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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)
SAM-dependent methyltransferase
This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesised that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping [2]. [1]. 10983982. RNA methylation under heat shock control. Bugl H, Fauman EB, Staker BL, Zheng F, Kushner SR, Saper MA,. Bardwell JC, Jakob U;. Mol Cell 2000;6:349-360.. [2]. 8385698. Computer-assisted identification of a putative methyltransferase. domain in NS5 protein of flaviviruses and lambda 2 protein of. reovirus.. Koonin EV;. J Gen Virol 1993;74:733-740. (from Pfam)
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