bacterioferritin [Marinomonas profundi]
bacterioferritin( domain architecture ID 10097036)
bacterioferritin regulates iron homeostasis in bacteria by capturing soluble but potentially toxic Fe(2+) and by compartmentalizing it in the form of a bioavailable ferric mineral inside the protein's hollow cavity
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Bacterioferritin | cd00907 | Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ... |
2-155 | 2.17e-76 | |||
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as cytochrome b1, are members of a broad superfamily of ferritin-like diiron-carboxylate proteins. Similar to ferritin in architecture, Bfr forms an oligomer of 24 subunits that assembles to form a hollow sphere with 432 symmetry. Up to 12 heme cofactor groups (iron protoporphyrin IX or coproporphyrin III) are bound between dimer pairs. The role of the heme is unknown, although it may be involved in mediating iron-core reduction and iron release. Each subunit is composed of a four-helix bundle which carries a diiron ferroxidase center; it is here that initial oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of ferric-hydroxyphosphate at the core. Some bacterioferritins are composed of two subunit types, one conferring heme-binding ability (alpha) and the other (beta) bestowing ferroxidase activity. : Pssm-ID: 153099 Cd Length: 153 Bit Score: 223.96 E-value: 2.17e-76
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Name | Accession | Description | Interval | E-value | |||
Bacterioferritin | cd00907 | Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ... |
2-155 | 2.17e-76 | |||
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as cytochrome b1, are members of a broad superfamily of ferritin-like diiron-carboxylate proteins. Similar to ferritin in architecture, Bfr forms an oligomer of 24 subunits that assembles to form a hollow sphere with 432 symmetry. Up to 12 heme cofactor groups (iron protoporphyrin IX or coproporphyrin III) are bound between dimer pairs. The role of the heme is unknown, although it may be involved in mediating iron-core reduction and iron release. Each subunit is composed of a four-helix bundle which carries a diiron ferroxidase center; it is here that initial oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of ferric-hydroxyphosphate at the core. Some bacterioferritins are composed of two subunit types, one conferring heme-binding ability (alpha) and the other (beta) bestowing ferroxidase activity. Pssm-ID: 153099 Cd Length: 153 Bit Score: 223.96 E-value: 2.17e-76
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Bfr | COG2193 | Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism]; |
3-155 | 1.68e-75 | |||
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism]; Pssm-ID: 441796 Cd Length: 152 Bit Score: 221.99 E-value: 1.68e-75
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bfr | TIGR00754 | bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ... |
1-156 | 1.00e-47 | |||
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to Bacteria, has also been designated cytochrome b1 and cytochrome b-557.Bacterioferritin is a homomultimer most species. In Neisseria gonorrhoeae, Synechocystis PCC6803, Magnetospirillum magnetotacticum, and Pseudomonas aeruginosa, two types of subunit are found in a heteromultimeric complex, with each species having one member of each type. At present, both types of subunit are including in this single model. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 162022 Cd Length: 157 Bit Score: 151.89 E-value: 1.00e-47
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PRK10635 | PRK10635 | bacterioferritin; Provisional |
1-155 | 4.89e-47 | |||
bacterioferritin; Provisional Pssm-ID: 182604 Cd Length: 158 Bit Score: 149.98 E-value: 4.89e-47
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Ferritin | pfam00210 | Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ... |
8-144 | 6.29e-32 | |||
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: 110.84 E-value: 6.29e-32
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DNAstvprot_Halo | NF041388 | DNA starvation/stationary phase protection protein DpsA; |
4-130 | 9.28e-06 | |||
DNA starvation/stationary phase protection protein DpsA; Pssm-ID: 469279 [Multi-domain] Cd Length: 171 Bit Score: 43.40 E-value: 9.28e-06
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Name | Accession | Description | Interval | E-value | |||
Bacterioferritin | cd00907 | Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ... |
2-155 | 2.17e-76 | |||
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as cytochrome b1, are members of a broad superfamily of ferritin-like diiron-carboxylate proteins. Similar to ferritin in architecture, Bfr forms an oligomer of 24 subunits that assembles to form a hollow sphere with 432 symmetry. Up to 12 heme cofactor groups (iron protoporphyrin IX or coproporphyrin III) are bound between dimer pairs. The role of the heme is unknown, although it may be involved in mediating iron-core reduction and iron release. Each subunit is composed of a four-helix bundle which carries a diiron ferroxidase center; it is here that initial oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of ferric-hydroxyphosphate at the core. Some bacterioferritins are composed of two subunit types, one conferring heme-binding ability (alpha) and the other (beta) bestowing ferroxidase activity. Pssm-ID: 153099 Cd Length: 153 Bit Score: 223.96 E-value: 2.17e-76
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Bfr | COG2193 | Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism]; |
3-155 | 1.68e-75 | |||
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism]; Pssm-ID: 441796 Cd Length: 152 Bit Score: 221.99 E-value: 1.68e-75
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bfr | TIGR00754 | bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ... |
1-156 | 1.00e-47 | |||
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to Bacteria, has also been designated cytochrome b1 and cytochrome b-557.Bacterioferritin is a homomultimer most species. In Neisseria gonorrhoeae, Synechocystis PCC6803, Magnetospirillum magnetotacticum, and Pseudomonas aeruginosa, two types of subunit are found in a heteromultimeric complex, with each species having one member of each type. At present, both types of subunit are including in this single model. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 162022 Cd Length: 157 Bit Score: 151.89 E-value: 1.00e-47
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PRK10635 | PRK10635 | bacterioferritin; Provisional |
1-155 | 4.89e-47 | |||
bacterioferritin; Provisional Pssm-ID: 182604 Cd Length: 158 Bit Score: 149.98 E-value: 4.89e-47
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Ferritin | pfam00210 | Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ... |
8-144 | 6.29e-32 | |||
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: 110.84 E-value: 6.29e-32
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Ferritin_like | cd00657 | Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ... |
9-139 | 1.25e-11 | |||
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF). Pssm-ID: 153097 Cd Length: 130 Bit Score: 58.28 E-value: 1.25e-11
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DNAstvprot_Halo | NF041388 | DNA starvation/stationary phase protection protein DpsA; |
4-130 | 9.28e-06 | |||
DNA starvation/stationary phase protection protein DpsA; Pssm-ID: 469279 [Multi-domain] Cd Length: 171 Bit Score: 43.40 E-value: 9.28e-06
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Blast search parameters | ||||
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