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:"
The structure of L14 comprises a five-stranded beta-barrel, a C-terminal loop region that contains two small alpha-helices, and a beta-ribbon that projects from the beta-barrel. An analysis of the structure and the conserved amino acids reveals three surface patches that probably mediate L14-RNA and L14-protein interactions within the ribosome. As a ribosomal protein, L14 has a role in the folding and stabilisation of ribosomal RNA, binding RNA at two sites (RNA-binding site 1 at the N-terminus and RNA-binding site 2 at the C-terminus). One RNA-binding site appears to recognise a distinct region of ribosomal RNA during particle assembly. The second site is smaller and may become occupied during the later compaction of the RNA. The surface hydrophobic patch is a likely site of protein-protein interaction (the protein-binding site), possibly with L19.
|Domain clusters (>95% seq id):||15|
|Domain clusters (>35% seq id):||3|
|Structural Clusters (5A):||1|
|Structural Clusters (9A):||1|