Source:http://linkedlifedata.com/resource/umls/id/C1514650
NCI: The REM repeat, which is also called rho effector or HR1 domain, was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal REM repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger. (pfam.wustl.edu/cgi-bin/getdesc?name=HR1)