InterPro : IPR009060

Name  UBA-like Short Name  UBA-like
Type  Domain Description  UBA domains are a commonly occurring sequence motif of approximately 45 amino acid residues that are found in diverse proteins involved in the ubiquitin/proteasome pathway, DNA excision-repair, and cell signalling via protein kinases []. HHR23A, the human homologue of yeast Rad23A is a nucleotide excision-repair protein that contains both an internal and a C-terminal UBA domain. The fold of the UBA domain consists of a compact three-helical bundle with a right-handed twist, andhave a conserved hydrophobic surface patch for protein-protein interactions. UBA-like domains can be found in other proteins as well, such as the TS-N domain in the elongation factor Ts (EF-Ts), which catalyses the recycling of the GTPase EF-Tu required for the binding of aminoacyl-tRNA top the ribosomal A site []; and the C-terminal domain of TAP/NXF1, which functions in nuclear export through the interaction of its UBA-like domain with FG nucleoporins [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



3 Child Features

Id Name Short Name Type
IPR005637 TAP C-terminal (TAP-C) domain TAP_C_dom Domain
IPR015228 Ubiquitin-associated Ubiq-assoc Domain
IPR015368 Ubiquitin-conjugating enzyme, C-terminal fungi UBA_C_fun Domain

3 Contains

Id Name Short Name Type
IPR003892 Ubiquitin system component Cue CUE Domain
IPR000449 Ubiquitin-associated domain/translation elongation factor EF-Ts, N-terminal UBA/Ts_N Domain
IPR018101 Translation elongation factor Ts, conserved site Transl_elong_Ts_CS Conserved_site

2 Found In

Id Name Short Name Type
IPR001816 Translation elongation factor EFTs/EF1B Transl_elong_EFTs/EF1B Family
IPR017346 Uncharacterised conserved protein UCP037991, UAS/UBX UCP037991_UAS/UBX Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Mueller TD Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions. 2002 J Mol Biol 319 1243-55
Wieden HJ Mechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu. Contribution of contacts at the guanine base. 2002 J Biol Chem 277 6032-6
Grant RP Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution. 2003 J Mol Biol 326 849-58

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)