EC Number   |
Subunits |
Reference |
|---|
   3.6.4.B7 | ? |
x * 35867, calculated from sequence |
-, 726059 |
| 3.6.4.B7 | ? |
x * 35900, about, sequence calculation |
-, 757584 |
| 3.6.4.B7 | ? |
x * 38400, SDS-PAGE, calculated from sequence |
725340 |
| 3.6.4.B7 | ? |
x * 49400, recombinant enzyme, SDS-PAGE |
-, 757864 |
| 3.6.4.B7 | More |
enzyme domain organization, overview |
-, 733620 |
| 3.6.4.B7 | More |
enzyme domain organization, structure comparisons, overview |
-, 733620 |
| 3.6.4.B7 | More |
highly electrostatic secondary structure elements of the ATPase domain of RadA: helix 1 (D352-K367), loop 1 (R496-R503) and loop 2 (E524-D529) |
-, 757833 |
| 3.6.4.B7 | More |
primary structures of PhoRadA intein, secondary structure based on the determined NMR model. Comparison between the NMR and crystal structures of PhoRadA intein |
-, 734472 |
| 3.6.4.B7 | More |
RadA has four well-conserved motifs: a potential C4-type zinc-binding motif at the N-terminal domain, a central canonical RecA-like ATPase domain (H1-H4 motifs) and KNRFG motif, and the P/LonC domain at the C-terminus domain |
-, 757864 |
| 3.6.4.B7 | More |
RadA is a 460 amino acid protein that has three well-conserved domains also found in other proteins, as well as a 5-amino acid motif highly conserved among radA orthologs. The N-terminal 30 amino acids form a putative zinc-finger domain with a C4 motif, CXXC-Xn-CXXC |
756571 |
