The domain within your query sequence starts at position 177 and ends at position 298; the E-value for the Ribosomal_L2_C domain shown below is 1.32e-30.

AQEGDAHPLGALPVGTLINNVESEPGRGAQYIRAAGTCGVLLRKVNGTAIIQLPSKRQMQ
VLESCTATVGRVSNVNHNQRVIGKAGRNRWLGKRPNSGLWQRKGGWAGRKIRPLPPMKSY
VK

Ribosomal_L2_C

Ribosomal Proteins L2, C-terminal domain		 Ribosomal_L2_C
SMART accession number:SM01382
Description: -
Interpro abstract (IPR022669):

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 [ (PUBMED:11297922) (PUBMED:11290319) ]. 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.

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 [ (PUBMED:11290319) (PUBMED:11114498) ].

Ribosomal protein L2 is one of the proteins from the large ribosomal subunit. This entry represents the best conserved region located in the C-terminal section of these proteins.In Escherichia coli, L2 is known to bind to the 23S rRNA and to have peptidyltransferase activity. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities [ (PUBMED:1579444) ], groups:

  • Eubacterial L2.
  • Algal and plant chloroplast L2.
  • Cyanelle L2.
  • Archaebacterial L2.
  • Plant L2.
  • Slime mold L2.
  • Marchantia polymorpha mitochondrial L2.
  • Paramecium tetraurelia mitochondrial L2.
  • Fission yeast K5, K37 and KD4.
  • Yeast YL6.
  • Vertebrate L8.
GO process:translation (GO:0006412)
GO component:ribosome (GO:0005840)
GO function:structural constituent of ribosome (GO:0003735)
Family alignment:
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There are 22837 Ribosomal_L2_C domains in 22831 proteins in SMART's nrdb database.

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