EC Number   |
General Information |
Reference |
|---|
    2.7.9.3 | evolution |
selenoproteins (containing the 21st proteinogenic amino acid selenocysteine) play important roles throughout all domains of life. A number of taxa have small selenoproteomes, and Hymenopteran insects appear to have fully lost selenoproteins. Nevertheless, their genomes contain genes for several proteins of the selenocysteine insertion machinery, including selenophosphate synthetase 1 (SELD/SPS1) |
738814 |
| 2.7.9.3 | evolution |
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common, e.g. Drosophila melanogaster possesses three selenoprotein genes, while Drosophila willistoni has replaced Sec with Cys in them and lost the capacity to synthesize Sec. Unequal selective pressure on SPS1 and SPS2 genes after duplication, overview |
738336 |
| 2.7.9.3 | evolution |
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. At the root of ascidians, the ancestral SPS2-Sec gene acquired a novel SPS-Gly transcript isoform through alternative exon usage at the 5'-end. Then, at the root of the ascidian lineage, Styelidae and Pyuridae, the SPS-Sec transcript of this dual SPS1/SPS2 gene (SPS-ae) retrotransposed to the genome creating a novel SPS2-Sec gene (GDR). This presumably triggered the loss of Sec from the parental gene, which, because both the SECIS and the UGA containing exon degenerated (SL), specialized only in the production of SPS1-Gly. Parallel gene duplications of SPS proteins in metazoa, phylogenetic analysis, overview |
738336 |
| 2.7.9.3 | evolution |
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. In Caenorhabditis elegans, the entire pathway is maintained only to synthesize a single selenoprotein. Unequal selective pressure on SPS1 and SPS2 genes after duplication, overview |
738336 |
| 2.7.9.3 | evolution |
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. Phylogenetic profile of SPS and selenium utilization traits in prokaryotes, overview |
738336 |
| 2.7.9.3 | evolution |
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. Unequal selective pressure on SPS1 and SPS2 genes after duplication, overview |
738336 |
| 2.7.9.3 | evolution |
SEPHS1 and SEPHS2 most likely segregate from their common ancestor prior to speciation |
761118 |
| 2.7.9.3 | evolution |
the dimeric organization is functionally important throughout the domains of life |
-, 762206 |
| 2.7.9.3 | malfunction |
in the enzyme knockout mutant, the function of SPS2 proteins is significantly inhibited, it is possible that the expression levels of selenoproteins in fruit flies might be reduced |
738986 |
| 2.7.9.3 | malfunction |
isoform SPS2 absence severely hampers the parasite survival in the presence of an oxidizing environment that results in an apoptotic-like phenotype and cell death |
723131 |
