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CATH Superfamily 1.10.8.10

Ubiquitin-associated (UBA) domain

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:

"
DNA helicase RuvA subunit, C-terminal domain
".

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 14692: 50S ribosomal protein L3 glutamine methyltransfera...

There are 4 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
Ribosomal protein L3 N(5)-glutamine methyltransferase. [EC: 2.1.1.298]
S-adenosyl-L-methionine + [ribosomal protein L3]-L-glutamine = S-adenosyl-L-homocysteine + [ribosomal protein L3]-N(5)-methyl-L- glutamine.
  • Modifies the glutamine residue in the glycylglycylglutamine (GGQ) motif of ribosomal protein L3 (Gln(150) in the protein from the bacterium Escherichia coli).
  • The enzyme does not act on peptide chain release factor 1 or 2.
  • Formerly EC 2.1.1.n15.
 2592 A0A010PD71 A0A010S494 A0A011NC02 A0A011NJM1 A0A011Q796 A0A014LYX2 A0A017IE81 A0A022GR00 A0A022PI53 A0A023C3D6
(2582 more...)
Site-specific DNA-methyltransferase (adenine-specific). [EC: 2.1.1.72]
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA.
  • This is a large group of enzymes, most of which form so-called 'restriction-modification systems', with nucleases that possess similar site specificity (the nucleases are listed as either EC 3.1.21.3, EC 3.1.21.4 and EC 3.1.21.5).
  • See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/
 5 A0A1L9EZ22 A0A1N6MVT3 A6VXI6 E6QRI8 Q7VRU7
Protoporphyrinogen oxidase. [EC: 1.3.3.4]
Protoporphyrinogen-IX + 3 O(2) = protoporphyrin-IX + 3 H(2)O(2).
  • Also slowly oxidizes mesoporphyrinogen IX.
 3 A0A0T8L8E6 A0A137YDC8 F2N5U6
Chorismate synthase. [EC: 4.2.3.5]
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate.
  • The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH.).
  • Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction.
  • Formerly EC 4.6.1.4.
 1 A0A0A2VUU5
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