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IPR008554 is a Glutaredoxin-like.
<p>Glutaredoxins [[cite:PUB00001738], [cite:PUB00000560], [cite:PUB00002504]], also known as thioltransferases (disulphide reductases), are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [[cite:PUB00014033]].</p> <p>Glutaredoxin functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. Like thioredoxin (TRX), which functions in a similar way, glutaredoxin possesses an active centre disulphide bond [[cite:PUB00015562]]. It exists in either a reduced or an oxidized form where the two cysteine residues are linked in an intramolecular disulphide bond. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH ->GSH reductase ->GSH ->GRX ->protein substrates [[cite:PUB00023503], [cite:PUB00030238], [cite:PUB00080927], [cite:PUB00080925]]. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress.</p> <p>Glutaredoxin has been sequenced in a variety of species. On the basis of extensive sequence similarity, it has been proposed [[cite:PUB00005575]] that Vaccinia virus protein O2L is most probably a glutaredoxin. Finally, it must be noted that Bacteriophage T4 thioredoxin seems also to be evolutionary related. In position 5 of the pattern T4 thioredoxin has Val instead of Pro.</p> <p>This family contains several viral glutaredoxins, and many related bacterial and eukaryotic proteins of unknown function. The best characterised member of this family is G4L ([swissprot:P68460]) from Vaccinia virus (strain Western Reserve/WR) (VACV), which is necessary for virion morphogenesis and virus replication [[cite:PUB00020627]]. This is a cytoplasmic protein which functions as a shuttle in a redox pathway between membrane-associated E10R and L1R or F9L [[cite:PUB00020628]].</p>
This description is obtained from EB-eye REST.
Transcript | Name | Description | Predicted domains | Domain count |
---|---|---|---|---|
– | Thioredoxin superfamily protein isoform 3 [Theobroma cacao] gi|508724352|gb|EOY16249.1| | 13 | ||
– | Glutaredoxin-like protein; TAIR: AT4G08280.2 Thioredoxin superfamily protein; Swiss-Prot: sp|Q05530|YD286_YEAST Glutaredoxin-like protein YDR286C; TrEMBL-Plants: tr|I3SYL7|I3SYL7_LOTJA Glutaredoxin-like protein; Found in the gene: LotjaGi1g1v0258300 | 13 |
A list of co-occurring predicted domains within the L. japonicus gene space:
Predicted domain | Source | Observations | Saturation (%) |
---|---|---|---|
SignalP-TM | SignalP_GRAM_NEGATIVE | 1 | 50.00 |