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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)
pseudouridine synthase
Members of this family are involved in modifying bases in RNA molecules. They carry out the conversion of uracil bases to pseudouridine. This family includes RluD Swiss:P33643, a pseudouridylate synthase that converts specific uracils to pseudouridine in 23S rRNA. RluA from E. coli converts bases in both rRNA and tRNA [1]. [1]. 7493321. A dual-specificity pseudouridine synthase: an Escherichia coli synthase purified and cloned on the basis of its specificity for psi 746 in 23S RNA is also specific for psi 32 in tRNA(phe). Wrzesinski J, Nurse K, Bakin A, Lane BG, Ofengand J;. RNA 1995;1:437-448. (from Pfam)
16S rRNA pseudouridine(516) synthase
16S rRNA pseudouridine(516) synthase catalyzes the formation of pseudouridine at position 516 in 16S rRNA during assembly of the 30S ribosomal subunit
This HMM identifies panels of pseudouridine synthase enzymes that RNA modifications involved in maturing the protein translation apparatus. Counts per genome vary: two in Staphylococcus aureus, three in Pseudomonas putida, four in E. coli, etc.
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