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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)
tRNA synthetases class I (W and Y)
tyrosine--tRNA ligase
tyrosine--tRNA ligase catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr)
This HMM for tyrosine--tRNA ligase identifies proteins with a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples.
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