Short name: DFDF


Sm and Sm-like proteins of the RNA-binding Lsm (like Sm) domain family are found in all domains of life and are generally involved in important RNA- processing tasks. Lsm13-16 homologs share a domain organisation consisting of a divergent N-terminal Lsm domain and a central or C-terminal consensus motif DFDF-x(7)-F closely preceded and followed by further phenylalanines and charged aspartates/glutamates and arginines/lysines/histidines. The variable seven-residue tract of this consensus motif usually contains an asparagine at the third or fourth position except of one sequence where the asparagine is replaced by a glycine. In few other sequences, the DFDF box is replaced by a DYDF or EFDF box
. The DFDF domain is a heterodimerization domain, which adopts a helical conformation upon binding. It folds into two consecutive alpha helices that are preceded and connected by the FDF and a related FDK sequence
Two other strongly conserved FFD box and TFG box sequence motifs Y-x-K-x(3)- FFD-x-[IL]-S and [RKH]-x(2,5)-E-x(0-2)-[RK]-x(3,4)-[DE]-TFG contained in Lsm13-15, but not Lsm16, homologs succeed the DFDF-x(7)-F motif and are also predicted to be of helical nature
This entry represents the DFDF domain.
Contributing Member Database Entry


1.^Novel Sm-like proteins with long C-terminal tails and associated methyltransferases. Albrecht M, Lengauer T. FEBS Lett. 569, 18-26, (2004). View articlePMID: 15225602

2.^Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B. Tritschler F, Braun JE, Eulalio A, Truffault V, Izaurralde E, Weichenrieder O. Mol. Cell 33, 661-8, (2009). View articlePMID: 19285948

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