SCOPe 2.08: Domain d1feba1: 1feb A:1-169,A:287-357

Lineage for d1feba1 (1feb A:1-169,A:287-357)

1. Root: SCOPe 2.08

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

3. Fold c.3: FAD/NAD(P)-binding domain [51904] (1 superfamily)
   core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander

4. Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (9 families)

5. Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (25 proteins)
   duplication: both domains have similar folds and functions
   most members of the family contain common C-terminal alpha+beta domain

6. Protein Trypanothione reductase, N- and C-terminal domain [418954] (3 species)

7. Species Crithidia fasciculata [TaxId:5656] [419410] (6 PDB entries)

8. Domain d1feba1: 1feb A:1-169,A:287-357 [30493]
   Other proteins in same PDB: d1feba2, d1feba3, d1febb2, d1febb3
   complexed with fad
   has additional insertions and/or extensions that are not grouped together

Details for d1feba1

PDB Entry: 1feb, 2 Å

PDB Description: unliganded crithidia fasciculata trypanothione reductase at 2.0 angstrom resolution

PDB Compounds: (A:) trypanothione reductase

SCOPe Domain Sequences for d1feba1:

Sequence; same for both SEQRES and ATOM records:

>d1feba1 c.3.1.5 (A:1-169,A:287-357) Trypanothione reductase, N- and C-terminal domain {Crithidia fasciculata [TaxId: 5656]}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d

Timeline for d1feba1:

• d1feba1 first appeared (with stable ids) in SCOP 1.55
  
• d1feba1 appears in SCOPe 2.07