LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Domain |
| Description | 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 motifDFDF-x(7)-F closely preceded and followed by further phenylalanines and charged aspartates/glutamates and arginines/lysines/histidines. The variableseven-residue tract of this consensus motif usually contains an asparagine at the 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 a DYDF or EFDF box []. The DFDF domain is a heterodimerization domain, whichadopts a helical conformation upon binding. It folds into two consecutive 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 also predicted to be of helical nature [].This entry represents the DFDF domain. |
| Short Name | DFDF |
