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IPR003256

Description

IPR003256 is a Large ribosomal subunit protein uL24.

<p>Ribosomal protein uL24 is one of the proteins from the large ribosomal subunit. In their mature form, these proteins have 103 to 150 amino-acid residues.</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 , while the GO metadata was last updated on .

GO term Namespace Name Definition Relationships
Molecular function Structural constituent of ribosome The action of a molecule that contributes to the structural integrity of the ribosome.
Cellular component Ribosome An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.
Biological process Translation The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.

Associated Lotus transcripts 8

Transcript Name Description Predicted domains Domain count
PREDICTED: 50S ribosomal protein L24, chloroplastic-like [Cicer arietinum] gi|502083995|ref|XP_004487627.1| 21
PREDICTED: 50S ribosomal protein L24-like isoform X1 [Cicer arietinum] gi|502082834|ref|XP_004487287.1| 15
50S ribosomal protein L24; TAIR: AT5G23535.1 KOW domain-containing protein; Swiss-Prot: sp|Q47LK4|RL24_THEFY 50S ribosomal protein L24; TrEMBL-Plants: tr|I3S275|I3S275_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0516200 16
50S ribosomal protein L24; TAIR: AT5G23535.1 KOW domain-containing protein; Swiss-Prot: sp|Q47LK4|RL24_THEFY 50S ribosomal protein L24; TrEMBL-Plants: tr|I3S275|I3S275_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0516200 16
50S ribosomal L24-like protein; TAIR: AT5G54600.1 Translation protein SH3-like family protein; Swiss-Prot: sp|P11893|RK24_PEA 50S ribosomal protein L24, chloroplastic; TrEMBL-Plants: tr|C6T0A2|C6T0A2_SOYBN Putative uncharacterized protein; Found in the gene: LotjaGi3g1v0233600 22
50S ribosomal protein L24; TAIR: AT5G23535.1 KOW domain-containing protein; Swiss-Prot: sp|A9VP88|RL24_BACWK 50S ribosomal protein L24; TrEMBL-Plants: tr|I3S275|I3S275_LOTJA Uncharacterized protein; Found in the gene: LotjaGi5g1v0169700 16
50S ribosomal protein L24; TAIR: AT5G23535.1 KOW domain-containing protein; Swiss-Prot: sp|A9VP88|RL24_BACWK 50S ribosomal protein L24; TrEMBL-Plants: tr|I3S275|I3S275_LOTJA Uncharacterized protein; Found in the gene: LotjaGi5g1v0169700 16
50S ribosomal L24-like protein; TAIR: AT5G23535.1 KOW domain-containing protein; Swiss-Prot: sp|A9VP88|RL24_BACWK 50S ribosomal protein L24; TrEMBL-Plants: tr|I3S275|I3S275_LOTJA Uncharacterized protein; Found in the gene: LotjaGi5g1v0169700 16

Co-occuring domains 1

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

Predicted domain Source Observations Saturation (%)
cd06089 CDD 1 12.50