Pseudouridylate Synthase 10 (PUS10)

Pseudouridination, the isomerization of uridine to pseudouridine, is the most common posttranscriptional nucleotide modification found in RNA and is essential for biologic functions such as spliceosome biogenesis. Pseudouridylate synthases, such as PUS10, catalyze pseudouridination of structural RNAs, including transfer, ribosomal, and splicing RNAs. These enzymes also act as RNA chaperones, facilitating the correct folding and assembly of tRNAs.The deduced 529-amino acid protein contains an N-terminal accessory domain and a C-terminal catalytic domain. The accessory domain contains a THUMP domain involved in RNA binding and 4 cysteine residues that coordinate zinc. The catalytic domain contains 5 conserved pseudouridylate synthase motifs, including the putative catalytic residue asp344.