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RNase E/G, Thioredoxin-like domain
ribonuclease E/G
Ribonuclease E and Ribonuclease G are related enzymes that cleave a wide variety of RNAs [1]. [1]. 16237448. Structure of Escherichia coli RNase E catalytic domain and. implications for RNA turnover.. Callaghan AJ, Marcaida MJ, Stead JA, McDowall KJ, Scott WG,. Luisi BF;. Nature. 2005;437:1187-1191. (from Pfam)
ribonuclease E
ribonuclease E/G similar to archaeon Pyrococcus furiosus FAU-1, a RNA-binding AU-1 protein, which has RNA loop-binding activity; ribonuclease E and G are paralogs and are involved in rapid turnover of mRNA in bacteria
Rne/Rng family ribonuclease
This model describes ribonuclease G (formerly CafA, cytoplasmic axial filament protein A), the N-terminal domain of ribonuclease E in which ribonuclease activity resides, and related proteins. In E. coli, both RNase E and RNase G have been shown to play a role in the maturation of the 5' end of 16S RNA. The C-terminal half of RNase E (excluded from the seed alignment for this model) lacks ribonuclease activity but participates in mRNA degradation by organizing the degradosome.
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