PROSITE documentation PDOC51336

DM10 domain profile

DM10 domains contain ~105 residues and are of unknown function. In both Chlamydomonas and mammals, this module has to date been identified in only two types of proteins. The first is the nm23-H7 class of nucleoside diphosphate kinase (NDK7) that consists of an N-terminal DM10 domain and two functional catalytic NDK modules (see <PDOC00409>). In Chlamydomonas, this protein (termed p40 is tightly associated with the flagellar axoneme. The second family of proteins containing DM10 domains is exemplified by Chlamydomonas Rib72, which consists of three repeated DM10 regions followed by a C-terminal domain containing two EF-hands that are predicted to bind Ca(2+) (see <PDOC00018>). The domain structure of mammalian Efhc1 is essentially identical to that of Chlamydomonas Rib72. Orthologous proteins are present in many other organisms that contain motile cilia including mouse, rat, Ciona, sea urchin, Leishmania, and trypanosomes. However, no obvious Rib72/Efhc1 relative has been identified in higher plants, or in the Caenorhabditis elegans genome, which encodes only one DM10 domain-containing protein. In Chlamydomonas and likely also mammals, DM10 domain-containing protein are tightly bound to the flagellar doublet microtubules. This suggests that DM10 domains might act as flagellar NDK regulatory modules or as units specifically involved in axonemal targeting or assembly [1].

DM10 domains are predicted to have the same organization of secondary structural elements; this includes seven β strands, with a short 3-4 residue helix after the first strand, and a more extended α helical region at the C-terminus [1].

The profile we developed covers the entire DM10 domain.