InterPro : IPR019926

Name  Ribosomal protein L3, conserved site Short Name  Ribosomal_L3_CS
Type  Conserved_site Description  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 [, ]. 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 [, ].Ribosomal protein L3 is one of the proteins from the large ribosomal subunit. In Escherichia coli, L3 is known tobind to the 23S rRNA and may participate in the formation of the peptidyltransferase centre of the ribosome. Itbelongs to a family of ribosomal proteins which, on the basis of sequence similarities includes bacterial, red algal, cyanelle, mammalian, yeast and Arabidopsis thalianaL3 proteins; archaeal Haloarcula marismortuiHmaL3 (HL1), and yeast mitochondrial YmL9 [, , ].This entry represents a short conserved region located in the central section of ribosomal L3 proteins.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

4 Found In

Id Name Short Name Type
IPR009000 Translation protein, beta-barrel domain Transl_B-barrel Domain
IPR000597 Ribosomal protein L3 Ribosomal_L3 Family
IPR019927 Ribosomal protein L3, bacterial/organelle-type Ribosomal_L3_bac/org-type Family
IPR019928 Ribosomal protein L3, archaeal Ribosomal_L3_arc Family

0 Parent Features

6 Publications

First Author Title Year Journal Volume Pages
Ramakrishnan V Atomic structures at last: the ribosome in 2000. 2001 Curr Opin Struct Biol 11 144-54
Maguire BA The ribosome in focus. 2001 Cell 104 813-6
Chandra Sanyal S The end of the beginning: structural studies of ribosomal proteins. 2000 Curr Opin Struct Biol 10 633-6
Graack HR YmL9, a nucleus-encoded mitochondrial ribosomal protein of yeast, is homologous to L3 ribosomal proteins from all natural kingdoms and photosynthetic organelles. 1992 Eur J Biochem 206 373-80
Herwig S Primary structures of ribosomal proteins L3 and L4 from Bacillus stearothermophilus. 1992 Eur J Biochem 207 877-85
Arndt E Organization and nucleotide sequence of a gene cluster coding for eight ribosomal proteins in the archaebacterium Halobacterium marismortui. 1990 J Biol Chem 265 3034-9

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)