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: 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 10027: Double-stranded RNA-specific editase 1

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
Adenosine deaminase. [EC: 3.5.4.4]
Adenosine + H(2)O = inosine + NH(3).
    70 A0A0Q5SRT4 A0A0Q5SRT4 A0A0Q5SS31 A0A0Q5SS31 A0A0Q5SVB8 A0A0Q5SVB8 A0A0Q5T491 A0A0Q5T491 A0A0Q5T5Q8 A0A0Q5T5Q8
    (60 more...)
    Double-stranded RNA adenine deaminase. [EC: 3.5.4.37]
    Adenine in double-stranded RNA + H(2)O = hypoxanthine in double-stranded RNA + NH(3).
    • This eukaryotic enzyme is involved in RNA editing.
    • It destabilizes double-stranded RNA through conversion of adenosine to inosine.
    • Inositol hexakisphosphate is required for activity.
    12 P51400 P51400 P51400 P51400 P78563 P78563 P78563 P78563 Q91ZS8 Q91ZS8
    (2 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.
    4 Q83FY2 Q83FY2 Q83I82 Q83I82
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