Cloned (Comment) | Organism |
---|---|
gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis | Branchiostoma floridae |
gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis | Trichoplax adhaerens |
gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis | Ixodes scapularis |
gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis | Daphnia pulex |
gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis | Apis mellifera |
gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis | Drosophila melanogaster |
gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis | Trypanosoma brucei |
gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis | Micromonas pusilla |
gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis | Coccomyxa subellipsoidea |
gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis | Selaginella moellendorffii |
gene QSOX, isozyme QSOX1 has two splising variants 1a and 1b, DNA and amino acid sequence comparisons and phylogenetic analysis | Homo sapiens |
gene QSOX, isozyme QSOX1 has two splising variants 1a and 1b, DNA and amino acid sequence comparisons and phylogenetic analysis | Arabidopsis thaliana |
gene QSOX1, DNA and amino acid sequence comparisons and phylogenetic analysis | Perkinsus marinus |
gene QSOX1, DNA and amino acid sequence comparisons and phylogenetic analysis | Mus musculus |
gene QSOX1, DNA and amino acid sequence comparisons and phylogenetic analysis | Gallus gallus |
gene QSOX1, DNA and amino acid sequence comparisons and phylogenetic analysis | Xenopus tropicalis |
gene QSOX1, DNA and amino acid sequence comparisons and phylogenetic analysis | Danio rerio |
gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis | Perkinsus marinus |
gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis | Homo sapiens |
gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis | Mus musculus |
gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis | Gallus gallus |
gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis | Danio rerio |
gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis | Arabidopsis thaliana |
gene QSOX3, DNA and amino acid sequence comparisons and phylogenetic analysis | Perkinsus marinus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Apis mellifera | A0A7M7FYF7 | - |
- |
Arabidopsis thaliana | Q8W4J3 | - |
- |
Arabidopsis thaliana | Q9ZU40 | - |
- |
Branchiostoma floridae | C3ZHZ6 | - |
- |
Coccomyxa subellipsoidea | I0YJW9 | - |
- |
Coccomyxa subellipsoidea c-169 | I0YJW9 | - |
- |
Danio rerio | B0UXN0 | - |
- |
Danio rerio | F1QJL3 | - |
- |
Daphnia pulex | E9HEH3 | - |
- |
Drosophila melanogaster | C0PVB3 | - |
- |
Drosophila melanogaster | Q7JQR3 | - |
- |
Drosophila melanogaster | Q9VD61 | - |
- |
Drosophila melanogaster | Q9VD62 | - |
- |
Gallus gallus | F1P458 | - |
- |
Gallus gallus | Q8JGM4 | - |
- |
Homo sapiens | O00391 | - |
- |
Homo sapiens | Q6ZRP7 | - |
- |
Ixodes scapularis | B7PLS2 | - |
- |
Micromonas pusilla | C1MIM3 | - |
- |
Mus musculus | Q3TMX7 | - |
- |
Mus musculus | Q8BND5 | - |
- |
Perkinsus marinus | - |
- |
- |
Selaginella moellendorffii | D8TF00 | - |
- |
Trichoplax adhaerens | B3RPG3 | - |
- |
Trypanosoma brucei | Q25B82 | - |
- |
Xenopus tropicalis | Q501L2 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Perkinsus marinus | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Mus musculus | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Homo sapiens | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Arabidopsis thaliana | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Gallus gallus | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Xenopus tropicalis | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Danio rerio | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Branchiostoma floridae | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Trichoplax adhaerens | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Ixodes scapularis | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Daphnia pulex | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Apis mellifera | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Drosophila melanogaster | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Trypanosoma brucei | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Micromonas pusilla | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Coccomyxa subellipsoidea | |
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor | Selaginella moellendorffii |
Subunits | Comment | Organism |
---|---|---|
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Perkinsus marinus |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Mus musculus |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Homo sapiens |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Arabidopsis thaliana |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Gallus gallus |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Xenopus tropicalis |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Danio rerio |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Branchiostoma floridae |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Trichoplax adhaerens |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Ixodes scapularis |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Daphnia pulex |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Apis mellifera |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Drosophila melanogaster |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Trypanosoma brucei |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Micromonas pusilla |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Coccomyxa subellipsoidea |
More | enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview | Selaginella moellendorffii |
Synonyms | Comment | Organism |
---|---|---|
QSOX | - |
Mus musculus |
QSOX | - |
Homo sapiens |
QSOX | - |
Arabidopsis thaliana |
QSOX | - |
Gallus gallus |
QSOX | - |
Xenopus tropicalis |
QSOX | - |
Danio rerio |
QSOX | - |
Branchiostoma floridae |
QSOX | - |
Trichoplax adhaerens |
QSOX | - |
Ixodes scapularis |
QSOX | - |
Daphnia pulex |
QSOX | - |
Apis mellifera |
QSOX | - |
Drosophila melanogaster |
QSOX | - |
Trypanosoma brucei |
QSOX | - |
Micromonas pusilla |
QSOX | - |
Coccomyxa subellipsoidea |
QSOX | - |
Selaginella moellendorffii |
QSOx1 | - |
Perkinsus marinus |
QSOx1 | - |
Mus musculus |
QSOx1 | - |
Homo sapiens |
QSOx1 | - |
Arabidopsis thaliana |
QSOx1 | - |
Gallus gallus |
QSOx1 | - |
Xenopus tropicalis |
QSOx1 | - |
Danio rerio |
QSOx1 | - |
Ixodes scapularis |
QSOX2 | - |
Perkinsus marinus |
QSOX2 | - |
Homo sapiens |
QSOX2 | - |
Mus musculus |
QSOX2 | - |
Gallus gallus |
QSOX2 | - |
Danio rerio |
QSOX2 | - |
Arabidopsis thaliana |
QSOX3 | - |
Perkinsus marinus |
SOX | - |
Trypanosoma brucei |
sulfhydryl oxidase | - |
Daphnia pulex |
General Information | Comment | Organism |
---|---|---|
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Perkinsus marinus |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Mus musculus |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Homo sapiens |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Arabidopsis thaliana |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Gallus gallus |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Xenopus tropicalis |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Danio rerio |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Branchiostoma floridae |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Trichoplax adhaerens |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Ixodes scapularis |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Daphnia pulex |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Apis mellifera |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Drosophila melanogaster |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Trypanosoma brucei |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Micromonas pusilla |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Coccomyxa subellipsoidea |
evolution | evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa | Selaginella moellendorffii |