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:

"
Erythroid Transcription Factor GATA-1, subunit 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.
« Back to all FunFams

FunFam 4290: GATA transcription factor AreB

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].
    2 A0A0C9M9E8 A0A168LQ02
    RNA helicase. [EC: 3.6.4.13]
    ATP + H(2)O = ADP + phosphate.
    • RNA helicases utilize the energy from ATP hydrolysis to unwind RNA.
    • Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity.
    • Some helicases unwind DNA as well as RNA.
    • May be identical with EC 3.6.4.12 (DNA helicase).
    1 F4PW16
    DNA-directed RNA polymerase. [EC: 2.7.7.6]
    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
    • Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time.
    • Can initiate a chain de novo.
    • In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized.
    • See also EC 2.7.7.19 and EC 2.7.7.48.
    1 K0KH89