| Description | Striated fibre assemblin (SFA), an acidic 33kDa protein, is the major component of striated microtubule-associated fibres (SMAFs) in the flagellar basal apparatus of green flagellates. In Chlamydomonas, and other green flagellates, the SMAFs form a cross-like pattern and run alongside the proximal parts of four bundles of flagellar root microtubules.The sequence of SFA contains two structurally distinct domains [ ]. The head domain, with ~30 residues, contains all the prolines (3-8 depending on species) and is rich in hydroxyamino acids. This non-helical domain is further characterised by the presence of repetitive SP-motifs, some of them in the context SP(M/T)R, which is a putative substrate for p34-CDC2 kinase. The rod domain, with ~250 residues, is predicted to be mostly α-helical (the α-helix content was estimated to be 76% for the entire molecule or 85% for the postulated rod domain). This domain shows a pronounced coiled-coil-forming ability and contains a 29-residue repeat pattern based on four heptads, followed by a skip residue. The rod domains of SF-assemblin and beta-giardin from protozoan Giardia have the same length and display 42% sequence similarity [, ]. | Name | SF-assemblin/beta-giardin |
| Short Name | SF_assemblin/giardin_b | Type | Family |
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