EC Number |
Subunits |
Reference |
---|
2.7.7.B22 | ? |
x * 80000, about, recombinant His6-tagged enzyme, SDS-PAGE |
739044 |
2.7.7.B22 | ? |
x * 90000, about, recombinant full-length enzyme, SDS-PAGE |
739041 |
2.7.7.B22 | dimer |
2 * 68000, wild-type, calulated from sequence |
760589 |
2.7.7.B22 | dimer |
tertiary structure of SB transposase and protein core, overview |
739123 |
2.7.7.B22 | homodimer |
- |
739105 |
2.7.7.B22 | homodimer |
2 * 16379, calculated from sequence |
723834 |
2.7.7.B22 | monomer |
1 * 64000, mutant lacking the RING-finger domain, calculated from sequence |
760589 |
2.7.7.B22 | More |
AcTPase is an 807aa protein and consists of three N-terminal nuclear localization signals (residues 44-206), a bipartite DNA binding domain (159-206), a catalytic core domain, and a highly conserved C-terminal dimerization domain (674-754). The catalytic core domain of AcTPase is thought to form a retroviral integrase-like fold |
739041 |
2.7.7.B22 | More |
amino acid sequence analysis based on Phyre2 prediction suggests that Tgf2 transposase contains an N-terminal zinc finger BED domain (65-120 aa), a helix-turn-helix (HTH) binding structure (163-201 aa) and an RNase-H domain (211-683 aa) with an insertion domain (362-493 aa). The cNLS mapper predicts the presence of a monopartite NLS (656-670 aa) of 15 amino acids (LLFSPKRARLDTNNF) within the RNase-H domain at the C-terminus of Tgf2 transposase. This predicted NLS is located downstream of the DDE residues (D228, D295 and E648). Construction of a 3D model of the NLS and DDE signature of Tgf2 transposase, molecular architecture of full-length Tgf2 transposase overview |
738323 |
2.7.7.B22 | More |
domain structure of SB transposase enzyme, and solution conformation of full-length DNA-binding domain of SB transposase, [15N,1H]-HSQC spectra, overview. The DNA-binding domain is predicted to have two subdomains, PAI and RED, containing three alpha-helices. Residues 97-123 represent a nuclear localization signal (NLS). The catalytic domain contains three conserved catalytic residues, the DDE motif. NMR solution structure of the PAI subdomain, overview |
739601 |