InterPro : IPR002171

Name  Ribosomal protein L2 Short Name  Ribosomal_L2
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 leastin 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 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 [], groups:Eubacterial L2.Algal and plant chloroplast L2.Cyanelle L2.Archaebacterial L2.Plant L2.Slime mold L2.Marchantia polymorphamitochondrial L2.Paramecium tetraureliamitochondrial L2.Fission yeast K5, K37 and KD4.Yeast YL6.Vertebrate L8.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

2 Child Features

Id Name Short Name Type
IPR005880 Ribosomal protein L2, bacterial/organellar-type Ribosomal_L2_bac/org-type Family
IPR023672 Ribosomal protein L2, archaeal-type Ribosomal_L2_arc Family

7 Contains

Id Name Short Name Type
IPR012340 Nucleic acid-binding, OB-fold NA-bd_OB-fold Domain
IPR008991 Translation protein SH3-like domain Translation_prot_SH3-like Domain
IPR022669 Ribosomal protein L2, C-terminal Ribosomal_L2_C Domain
IPR022666 Ribosomal Proteins L2, RNA binding domain Rbsml_prot_L2_RNA-bd_dom Domain
IPR014722 Ribosomal protein L2 domain 2 Rib_L2_dom2 Domain
IPR014726 Ribosomal protein L2, domain 3 Ribosomal_L2_dom3 Domain
IPR022671 Ribosomal protein L2, conserved site Ribosomal_L2_CS Conserved_site

0 Found In

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
Marty I cDNA nucleotide sequence and expression of a tobacco cytoplasmic ribosomal protein L2 gene. 1992 Nucleic Acids Res 20 1517-22



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)