Protein Family Models

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)

Date:

2024-10-16

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)

Date:

2024-10-16

RluA family pseudouridine synthase catalyzes the isomerization of specific uridines in rRNA or tRNA to pseudouridines

Date:

2017-10-02

In E. coli, RluD (SfhB) modifies uridine to pseudouridine at 23S RNA U1911, 1915, and 1917, RluC modifies 955, 2504 and 2580, and RluA modifies U746 and tRNA U32. An additional homolog from E. coli outside this family, TruC (SP|Q46918), modifies uracil-65 in transfer RNAs to pseudouridine.

Date:

2024-05-30