SCOPe 2.04: Domain d1hqoa2: 1hqo A:106-200

Lineage for d1hqoa2 (1hqo A:106-200)

1. Root: SCOPe 2.04

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)

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

6. Protein Yeast prion protein ure2p, nitrogen regulation fragment [52886] (1 species)
   similar to class phi enzymes

7. Species Baker's yeast (Saccharomyces cerevisiae) [TaxId:4932] [52887] (8 PDB entries)

8. Domain d1hqoa2: 1hqo A:106-200 [33043]
   Other proteins in same PDB: d1hqoa1, d1hqob1

Details for d1hqoa2

PDB Entry: 1hqo, 2.3 Å

PDB Description: crystal structure of the nitrogen regulation fragment of the yeast prion protein ure2p

PDB Compounds: (A:) ure2 protein

SCOPe Domain Sequences for d1hqoa2:

Sequence; same for both SEQRES and ATOM records:

>d1hqoa2 c.47.1.5 (A:106-200) Yeast prion protein ure2p, nitrogen regulation fragment {Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932]}
fqeqplegytlfshrsapngfkvaivlselgfhyntifldfnlgehrapefvsvnpnarv
palidhgmdnlsiwesgaillhlvnkyyketgnpl

Timeline for d1hqoa2:

• d1hqoa2 first appeared (with stable ids) in SCOP 1.55
  
• d1hqoa2 appears in SCOPe 2.03
  
• d1hqoa2 appears in SCOPe 2.05
  
• d1hqoa2 appears in the current release, SCOPe 2.08