Sandbox Reserved 935: Difference between revisions
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==Homologs== | ==Homologs== | ||
There are homologs for the kinase domain of BRI1 not only in plants but also in other eukaryotes <ref name=Bojar2014 />. Homologs in plants have similar domain structure in the whole protein, but in animals the other domains than kinase domain are different. The closest similarity to the kinase domain of BRI1 in ''Arabidopsis thaliana'' is interleukin-1 receptor-associated kinase 4 (IRAK4) in human and mouse. Similar kinase in ''Drosophila melanogaster'' is called Pelle-kinase. | There are homologs for the kinase domain of BRI1 not only in plants but also in other eukaryotes <ref name=Bojar2014 />. Homologs in plants have similar domain structure in the whole protein, but in animals the other domains than kinase domain are different. The closest similarity to the kinase domain of BRI1 in ''Arabidopsis thaliana'' is interleukin-1 receptor-associated kinase 4 (IRAK4) in human and mouse. Similar kinase in ''Drosophila melanogaster'' is called Pelle-kinase. Structural similarity between kinase domains of BRI1 and human IRAK4 is high and they both are dual-specificity kinases. It seems likely that the last common ancestor of Pelle/IRAK kinases and plant receptor kinases already had both serine-threonine and tyrosine activity and this feature has been preserved in both animals and plants <ref name=Bojar2014 />. | ||
[[Image:BRI1_phylogeny3.jpg|thumb|1200px|alt=Figure|Phylogeny of close relatives to BRI1. Based on amino acid sequences of kinase domain, ClustalW alignment and ML tree.]] | [[Image:BRI1_phylogeny3.jpg|thumb|1200px|alt=Figure|Phylogeny of close relatives to BRI1. Based on amino acid sequences of kinase domain, ClustalW alignment and ML tree.]] | ||
