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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 61135: Putative histone-lysine N-methyltransferase ASH1L

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
Histone-lysine N-methyltransferase. [EC: 2.1.1.43]
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
    		 116 A0A026X0W3 A0A060VWG4 A0A061IHJ3 A0A061IK22 A0A087XT37 A0A087ZS57 A0A091D1P9 A0A091F0A9 A0A091I2K6 A0A091RNZ9
    (106 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 A0A1B0AAH9 A0A1B0G4F7
    Threonine ammonia-lyase. [EC: 4.3.1.19]
    L-threonine = 2-oxobutanoate + NH(3).
    • The reaction catalyzed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16), followed by tautomerization to an imine form and hydrolysis of the C-N bond.
    • The latter reaction, which can occur spontaneously, is also be catalyzed by EC 3.5.99.10.
    • The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17.
    • Formerly EC 4.2.1.16.
    		 1 A0A060S9S2