Fig. 4: (a) Molecular structure of CpATFL1. The protein structure was built based on the ab initio approach from the QUARK server. The highlighted pink region represents the conserved critical amino acids for the activity of TFL1 as a repressor with a reference amino acid, Phe at the position 120, situated towards the bottom region. (b) Multiple sequence alignment of FT and TFL1 homologues in A. thaliana (ATH), Zea mays (ZCN), O. sativa (Os), B. distachyon and C. pallens. Sequences were aligned using the MUSCLE alignment tool. The level of conservation of amino acids is represented by the colour graph at the bottom of the alignment. Red represents stronger conservation while black represents variable amino acid sites. The red asterisk represents the critical amino acid change (Glu-> Gln) in CpATFL1 which may be responsible for its floral-promoting activity. (c) Codon usage between ZCN1, a TFL1 homologue in Z. mays, and CpATFL1. * represents the single nucleotide change coding for amino acid at position 150. (d) Electrostatic surface charge for ZCN8, ZCN1 and CpATFL1 . Electrostatic surface potential for each sequence was calculated from the CHARMM server. Protein structures were viewed using the pymol represented by the amino acid at position 150 and a reference amino acid, Phe, at position 120 to orient the structures.