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CATH Superfamily 3.90.730.10

Ribonuclease T2-like

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:

"
Ribonuclease T2-like
".

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 7: Ribonuclease T2

There are 1 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
Ribonuclease T(2). [EC: 4.6.1.19]
RNA + H(2)O = an (RNA fragment)-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-(RNA fragment).
  • A widely distributed family of related enzymes found in protozoans, plants, bacteria, animals and viruses that cleave ssRNA 3'-phosphate group with little base specificity.
  • The enzyme catalyzes a two-stage endonucleolytic cleavage.
  • The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending with a 2',3'-cyclic phosphodiester, which are released from the enzyme.
  • The enzyme then hydrolyzes the cyclic products in a second reaction that takes place only when all the susceptible 3',5'-phosphodiester bonds have been cyclised.
  • The second reaction is a reversal of the first reaction using the hydroxyl group of water instead of the 5'-hydroxyl group of ribose.
  • The overall process is that of a phosphorus-oxygen lyase followed by hydrolysis to form the 3'-nucleotides.
  • Formerly EC 2.7.7.17, EC 3.1.4.23, and EC 3.1.27.1.
 5 P42814 P42814 Q1ECE2 Q1ECE2 Q7M438
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