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InterPro: IPR002999 Tudor domain
Protein matches
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UniProtKB Matches: 798 proteins |
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Accession
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IPR002999 Tudor |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR018351 Tudor subgroup
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Found in
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IPR008191 Maternal tudor protein
IPR016685 RNA-induced silencing complex, nuclease component Tudor-SN
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Contains
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IPR019023 Lamin-B receptor of TUDOR domain
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GO Term annotation
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Function
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GO:0003676 nucleic acid binding
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InterPro annotation
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Entry Details in BioMart
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Abstract
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The drosophila tudor protein is encoded by a 'posterior group' gene,
which when mutated disrupt normal abdominal segmentation and pole
cell formation. Another drosophila gene, homeless, is required for
RNA localization during oogenesis. The tudor protein contains
multiple repeats of a domain which is also found in homeless [1].
The tudor domain is found in many proteins that colocalise with
ribonucleoprotein or single-strand DNA-associated complexes in the
nucleus, in the mitochondrial membrane, or at kinetochores.
It is not known whether the domain binds directly to RNA and ssDNA, or
controls interactions with the nucleoprotein complexes. At least one
tudor-containing protein, homeless, also contains a zinc finger
typical of RNA-binding proteins [1].
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 [2].
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Structural links
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Database links
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Interactions
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This domain has been experimentally proven to be involved in Protein:Protein interactions. Representative
data is shown with the following
example proteins:
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Example proteins
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A8MW92 Tudor domain-containing protein PHF20L1
O04716 DNA mismatch repair protein Msh6-1
P10383 Protein ovarian tumor locus
P34344 Putative protein tag-250
Q02395 Metal-response element-binding transcription factor 2
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR019786 |
Zinc finger, PHD-type, conserved site |
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| IPR019787 |
Zinc finger, PHD-finger |
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| IPR000432 |
DNA mismatch repair protein MutS, C-terminal |
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| IPR011011 |
Zinc finger, FYVE/PHD-type |
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| IPR015536 |
DNA mismatch repair protein MutS-homologue MSH6 |
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| IPR016151 |
DNA mismatch repair protein MutS, N-terminal |
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| IPR007861 |
DNA mismatch repair protein MutS, clamp |
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| IPR007860 |
DNA mismatch repair protein MutS, connector |
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| IPR007696 |
DNA mismatch repair protein MutS, core |
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| IPR007695 |
DNA mismatch repair protein MutS-like, N-terminal |
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| IPR002999 |
Tudor domain |
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| IPR017261 |
DNA mismatch repair protein Msh6 |
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| IPR008191 |
Maternal tudor protein |
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| IPR001965 |
Zinc finger, PHD-type |
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| IPR003323 |
Ovarian tumour, otubain |
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| IPR018351 |
Tudor subgroup |
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| IPR014002 |
Tudor-like, plant |
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PDB Chain |
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ModBase |
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SWISS-MODEL |
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Additional Reading
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Lee J, Thompson JR, Botuyan MV, Mer G.
Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor.
Nat. Struct. Mol. Biol. 15 2008 109-11
[PubMed: 18084306]
http://dx.doi.org/10.1038/nsmb1326
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Huang Y, Fang J, Bedford MT, Zhang Y, Xu RM.
Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A.
Science 312 2006 748-51
[PubMed: 16601153]
http://dx.doi.org/10.1126/science.1125162
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Sprangers R, Groves MR, Sinning I, Sattler M.
High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues.
J. Mol. Biol. 327 2003 507-20
[PubMed: 12628254]
http://dx.doi.org/10.1016/S0022-2836(03)00148-7
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Narayanan U, Achsel T, Luhrmann R, Matera AG.
Coupled in vitro import of U snRNPs and SMN, the spinal muscular atrophy protein.
Mol. Cell 16 2004 223-34
[PubMed: 15494309]
http://dx.doi.org/10.1016/j.molcel.2004.09.024
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InterPro 24.0
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