The Tudor domain is a domain of around 50-70 amino acids which was first
identified as a repeat present in 10 copies in Drosophila Tudor protein [1,2].
The Tudor domain is found in one or several copies in many eukaryotic proteins
that colocalize with ribonucleoprotein or single-stranded DNA-associated
complexes in the nucleus, in the mitochondrial membrane, or at kinetochores.
The Tudor domain can be found in association with other domains, such as a
staphylococcal nuclease (SN)-fold (see <PDOC00865>), a OTU domain (see
<PDOC50802>), a KH domain (see <PDOC50084>), a DEAD/DEAH box helicase domain
(see <PDOC00039>) or a coiled-coil domain. An insufficient amount of
functional information concerning the proteins containing a Tudor domain is
currently available from which to ascribe putative functions to Tudor domains.
However, it is likely that Tudor domains function as protein-protein
interaction motifs during RNA metabolism and/or transport and do not bind to
RNA directly [1,3,4].
The resolution of the solution structure of the Tudor domain of human SMN
revealed that the Tudor domain forms a strongly bent antiparallel β-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 .
Some proteins known to contain a Tudor domain are listed below:
Drosophila Tudor, a protein required during oogenesis for the formation of
primordial germ cells and for normal abdominal segmentation.
Drosophila Homeless (HLS), a protein belonging to the DE-H family of RNA-
dependent ATPases that is required for RNA localization during oogenesis.
HLS might function during the processing of pre-mRNA whose products direct
microtubules organization, which is required for mRNA transport.
Drosophila ovarian tumor protein (OTU). OTU is required at multiple stages
of oogenesis and the Tudor domain is required for its early function. A
portion of OTU cofractionates with mRNA/protein complexes (mRNPs) .
Mammalian survival of motor neuron protein (SMN). SMN participates in small
nuclear ribonucleoprotein (snRNP) particles assembly in the cytoplasm and
may also affect splicing more directly in the nucleus. In human, defects of
the SMN protein are associated with spinal muscular atrophy (SMA), a
disease in which the anterior horn cells in the spinal corn die, resulting
in progressive muscle weakness and ultimately, in some cases, in the
inability to breathe and swallow.
Human A-kinase anchor protein 1 (AKAP1). It binds to type I and II
regulatory subunits of protein kinase a and anchors them to the cytoplasmic
face of the mitochondrial outer membrane. An alternatively spliced version
of AKAP1 (S-AKAP84) participates in spermiogenesis, probably by
facilitating ordering of spermatid mitochondria.
Human p100, a nuclear protein that coactivates gene expression mediated by
the Epstein-Barr virus nuclear antigen 2 (EBNA-2). The p100 protein is also
able to bind single-stranded DNA.
Human Tudor and KH domain-containing protein (TDRKH) .
Rat Tudor repeat associator with PCTAIRE 2 (Trap). Trap contains five Tudor
domains and interacts with the N-terminal domain of PCTAIRE 1 and 2,
members of Cdk-related kinases which is highly expressed in the nervous
Caenorhabditis elegans hypothetical protein C56G2.1.
Rice Rp120, a protein that binds to a wide range of mRNAs expressed during
seed development and is associated with the cytoskeleton .
The profile we developed covers the entire Tudor domain.
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