SCOPe 2.08: Domain d1exia2: 1exi A:121-277

Lineage for d1exia2 (1exi A:121-277)

1. Root: SCOPe 2.08

2. Class d: Alpha and beta proteins (a+b) [53931] (396 folds)

3. Fold d.60: Probable bacterial effector-binding domain [55135] (1 superfamily)
   duplication of beta-alpha-beta(2) motif: antiparallel beta sheet forms barrel (n=6, S=12)

4. Superfamily d.60.1: Probable bacterial effector-binding domain [55136] (5 families)

5. Family d.60.1.1: Multidrug-binding domain of transcription activator BmrR [55137] (2 proteins)
   automatically mapped to Pfam PF06445

6. Protein Multidrug-binding domain of transcription activator BmrR [55138] (1 species)

7. Species Bacillus subtilis [TaxId:1423] [55139] (6 PDB entries)
   Uniprot P39075

8. Domain d1exia2: 1exi A:121-277 [39531]
   Other proteins in same PDB: d1exia1
   protein/DNA complex; complexed with 118, zn

Details for d1exia2

PDB Entry: 1exi, 3.12 Å

PDB Description: crystal structure of transcription activator bmrr, from b. subtilis, bound to 21 base pair bmr operator and tpsb

PDB Compounds: (A:) multidrug-efflux transporter regulator

SCOPe Domain Sequences for d1exia2:

Sequence; same for both SEQRES and ATOM records:

>d1exia2 d.60.1.1 (A:121-277) Multidrug-binding domain of transcription activator BmrR {Bacillus subtilis [TaxId: 1423]}
lgevfvldeeeiriiqteaegigpenvlnasysklkkfiesadgftnnsygatfsfqpyt
sidemtyrhiftpvltnkqissitpdmeittipkgryaciaynfspehyflnlqklikyi
adrqltvvsdvyeliipihyspkkqeeyrvemkiria

Timeline for d1exia2:

• d1exia2 first appeared (with stable ids) in SCOP 1.55
  
• d1exia2 appears in SCOPe 2.07