SMART: Pfam domain RraA-like

RraA-like

PFAM accession number:	PF03737
Interpro abstract (IPR005493):	This entry represents the regulator of ribonuclease E activity A (RraA). These proteins contain a swivelling 3-layer beta/beta/alpha domain that appears to be mobile in most multi-domain proteins known to contain it. These proteins are structurally similar, and may have distant homology, to the phosphohistidine domain of pyruvate phosphate dikinase. The RraA fold is an ancient platform that has been adapted for a wide range of functions. RraA had been identified as a putative demethylmenaquinone methyltransferase and was annotated as MenG, but further analysis showed that RraA lacked the structural motifs usually required for methylases [ (PUBMED:14499605) ]. The Escherichia coli protein regulator RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing [ (PUBMED:14499605) ]. RNase E forms the core of a large RNA-catalysis machine termed the degradosomes. RraA (and RraB) causes remodelling of degradosome composition, which is associated with alterations in RNA decay and global transcript abundance and as such is a bacterial mechanism for the regulation of RNA cleavage. This fold is also found in 4-hydroxy-4-methyl-2-oxoglutarate aldolase, also known as RraA-like protein [ (PUBMED:24359411) ] and at the C terminus of the DlpA protein Q48806 .

PFAM accession number:

PF03737

Interpro abstract (IPR005493):

This entry represents the regulator of ribonuclease E activity A (RraA). These proteins contain a swivelling 3-layer beta/beta/alpha domain that appears to be mobile in most multi-domain proteins known to contain it. These proteins are structurally similar, and may have distant homology, to the phosphohistidine domain of pyruvate phosphate dikinase. The RraA fold is an ancient platform that has been adapted for a wide range of functions. RraA had been identified as a putative demethylmenaquinone methyltransferase and was annotated as MenG, but further analysis showed that RraA lacked the structural motifs usually required for methylases [ (PUBMED:14499605) ].

The Escherichia coli protein regulator RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing [ (PUBMED:14499605) ]. RNase E forms the core of a large RNA-catalysis machine termed the degradosomes. RraA (and RraB) causes remodelling of degradosome composition, which is associated with alterations in RNA decay and global transcript abundance and as such is a bacterial mechanism for the regulation of RNA cleavage.

This fold is also found in 4-hydroxy-4-methyl-2-oxoglutarate aldolase, also known as RraA-like protein [ (PUBMED:24359411) ] and at the C terminus of the DlpA protein Q48806 .

This is a PFAM domain. For full annotation and more information, please see the PFAM entry RraA-like