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CATH Superfamily 2.60.210.10

Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A

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:

"
Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
".

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 2360: TNF receptor-associated factor 6

There are 4 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
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.
 40 A0A024R8H5 A0A024R8H5 A0A096MX12 A0A096MX12 A0A1L8GE35 A0A1L8GE35 A7XUJ6 A7XUJ6 B5DF45 B5DF45
(30 more...)
Meprin B. [EC: 3.4.24.63]
Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of 5-His-|-Leu-6, 6-Leu-|-Cys-7, 14-Ala-|-Leu-15 and 19-Cys-|-Gly-20 bonds in insulin B chain.
  • Inhibited by EDTA and 1,10-phenanthroline, but not by phosphoramidon, captopril or thiorphan.
  • Belongs to peptidase family M12A.
 6 P28826 P28826 Q16820 Q16820 Q61847 Q61847
Meprin A. [EC: 3.4.24.18]
Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.
  • A membrane-bound metalloendopeptidase of rat and mouse kidney and intestinal brush borders, and salivary ducts.
  • Differences from EC 3.4.24.11 include insensitivity to phosphoramidon and thiorphan.
  • PABA-peptide hydrolase is a very similar enzyme found in human intestinal microvilli.
  • Belongs to peptidase family M12A.
 6 P28825 P28825 Q16819 Q16819 Q64230 Q64230
Non-specific serine/threonine protein kinase. [EC: 2.7.11.1]
ATP + a protein = ADP + a phosphoprotein.
  • This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date.
  • Formerly EC 2.7.1.37 and EC 2.7.1.70.
 4 B7P7P1 B7P7P1 E0VKY3 E0VKY3