Description

IPR031168 is a TrmE-type guanine nucleotide-binding domain.

<p>The P-loop guanosine triphosphatases (GTPases) control a multitude of biological processes, ranging from cell division, cell cycling, and signal transduction, to ribosome assembly and protein synthesis. GTPases exert their control by interchanging between an inactive GDP-bound state and an active GTP-bound state, thereby acting as molecular switches. The common denominator of GTPases is the highly conserved guanine nucleotide-binding (G) domain that is responsible for binding and hydrolysis of guanine nucleotides.</p> <p>TrmE (also called MnmE, ThdF or MSS1) contains a canonical G domain and is conserved in all three kingdoms of life. It is involved in the modification of uridine bases (U34) at the first anticodon (wobble) position of tRNAs decoding two-family box triplets. TrmE is organised as a multidomain protein consisting of an ~220-amino acid N-terminal domain, probably required for self-assembly, a middle GTPase domain, of about 160 residues, and an ~75-amino acid C-terminal domain, which contains a highly conserved CxGK motif. TrmE contains at least four of the five conserved nucleotide-binding motifs G1 (GxxxxGK[ST] or P- loop), G2 (T), G3 (DxxG) and G4 ([NT]KxD). The totally invariant alanine in the SA[KL] (G5) motif of Ras anGalph proteins is less well conserved [[cite:PUB00013952], [cite:PUB00074841], [cite:PUB00074842], [cite:PUB00038393], [cite:PUB00037510]].</p> <p>TrmE functions as a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance [[cite:PUB00081019]].</p> <p>This entry represents the TmrE-type G domain. The structure of the TrmE-type G domain consists of a a canonical Ras-like fold: central four-stranded β-sheet flanked by five α-helices. It dimerises in a potassium-dependent manner [[cite:PUB00038393], [cite:PUB00037510]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 3

Co-occuring domains 1

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