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:"
Large subunits that lack L16 are defective in peptidyl transferase activity, peptidyl-tRNA hydrolysis activity, association with the 30S subunit, binding of aminoacyl-tRNA and interaction with antibiotics. L16 is required for the function of elongation factor P (EF-P), a protein involved in peptide bond synthesis through the stimulation of peptidyl transferase activity by the ribosome. All known mutations in L16 confer antibiotic resistance in bacteria (such as resistance to avilamycin and evernimicin), suggesting a direct participation of L16 in the binding site for antibiotics. The GTPase RbgA (YlqF) is essential for the assembly of the large subunit, and it is believed to regulate the incorporation of L16.
Additionally, L10 exhibits other cellular activities, in particular the human L10 which works as a tumour suppressor (QM). Studies in yeast have shown that L10 incorporation is a prerequisite for ribosomal subunit joining and translation initiation, and it also represents a key step for the nuclear export of the large ribosomal subunit.
|Domain clusters (>95% seq id):||17|
|Domain clusters (>35% seq id):||5|
|Structural Clusters (5A):||1|
|Structural Clusters (9A):||1|