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S4 domain-containing protein
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. [1]. 10093218. Novel predicted RNA-binding domains associated with the translation machinery. Aravind L, Koonin EV;. J Mol Evol 1999;48:291-302. [2]. 9707415. 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. Davies C, Gerstner RB, Draper DE, Ramakrishnan V, White SW;. EMBO J 1998;17:4545-4558. (from Pfam)
Ribosomal protein S4/S9 N-terminal domain
This family includes small ribosomal subunit S9 from prokaryotes and S16 from metazoans. This domain is predicted to bind to ribosomal RNA [1]. This domain is composed of four helices in the known structure. However the domain is discontinuous in sequence and the alignment for this family contains only the first three helices. [1]. 9707415. 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. Davies C, Gerstner RB, Draper DE, Ramakrishnan V, White SW;. EMBO J 1998;17:4545-4558. (from Pfam)
ribosomal protein uS4 family protein
universal ribosomal protein uS4 family protein similar to Homo sapiens U3 small nucleolar ribonucleoprotein protein IMP3 that is required for the early cleavages during pre-18S ribosomal RNA processing
30S ribosomal protein S4
Primary rRNA binding protein; nucleates 30S assembly; involved in translational accuracy with proteins S5 and S12; interacts with protein S5; involved in autogeneously regulating ribosomal proteins by binding to pseudoknot structures in the polycistronic mRNA; interacts with transcription complex and functions similar to protein NusA in antitermination
This model finds organelle (chloroplast and mitochondrial) ribosomal protein S4 as well as bacterial ribosomal protein S4.
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