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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 61360: Probable histone acetyltransferase HAC-like 1

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
Histone acetyltransferase. [EC: 2.3.1.48]
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine.
  • A group of enzymes acetylating histones.
  • Several of the enzymes can also acetylate lysines in other proteins.
 12 A0A0B2QLV0 A0A0B2RUN2 A0A0B2RY53 A0A151SGK7 A0A178WJZ4 Q5Z8V7 Q6YXY2 Q9C5X9 Q9FWQ5 Q9LE42
(2 more...)
Porphobilinogen synthase. [EC: 4.2.1.24]
2 5-aminolevulinate = porphobilinogen + 2 H(2)O.
  • The enzyme catalyzes the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430.
  • The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis.
  • In humans, the enzyme is a primary target for the environmental toxin Pb.
  • The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation.
 2 A0A0E0E625 A0A0E0E626
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