in response to stress induced by both heat shock and tunicamycin treatment.
  • Can induce apoptosis in a caspase-independent manner through its peptidase activity and in a caspase-dependent manner by disrupting the interaction between caspase and the inhibitor of apoptosis (IAP).
  • Belongs to peptidase family S1B.
 3 A0A0E0UA68 C6ASW9 M4MU44
2-alkenal reductase (NAD(P)(+)). [EC: 1.3.1.74]
A n-alkanal + NAD(P)(+) = an alk-2-enal + NAD(P)H.
  • Highly specific for 4-hydroxynon-2-enal and non-2-enal.
  • Alk-2-enals of shorter chain have lower affinities.
  • Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one.
  • Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid.
  • Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones (cf. EC 1.3.1.102).
 3 A6U763 A6X2C5 B5ZVF9
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