InterPro : IPR012336

Name  Thioredoxin-like fold Short Name  Thioredoxin-like_fold
Type  Domain 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 alpha/beta/alpha 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 alpha-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 [], glutaredoxon [], hybrid peroxiredoxin hyPrx5 []Thioredoxin-like 2Fe-2S ferredoxin []
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

7 Child Features

Id Name Short Name Type
IPR013766 Thioredoxin domain Thioredoxin_domain Domain
IPR000866 Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant AhpC/TSA Domain
IPR013740 Redoxin Redoxin Domain
IPR004045 Glutathione S-transferase, N-terminal Glutathione_S-Trfase_N Domain
IPR024253 Phosducin, thioredoxin-like domain Phosducin_thioredoxin-like_dom Domain
IPR011649 KaiB domain KaiB_domain Domain
IPR012941 Phenol hydroxylase, C-terminal dimerisation domain Phe_hydrox_C_dim_dom Domain

8 Contains

Id Name Short Name Type
IPR019479 Peroxiredoxin, C-terminal Peroxiredoxin_C Domain
IPR002109 Glutaredoxin Glutaredoxin Domain
IPR017937 Thioredoxin, conserved site Thioredoxin_CS Conserved_site
IPR011767 Glutaredoxin active site GLR_AS Active_site
IPR004879 Domain of unknown function DUF255 DUF255 Domain
IPR018219 Thiol peroxidase conserved site Tpx_CS Conserved_site
IPR018233 Calsequestrin, conserved site Calsequestrin_CS Conserved_site
IPR008261 Iodothyronine deiodinase, active site Iodothyronine_deiodinase_AS Active_site

13 Found In

Id Name Short Name Type
IPR012883 ERp29, N-terminal ERp29_N Domain
IPR014109 Type-F conjugative transfer system pilin assembly thiol-disulphide isomerase TrbB Thiol-disulphide_isomerase_rbB Family
IPR016639 Glutathione S-transferase (GST) GST Family
IPR017346 Uncharacterised conserved protein UCP037991, UAS/UBX UCP037991_UAS/UBX Family
IPR003083 S-crystallin S-crystallin Family
IPR014111 Type IV conjugative transfer system protein TraF T4SS_TraF Family
IPR014440 HCCA isomerase/glutathione S-transferase kappa HCCAis_GSTk Family
IPR012863 Protein of unknown function DUF1636 DUF1636 Family
IPR017167 Uncharacterised conserved protein UCP037291, glutaredoxin-related UCP037291_glutaredoxin-rel Family
IPR009737 Sucraseferredoxin-like Suc_Fer-like Family
IPR010350 Protein of unknown function DUF942, thioredoxin-like DUF942_thioredox Family
IPR010296 Protein of unknown function DUF899, thioredoxin-like DUF899_thioredox Family
IPR021170 DnaJ homolog, subfamily C DnaJ_homolog_subfam-C Family

0 Parent Features

20 Publications

First Author Title Year Journal Volume Pages
Epp O The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. 1983 Eur J Biochem 133 51-69
Reuter K Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein. 1999 J Mol Biol 294 515-25
Martin P Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme. 2001 Structure 9 1071-81
McCarthy AA Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. 2000 Nat Struct Biol 7 196-9
Garces RG Anabaena circadian clock proteins KaiA and KaiB reveal a potential common binding site to their partner KaiC. 2004 EMBO J 23 1688-98
Liepinsh E Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer. 2001 Structure 9 457-71
Buchanan BB Redox regulation: a broadening horizon. 2005 Annu Rev Plant Biol 56 187-220
Wang S Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum. 1998 Nat Struct Biol 5 476-83
Guddat LW Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability. 1997 Protein Sci 6 1893-900
Xia TH NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins. 1992 Protein Sci 1 310-21
Yeh AP High resolution crystal structures of the wild type and Cys-55-->Ser and Cys-59-->Ser variants of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus. 2002 J Biol Chem 277 34499-507
Kim SJ The tetrameric structure of Haemophilus influenza hybrid Prx5 reveals interactions between electron donor and acceptor proteins. 2003 J Biol Chem 278 10790-8
Brockmann C The oxidized subunit B8 from human complex I adopts a thioredoxin fold. 2004 Structure 12 1645-54
Nardini M Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6 Angstrom resolution. 2004 Biochem Biophys Res Commun 318 470-6
Heras B Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. 2004 Proc Natl Acad Sci U S A 101 8876-81
Kemmink J The structure in solution of the b domain of protein disulfide isomerase. 1999 J Biomol NMR 13 357-68
Gaudet R Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin. 1996 Cell 87 577-88
Katti SK Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution. 1990 J Mol Biol 212 167-84
Ferguson AD NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family. 2006 J Biol Chem 281 3536-43
Téllez-Sanz R Calorimetric and structural studies of the nitric oxide carrier S-nitrosoglutathione bound to human glutathione transferase P1-1. 2006 Protein Sci 15 1093-105



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)