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: waiting to be named.
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: waiting to be named.
L4 is among the largest ribosomal proteins, playing a crucial role in the early assembly of the large subunit. It consists of a single domain and exhibits an alpha/beta fol with an open beta-sheet topology. L4 has a well defined and conserved hydrophobic core which stabilises the overall structure. L4 in yeast has been shown to bind to 25S rRNA. L4 was the first protein shown to inhibit not only the translation but also the transcription of its S10 operon. Escherichia coli L4 seems to exhibit separate rRNA- (N-terminal) and mRNA- (C-terminal) binding modules.
Structures | |
---|---|
Domains: | 132 |
Domain clusters (>95% seq id): | 12 |
Domain clusters (>35% seq id): | 7 |
Unique PDBs: | 132 |
Alignments | |
Structural Clusters (5A): | 1 |
Structural Clusters (9A): | 1 |
FunFam Clusters: | 51 |
Function | |
Unique EC: | |
Unique GO: | 64 |
Taxonomy | |
Unique Species: | 17963 |