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Protein Domain : IPR019972

Name  Ribosomal protein L14 conserved site Short Name  Ribosomal_L14_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 L14 is one of the proteins from the large ribosomal subunit.In eubacteria, L14 is known to bind directly to the 23S rRNA. It belongs to a family of ribosomal proteins, which have been grouped on the basis of sequence similarities []. Based on amino-acid sequence homology, it is predicted that ribosomal protein L14 is a member of a recently identified family of structurally related RNA-binding proteins []. L14 is a protein of 119 to 137 amino-acid residues.This entry represents a conserved region located in the C-terminal half of these proteins.

Publication Counts Displayer

0 Child Features

0 Contains

1 Cross References

Source . Name

Subject . Primary Identifier
PS00049 PROSITE IPR019972

2 Data Sets

Name URL
TrEMBL data set
InterPro data set  

3 Found In

DB identifier Name Short Name Type
IPR000218 Ribosomal protein L14b/L23e Ribosomal_L14b/L23e Family
IPR019971 Ribosomal protein L14P, archaeal Ribosomal_L14P_arc Family
IPR005745 Ribosomal protein L14, bacterial-type Ribosomal_L14_bac-type Family

0 GO Annotation

0 Ontology Annotations

0 Parent Features

11 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0071808 P48159 Drosophila melanogaster
FBpp0278667 Q28X51 Drosophila pseudoobscura
FBpp0169762 B4KSL0 Drosophila mojavensis
A8X815_CAEBR A8X815 Caenorhabditis briggsae
B4LMW0_DROVI B4LMW0 Drosophila virilis
H2WKB6_CAEJA H2WKB6 Caenorhabditis japonica
G0MPG5_CAEBE G0MPG5 Caenorhabditis brenneri
RL23_CAEEL P48158 Caenorhabditis elegans
A8E792_DROME A8E792 Drosophila melanogaster
B4P8L1_DROYA B4P8L1 Drosophila yakuba
E3LYX5_CAERE E3LYX5 Caenorhabditis remanei