LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Domain |
| Description | This entry represents the PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain found in 60S ribosome subunit biogenesis protein NIP7, some UPF0113 family members, such as KD93, and similar proteins found in eukaryotes and some archaeal species [ , , ]. PUA domains are predicted to bind RNA molecules with complex folded structures []. NIP7 is required for efficient 60S ribosome subunit biogenesis and has been shown to interact with another essential nucleolar protein, Nop8p, and the exosome subunit Rrp43p. These proteins are required for 60S subunit synthesis and may be part of a dynamic complex involved in this process. Nip7 orthologues share a two-domain architecture with the C-terminal PUA domain mediating interaction with RNA, suggesting that Nip7 is an adaptor protein with the C-terminal domain interacting with RNA targets and the N-terminal domain mediating interaction with protein targets. Structural analyses of the RNA-interacting surfaces of the orthologues from Saccharomyces cerevisiae and Pyrococcus abyssi Nip7 indicate that, in the archaeal PUA domain, C-terminal positively charged residues (arginines and lysines) are involved in RNA interaction while equivalent positions in eukaryotic orthologues are occupied by mostly hydrophobic residues. Both proteins can bind specifically to polyuridine, and RNA interaction requires specific residues of the PUA domain as determined by site-directed mutagenesis [ , , ]. |
| Short Name | UPF0113_PUA |
