InterPro : IPR002942

Name  RNA-binding S4 domain Short Name  S4_RNA-bd
Type  Domain Description  The S4 domain is a small domain consisting of 60-65 amino acid residuesthat was detected in the bacterial ribosomal protein S4, eukaryoticribosomal S9, two families of pseudouridine synthases, a novel familyof predicted RNA methylases, a yeast protein containing a pseudouridinesynthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases,and a number of uncharacterised, small proteins that may be involved intranslation regulation []. The S4 domain probably mediates binding to RNA [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

1 Contains

Id Name Short Name Type
IPR018079 Ribosomal protein S4, conserved site Ribosomal_S4_CS Conserved_site

8 Found In

Id Name Short Name Type
IPR000876 Ribosomal protein S4e Ribosomal_S4e Family
IPR002307 Tyrosine-tRNA ligase Tyr-tRNA-ligase Family
IPR006225 Pseudouridine synthase, RluC/RluD PsdUridine_synth_RluC/D Family
IPR005710 Ribosomal protein S4/S9, eukaryotic/archaeal Ribosomal_S4/S9_euk/arc Family
IPR004538 Haemolysin A Haemolysin_A Family
IPR014330 RNA-binding S4-related,YaaA RNA-bd_S4-rel_YaaA Family
IPR017506 Photosystem II S4 PSII_S4 Family
IPR005709 Ribosomal protein S4, bacterial-type Ribosomal_S4_bac-type Family

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Davies C 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. 1998 EMBO J 17 4545-58
Aravind L Novel predicted RNA-binding domains associated with the translation machinery. 1999 J Mol Evol 48 291-302



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)