MULTISPECIES: Dps family protein [Staphylococcus]
Dps family protein( domain architecture ID 10002504)
Dps family protein similar to DNA starvation/stationary phase protection protein that binds and protects DNA from cleavage caused by reactive oxygen species; belongs to the ferritin-like superfamily of diiron-containing four-helix-bundle proteins
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Dps | COG0783 | DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and ... |
1-146 | 2.71e-62 | |||
DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and metabolism, Defense mechanisms]; : Pssm-ID: 440546 [Multi-domain] Cd Length: 156 Bit Score: 188.12 E-value: 2.71e-62
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Dps | COG0783 | DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and ... |
1-146 | 2.71e-62 | |||
DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and metabolism, Defense mechanisms]; Pssm-ID: 440546 [Multi-domain] Cd Length: 156 Bit Score: 188.12 E-value: 2.71e-62
|
|||||||
DPS | cd01043 | DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved ... |
9-146 | 6.93e-62 | |||
DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic. Pssm-ID: 153102 Cd Length: 139 Bit Score: 186.60 E-value: 6.93e-62
|
|||||||
Ferritin | pfam00210 | Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ... |
8-146 | 2.83e-29 | |||
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins. Pssm-ID: 459712 Cd Length: 141 Bit Score: 103.91 E-value: 2.83e-29
|
|||||||
PRK09448 | PRK09448 | DNA starvation/stationary phase protection protein Dps; Provisional |
5-146 | 3.22e-19 | |||
DNA starvation/stationary phase protection protein Dps; Provisional Pssm-ID: 236521 Cd Length: 162 Bit Score: 78.49 E-value: 3.22e-19
|
|||||||
DNAstvprot_Halo | NF041388 | DNA starvation/stationary phase protection protein DpsA; |
7-127 | 2.91e-17 | |||
DNA starvation/stationary phase protection protein DpsA; Pssm-ID: 469279 [Multi-domain] Cd Length: 171 Bit Score: 73.83 E-value: 2.91e-17
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Dps | COG0783 | DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and ... |
1-146 | 2.71e-62 | |||
DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and metabolism, Defense mechanisms]; Pssm-ID: 440546 [Multi-domain] Cd Length: 156 Bit Score: 188.12 E-value: 2.71e-62
|
|||||||
DPS | cd01043 | DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved ... |
9-146 | 6.93e-62 | |||
DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic. Pssm-ID: 153102 Cd Length: 139 Bit Score: 186.60 E-value: 6.93e-62
|
|||||||
Ferritin | pfam00210 | Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ... |
8-146 | 2.83e-29 | |||
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins. Pssm-ID: 459712 Cd Length: 141 Bit Score: 103.91 E-value: 2.83e-29
|
|||||||
PRK09448 | PRK09448 | DNA starvation/stationary phase protection protein Dps; Provisional |
5-146 | 3.22e-19 | |||
DNA starvation/stationary phase protection protein Dps; Provisional Pssm-ID: 236521 Cd Length: 162 Bit Score: 78.49 E-value: 3.22e-19
|
|||||||
DNAstvprot_Halo | NF041388 | DNA starvation/stationary phase protection protein DpsA; |
7-127 | 2.91e-17 | |||
DNA starvation/stationary phase protection protein DpsA; Pssm-ID: 469279 [Multi-domain] Cd Length: 171 Bit Score: 73.83 E-value: 2.91e-17
|
|||||||
Bfr | COG2193 | Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism]; |
5-141 | 1.48e-06 | |||
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism]; Pssm-ID: 441796 Cd Length: 152 Bit Score: 44.80 E-value: 1.48e-06
|
|||||||
Blast search parameters | ||||
|