Cloned (Comment) | Organism |
---|---|
a single SPS gene, phylogenetic analysis | Ciona intestinalis |
gene ptuf/SelD or SPS1, genetic structure analysis, SPS1-UGA might perhaps be translated by a readthrough mechanism not involving Sec insertion. In this respect, there is growing evidence for abundant stop codon readthrough in insects, with UGA being the most frequently observed readthrough codon in Drosophila | Drosophila melanogaster |
gene seld-1, genetic structure analysis | Caenorhabditis elegans |
gene SPS, phylogenetic analysis | Oikopleura dioica |
gene SPS, phylogenetic analysis | Molgula tectiformis |
gene SPS2, phylogenetic analysis | Botryllus schlosseri |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli | |
Mg2+ | required | Homo sapiens | |
Mg2+ | required | Drosophila melanogaster | |
Mg2+ | required | Caenorhabditis elegans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + selenide + H2O | Escherichia coli | - |
AMP + selenophosphate + phosphate | - |
? | |
ATP + selenide + H2O | Homo sapiens | - |
AMP + selenophosphate + phosphate | - |
? | |
ATP + selenide + H2O | Drosophila melanogaster | - |
AMP + selenophosphate + phosphate | - |
? | |
ATP + selenide + H2O | Caenorhabditis elegans | - |
AMP + selenophosphate + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Botryllus schlosseri | - |
contains an active SPS2-Sec and an inactive SPS1-Gly isozyme | - |
Caenorhabditis elegans | O62461 | - |
- |
Ciona intestinalis | - |
- |
- |
Drosophila melanogaster | O18373 | gene ptuf/SelD or SPS1 | - |
Escherichia coli | - |
- |
- |
Homo sapiens | Q99611 | Sephs2 | - |
Molgula tectiformis | - |
contains an active SPS-Sec and an inactive SPS-Gly isozyme | - |
no activity in Acyrthosiphon pisum | - |
selenoprotein genes are converted to Cys homologues or lost, and the Sec machinery degenerated and/or disappeared | - |
no activity in Coleoptera | - |
selenoprotein genes are converted to Cys homologues or lost, and the Sec machinery degenerated and/or disappeared | - |
no activity in Drosophila willistoni | - |
- |
- |
no activity in Endopterygota | - |
selenoprotein genes are converted to Cys homologues or lost, and the Sec machinery degenerated and/or disappeared | - |
no activity in Hymenoptera | - |
selenoprotein genes are converted to Cys homologues or lost, and the Sec machinery degenerated and/or disappeared | - |
no activity in Lepidoptera | - |
selenoprotein genes are converted to Cys homologues or lost, and the Sec machinery degenerated and/or disappeared | - |
Oikopleura dioica | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + selenide + H2O | - |
Escherichia coli | AMP + selenophosphate + phosphate | - |
? | |
ATP + selenide + H2O | - |
Homo sapiens | AMP + selenophosphate + phosphate | - |
? | |
ATP + selenide + H2O | - |
Drosophila melanogaster | AMP + selenophosphate + phosphate | - |
? | |
ATP + selenide + H2O | - |
Caenorhabditis elegans | AMP + selenophosphate + phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
SelD | - |
Escherichia coli |
SelD | - |
Ciona intestinalis |
SelD | - |
Homo sapiens |
SelD | - |
Drosophila melanogaster |
SelD | - |
Oikopleura dioica |
SelD | - |
Molgula tectiformis |
SelD | - |
Botryllus schlosseri |
seld-1 | - |
Caenorhabditis elegans |
selenide water dikinase | - |
Homo sapiens |
selenide water dikinase | - |
Drosophila melanogaster |
selenide water dikinase | - |
Caenorhabditis elegans |
selenophosphate synthetase | - |
Escherichia coli |
selenophosphate synthetase | - |
Ciona intestinalis |
selenophosphate synthetase | - |
Homo sapiens |
selenophosphate synthetase | - |
Drosophila melanogaster |
selenophosphate synthetase | - |
Caenorhabditis elegans |
selenophosphate synthetase | - |
Oikopleura dioica |
selenophosphate synthetase | - |
Molgula tectiformis |
selenophosphate synthetase | - |
Botryllus schlosseri |
Sephs2 | - |
Homo sapiens |
SPS | - |
Escherichia coli |
SPS | - |
Ciona intestinalis |
SPS | - |
Caenorhabditis elegans |
SPS | - |
Oikopleura dioica |
SPS | - |
Molgula tectiformis |
SPS | - |
Botryllus schlosseri |
SPS1 | - |
Drosophila melanogaster |
Sps2 | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli | |
ATP | - |
Homo sapiens | |
ATP | - |
Drosophila melanogaster | |
ATP | - |
Caenorhabditis elegans |
General Information | Comment | Organism |
---|---|---|
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 | Drosophila melanogaster |
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 | Ciona intestinalis |
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 | Oikopleura dioica |
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 | Molgula tectiformis |
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 | Botryllus schlosseri |
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 | Caenorhabditis elegans |
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 | Escherichia coli |
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 | Homo sapiens |
additional information | SPS2, i.e. Sephs2, invertebrates is a selenoprotein | Homo sapiens |
physiological function | Drosophila SPS1 (i.e., ptuf/SelD) lacks the ability to catalyze selenide-dependent ATP hydrolysis or to complement SelD deficiency in Escherichia coli. Drosophila SPS1 has been proposed to be involved in vitamin B6 metabolism and in redox homeostasis since it protects from damage induced by reactive oxygen species | Drosophila melanogaster |