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Fig. 1. (A) Schematic diagram of the Hydra viridis HvAPX1 mRNA depicting
the region coding for the plant peroxidase domain and other putative
structural elements. UTR, untranslated region; SigP, ER signal peptide. (B)
Multiple amino acid sequence comparison of the plant peroxidase domain (amino
acids 48-229) of HvAPX1 with the plant ascorbate peroxidases from
Zantedischia aethiopica, AAC085761, (Magnoliaceae), Euglena
gracilis, BAC054841 (Euglenida), Galdieria partita, BAC411991
(Rhodophyceae). NCBI BLAST search ranked these plant peroxidases highest in
amino acid scores. Additionally ascorbate peroxidase from symbiotic
Chlorella, which is in the aligned region identical to free living
Chlorella 211-11b is shown. Comparison was carried out with ClustalW
under standard parameter settings. Similarities between HvAPX1 and the other
sequences are shaded. Residues that are conserved between Hydra and
in at least three other sequences are shown in white capitals on a black
background. Residues conserved between Hydra and two or one of the
other sequences are shaded dark or light grey respectively. The number of
conserved residues between HvAPX1 and the aligned sequences are as follows:
Hydra/Zantedischia=74 (41%), the expect as given by NCBI
BLAST analysis is 2e-09; Hydra/Euglena=73 (41%),
expect=1e-08; Hydra/Galdieria=70 (39%), expect=1e-08;
Hydra/Chlorella=65 (36%), expect=0.83. Five amino acids implicated in
the redox activity of plant ascorbate peroxidases are located within the plant
peroxidase domain of HvAPX1 (indicated by the letters R and H and one asterisk
above the aligned blocks). Seven boxes (I-VII) of high similarity between
HvAPX1 and all ascorbate peroxidases aligned by NCBI BLASTp are framed in
grey.
