InterPro : IPR008991

Name  Translation protein SH3-like domain Short Name  Translation_prot_SH3-like
Type  Domain Description  The fundamental activity of the ribosome is two-fold: to decode the message of the mRNA in the small subunit, and to form a peptide bond between peptidyl-tRNA and aminoacyl-tRNA by a peptidyl transferase activity in the large subunit. Several prokaryotic and eukaryotic proteins that are involved in the translation process contain an SH3-like domain. The structure of the translation protein SH3-like domain is a partly opened beta barrel, where the last strand is interrupted by a 3-10 helical turn. The structure of the RNA-binding C-terminal domain of the Bacillus stearothermophilus(Geobacillus stearothermophilus) ribosomal protein L2 has been shown to adopt the SH3-like barrel topology []. The L2 protein is located near the peptidyl transferase centre in the large ribosomal subunit where it may contribute to peptidyl transferase activity, and is involved in the assembly of the 23SrRNA. Likewise, the N-terminal domain of the ubiquitous eukaryotic translation elongation factor 5a (IF5A) protein adopts the SH3-like barrel topology [, ]. IF5A, previously thought to be an initiation factor, is now considered to be involved in translation elongation []and in cell-cycle regulation. IF5A acts as a cofactor of the Rev protein in HIV-1-infected cells and of the Rex protein in T-cell leukaemia virus 1-infected cells.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



1 Child Features

Id Name Short Name Type
IPR022669 Ribosomal protein L2, C-terminal Ribosomal_L2_C Domain

8 Contains

Id Name Short Name Type
IPR005824 KOW KOW Domain
IPR014722 Ribosomal protein L2 domain 2 Rib_L2_dom2 Domain
IPR014726 Ribosomal protein L2, domain 3 Ribosomal_L2_dom3 Domain
IPR019769 Translation elongation factor, IF5A, hypusine site Trans_elong_IF5A_hypusine_site PTM
IPR005825 Ribosomal protein L24/L26, conserved site Ribosomal_L24/26_CS Conserved_site
IPR018259 Ribosomal protein L21e, conserved site Ribosomal_L21e_CS Conserved_site
IPR022671 Ribosomal protein L2, conserved site Ribosomal_L2_CS Conserved_site
IPR015869 Transcription antitermination protein, NusG, bacteria, conserved site Transcrpt_antiterm_NusG_bac_CS Conserved_site

11 Found In

Id Name Short Name Type
IPR002171 Ribosomal protein L2 Ribosomal_L2 Family
IPR005880 Ribosomal protein L2, bacterial/organellar-type Ribosomal_L2_bac/org-type Family
IPR003256 Ribosomal protein L24 Ribosomal_L24 Family
IPR001884 Translation elongation factor IF5A Transl_elong_IF5A Family
IPR001147 Ribosomal protein L21e Ribosomal_L21e Family
IPR010215 Transcription antitermination protein RfaH Transcription_antiterm_RfaH Family
IPR011768 Translation elongation factor P Transl_elongation_fac_P Family
IPR001062 Transcription antitermination protein, NusG Transcrpt_antiterm_NusG Family
IPR011590 Transcription elongation factor Spt5, archaeal Spt5_arc Family
IPR011897 Translation elongation factor P-like, YeiP Transl_elong_p-like_YeiP Family
IPR020599 Translation elongation factor P/YeiP Transl_elong_fac_P/YeiP Family

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Peat TS Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 A resolution. 1998 Structure 6 1207-14
Saini P Hypusine-containing protein eIF5A promotes translation elongation. 2009 Nature 459 118-21
Nakagawa A The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome. 1999 EMBO J 18 1459-67
Kim KK Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 A resolution. 1998 Proc Natl Acad Sci U S A 95 10419-24

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)