The domain within your query sequence starts at position 34 and ends at position 134; the E-value for the Thioredoxin domain shown below is 5.9e-14.
RVQPMTASNWTLVMEGEWMLKFYAPWCPSCQQTDSEWETFAKNGETLQISVGKVDVIQEP GLSGRFFVTTLPAFFHAKDGIFRRYRGPGIYEDLQNYILEK
Thioredoxin |
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PFAM accession number: | PF00085 |
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Interpro abstract (IPR013766): | Thioredoxins [ (PUBMED:3896121) (PUBMED:2668278) (PUBMED:7788289) (PUBMED:7788290) ] are small disulphide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. In the NADPH-dependent protein disulphide reduction, thioredoxin reductase (TR) catalyses the reduction of oxidised thioredoxin (trx) by NADPH using FAD and its redox-active disulphide; reduced thioredoxin then directly reduces the disulphide in the substrate protein [ (PUBMED:3896121) ]. Thioredoxin is present in prokaryotes and eukaryotes and the sequence around the redox-active disulphide bond is well conserved. All thioredoxins contain a cis-proline located in a loop preceding beta-strand 4, which makes contact with the active site cysteines, and is important for stability and function [ (PUBMED:8590004) ]. Thioredoxin belongs to a structural family that includes glutaredoxin, glutathione peroxidase, bacterial protein disulphide isomerase DsbA, and the N-terminal domain of glutathione transferase [ (PUBMED:7788290) ]. Thioredoxins have a beta-alpha unit preceding the motif common to all these proteins. A number of eukaryotic proteins contain domains evolutionary related to thioredoxin, most of them are protein disulphide isomerases (PDI). PDI ( EC 5.3.4.1 ) [ (PUBMED:3371540) (PUBMED:2537773) (PUBMED:7940678) ] is an endoplasmic reticulum multi-functional enzyme that catalyses the formation and rearrangement of disulphide bonds during protein folding [ (PUBMED:7913469) ]. All PDI contains two or three (ERp72) copies of the thioredoxin domain, each of which contributes to disulphide isomerase activity, but which are functionally non-equivalent [ (PUBMED:7983029) ]. Moreover, PDI exhibits chaperone-like activity towards proteins that contain no disulphide bonds, i.e. behaving independently of its disulphide isomerase activity [ (PUBMED:7635143) ]. The various forms of PDI which are currently known are:
Bacterial proteins that act as thiol:disulphide interchange proteins that allows disulphide bond formation in some periplasmic proteins also contain a thioredoxin domain. These proteins include:
This entry represents the thioredoxin domain. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Thioredoxin