The domain within your query sequence starts at position 15 and ends at position 80; the E-value for the Glutaredoxin domain shown below is 3.8e-19.

VVVFIKPTCPYCRKTQEILSQLPFKQGLLEFVDITATNNTSAIQDYLQQLTGARTVPRVF
IGKDCI

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 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