This entry includes fission yeast ribonucleases P/MRP protein subunit Pop7 and its homologue, Rpp20, from animals. Pop7/Rpp20 is a component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. They are also a component of RNase MRP complex, which cleaves pre-rRNA sequences [, ].
This entry represents the beta-α-β-α-β-beta fold found in Alba proteins, which are archaeal and eukaryotic DNA- or RNA-bindingproteins involved in RNA metabolism and have the function of a chromosomal protein in some archaea. This fold is similar to the folds of DNase I and the C-terminaldomain of the translation initiation factor IF3. This fold can also be found in eukaryotic RNase P/RNase MRP components Pop6 and Pop7 [].
Subunit Pop7 is a component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. It is also a component of RNase MRP, which cleaves pre-rRNA sequences [, ]. In yeasts, RNase P consists of an RNA moiety and at least 9 protein subunits including Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rpp1 and Rpp2. The RNase MRP complex consists of an RNA moiety and at least 10 protein subunits including Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rmp1, Rpp1 and Snm1, many of which are shared with the RNase P complex.
