F-type lectins - sequence alignment
Regions of secondary structure are indicated above the alignment and coloured to correspond with the structure of AAA, left. 310 helices (a1-a4) are highlighted in red. Beta-strands in the large beta-sheet (b2-4, 6, 7, 9, 10) are highlighted in blue and those in the small beta-sheet (b5, 8, 11) in yellow. The loops which encircle the ligand-binding site (1-5) are highlighted in grey. Cysteine residues are highlighted in yellow with the disulphide pairings (1-3) indicated above the alignment. Selected residues that are conserved in all or nearly all F-type domains are highlighted in green where identical and in cyan where the character of the residue is preserved. Residues contributing main chain or side chain oxygen atoms to coordinate Ca2+ in AAA and SP2159, and the conserved equivalents in other proteins, are highlighted in orange. Residues involved in fucose binding in AAA and SP2159, and the conserved equivalents in other proteins, are highlighted in magenta (hydrogen bonds to the ring hydroxyl groups or ring oxygen) and pink (forming the hydrophobic pocket binding the methyl group). Individual F-type domains within a single polypeptide are indicated a, b, c etc.
- Vertebrates
- Anguilla anguilla (AA) Agglutinin Q7SIC1 Morone saxatilis (MS) FBP32 Q2LK81 FBP32II Q2LK88 Oncorhynchus mykiss (OM) FBPL4 Q2LK91 Fundulus heteroclitus (FH) fucolectin Q654Q0 Xenopus laevis (XL) PXN-FBPL Q2LK77 (domain e = PXN1 P49263) II-FBPL Q2LK76 X-epilectin Q64GD1 Monodelphis domestica (MD) 24867 17963
- Invertebrates
- Strongylocentrotus pupuratus (SP) CRL Q6RSH4 788755 XP_788755 783458 XP_783458 Drosophila melanogaster (DM) furrowed P91658 CG9095 Q9VXX7 Caenorhabditis elegans (CE) C54G4.4 Q18849
- Prokaryotes
- Acidiphilium cryptum JF-5 (AC) Q2DD02 Streptococcus pneumoniae TIGR4 (SP) SP_2159 Q97N96 SP_0833 Q97RI2
- Saccharophagus degradans 2-40 (SD) Sde_3709 Q21EB5 Solibacter usitatus Ellin 6076 (SU) 6955 Q449Z0
- Gluconobacter oxydans 621H (GO) GOX0967 Q5FSA7 GOX0982 Q5FS92
Beta-strands in the three-stranded sheet are coloured yellow and those in the five-stranded sheet are coloured blue. 310 helices are coloured red. The fucose ligand is shown in purple and the Ca2+ ion in blue. Protein Data Bank structure ID: 1K12.
