Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message

IPR018496

Description

IPR018496 is a Pseudouridine synthase, RsuA/RluB/E/F, conserved site.

<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> <p>This entry represents several different pseudouridine synthases from family 3, including: RsuA (acts on small ribosomal subunit), RluB, RluE and RluF (act on large ribosomal subunit).</p>

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 , while the GO metadata was last updated on .

GO term Namespace Name Definition Relationships
Biological process Pseudouridine synthesis The intramolecular conversion of uridine to pseudouridine within an RNA molecule. This posttranscriptional base modification occurs in tRNA, rRNA, and snRNAs.
Molecular function RNA binding Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
Biological process RNA modification The covalent alteration of one or more nucleotides within an RNA molecule to produce an RNA molecule with a sequence that differs from that coded genetically.
Molecular function Intramolecular transferase activity Catalysis of the transfer of a functional group from one position to another within a single molecule.

Associated Lotus transcripts 3

Transcript Name Description Predicted domains Domain count
Pseudouridine synthase family protein isoform 2, partial [Theobroma cacao] gi|508726877|gb|EOY18774.1| 22
Pseudouridine synthase family protein isoform 3 [Theobroma cacao] gi|508726878|gb|EOY18775.1| 22
Ribosomal large subunit pseudouridine synthase B; TAIR: AT2G39140.1 pseudouridine synthase family protein; Swiss-Prot: sp|P35159|RLUB_BACSU Ribosomal large subunit pseudouridine synthase B; TrEMBL-Plants: tr|A0A151SE04|A0A151SE04_CAJCA Ribosomal large subunit pseudouridine synthase B; Found in the gene: LotjaGi5g1v0270600 25

Co-occuring domains 1

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

Predicted domain Source Observations Saturation (%)
mobidb-lite MobiDBLite 1 33.33