This superfamily comprises the N-terminal RNA-binding domain of the ribosomal protein L10 found in the large subunit (50S) of the bacterial ribosome. The entry contains homologues such as archaebacterial acidic ribosomal protein P0 homologue (L10E) and the eukaryotic 60S ribosomal protein P0 (L10E). The RNA-binding domain and the adjacent domain are thought to exist in archaeal L10 and eukaryotic P0 proteins only. Structurally, this domain contains three alpha-helices on each side of the five-stranded anti-parallel beta-sheet.

The large ribosomal subunit contains a highly flexible and functionally important lateral protuberance called the 'stalk' (L7/L12 stalk in Bacteria, L12 stalk in Archaea, and P1/P2 stalk in Eukarya). The stalk is involved in the formation of the so-called 'GTPase-associated site' and plays a key role in the interaction of ribosome with translation factors and in the control of translation accuracy. The L7/12 stalk is formed by two or three copies of the L7/L12 dimer bound to the C-terminal tail of protein L10. The N-terminal domain of L10 binds to a segment of domain II of 23S rRNA near the binding site for ribosomal protein L11. This superfamily includes the N-terminal domain of L10 in bacteria, and the domain I from the N-terminal fragment characterised in archaea. It is important to note that domain II of MjaL10NTF (insertion in domain I) is absent in bacteria.

PFAM:PF00466, INTERPRO:IPR001790,PMID:15989950,PMID:20399793