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InterPro: IPR002999 Tudor domain

Protein matchesHelp
UniProtKB
Matches:
798 proteins
AccessionHelp IPR002999 Tudor
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR018351 Tudor subgroup
Found in IPR008191 Maternal tudor protein
IPR016685 RNA-induced silencing complex, nuclease component Tudor-SN
Contains IPR019023 Lamin-B receptor of TUDOR domain
GO Term annotationHelp
Function GO:0003676 nucleic acid binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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].

Structural linksHelp
SCOP: b.34.9.1
CATH: 2.30.30.140
Database linksHelp
PROSITE doc: PDOC50304
Blocks: IPB002999
InteractionsHelp
This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002999 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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
IPR019787 Zinc finger, PHD-finger
IPR000432 DNA mismatch repair protein MutS, C-terminal
IPR011011 Zinc finger, FYVE/PHD-type
IPR015536 DNA mismatch repair protein MutS-homologue MSH6
IPR016151 DNA mismatch repair protein MutS, N-terminal
IPR007861 DNA mismatch repair protein MutS, clamp
IPR007860 DNA mismatch repair protein MutS, connector
IPR007696 DNA mismatch repair protein MutS, core
IPR007695 DNA mismatch repair protein MutS-like, N-terminal
IPR002999 Tudor domain
IPR017261 DNA mismatch repair protein Msh6
IPR008191 Maternal tudor protein
IPR001965 Zinc finger, PHD-type
IPR003323 Ovarian tumour, otubain
IPR018351 Tudor subgroup
IPR014002 Tudor-like, plant
PDB Chain
ModBase
SWISS-MODEL

PublicationsHelp
1. Ponting CP.
Tudor domains in proteins that interact with RNA.
Trends Biochem. Sci. 22 51-2 1997 [PubMed: 9048482]
http://dx.doi.org/10.1016/S0968-0004(96)30049-2
2. Selenko P, Sprangers R, Stier G, Buhler D, Fischer U, Sattler M.
SMN tudor domain structure and its interaction with the Sm proteins.
Nat. Struct. Biol. 8 27-31 2001 [PubMed: 11135666]
http://dx.doi.org/10.1038/83014

Additional ReadingHelp
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
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
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
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