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Supporting Information Legends Figure S1. Rice flo6 mutant showed slightly shorter than wild type. (a) Comparison of wild type and flo6 mutant plants after heading. (b) Comparison of height between wild-type and flo6 mutant plants. Values are means ± SD (n=25). The asterisk indicates statistical significance between the wild type and mutants by Student’s t-test (**P < 0.01). Figure S2. Altered gelatinization properties in flo6 mutant seeds. (a) Starch of flo6 mutant seeds is hard to gelatinize in urea solutions. Starch powder was mixed with urea solutions of various concentrations (1 – 9 M). (b) The most significant difference was observed for 5 M urea. (c) The swollen volume of wild-type and flo6 starch in urea solutions of various concentrations (1 – 9 M). Figure S3. The plastid localization of FLO6 is critical for its function. (a) Functional complementation of the flo6 mutant using FLO6-GFP and GFP-FLO6, respectively. (b) Fluorescence micrographs of young leaves from transgenic lines expressing FLO6-GFP and GFP-FLO6. Bars = 10 μm. Figure S4. Multiple sequence alignment of CBM48-containing proteins. Protein alignment of starch-binding domains of FLO6 and other proteins. Conserved residues involved in binding are marked with asterisks. Figure S5. Yeast two-hybrid interactions between FLO6 and starch synthesis enzymes. The full-size FLO6 cDNA was fused with a DNA binding domain construct (BD), and starch synthesis enzymes were fused with an activation domain construct (AD). AGPL1, AGPL2, AGPL4 indicate ADP glucose pyrophosphorylase large subunit, respectively; BEI, BEIIb indicate branching enzyme I and IIb, respectively; PHOL indicates plastidial phosphorylase; PUL indicates pullulanase; GBSS indicates granule-bound starch synthase I; SSIIa indicates soluble starch synthase IIa; ISA1, ISA2 indicates corresponding isoamylase isozymes. The transformants were grown on DDO (SD/-Leu-Trp) and QDO (SD/-Leu-Trp-His-Ade/X-α-gal) medium.