SMART: Pfam domain SF-assemblin

SF-assemblin

PFAM accession number:	PF06705
Interpro abstract (IPR008374):	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 [ (PUBMED:8491776) ]. 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 alpha- helical (the alpha-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 [ (PUBMED:8491776) (PUBMED:19214572) ].
GO function:	structural constituent of cytoskeleton (GO:0005200)

PFAM accession number:

PF06705

Interpro abstract (IPR008374):

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 [ (PUBMED:8491776) ]. 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 alpha- helical (the alpha-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 [ (PUBMED:8491776) (PUBMED:19214572) ].

GO function:

structural constituent of cytoskeleton (GO:0005200)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SF-assemblin