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Literature summary for 1.8.3.2 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)

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

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

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

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

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

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