The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modificatio ...
The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was detected also in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in the regulation of the expression of other genes [1]. It is predicted that the PUA domain is an RNA binding domain.
This domain is found at the C-terminal end of Protein SHQ1 homolog from humans and similar eukaryotic proteins. SHQ1 is a factor required for the biogenesis and assembly of H/ACA small nucleolar ribonucleoparticle (snoRNP), which are essential for ri ...
This domain is found at the C-terminal end of Protein SHQ1 homolog from humans and similar eukaryotic proteins. SHQ1 is a factor required for the biogenesis and assembly of H/ACA small nucleolar ribonucleoparticle (snoRNP), which are essential for ribosomal RNA and telomerase RNA processing and metabolism. This protein contains two domains: an N-terminal CS or HSP20-like domain (Pfam:PF21413) and a C-terminal region called the Shq1 domain (this entry). This domain adopts a mostly helical structure that consists of 17 alpha-helices and two short beta-strands [1,2].