| Primary Identifier | IPR036249 | Type | Homologous_superfamily |
| Short Name | Thioredoxin-like_sf |
| 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 [] |
