Description

IPR014780 is a tRNA pseudouridine synthase II, TruB.

<p>This family represents TruB proteins found in the three domains of life which includes bacterial TruB, TruB1 from mammals and PUS4 from yeast. TruB is responsible for the pseudouridine residue present in the T loops of virtually all tRNAs. TruB recognises the preformed 3D structure of the T loop primarily through shape complementarity. It accesses its substrate uridyl residue by flipping out the nucleotide and disrupts the tertiary structure of tRNA [[cite:PUB00026665]].</p> <p>Saccharomyces cerevisiae tRNA pseudouridine synthase 4 (PUS4, also known as YNL292w), is the pseudouridine 55 synthase of both cytosolic and mitochondrial compartments, active at no other position on tRNA and the only enzyme active at that position in the species [[cite:PUB00114190]]. It also catalyses the pseudouridylation of mRNAs with the consensus sequence 5'-GGUUCRA-3' [[cite:PUB00100731]]. A distinct yeast protein centromere/microtubule-binding protein CBF5 (also known as YLR175w), is an rRNA pseudouridine synthase, and the archaeal set is much more similar to CBF5 than to PUS4 (see [interpro:IPR004802]). It is unclear whether the archaeal proteins found by this model are tRNA pseudouridine 55 synthases like TruB, rRNA pseudouridine synthases like CBF5, or (as suggested by the absence of paralogs in the Archaea) both. CBF5 likely has additional, eukaryotic-specific functions.</p> <p>Pseudouridine synthases catalyse the isomerisation of uridine to pseudouridine (Psi) in a variety of RNA molecules, and may function as RNA chaperones. Pseudouridine is the most abundant modified nucleotide found in all cellular RNAs. There are four distinct families of pseudouridine synthases that share no global sequence similarity, but which do share the same fold of their catalytic domain(s) and uracil-binding site and are descended from a common molecular ancestor. The catalytic domain consists of two subdomains, each of which has an α+β structure that has some similarity to the ferredoxin-like fold (note: some pseudouridine synthases contain additional domains). The active site is the most conserved structural region of the superfamily and is located between the two homologous domains. These families are [[cite:PUB00045922], [cite:PUB00092579]]:</p> <ul><li>Pseudouridine synthase I, TruA.</li> <li>Pseudouridine synthase II, TruB, which contains and additional C-terminal PUA domain.</li> <li>Pseudouridine synthase RsuA. RluB, RluE and RluF are also part of this family.</li> <li>Pseudouridine synthase RluA. TruC, RluC and RluD belong to this family.</li> <li>Pseudouridine synthase TruD, which has a natural circular permutation in the catalytic domain, as well as an insertion of a family-specific α+β subdomain.</li></ul>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 4

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: