| Primary Identifier | IPR025762 | Type | Domain |
| Short Name | DFDF |
| description | Sm and Sm-like proteins of the RNA-binding Lsm (like Sm) domain family arefound in all domains of life and are generally involved in important RNA-processing tasks. Lsm13-16 homologs share a domain organisation consisting ofa divergent N-terminal Lsm domain and a central or C-terminal consensus motifDFDF-x(7)-F closely preceded and followed by further phenylalanines andcharged aspartates/glutamates and arginines/lysines/histidines. The variableseven-residue tract of this consensus motif usually contains an asparagine atthe third or fourth position except of one sequence where the asparagine isreplaced by a glycine. In few other sequences, the DFDF box is replaced by aDYDF or EFDF box []. The DFDF domain is a heterodimerization domain, whichadopts a helical conformation upon binding. It folds into twoconsecutive alpha helices that are preceded and connected by the FDF and arelated 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 inLsm13-15, but not Lsm16, homologs succeed the DFDF-x(7)-F motif and are alsopredicted to be of helical nature [].This entry represents the DFDF domain. |
