Protein Domain : IPR020069

Type:  Domain Name:  Ribosomal protein L9, C-terminal
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 L9 is one of the proteins from the large ribosomal subunit. In Escherichia coli, L9 is known to bind directly to the 23S rRNA. It belongs to a family of ribosomal proteins grouped on the basis of sequence similarities [].The crystal structure of Bacillus stearothermophilusL9 shows the 149-residue protein comprises two globular domains connected by a rigid linker []. Each domain contains an rRNA binding site, and the protein functions as astructural protein in the large subunit of the ribosome. The C-terminal domain consists of two loops, an alpha-helix and a three-stranded mixed parallel, anti-parallel beta-sheet packed against the central alpha-helix. The long central alpha-helix is exposed to solvent in the middle and participates in thehydrophobic cores of the two domains at both ends. Short Name:  Ribosomal_L9_C

0 Child Features

0 Contains

3 Cross Referencess

Identifier
PF03948
G3DSA:3.10.430.100
SSF55653

2 Found Ins

DB identifier Type Name
IPR020594 Family Ribosomal protein L9, bacteria/chloroplast
IPR000244 Family Ribosomal protein L9

0 GO Annotation

0 Ontology Annotations

0 Parent Features

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
447126 D8SWY0 PAC:15422955 Selaginella moellendorffii 230  
270732 D8RC52 PAC:15422510 Selaginella moellendorffii 194  
evm.model.supercontig_47.1 PAC:16420610 Carica papaya 196  
evm.model.supercontig_69.87 PAC:16424961 Carica papaya 219  
29700.m000768 B9S7H0 PAC:16806107 Ricinus communis 225  
29589.m001267 B9SCL1 PAC:16803308 Ricinus communis 210  
Cucsa.032260.1 PAC:16952424 Cucumis sativus 218  
Cucsa.197130.1 PAC:16968379 Cucumis sativus 188  
Cucsa.207500.2 A0A0A0LXN8 PAC:16969244 Cucumis sativus 198  
Cucsa.207500.3 A0A0A0LXN8 PAC:16969245 Cucumis sativus 198  
Cucsa.207500.5 PAC:16969247 Cucumis sativus 194  
Cucsa.207500.1 PAC:16969243 Cucumis sativus 246  
orange1.1g047111m A0A067DK69 PAC:18125361 Citrus sinensis 106  
orange1.1g027812m A0A067DHI3 PAC:18116741 Citrus sinensis 218  
orange1.1g038179m A0A067DDH9 PAC:18114980 Citrus sinensis 221  
orange1.1g033453m A0A067EYX8 PAC:18104303 Citrus sinensis 119  
orange1.1g031586m A0A067FAS6 PAC:18104302 Citrus sinensis 157  
orange1.1g033584m A0A067FA01 PAC:18104304 Citrus sinensis 116  
orange1.1g029171m A0A067F2G6 PAC:18104300 Citrus sinensis 198  
orange1.1g029153m A0A067F2G6 PAC:18104301 Citrus sinensis 198  
orange1.1g032091m A0A067EC40 PAC:18121076 Citrus sinensis 147  
AT5G53070.1 Q9LVU5 PAC:19666640 Arabidopsis thaliana 221  
AT3G44890.1 P25864 PAC:19663947 Arabidopsis thaliana 197  
Thhalv10023194m V4MDS2 PAC:20202432 Eutrema salsugineum 100  
Thhalv10014627m V4NBC1 PAC:20204934 Eutrema salsugineum 220  
Thhalv10002672m V4LCQ2 PAC:20196486 Eutrema salsugineum 197  
Thhalv10002671m V4LCQ2 PAC:20196487 Eutrema salsugineum 197  
Ciclev10029220m V4UEF5 PAC:20813783 Citrus clementina 227  
Ciclev10029219m V4UEF5 PAC:20813782 Citrus clementina 227  
Ciclev10022175m V4TQS8 PAC:20810372 Citrus clementina 218  

5 Publications

First Author Title Year Journal Volume Pages PubMed ID
            11297922
            11290319
            11114498
            8306963
            12051860