Protein Domain : IPR005709

Type:  Family Name:  Ribosomal protein S4, bacterial-type
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 S4, is one of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. This entry consists of organelle (chloroplast and mitochondrial) ribosomal protein S4 as well as bacterial ribosomal protein S4. Short Name:  Ribosomal_S4_bac-type

0 Child Features

3 Contains

DB identifier Type Name
IPR002942 Domain RNA-binding S4 domain
IPR001912 Domain Ribosomal protein S4/S9, N-terminal
IPR018079 Conserved_site Ribosomal protein S4, conserved site

2 Cross Referencess

Identifier
TIGR01017
MF_01306_B

0 Found In

3 GO Annotations

GO Term Gene Name
GO:0003735 IPR005709
GO:0006412 IPR005709
GO:0015935 IPR005709

3 Ontology Annotations

GO Term Gene Name
GO:0003735 IPR005709
GO:0006412 IPR005709
GO:0015935 IPR005709

1 Parent Features

DB identifier Type Name
IPR022801 Family Ribosomal protein S4/S9

182 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
ATCG00380.1 P56799 PAC:19637985 Arabidopsis thaliana 201  
Thecc1EG046386t1 PAC:27459546 Theobroma cacao 201  
Migut.D01426.1.p PAC:28927742 Mimulus guttatus 201  
Araha.11756s0185.1.p PAC:28856679 Arabidopsis halleri 206  
Glyma.01G153400.1.p K7K414 PAC:30543703 Glycine max 185  
Medtr4g051220.1 G7ZW80 PAC:31113463 Medicago truncatula 201  
Medtr0002s0590.1 A0A072TLH3 PAC:31084740 Medicago truncatula 336  
Bradi2g13108.1.p B3TN53 PAC:32771538 Brachypodium distachyon 201  
Aqcoe2G188200.1.p PAC:33058197 Aquilegia coerulea 199  
LOC_Os10g38214.1 PAC:33100767 Oryza sativa 201  
LOC_Os04g16764.1 PAC:33112958 Oryza sativa 201  
LOC_Os04g16738.1 PAC:33112702 Oryza sativa 201  
Brdisv20Bd21Ref1016420m.p B3TN53 PAC:33434658 Brachypodium distachyon Bd21 AnntCtrl 201  
Brdisv1pangenome1000697m.p PAC:33659096 Brachypodium distachyon Pangenome 216  
Brdisv1pangenome1000668m.p PAC:33624182 Brachypodium distachyon Pangenome 206  
Brdisv1pangenome1000769m.p PAC:33599072 Brachypodium distachyon Pangenome 187  
Brdisv1pangenome1006552m.p PAC:33657258 Brachypodium distachyon Pangenome 163  
Brdisv1pangenome1010824m.p PAC:33621948 Brachypodium distachyon Pangenome 206  
Brdisv1pangenome1011453m.p PAC:33658425 Brachypodium distachyon Pangenome 170  
Brdisv1pangenome1013115m.p PAC:33623843 Brachypodium distachyon Pangenome 197  
Brdisv1pangenome1029688m.p B3TN53 PAC:33617196 Brachypodium distachyon Pangenome 201  
Brdisv1ABR21046546m.p B3TN53 PAC:33750196 Brachypodium distachyon ABR2 201  
Brdisv1Bis-11045397m.p B3TN53 PAC:33769921 Brachypodium distachyon Bis-1 201  
Brdisv1ABR31046628m.p B3TN53 PAC:34006133 Brachypodium distachyon ABR3 201  
Brdisv1BdTR1i1046993m.p B3TN53 PAC:34071520 Brachypodium distachyon BdTR1i 201  
Brdisv1BdTR8i1006379m.p PAC:34214941 Brachypodium distachyon BdTR8i 177  
Brdisv1BdTR12c1040010m.p PAC:34403996 Brachypodium distachyon BdTR12c 197  
Brdisv1ABR81005661m.p PAC:34577442 Brachypodium distachyon ABR8 216  
Brdisv1BdTR11G1006545m.p PAC:34615600 Brachypodium distachyon BdTR11g 177  
Brdisv1Mig31046398m.p B3TN53 PAC:35520256 Brachypodium distachyon Mig3 201  

3 Publications

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