3D models of yeast RNase P/MRP proteins Rpp1p and Pop3p.
Sensitive profile searches and fold recognition were used to predict the structures of two yeast RNase P/MRP proteins. Rpp1p, which is one of the subunits common to eukaryotes and archaea, is predicted to adopt the seven-stranded TIM-barrel fold found in PHP phosphoesterases. Pop3p, initially thought to be one of the RNase P/MRP subunits unique to yeast, has been assigned the L7Ae/L30e fold. This RNA-binding fold is also present in human RNase P subunit Rpp38, raising the possibility that Pop3p and Rpp38 are functional homologs.
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D000595:Amino Acid Sequence; D001324:Autoantigens / Q000737:chemistry; D003198:Computer Simulation; D004722:Endoribonucleases / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D021122:Protein Subunits; D043262:Ribonuclease P / Q000737:chemistry* / Q000235:genetics; D012260:Ribonucleases; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D001324:Autoantigens; D021122:Protein Subunits; D029701:Saccharomyces cerevisiae Proteins; D004722:Endoribonucleases; C497386:POP3 protein, S cerevisiae; D012260:Ribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; C108353:RPP1 protein, S cerevisiae; C104645:RPP38 protein, human; D043262:Ribonuclease P