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CATH Superfamily 3.20.20.150

Divalent-metal-dependent TIM barrel enzymes

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Divalent-metal-dependent TIM barrel enzymes
".

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 16: Protein arginine N-methyltransferase

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
Type II protein arginine methyltransferase. [EC: 2.1.1.320]
2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L- homocysteine + [protein]-N(omega),N(omega')-dimethyl-L-arginine.
  • The enzyme catalyzes the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine.
  • The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins.
  • Cf. EC 2.1.1.319, EC 2.1.1.321 and EC 2.1.1.322.
  • Formerly EC 2.1.1.23, EC 2.1.1.124, EC 2.1.1.125 and EC 2.1.1.126.
 5 A2X0Q3 I1NX48 I1NX48 Q6YXZ7 Q6YXZ7
Type I protein arginine methyltransferase. [EC: 2.1.1.319]
2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L- homocysteine + [protein]-N(omega),N(omega)-dimethyl-L-arginine.
  • This eukaryotic enzyme catalyzes the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues.
  • Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific.
  • The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues.
  • PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells.
  • Cf. EC 2.1.1.320, EC 2.1.1.321 and EC 2.1.1.322.
  • Formerly EC 2.1.1.23, EC 2.1.1.124, EC 2.1.1.125 and EC 2.1.1.126.
 1 Q8GWT4
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