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CATH Superfamily 3.30.40.10

Zinc/RING finger domain, C3HC4 (zinc finger)

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:

"
Zinc/RING finger domain, C3HC4 (zinc finger)
".

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 60826: Histone deacetylase 6 isoform A

There are 5 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
Ubiquitinyl hydrolase 1. [EC: 3.4.19.12]
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
  • Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides.
  • Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals.
  • Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde).
  • Belongs to peptidase family C12.
 239 A0A024RBD7 A0A060WH29 A0A060WIL2 A0A060XY77 A0A061IQJ4 A0A087QPS9 A0A087RGJ9 A0A087VN41 A0A087X3V5 A0A087Y5M0
(229 more...)
Histone deacetylase. [EC: 3.5.1.98]
Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
  • A class of enzymes that remove acetyl groups from N(6)-acetyl-lysine residues on a histone.
  • The reaction of this enzyme is opposite to that of EC 2.3.1.48.
  • Histone deacetylases (HDACs) can be organized into three classes depending on sequence similarity and domain organization.
  • Histone acetylation plays an important role in regulation of gene expression.
  • In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation.
  • May be identical to EC 3.5.1.17.
 10 A0A024QZ26 A0A061HX70 M9NGF7 M9PJN5 Q20296 Q86NK9 Q8IR37 Q8IR38 Q9UBN7 Q9Z2V5
Transferred entry: 2.3.2.23, 2.3.2.27 and 6.2.1.45. [EC: 6.3.2.19]
    		6 A0A0B2Q5F7 A0A0B2QLR0 A0A0B7FVQ4 M2XFL2 M2XYR3 W1QAB9
    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.
    		 2 Q7Z569 Q99MP8
    Glucuronosyltransferase. [EC: 2.4.1.17]
    UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside.
    • Family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines and fatty acids.
    • Some of the activities catalyzed were previously listed separately as EC 2.4.1.42, EC 2.4.1.59, EC 2.4.1.61, EC 2.4.1.76, EC 2.4.1.77, EC 2.4.1.84, EC 2.4.1.107 and EC 2.4.1.108.
    		 1 A0A171AW45