This superfamily entry contains the ribosomal protein L16 found in the 50S subunit of the bacterial, mitochondrial and plastid ribosome, as well as its eukaryotic and archaeal homologue found in the 60S subunit, L10 (or RPL10). L16 and L10e exhibit structural differences, especially at the N-terminal region. This structural domain exhibits an alpha/beta-hammerhead fold, where the beta-hammerhead motif is similar to that in barrel-sandwich hybrids. L10 and L16 contribute to the architecture of the tRNA binding site on the large ribosomal subunit.

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.

PFAM:PF00252, INTERPRO:IPR036920,PMID:15561149,PMID:12384386,PMID:18258260