thioredoxin family protein [Gemmiger sp. An50]
thioredoxin domain-containing protein( domain architecture ID 144)
thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif
List of domain hits
Name | Accession | Description | Interval | E-value | ||
HemE super family | cl43134 | Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ... |
59-122 | 8.22e-11 | ||
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis The actual alignment was detected with superfamily member COG0407: Pssm-ID: 440176 [Multi-domain] Cd Length: 336 Bit Score: 61.01 E-value: 8.22e-11
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Thioredoxin_like super family | cl00388 | Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ... |
171-248 | 2.39e-04 | ||
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others. The actual alignment was detected with superfamily member pfam13192: Pssm-ID: 469754 [Multi-domain] Cd Length: 71 Bit Score: 38.35 E-value: 2.39e-04
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HemE super family | cl43134 | Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ... |
1-56 | 4.44e-03 | ||
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis The actual alignment was detected with superfamily member COG0407: Pssm-ID: 440176 [Multi-domain] Cd Length: 336 Bit Score: 37.89 E-value: 4.44e-03
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Name | Accession | Description | Interval | E-value | ||
HemE | COG0407 | Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ... |
59-122 | 8.22e-11 | ||
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis Pssm-ID: 440176 [Multi-domain] Cd Length: 336 Bit Score: 61.01 E-value: 8.22e-11
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URO-D_like | cd03465 | The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
67-121 | 1.47e-05 | ||
The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane. Pssm-ID: 239548 Cd Length: 330 Bit Score: 45.40 E-value: 1.47e-05
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Thioredoxin_3 | pfam13192 | Thioredoxin domain; |
171-248 | 2.39e-04 | ||
Thioredoxin domain; Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 38.35 E-value: 2.39e-04
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HemE | COG0407 | Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ... |
1-56 | 4.44e-03 | ||
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis Pssm-ID: 440176 [Multi-domain] Cd Length: 336 Bit Score: 37.89 E-value: 4.44e-03
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Name | Accession | Description | Interval | E-value | ||
HemE | COG0407 | Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ... |
59-122 | 8.22e-11 | ||
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis Pssm-ID: 440176 [Multi-domain] Cd Length: 336 Bit Score: 61.01 E-value: 8.22e-11
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URO-D_like | cd03465 | The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
67-121 | 1.47e-05 | ||
The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane. Pssm-ID: 239548 Cd Length: 330 Bit Score: 45.40 E-value: 1.47e-05
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Thioredoxin_3 | pfam13192 | Thioredoxin domain; |
171-248 | 2.39e-04 | ||
Thioredoxin domain; Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 38.35 E-value: 2.39e-04
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HemE | COG0407 | Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ... |
1-56 | 4.44e-03 | ||
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis Pssm-ID: 440176 [Multi-domain] Cd Length: 336 Bit Score: 37.89 E-value: 4.44e-03
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Blast search parameters | ||||
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