Fig. 2.

Amino acid sequence alignment of CBM20s from human laforin and its taxonomically different orthologues. The CBM20 positions involved in starch binding sites 1 and 2 [1,22,45] are signified by numbers “1” and “2”, respectively, below the alignment. The individual residues are coloured as follows: Trp – yellow; Phe, Tyr – red; His – brown; Lys, Arg – cyan; Val, Leu, Ile – blue; Asp, Glu – green; Asp, Gln – dark yellow; Cys – magenta; Met - purple; Ala, Ser, Thr – gray; Gly, Pro – black. The green and red lanes above the alignment discriminate the borders of CBM20 segments (green) from two inserts (red) present in sequences from parasitic coccidia. For details concerning the studied sequences and their colouring scheme, please see Table 1. The individual laforins are marked by the binomial name of the organism preceded by the accession number from the UniProt database (except for the cnidarian Exaiptasia pallida preceded by the GenBank accession number). If there are more CBM20 copies in a single laforin sequence, there are digits “1” and eventually “2” following the accession number from the database. The order of the individual CBM20s is numbered from the CBM20, which directly precedes the catalytic DSP (without a number), toward the N-terminus.