Description

IPR020095 is a Pseudouridine synthase I, TruA, C-terminal.

<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 superfamily represents the Pseudouridine synthase I (TruA) C-terminal domain.</p> <p>TruA from Escherichia coli modifies positions uracil-38, U-39 and/or U-40 in tRNA [[cite:PUB00015686], [cite:PUB00042017]]. TruA contains one atom of zinc essential for its native conformation and tRNA recognition and has a strictly conserved aspartic acid that is likely to be involved in catalysis [[cite:PUB00000455]]. These enzymes are dimeric proteins that contain two positively charged, RNA-binding clefts along their surface. Each cleft contains a highly conserved aspartic acid located at its centre. The structural domains have a topological similarity to those of other RNA-binding proteins, though the mode of interaction with tRNA appears to be unique.</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 April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 18

Co-occuring domains 1

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