The domain within your query sequence starts at position 21 and ends at position 76; the E-value for the Glutaredoxin domain shown below is 5.7e-7.

QDVVRFLEANKIEFEEVDITMSEEQRQWMYKNIPPEKKPAQGNPLPPQIFNGDRYC

Glutaredoxin

Glutaredoxin
PFAM accession number:PF00462
Interpro abstract (IPR002109):

Glutaredoxins [(PUBMED:3152490), (PUBMED:3286320), (PUBMED:2668278)], 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 [(PUBMED:14713336)].

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 [(PUBMED:14962389)]. 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 [(PUBMED:9860827), (PUBMED:10493864), (PUBMED:15814611), (PUBMED:15706083)]. 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.

Glutaredoxin has been sequenced in a variety of species. On the basis of extensive sequence similarity, it has been proposed [(PUBMED:1994586)] 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.

This entry represents Glutaredoxin.

GO process:cell redox homeostasis (GO:0045454)
GO function:protein disulfide oxidoreductase activity (GO:0015035), electron transfer activity (GO:0009055)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Glutaredoxin