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: waiting to be named.
Folding of the ribosomal protein S6 is a malleable process controlled by two competing, and partly overlapping, folding nuclei. The structure of S6 is composed of two cooperative subunits or 'foldons', sigma1 and sigma2, that also act as competing nuclei in the folding process. PMID:22117065. In E. coli, ribosomal protein S6 is known to bind 16S rRNA, together with S18.
Elongation factor eEF1B alpha (also known as EF1B, EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta).
In P. aeruginosa, PilM/N/O/P proteins are essential for T4P biogenesis, the periplasmic domains of PilN and PilO interact to form a heterodimer. PilO was shown to play a key role in the proper folding of PilN.
|Domain clusters (>95% seq id):||14|
|Domain clusters (>35% seq id):||9|
|Structural Clusters (5A):||2|
|Structural Clusters (9A):||2|