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"3D models of yeast RNase P/MRP proteins Rpp1p and Pop3p." |
Dlakic M |
Published 2005-01-01 in RNA volume 11 .
Pubmed ID: 15613537
| 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. |
This publication refers to the following RNApathwaysDB entries:
Proteins
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