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CATH Superfamily 3.65.10.20

RNA 3'-terminal phosphate cyclase domain

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:

"
RNA 3'-terminal phosphate cyclase 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 8: RNA 3'-terminal phosphate cyclase

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
RNA 3'-terminal-phosphate cyclase (ATP). [EC: 6.5.1.4]
ATP + (RNA)-3'-(3'-phospho-ribonucleoside) = AMP + diphosphate + (RNA)- 3'-(2',3'-cyclophospho)-ribonucleoside.
  • The enzyme converts the 3'-terminal phosphate of various RNA substrates into the 2',3'-cyclic phosphodiester in an ATP-dependent reaction.
  • Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a histidine residue.
  • The adenylate group is then transferred to the 3'-phosphate terminus of the substrate, forming the capped structure (RNA)- 3'-(5'-diphosphoadenosine).
  • Finally, the enzyme catalyzes an attack of the vicinal O-2' on the 3'-phosphorus, which results in formation of cyclic phosphate and release of the adenylate.
  • The enzyme also has a polynucleotide 5' adenylation activity.
  • Cf. EC 6.5.1.5.
 32 A0A0E3MBS3 A0A0E3MBS3 A0A0E3MBS3 C3MKC1 C3MKC1 C3MKC1 C3MU91 C3MU91 C3N179 C3N179
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