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CATH Superfamily 3.30.420.10

Ribonuclease H-like superfamily/Ribonuclease H

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:

"
Ribonuclease H-like superfamily/Ribonuclease H
".

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 45748: Ribonuclease D

There are 3 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 D. [EC: 3.1.13.5]
Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
  • Alteration of the 3'-terminal base has no effect on the rate of hydrolysis whereas modification of the 3'-terminal sugar has a major effect.
  • tRNA terminating with a 3'-phosphate is completely inactive.
  • This enzyme can convert a tRNA precursor into a mature tRNA.
 6272 A0A010P7W1 A0A010P7W1 A0A010T9E7 A0A010T9E7 A0A011P602 A0A011P602 A0A011SUR8 A0A011SUR8 A0A011SXT9 A0A011SXT9
(6262 more...)
Ribonuclease III. [EC: 3.1.26.3]
Endonucleolytic cleavage to 5'-phosphomonoester.
  • An endoribonuclease that cleaves double-stranded RNA molecules.
  • The cleavage can be either a single-stranded nick or double-stranded break in the RNA, depending in part upon the degree of base-pairing in the region of the cleavage site.
  • Specificity is conferred by negative determinants, i.e., the presence of certain Watson-Crick base-pairs at specific positions that strongly inhibit cleavage.
  • RNase III is involved in both rRNA processing and mRNA processing and decay.
 20 A0A017HRI0 A0A017HRI0 A0A059E838 A0A059E838 A0A090RCT9 A0A090RCT9 A0A090SQW6 A0A090SQW6 A0A160U280 A0A160U280
(10 more...)
Endopeptidase Clp. [EC: 3.4.21.92]
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
  • Belongs to peptidase family S14.
 2 U2XR06 U2XR06
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