Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
4Fe-4S double cluster binding domain-containing protein
QueG-associated DUF1730 domain-containing protein
This domain of unknown function occurs in Epoxyqueuosine reductase QueG, an iron-sulfur cluster-binding protein, together with the 4Fe-4S binding domain (Pfam:PF00037). QueG catalyses the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr) [1]. [1]. 21502530. Discovery of epoxyqueuosine (oQ) reductase reveals parallels. between halorespiration and tRNA modification.. Miles ZD, McCarty RM, Molnar G, Bandarian V;. Proc Natl Acad Sci U S A. 2011;108:7368-7372. (from Pfam)
epoxyqueuosine reductase
epoxyqueuosine reductase catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr)
tRNA epoxyqueuosine(34) reductase QueG
This model was rebuilt to exclude archaeal homologs, now that there is new information that bacterial members are epoxyqueuosine reductase, QueG, involved in queuosine biosynthesis for tRNA maturation.
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on