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monomer
1 * 64000, mutant lacking the RING-finger domain, calculated from sequence
octamer
a tetramer of dimers, the dimer is the fundamental catalytic unit
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x * 80000, about, recombinant His6-tagged enzyme, SDS-PAGE
?
x * 90000, about, recombinant full-length enzyme, SDS-PAGE
dimer
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tertiary structure of SB transposase and protein core, overview
dimer
2 * 68000, wild-type, calulated from sequence
homodimer
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homodimer
2 * 16379, calculated from sequence
additional information
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
additional information
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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
additional information
the full length Tgf2 transposase (L-Tgf2TPase) consisted of several functional domains: an N-terminal BED zinc finger domain (Cx2Cx19Hx4H, 65-120 aa) involved in DNA binding, dimerization domain defined by amino acids 153-213, presumably involved in the formation of oligomers, as well as in DNA binding, and a C-terminus RNase-H domain comprises amino acids 211-683 presumably the core catalytic domain for DNA excision and transposition. Three conserved amino acids residues (DDE) are identified in the RNase-H catalytic domain of Tgf2 transposase, residues of the DDE (D228, D295 and E648) are extremely close in their spatial distribution. A CX2H motif within the RNase-H catalytic domain of Tgf2 transposase is also identified, which which functions as insertion domain for the correct positioning of the final E648 residue of the catalytic triad in the active site. A monopartite nuclear localization signal (NLS, 656-670 aa) is found at the C-terminus. Domain organization, modeling, overview
additional information
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the full length Tgf2 transposase (L-Tgf2TPase) consisted of several functional domains: an N-terminal BED zinc finger domain (Cx2Cx19Hx4H, 65-120 aa) involved in DNA binding, dimerization domain defined by amino acids 153-213, presumably involved in the formation of oligomers, as well as in DNA binding, and a C-terminus RNase-H domain comprises amino acids 211-683 presumably the core catalytic domain for DNA excision and transposition. Three conserved amino acids residues (DDE) are identified in the RNase-H catalytic domain of Tgf2 transposase, residues of the DDE (D228, D295 and E648) are extremely close in their spatial distribution. A CX2H motif within the RNase-H catalytic domain of Tgf2 transposase is also identified, which which functions as insertion domain for the correct positioning of the final E648 residue of the catalytic triad in the active site. A monopartite nuclear localization signal (NLS, 656-670 aa) is found at the C-terminus. Domain organization, modeling, overview
additional information
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in contrast to other members of the P-element superfamily, it has unusually long terminal inverted-repeats (TIRs) that resemble those of Foldback elements. The synaptic complex between Galileo ends may be a complicated structure containing higher-order multimers of the transposase
additional information
P13988; P13989
trypsin peptide mapping of TnsC
additional information
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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
additional information
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the SB100X catalytic domain assumes an RNaseH-fold with all catalytic residues assembled in the active site, it contains conserved alpha-helices and beta-strands, structure modeling of the SB transposase/transposon end/target DNA complex using crystal structure, PDB ID 3HOS, overview
additional information
while isolated dimers are active in vitro for all the chemical steps of transposition, only octamers are active in vivo. The octamer can provide not only multiple specific DNA-binding domains to recognize repeated subterminal sequences within the transposon ends, which are important for activity, but also multiple non-specific DNA binding surfaces for target capture, bipartite DNA recognition at hAT transposon ends. Overall architecture of the Hermes transpososome, the nucleoprotein assembly that carries out DNA transposition, overview
additional information
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while isolated dimers are active in vitro for all the chemical steps of transposition, only octamers are active in vivo. The octamer can provide not only multiple specific DNA-binding domains to recognize repeated subterminal sequences within the transposon ends, which are important for activity, but also multiple non-specific DNA binding surfaces for target capture, bipartite DNA recognition at hAT transposon ends. Overall architecture of the Hermes transpososome, the nucleoprotein assembly that carries out DNA transposition, overview
additional information
the C-terminal 7 residues of the RING-finger domain are critical for dimer formation
additional information
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
additional information
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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