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IPR017905 is a ERV/ALR sulfhydryl oxidase domain.
<p>The ~100-residue ERV/ALR sulphydryl oxidase domain is a versatile module adapted for catalysis of disulphide bond formation in various organelles and biological settings. The ERV/ALR sulphydryl oxidase domain has a Cys-X-X-Cys dithiol/disulphide motif adjacent to a bound FAD cofactor, enabling transfer of electrons from thiol substrates to non-thiol electron acceptors. ERV/ALR family members differ in their N- or C-terminal extensions, which typically contain at least one additional disulphide bond, the hypothesised 'shuttle' disulphide. In yeast ERV1, a mitochondrial enzyme, the shuttle disulphide is N-terminal to the catalytic core; in yeast ERV2, present in the endoplasmic reticulum, it is C-terminal. The N- and C-terminal extensions can be entire domains, such as the thioredoxin-like domains ([prositedoc:PDOC00172]) or short segments that do not seem to be distinct domains. Proteins of the ERV/ALR family are encoded by all eukaryotes and cytoplasmic DNA viruses (poxviruses, African swine fever virus, iridoviruses, and Paramecium bursaria Chlorella virus 1) [[cite:PUB00043720], [cite:PUB00013604], [cite:PUB00026507], [cite:PUB00041418], [cite:PUB00043721]].</p> <p>The ERV/ALR sulphydryl oxidase domain contains a four-helix bundle (helices α1-α4) and an additional single turn of helix (α5) packed perpendicular to the bundle [[cite:PUB00043722], [cite:PUB00041418]]. The FAD prosthetic group is housed at the mouth of the 4-helix bundle and communicates with the pair of juxtaposed cysteine residues that form the proximal redox active site [[cite:PUB00043721]].</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Thiol oxidase activity | Catalysis of the reaction: 4 R'C(R)SH + O2 = 2 R'C(R)S-S(R)CR' + 2 H2O. | ||
| Biological process | Oxidation-reduction process | A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: FAD-linked sulfhydryl oxidase ERV1-like [Cicer arietinum] gi|502158492|ref|XP_004511174.1| | 7 | ||
| – | PREDICTED: FAD-linked sulfhydryl oxidase ERV1-like [Cicer arietinum] gi|502158492|ref|XP_004511174.1| | 7 | ||
| – | PREDICTED: FAD-linked sulfhydryl oxidase ERV1-like [Cicer arietinum] gi|502158492|ref|XP_004511174.1| | 7 | ||
| – | PREDICTED: FAD-linked sulfhydryl oxidase ERV1-like [Cicer arietinum] gi|502158492|ref|XP_004511174.1| | 7 | ||
| – | PREDICTED: sulfhydryl oxidase 1-like [Glycine max] gi|356536226|ref|XP_003536640.1| | 25 | ||
| – | Protein disulfide isomerase family [Glycine max] gi|317175939|dbj|BAJ54084.1| | 10 | ||
| – | Sulfhydryl oxidase; TAIR: AT1G49880.1 Erv1/Alr family protein; Swiss-Prot: sp|Q8GXX0|ERV1_ARATH FAD-linked sulfhydryl oxidase ERV1; TrEMBL-Plants: tr|A0A151SFK0|A0A151SFK0_CAJCA Sulfhydryl oxidase; Found in the gene: LotjaGi4g1v0245500 | 9 | ||
| – | Sulfhydryl oxidase; TAIR: AT2G01270.1 quiescin-sulfhydryl oxidase 2; Swiss-Prot: sp|Q9ZU40|QSOX2_ARATH Sulfhydryl oxidase 2; TrEMBL-Plants: tr|K7LLL4|K7LLL4_SOYBN Sulfhydryl oxidase; Found in the gene: LotjaGi5g1v0331700 | 27 | ||
| – | Sulfhydryl oxidase; TAIR: AT1G15020.2 quiescin-sulfhydryl oxidase 1; Swiss-Prot: sp|Q8W4J3|QSOX1_ARATH Sulfhydryl oxidase 1; TrEMBL-Plants: tr|A0A0B2PBV9|A0A0B2PBV9_GLYSO Sulfhydryl oxidase; Found in the gene: LotjaGi5g1v0331700 | 27 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| TRANSMEMBRANE | Phobius | 1 | 11.11 |