Alignment And Comparison Of The Amino Acid Sequences Of Sbp From All Organisms

Alignment And Comparison Of The Amino Acid Sequences Of Sbp From All Organisms

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Alignment and comparison of the amino acid sequences of SBP from all organisms that examined in present study showed the present of conserved motifs such as xCCx (Schild et al., 2014), KDEL, CxxC, HxD and HxxD (Flemetakis et al.,2002, Agalou et al., 2006). In particular, Se-binding motif xCCx in SBP1 of Arabidopsis thaliana plant, which described by Schild et al. (2014), contains two Cys residues (Cys 21 and Cys22) which could bind a single atom of selenium to form a R-S-Se (II)-S-R-type complex. Consequently, it is concluded, that among all representative species (photosynthetic organisms), it appears only in Plant Kingdom with the exception of the monocotyledons plants (Zea, Oryza, Hordeum, Triticum). Ying et al. (2015), based on the homology of Arabidopsis thaliana and human SBP1, predicated that cysteine 5 and 8 (CxxC motif) were possible candidates for selenium binding in the human SBP1 protein. Together with cysteine 57, they were known as critical for both its interaction with GPx1 and its biological function (Raucchi et al., 2011). This Cysteine (Cys57) is present in this study in Craniota species except Bos (Certatiodactyla), Mus/ Rattus (Muroidea), Equus (Perissodactyla), Sarcophilis/ Monodephis (Metatheria), Triaenodon (Galeoidea), whereas Cys5 and Cys8 are present in all Craniota species (Raucci et al., 2011).
The second motif KDEL appears as *DEL in all the examined species except Psyscommitrella (the only in Bryophyta) and Amphideon (the only in Sponges), which have a mutation (*DEI). This motif is an endoplasmic reticulum (ER) retention signal which plays a critical role in the localisation in the ER of eukaryotic cells of many soluble proteins contained in the cisternal lumen (Stornaiuolo et al., 2002).
The CxxC m...


... middle of paper ...


...lative sequence homology of each member of the clades. Each clade is denoted by different colour shading.

To explore the evolutionary relationship between SBP proteins, multiple sequence alignment of protein sequences from different species was performed using ClustalW2 program and phylogenetic tree was generated using MEGA4 software. All the members SBP family were divided into five major clades (Archaea (Halobacteria), Archaeplastida/Protista (Rhodophyta), Bacteria (Proteobacteria, Chloroflexi, Cyanobacteria), Plants, Animalia (Mammalia, Amphibia, Aves, Pisces, Cephalochordota, Anthozoa)). Interestingly, SBP proteins with similar domain architecture were clustered in same clades.
In order to study the phylogenetic relationship of SBP family among the Plant Kingdom, SBP proteins were identified from the representatives of dicotyledonous and monocotyledonous plants.

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