|PROSITE documentation PDOC51195 [for PROSITE entry PS51195]|
RNA helicases from the DEAD-box family are found in almost all organisms and have important roles in RNA metabolism such as splicing, RNA transport, ribosome biogenesis, translation and RNA decay. They are enzyme that unwind double-stranded RNA molecules in an energy dependent fashion through the hydrolysis of NTP. DEAD-box RNA helicases belong to superfamily 2 (SF2) of helicases. As other SF1 and SF2 members they contain seven conserved motifs which are characteristic of these two superfamilies (see <PDOC51192>) . DEAD-box is named after the amino acids of motif II or Walker B (Mg2+-binding aspartic acid). Besides these seven motifs, DEAD-box RNA helicases contain a conserved cluster of nine amino-acids (the Q motif) with an invariant glutamine located N-terminally of motif I. An additional highly conserved but isolated aromatic residue is also found upstream of these nine residues . The Q motif is characteristic of and unique to DEAD box family of helicases. It is supposed to control ATP binding and hydrolysis, and therefore it represents a potential mechanism for regulating helicase activity.
Several structural analyses of DEAD-box RNA helicases have been reported (see <PDB:1HV8>) [3,4]. The Q motif is located in close proximity to motif I. The conserved glutamine and aromatic residues interact with the ADP molecule.
Some proteins known to contain a Q motif:
The profile we developed stretches from the conserved aromatic residue to one amino acid after the glutamine of the Q motif.Last update:
April 2006 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Koonin E.V., Gorbalenya A.E.|
|Title||Autogenous translation regulation by Escherichia coli ATPase SecA may be mediated by an intrinsic RNA helicase activity of this protein.|
|Source||FEBS. Lett. 298:6-8(1992).|
|2||Authors||Tanner N.K., Cordin O., Banroques J., Doere M., Linder P.|
|Title||The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis.|
|Source||Mol. Cell 11:127-138(2003).|
|3||Authors||Story R.M., Li H., Abelson J.N.|
|Title||Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 98:1465-1470(2001).|
|4||Authors||Benz J., Trachsel H., Baumann U.|
|Title||Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae--the prototype of the DEAD box protein family.|