Protein Domain : Thioredoxin-like superfamily IPR036249

Type	Homologous_superfamily
Description	Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2), where a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system, the NADP/thioredoxin system, and the glutathione/glutaredoxin system [ ]. Several of these disulphide proteins share a common structure, consisting of a three-layer α/β/α core. Proteins that contain domains with a thioredoxin-like fold include:Arsenate reductase (ArsC) [ ] Calsequestrin (contains three tandem repeats of this fold) [ ] Circadian oscillation regulator KaiB [ ] Disulphide bond isomerase DsbC and DsbG (C-terminal domain) [ , ] Disulphide bond facilitator DsbA (contains an α-helical insertion) [ ] Endoplasmic reticulum protein ERP29 (N-terminal domain) [ ] Glutathione S-transferase (GST) (N-terminal domain) [ ] Mitochondrial ribosomal protein L51/S25/CI-B8 domain (variable positions for Cys residues in active site) [ ] Phosducin [ ] Protein disulphide isomerase (PDI) (contains two tandem repeats of this fold) [ ] Glutathione peroxidase-like enzymes [ ] Selenoprotein W-related [ ] SH3-binding glutamic acid-rich protein like (SH3BGR) (lacks both conserved Cys residues) [ ] Spliceosomal protein U5-15Kd [ ] Thioltransferases, including thioredoxin [ ], glutaredoxin [], hybrid peroxiredoxin hyPrx5 [] Thioredoxin-like 2Fe-2S ferredoxin [ ]
Short Name	Thioredoxin-like_sf