Figure 6.

S. domuncula related β-carotenoid oxygenases. (A) The two sponge putative carotenoid oxygenases (rBCO1_SUBDO; rBCO2_SUBDO) were aligned with the S. domuncula carotene dioxygenase (CDO1_SUBDO). Residues conserved (identical or similar with respect to their physico-chemical properties) in all three sequences are shown in white on black; those that share similarity only in two sequences are in black on gray. The characteristic signatures, the pyrokinin signature [pyrokinin] and the signature for the retinal pigment epithelial membrane protein superfamily [RPEMB], are marked; (B) For phylogenetic analyses, the three sponge oxygenases were aligned with the two cnidarian putative β-carotenoid oxygenases from N. vectensis (BCO_NEMAVEC) and from H. magnipapillata (BCO_HYDRA) together with the carotenoid oxygenase from the cyanobacteria, from N. punctiforme (BCO_NOSTOC) and from P. marinus (BCO_PROCHLORO). Additionally, selected carotene dioxygenases have been included; from human (BCD2_HUMAN; EAW67189.1), from Xenopus tropicalis (BCMO-II_XENTROP; XP_002942801.1), from Taeniopygia guttata (BCMO-II_TAENGUT; XP_002189781.1), from Branchiostoma floridae (BCDr_BRAFLD; XP_002605888.1) and from Caenorhabditis elegans (BCMO1_CAEEL; NP_496729.2), as well as the yeast Bfr2p from Saccharomyces cerevisiae (BFR_YEAST; EGA87437.1). As an outgroup sequence to root the tree, the 9-cis-epoxycarotenoid dioxygenase from Arabidopsis thaliana (CCD_ARATH; NP_191911.1) has been selected. The degree of support of internal branches was assessed by bootstrapping (1000 replicates) and the evolutionary distance was calculated (0.1 aa substitutions per position in the sequence).