Description

IPR001854 is a Large ribosomal subunit protein uL29.

<p>This family includes ribosomal proteins, which constitute the uL29 family [[cite:PUB00080279]]. These were previously known as L29 from eubacteria and archaea and L35 from eukaryotes.</p> <p>Ribosomal protein uL29 is one of the proteins from the large ribosomal subunit. uL29 belongs to a family of ribosomal proteins of 63 to 138 amino-acid residues which, on the basis of sequence similarities, groups: </p> <ul> <li>Red algal uL29.</li> <li>Bacterial uL29.</li> <li>Mammalian uL29 (known as L35)</li> <li>Caenorhabditis elegans uL29 (known as L35) (ZK652.4).</li> <li>Yeast uL29 (known as L35).</li></ul> <p>uL29 is located on the surface of the large ribosomal subunit, where it participates in forming a protein ring that surrounds the polypeptide exit channel, providing structural support for the ribosome [[cite:PUB00079483]]. uL29 is involved in forming the translocon binding site, along with L19, L22, L23, L24, and L31e. In addition, uL29 and L23 form the interaction site for trigger factor (TF) on the ribosomal surface, adjacent to the exit tunnel [[cite:PUB00080476]]. uL29 forms numerous interactions with L23 and with the 23S rRNA.</p> <p>Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [[cite:PUB00007068], [cite:PUB00007069]]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits.</p> <p>Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [[cite:PUB00007069], [cite:PUB00007070]].</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 12

Co-occuring domains 1

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