Protein Domain : IPR019928

Type:  Family Name:  Ribosomal protein L3, archaeal
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 to bind 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 archaeal L3 proteins. Short Name:  Ribosomal_L3_arc
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0 Child Features

1 Contains

DB identifier Type Name
IPR019926 Conserved_site Ribosomal protein L3, conserved site

2 Cross Referencess

Identifier
TIGR03626
MF_01325_A

0 Found In

4 GO Annotations

GO Term Gene Name
GO:0003735 IPR019928
GO:0006412 IPR019928
GO:0005622 IPR019928
GO:0005840 IPR019928

4 Ontology Annotations

GO Term Gene Name
GO:0003735 IPR019928
GO:0006412 IPR019928
GO:0005622 IPR019928
GO:0005840 IPR019928

1 Parent Features

DB identifier Type Name
IPR000597 Family Ribosomal protein L3

12 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Glyma.10G223400.1.p I1LDE9 PAC:30476299 Glycine max 389  
Ca_04373 PAC:40147124 Cicer arietinum 389  
evm.model.AsparagusV1_10.1806 A0A5P1E3K9 PAC:40550225 Asparagus officinalis 367  
Dioal.4783s0001.1.p PAC:40936458 Dioscorea alata 389  
Dioal.4783s0001.2.p PAC:40936459 Dioscorea alata 389  
Glyma.10G223450.7.p I1LDE9 PAC:41104294 Glycine max 389  
GlysoPI483463.10G188600.1.p A0A445IR59 PAC:41216132 Glycine soja 389  
GlymaLee.10G189100.1.p I1LDE9 PAC:41258063 Glycine max Lee 389  
Pavir.1KG294000.2.p PAC:41620473 Panicum virgatum 372  
Dioal.10G046400.2.p PAC:43478387 Dioscorea alata 389  
Dioal.10G046400.1.p PAC:43478386 Dioscorea alata 389  
Pl07G0000092200.1.v1 PAC:44359245 Phaseolus lunatus 389  

6 Publications

First Author Title Year Journal Volume Pages PubMed ID
            11297922
            11290319
            11114498
            1597181
            1499563
            2406244