InterPro : IPR002999

Name  Tudor domain Short Name  Tudor
Type  Domain Description  The drosophila tudor protein is encoded by a 'posterior group' gene,which when mutated disrupt normal abdominal segmentation and polecell formation. Another drosophila gene, homeless, is required forRNA localization during oogenesis. The tudor protein containsmultiple repeats of a domain which is also found in homeless [].The tudor domain is found in many proteins that colocalise withribonucleoprotein or single-strand DNA-associated complexes in thenucleus, in the mitochondrial membrane, or at kinetochores.It is not known whether the domain binds directly to RNA and ssDNA, orcontrols interactions with the nucleoprotein complexes. At least onetudor-containing protein, homeless, also contains a zinc fingertypical of RNA-binding proteins [].The resolution of the solution structure of the Tudor domain of human SMN revealed that the Tudor domain forms a strongly bent antiparallel beta-sheet with five strands forming a barrel-like fold. The structure exhibits a conserved negatively charged surface that interacts with the C-terminal Arg and Gly-rich tails of the spliceosomal Sm D1 and D3 proteins [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

1 Found In

Id Name Short Name Type
IPR016685 RNA-induced silencing complex, nuclease component Tudor-SN Silence_cplx_Nase-comp_TudorSN Family

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Ponting CP Tudor domains in proteins that interact with RNA. 1997 Trends Biochem Sci 22 51-2
Selenko P SMN tudor domain structure and its interaction with the Sm proteins. 2001 Nat Struct Biol 8 27-31



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)