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CATH Superfamily 3.90.70.10

Cysteine proteinases

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:

"
Cysteine proteinases
".

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 126: Genome polyprotein

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
Picornain 3C. [EC: 3.4.22.28]
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
  • From entero-, rhino-, aphto- and cardioviruses.
  • Larger than the homologous virus picornain 2A.
  • Belongs to peptidase family C3.
 9 P03305 P03306 P03307 P03308 P03309 P03310 P03311 P15072 P49303
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.
 9 P03305 P03306 P03307 P03308 P03309 P03310 P03311 P15072 P49303
L-peptidase. [EC: 3.4.22.46]
Autocatalytically cleaves itself from the polyprotein of the foot- and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
  • Best known from foot-and-mouth disease virus, but occurs in other aphthoviruses and cardioviruses.
  • Destruction of initiation factor eIF-4G has the effect of shutting off host-cell protein synthesis while allowing synthesis of viral proteins to continue.
  • The tertiary structure reveals a distant relationship to papain and, consistent with this, compound E-64 is inhibitory.
  • Belongs to peptidase family C28.
 9 P03305 P03306 P03307 P03308 P03309 P03310 P03311 P15072 P49303
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.
 9 P03305 P03306 P03307 P03308 P03309 P03310 P03311 P15072 P49303
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