InterPro : IPR005998

Name  Ribosomal protein L7, eukaryotic Short Name  Ribosomal_L7_euk
Type  Family 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 [, ].Eukaryotic ribosomal protein, L7, contains an N-terminal bZIP DNA binding domain and a second, DNA-binding domain has been mapped to the 50 C-terminal amino acids of the protein []. In addition to its role in translation, L7 has also been shown to be involved in nuclear-receptor mediated transcriptional control. There is no bacterial homologue of this protein.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

3 Contains

Id Name Short Name Type
IPR016082 Ribosomal protein L30, ferredoxin-like fold domain Ribosomal_L30_ferredoxin-like Domain
IPR012988 Ribosomal protein L30, N-terminal Ribosomal_L30_N Domain
IPR018038 Ribosomal protein L30, conserved site Ribosomal_L30_CS Conserved_site

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0 Parent Features

4 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
von Mikecz A Human ribosomal protein L7 carries two nucleic acid-binding domains with distinct specificities. 1999 Biochem Biophys Res Commun 258 530-6



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)