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CATH Superfamily 1.10.260.90

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: waiting to be named.

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 1: Genome polyprotein

There are 6 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
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).
 51 A0A024B7W1 A0A024B7W1 A0A142I5B9 A0A142I5B9 A0A2H4GY08 A0A2H4GY08 A0A2S1Q2P2 A0A2S1Q2P2 A0A3G5ALR9 A0A3G5ALR9
(41 more...)
Nucleoside-triphosphate phosphatase. [EC: 3.6.1.15]
NTP + H(2)O = NDP + phosphate.
  • The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria.
  • Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD.
  • The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.
 51 A0A024B7W1 A0A024B7W1 A0A142I5B9 A0A142I5B9 A0A2H4GY08 A0A2H4GY08 A0A2S1Q2P2 A0A2S1Q2P2 A0A3G5ALR9 A0A3G5ALR9
(41 more...)
RNA-directed RNA polymerase. [EC: 2.7.7.48]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
  • Catalyzes RNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time.
  • Can initiate a chain de novo.
  • See also EC 2.7.7.6.
 51 A0A024B7W1 A0A024B7W1 A0A142I5B9 A0A142I5B9 A0A2H4GY08 A0A2H4GY08 A0A2S1Q2P2 A0A2S1Q2P2 A0A3G5ALR9 A0A3G5ALR9
(41 more...)
Flavivirin. [EC: 3.4.21.91]
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
    		 51 A0A024B7W1 A0A024B7W1 A0A142I5B9 A0A142I5B9 A0A2H4GY08 A0A2H4GY08 A0A2S1Q2P2 A0A2S1Q2P2 A0A3G5ALR9 A0A3G5ALR9
    (41 more...)
    Methyltransferase cap1. [EC: 2.1.1.57]
    S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)- (purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)- methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)- [mRNA].
    • This enzyme catalyzes the methylation of the ribose on the first transcribed nucleotide of mRNA or snRNA molecules, which may be either guanosine or adenosine.
    • This methylation event is known as cap1, and occurs in all mRNAs and snRNAs of higher eukaryotes, including insects, vertebrates and their viruses.
    • The human enzyme can also methylate mRNA molecules that lack methylation on the capping 5'-triphosphoguanosine.
    • Formerly EC 2.1.1.58.
    		 51 A0A024B7W1 A0A024B7W1 A0A142I5B9 A0A142I5B9 A0A2H4GY08 A0A2H4GY08 A0A2S1Q2P2 A0A2S1Q2P2 A0A3G5ALR9 A0A3G5ALR9
    (41 more...)
    MRNA (guanine-N(7)-)-methyltransferase. [EC: 2.1.1.56]
    S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
    • Adds an N(7)-methylguanine cap to mRNA.
    • The nucleoside next to the terminal guanosine may be either guanosine or adenosine.
    		 51 A0A024B7W1 A0A024B7W1 A0A142I5B9 A0A142I5B9 A0A2H4GY08 A0A2H4GY08 A0A2S1Q2P2 A0A2S1Q2P2 A0A3G5ALR9 A0A3G5ALR9
    (41 more...)
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