| Primary Identifier | IPR008374 | Type | Family |
| Short Name | SF_assemblin/giardin_b |
| description | Striated fibre assemblin (SFA), an acidic 33kDa protein, is the majorcomponent of striated microtubule-associated fibres (SMAFs) in the flagellarbasal apparatus of green flagellates. In Chlamydomonas, and other greenflagellates, the SMAFs form a cross-like pattern and run alongside theproximal parts of four bundles of flagellar root microtubules.The sequence of SFA contains two structurally distinct domains []. Thehead domain, with ~30 residues, contains all the prolines (3-8 depending onspecies) and is rich in hydroxyamino acids. This non-helical domain isfurther characterised by the presence of repetitive SP-motifs, some of themin 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 alpha-helical (the α-helix content was estimated to be 76% for the entiremolecule or 85% for the postulated rod domain). This domain shows apronounced coiled-coil-forming ability and contains a 29-residue repeatpattern 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 [, ]. |
