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- Sequence alignment of Fbs-type F-box
associated domains in F-box proteins. The domain is also found in
some polypeptides
without F-boxes, but such domains are not included in the alignment.
Proteins containing an F-box together with an Fbs-type F-box associated
domain are found in a range of vertebrates. Although elements of the
glycosylation and protein targeting machinery are conserved in lower eukaryotes, the F-box associated domain is not present in proteins
from yeast, slime mold or fruit fly. Surprisingly, one protein with
an F-box domain in the relevant architectural context is present in the
invertebrate C elegans. Included in the alignment are all
human and murine proteins, plus a selection of other vertebrate proteins
and the example from C elegans.
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- Regions of secondary structure are
indicated above the alignment and coloured to correspond with the
structure of murine Fbs1/Fbx2, left. Alpha-helices (a1,2) are
highlighted in red,
beta-strands in one beta-sheet (b1,4,6,7,9) in
yellow, and
beta-strands in the opposite beta-sheet (b2,3,5,8,10) in
blue. Residues that are identical in over 75% of
the aligned sequences are highlighted in
green. Residues
that are similar in over 75% of the sequences are highlighted
in cyan. Residues which
interact with chitobiose in the Fbs1 structure are highlighted in
magenta. The
equivalent residues in other proteins are highlighted in
magenta if identical and in
pink if the character of
the residue is conserved.
- Accession numbers
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- Fbx2 (Fbs1): human
Q9UK22
Q5TGY0, mouse
Q80UW2, X tropicalis
17406, G gallus
04657.
- Fbx6b (Fbs2): human
Q9NRD1, mouse
Q9QZN4.
- Fbx17 (Fbx26 Fbg4): human
Q96EF6, mouse
Q9QZM8, X tropicalis
05327
- Fbx27 (Fbg5): human
Q8NI29, mouse
Q6DIA9.
- Fbx44 (Fbx30 Fbx6a Fbg3): human
Q9H4M3, mouse
Q8BK26, X tropicalis
27482,
25469 (novel), G gallus
04646.
- Fugu
153187; Tetraodon
Q4S5T2; C elegans C14B1.3
Q17962.
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- If alignments appear scrambled, please
maximise the width of your browser window.
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