Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR015365 is a Elongation factor P, C-terminal.
<p>Elongation factor P (EF-P) stimulates the peptidyltransferase activity in the prokaryotic 70S ribosome. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF-P binds near the streptomycine binding site of the 16S rRNA in the 30S subunit. EF-P interacts with domains 2 and 5 of the 23S rRNA. The L16 ribosomal protein of the 50S or its N-terminal fragment are required for EF-P mediated peptide bond synthesis, whereas L11, L15, and L7/L12 are not required in this reaction, suggesting that EF-P may function at a different ribosomal site than most other translation factors. EF-P is essential for cell viability and is required for protein synthesis [[cite:PUB00081045], [cite:PUB00081046], [cite:PUB00033952], [cite:PUB00033951]]. EF-P is mainly present in bacteria. The EF-P homologs in archaea and eukaryotes are the initiation factors aIF5A and eIF5A, respectively. EF-P has 3 domains (domains I, II, and III). Domains II and III are S1-like domains. This entry includes domain III (the second S1 domain of EF_P). Domains II and III of have structural homology to the eIF5A domain C, suggesting that domains II and III evolved by duplication. These domains adopt an OB-fold, with five β-strands forming a β-barrel in a Greek-key topology [[cite:PUB00015919]].</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Cellular component | Cytoplasm | All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. | ||
| Biological process | Peptide biosynthetic process | The chemical reactions and pathways resulting in the formation of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. This may include the translation of a precursor protein and its subsequent processing into a functional peptide. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: elongation factor P-like [Cicer arietinum] gi|502104488|ref|XP_004492556.1| | 30 | ||
| – | Elongation factor P; TAIR: AT3G08740.1 elongation factor P (EF-P) family protein; Swiss-Prot: sp|Q54760|EFP_SYNE7 Elongation factor P; TrEMBL-Plants: tr|I3T3T8|I3T3T8_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0456600 | 31 | ||
| – | Elongation factor P; TAIR: AT4G26310.1 elongation factor P (EF-P) family protein; Swiss-Prot: sp|A4YTY9|EFP_BRASO Elongation factor P; TrEMBL-Plants: tr|A0A0L9T427|A0A0L9T427_PHAAN Uncharacterized protein; Found in the gene: LotjaGi6g1v0031100 | 22 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 33.33 |