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Literature summary extracted from

  • Limor-Waisberg, K.; Ben-Dor, S.; Fass, D.
    Diversification of quiescin sulfhydryl oxidase in a preserved framework for redox relay (2013), BMC Evol. Biol., 13, 70 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.3.2 gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis Branchiostoma floridae
1.8.3.2 gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis Trichoplax adhaerens
1.8.3.2 gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis Ixodes scapularis
1.8.3.2 gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis Daphnia pulex
1.8.3.2 gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis Apis mellifera
1.8.3.2 gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis Drosophila melanogaster
1.8.3.2 gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis Trypanosoma brucei
1.8.3.2 gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis Micromonas pusilla
1.8.3.2 gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis Coccomyxa subellipsoidea
1.8.3.2 gene QSOX, DNA and amino acid sequence comparisons and phylogenetic analysis Selaginella moellendorffii
1.8.3.2 gene QSOX, isozyme QSOX1 has two splising variants 1a and 1b, DNA and amino acid sequence comparisons and phylogenetic analysis Homo sapiens
1.8.3.2 gene QSOX, isozyme QSOX1 has two splising variants 1a and 1b, DNA and amino acid sequence comparisons and phylogenetic analysis Arabidopsis thaliana
1.8.3.2 gene QSOX1, DNA and amino acid sequence comparisons and phylogenetic analysis Perkinsus marinus
1.8.3.2 gene QSOX1, DNA and amino acid sequence comparisons and phylogenetic analysis Mus musculus
1.8.3.2 gene QSOX1, DNA and amino acid sequence comparisons and phylogenetic analysis Gallus gallus
1.8.3.2 gene QSOX1, DNA and amino acid sequence comparisons and phylogenetic analysis Xenopus tropicalis
1.8.3.2 gene QSOX1, DNA and amino acid sequence comparisons and phylogenetic analysis Danio rerio
1.8.3.2 gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis Perkinsus marinus
1.8.3.2 gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis Homo sapiens
1.8.3.2 gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis Mus musculus
1.8.3.2 gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis Gallus gallus
1.8.3.2 gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis Danio rerio
1.8.3.2 gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis Arabidopsis thaliana
1.8.3.2 gene QSOX3, DNA and amino acid sequence comparisons and phylogenetic analysis Perkinsus marinus

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.2 Apis mellifera A0A7M7FYF7
-
-
1.8.3.2 Arabidopsis thaliana Q8W4J3
-
-
1.8.3.2 Arabidopsis thaliana Q9ZU40
-
-
1.8.3.2 Branchiostoma floridae C3ZHZ6
-
-
1.8.3.2 Coccomyxa subellipsoidea I0YJW9
-
-
1.8.3.2 Coccomyxa subellipsoidea c-169 I0YJW9
-
-
1.8.3.2 Danio rerio B0UXN0
-
-
1.8.3.2 Danio rerio F1QJL3
-
-
1.8.3.2 Daphnia pulex E9HEH3
-
-
1.8.3.2 Drosophila melanogaster C0PVB3
-
-
1.8.3.2 Drosophila melanogaster Q7JQR3
-
-
1.8.3.2 Drosophila melanogaster Q9VD61
-
-
1.8.3.2 Drosophila melanogaster Q9VD62
-
-
1.8.3.2 Gallus gallus F1P458
-
-
1.8.3.2 Gallus gallus Q8JGM4
-
-
1.8.3.2 Homo sapiens O00391
-
-
1.8.3.2 Homo sapiens Q6ZRP7
-
-
1.8.3.2 Ixodes scapularis B7PLS2
-
-
1.8.3.2 Micromonas pusilla C1MIM3
-
-
1.8.3.2 Mus musculus Q3TMX7
-
-
1.8.3.2 Mus musculus Q8BND5
-
-
1.8.3.2 Perkinsus marinus
-
-
-
1.8.3.2 Selaginella moellendorffii D8TF00
-
-
1.8.3.2 Trichoplax adhaerens B3RPG3
-
-
1.8.3.2 Trypanosoma brucei Q25B82
-
-
1.8.3.2 Xenopus tropicalis Q501L2
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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

EC Number Subunits Comment Organism
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Perkinsus marinus
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Mus musculus
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Homo sapiens
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Arabidopsis thaliana
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Gallus gallus
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Xenopus tropicalis
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Danio rerio
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Branchiostoma floridae
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Trichoplax adhaerens
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Ixodes scapularis
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Daphnia pulex
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Apis mellifera
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Drosophila melanogaster
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Trypanosoma brucei
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Micromonas pusilla
1.8.3.2 More enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview Coccomyxa subellipsoidea
1.8.3.2 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

EC Number Synonyms Comment Organism
1.8.3.2 QSOX
-
Mus musculus
1.8.3.2 QSOX
-
Homo sapiens
1.8.3.2 QSOX
-
Arabidopsis thaliana
1.8.3.2 QSOX
-
Gallus gallus
1.8.3.2 QSOX
-
Xenopus tropicalis
1.8.3.2 QSOX
-
Danio rerio
1.8.3.2 QSOX
-
Branchiostoma floridae
1.8.3.2 QSOX
-
Trichoplax adhaerens
1.8.3.2 QSOX
-
Ixodes scapularis
1.8.3.2 QSOX
-
Daphnia pulex
1.8.3.2 QSOX
-
Apis mellifera
1.8.3.2 QSOX
-
Drosophila melanogaster
1.8.3.2 QSOX
-
Trypanosoma brucei
1.8.3.2 QSOX
-
Micromonas pusilla
1.8.3.2 QSOX
-
Coccomyxa subellipsoidea
1.8.3.2 QSOX
-
Selaginella moellendorffii
1.8.3.2 QSOx1
-
Perkinsus marinus
1.8.3.2 QSOx1
-
Mus musculus
1.8.3.2 QSOx1
-
Homo sapiens
1.8.3.2 QSOx1
-
Arabidopsis thaliana
1.8.3.2 QSOx1
-
Gallus gallus
1.8.3.2 QSOx1
-
Xenopus tropicalis
1.8.3.2 QSOx1
-
Danio rerio
1.8.3.2 QSOx1
-
Ixodes scapularis
1.8.3.2 QSOX2
-
Perkinsus marinus
1.8.3.2 QSOX2
-
Homo sapiens
1.8.3.2 QSOX2
-
Mus musculus
1.8.3.2 QSOX2
-
Gallus gallus
1.8.3.2 QSOX2
-
Danio rerio
1.8.3.2 QSOX2
-
Arabidopsis thaliana
1.8.3.2 QSOX3
-
Perkinsus marinus
1.8.3.2 SOX
-
Trypanosoma brucei
1.8.3.2 sulfhydryl oxidase
-
Daphnia pulex

General Information

EC Number General Information Comment Organism
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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
1.8.3.2 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