Lineage for Protein: Transcription activator BmrR
- Root: SCOP 1.67
Class a: All alpha proteins [46456] (202 folds) 
Fold a.6: Putative DNA-binding domain [46954] (1 superfamily)
core: 3 helices; architecture is similar to that of the "winged helix" fold but topology is differentSuperfamily a.6.1: Putative DNA-binding domain [46955] (7 families) 
Family a.6.1.3: DNA-binding N-terminal domain of transcription activators [46962] (4 proteins)
includes a dimerisation, antiparallel coiled-coil subdomain
Protein Transcription activator BmrR [46963] (1 species)
followed by long alpha-helical linker
Species:
Bacillus subtilis [TaxId:1423] [46964] (2 PDB entries) - Domain for 1exi:
Domain d1exia1: 1exi A:3-120 [16310]
Other proteins in same PDB: d1exia2
protein/DNA complex; complexed with 118, zn
- Domain for 1exj:
Domain d1exja1: 1exj A:3-120 [16309]
Other proteins in same PDB: d1exja2
protein/DNA complex; complexed with 119, na, zn
- Domain for 1exi:
More info for Protein Transcription activator BmrR from a.6.1.3: DNA-binding N-terminal domain of transcription activators
Timeline for Protein Transcription activator BmrR from a.6.1.3: DNA-binding N-terminal domain of transcription activators:
- Protein Transcription activator BmrR from a.6.1.3: DNA-binding N-terminal domain of transcription activators first appeared (with stable ids) in SCOP 1.55, called Protein DNA-binding domain of transcription activator BmrR from a.6.1.3: DNA-binding domain of transcription activator BmrR
- Protein Transcription activator BmrR from a.6.1.3: DNA-binding N-terminal domain of transcription activators appears in SCOP 1.65
- Protein Transcription activator BmrR from a.6.1.3: DNA-binding N-terminal domain of transcription activators appears in SCOP 1.69
- Protein Transcription activator BmrR from a.6.1.3: DNA-binding N-terminal domain of transcription activators appears in the current release, SCOPe 2.08