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CATH Superfamily 1.10.533.10

Death Domain, Fas

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:

"
Death Domain, Fas
".

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 5221: Baculoviral IAP repeat-containing 2

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
Caspase-1. [EC: 3.4.22.36]
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.
  • Part of the family of inflammatory-caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice.
  • Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation.
  • Cleaves pro-interleukin-1-beta (pro-IL-1-beta) to form mature IL-1- beta, a potent mediator of inflammation.
  • Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-gamma-inducing factor.
  • Inhibited by Ac-Tyr-Val-Ala-Asp-CHO.
  • Caspase-11 plays a critical role in the activation of caspase-1 in mice whereas caspase-4 enhances its activation in humans.
  • Belongs to peptidase family C14.
 20 A0A1L8HDG9 A0A1L8HDG9 P29452 P29452 P29466 P29466 P43527 P43527 P55865 P55865
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RING-type E3 ubiquitin transferase. [EC: 2.3.2.27]
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
  • The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein.
  • The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26).
  • RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies.
  • Formerly EC 6.3.2.19 and EC 6.3.2.21.
 10 A1E2V0 A1E2V0 O08863 O08863 Q13489 Q13489 Q13490 Q13490 Q62210 Q62210
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