Supplementary Fig. 1. Nucleotide sequence alignment of BnPAP12 family members and AtPAP12. The start codon ATG and the stop codon are in bold face and solid-underlined, the putative polyadenylation signals are in italics and wave-underlined, and the introns are dash-underlined, while unspliced introns within BnPAP12-4, BnPAP12-5 and BnPAP12-7 are double-underlined. Two TSDsequences, left and right TIR sequences withinRepeater and the following four tandemrepeatsof BnPAP12-4 and BnPAP12-6 are also marked according to SupplementaryFig. 2A. Identical bases are in yellow background, with block similar bases in blue background and non-similar bases in no background.

SupplementaryFig. 2. (A) Alignment ofRepeater and the following four tandemrepeats of BnPAP12-4 with AtPAP12 and BnPAP12-1. The Repeater sequence in BnPAP12-4 is dash-underlined. The 10-bp left and right TIR sequences are solid-underlined.The 3-bp TSD sequence TAA is in italic bald face.(B) Multi-alignment of the 5' UTRs of BnPAP12 family members and AtPAP12. Purine-stretch in the 5' UTRs of BnPAP12 family is marked. CDS indicates coding sequence after the start codon ATG. (C) Alternative polyadenylation sites (pointed by filled triangles) and putative polyadenylation signals (PS1~PS3) of BnPAP12-2 and BnPAP12-7. Identical bases are in reverse display, with block similar bases in gray background and non-similar bases in no background.

SupplementaryFig. 3. Multi-alignment of deduced BnPAP12 proteins and AtPAP12. In the consensus line, the predicted conserved metallophos domain between Y212~Y411 is dash-underlined, the predicted 28-aa signal peptide/anchor from M1 to G28 is in bold face and solid-underlined, five motifs of conserved amino acid sequences (GDLG/GDLSY/GNHE/VLVH/GHVH) are in gray background, those conserved metal-coordinating residues D219, Y251, N285, H370, H407 and H409(D168, Y200, N234, H319, H356 and H358 in BnPAP12-1), as well as the bridging aspartate residue D248(D197 in BnPAP12-1) and the cysteine residue C429(C378 in BnPAP12-1) are in gray background and boxed.

Supplementary Fig. 4. Distribution of predicted secondary structures of seven members of BnPAP12 family. Numbers 50, 100, 150, 200 and 250 are counts of amino acids of each protein.α-helix, extended strand, β-turn and random coil are denoted as the longest, middle long, short and the shortest vertical bars respectively.






Supplementary Fig. 1


Supplementary Fig. 2


Supplementary Fig. 3

BnPAP12-1

BnPAP12-2

BnPAP12-3

BnPAP12-4

BnPAP12-5

BnPAP12-6

BnPAP12-7

Supplementary Fig. 4

1