| Ensembl ID | Symbol | Entrez ID | RBD | RBPome | PRI | Expresion | Pathway | Phenotype | Paralog | Ortholog | GO |
|---|---|---|---|---|---|---|---|---|---|---|---|
The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4, eukaryotic ribosomal S9, two families of pseudouridine synthases, a novel family of predicted RNA methylases, a yeast protein containing a pseudouridine synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterized, small proteins that may be involved in translation regulation [1]. The S4 domain probably mediates binding to RNA.
The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4, eukaryotic ribosomal S9, two families of pseudouridine synthases, a novel family of predicted RNA methylases, a yeast protein containing a pseudouridine synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterised, small proteins that may be involved in translation regulation [PUBMED:10093218]. The S4 domain probably mediates binding to RNA [PUBMED:9707415].
Aravind L, Koonin EV; , J Mol Evol 1999;48:291-302.: Novel predicted RNA-binding domains associated with the translation machinery. PUBMED:10093218 EPMC:10093218 .
Davies C, Gerstner RB, Draper DE, Ramakrishnan V, White SW; , EMBO J 1998;17:4545-4558.: The crystal structure of ribosomal protein S4 reveals a two-domain molecule with an extensive RNA-binding surface: one domain shows structural homology to the ETS DNA-binding motif. PUBMED:9707415 EPMC:9707415.
