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CATH Superfamily 3.40.50.150

Vaccinia Virus protein VP39

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:

"
Vaccinia Virus protein VP39
".

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 135748: Methyltransferase domain protein

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
Endothelin-converting enzyme 1. [EC: 3.4.24.71]
Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.
  • Phosphoramidon-sensitive.
  • Belongs to peptidase family M13.
 22 A0A061I8D8 A0A061I8D8 A0A0B2PEU1 A0A0B2PEU1 A0A0B2PVJ6 A0A0B2PVJ6 A0A0B2QY71 A0A0B2QY71 A0A0B2RKK8 A0A0B2RKK8
(12 more...)
Type I site-specific deoxyribonuclease. [EC: 3.1.21.3]
Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates; ATP is simultaneously hydrolyzed.
  • Large group of enzymes that have an absolute requirement for ATP (or dATP) and S-adenosyl-L-methionine.
  • They recognize specific short DNA sequences and cleave at sites remote from the recognition sequence.
  • Multifunctional proteins which also catalyze the reactions of EC 2.1.1.72 and EC 2.1.1.73, with similar site specificity.
  • Formerly EC 3.1.24.1 and EC 3.1.24.2.
  • See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/
 2 G0QX35 G0QX35
Phosphatidylethanolamine N-methyltransferase. [EC: 2.1.1.17]
S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L- homocysteine + phosphatidyl-N-methylethanolamine.
    		 2 G0QYY5 G0QYY5
    Polyprenyldihydroxybenzoate methyltransferase. [EC: 2.1.1.114]
    S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans- polyprenylbenzoate.
    • This enzyme is involved in ubiquinone biosynthesis.
    • Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone- 9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units.
    • However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units.
    • For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast.
    • The enzymes from yeast and rat also catalyze the methylation of 3-demethylubiquinol-6 and 3-demethylubiquinol-9, respectively (this activity is classified as EC 2.1.1.64).
    		 2 G0QIT7 G0QIT7
    Phosphoethanolamine N-methyltransferase. [EC: 2.1.1.103]
    S-adenosyl-L-methionine + ethanolamine phosphate = S-adenosyl-L- homocysteine + N-methylethanolamine phosphate.
    • The enzyme may catalyze the transfer of two further methyl groups to the product.
    		 2 G0QX35 G0QX35