SCOPe 2.06: Superfamily c.47.1: Thioredoxin-like

Lineage for Superfamily c.47.1: Thioredoxin-like

1. Root: SCOPe 2.06

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.47: Thioredoxin fold [52832] (2 superfamilies)
   core: 3 layers, a/b/a; mixed beta-sheet of 4 strands, order 4312; strand 3 is antiparallel to the rest

4. Superfamily c.47.1: Thioredoxin-like [52833] (24 families)

Families:

1. c.47.1.1: Thioltransferase [52834] (16 proteins)

2. c.47.1.2: PDI-like [52849] (3 proteins)
   duplication: contains two tandem repeats of this fold

3. c.47.1.3: Calsequestrin [52855] (1 protein)
   duplication: contains three tandem repeats of this fold

4. c.47.1.5: Glutathione S-transferase (GST), N-terminal domain [52862] (19 proteins)

5. c.47.1.6: Phosducin [52888] (1 protein)
   automatically mapped to Pfam PF02114

6. c.47.1.7: ERP29 N domain-like [52892] (3 proteins)
   automatically mapped to Pfam PF07912

7. c.47.1.8: spliceosomal protein U5-15Kd [52895] (2 proteins)
   automatically mapped to Pfam PF02966

8. c.47.1.9: DsbC/DsbG C-terminal domain-like [52898] (3 proteins)
   elaborated common fold

9. c.47.1.10: Glutathione peroxidase-like [52901] (29 proteins)

10. c.47.1.11: Thioredoxin-like 2Fe-2S ferredoxin [52918] (1 protein)

11. c.47.1.12: ArsC-like [69518] (4 proteins)
    Pfam PF03960

12. c.47.1.13: DsbA-like [100953] (4 proteins)
    contains an all-alpha subdomain insertion

13. c.47.1.14: SH3BGR (SH3-binding, glutamic acid-rich protein-like) [102446] (2 proteins)
    related to glutaredoxin 1 (GRX1) but lacks both conserved cysteine residues
    automatically mapped to Pfam PF04908

14. c.47.1.15: KaiB-like [102449] (3 proteins)
    Pfam PF07689; contains members with alternative folds

15. c.47.1.16: Txnl5-like [110612] (1 protein)
    Pfam PF06110

16. c.47.1.17: YuzD-like [117605] (1 protein)
    Pfam PF07315

17. c.47.1.18: YKR049C-like [142395] (1 protein)
    Pfam PF07955; DUF1687; contains an all-alpha insert subdomain

18. c.47.1.19: Atu2684-like [142398] (1 protein)
    Pfam PF06764; DUF1223; contains extra C-terminal domain of Immunoglobulin-like fold (48725), intimately associated with the N-terminal thioredixin-like domain and contributing to the active site

19. c.47.1.20: HyaE-like [142401] (2 proteins)
    Pfam PF07449; have evolved a different function; contains no conserved cysteine residues

20. c.47.1.21: NQO2-like [142405] (2 proteins)
    complex I 24 kDa subunit; contains 2Fe-2S cluster in the active site; includes extra N-terminal four-helical bundle
    automatically mapped to Pfam PF01257

21. c.47.1.22: Mitochondrial ribosomal protein L51/S25/CI-B8 domain [142408] (1 protein)
    Pfam PF05047; "minimalized" version of the thioredoxin-like fold; variable positions for cysteine residues in the putative active site

22. c.47.1.23: Selenoprotein W-related [142411] (4 proteins)
    Pfam PF05169; "minimalized" version of the thioredoxin-like fold

23. c.47.1.24: UAS domain [159589] (1 protein)
    SMART 00594

24. c.47.1.0: automated matches [191312] (1 protein)
    not a true family

More info for Superfamily c.47.1: Thioredoxin-like

Timeline for Superfamily c.47.1: Thioredoxin-like:

• Superfamily c.47.1: Thioredoxin-like first appeared (with stable ids) in SCOP 1.55
  
• Superfamily c.47.1: Thioredoxin-like appears in SCOPe 2.05
  
• Superfamily c.47.1: Thioredoxin-like appears in SCOPe 2.07
  
• Superfamily c.47.1: Thioredoxin-like appears in the current release, SCOPe 2.08