ferritin-like domain-containing protein [Sinorhizobium meliloti]
ferritin-like domain-containing protein( domain architecture ID 10007837)
uncharacterized ferritin-like iron-binding domain containing protein similar to Escherichia coli YciF, a bacterial stress response protein
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
YciE | COG3685 | Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism]; |
3-163 | 8.71e-73 | ||||
Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism]; : Pssm-ID: 442901 Cd Length: 165 Bit Score: 215.85 E-value: 8.71e-73
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Name | Accession | Description | Interval | E-value | ||||
YciE | COG3685 | Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism]; |
3-163 | 8.71e-73 | ||||
Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism]; Pssm-ID: 442901 Cd Length: 165 Bit Score: 215.85 E-value: 8.71e-73
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DUF892 | pfam05974 | Domain of unknown function (DUF892); This family consists of several hypothetical bacterial ... |
8-162 | 8.78e-64 | ||||
Domain of unknown function (DUF892); This family consists of several hypothetical bacterial proteins of unknown function. Pssm-ID: 428701 Cd Length: 156 Bit Score: 192.43 E-value: 8.78e-64
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YciF | cd07909 | YciF bacterial stress response protein, ferritin-like iron-binding domain; YciF is a bacterial ... |
9-154 | 8.81e-64 | ||||
YciF bacterial stress response protein, ferritin-like iron-binding domain; YciF is a bacterial protein of unknown function that is up-regulated when bacteria experience stress conditions, and is highly conserved in a broad range of bacterial species. YciF has a ferritin-like domain. 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: 153118 Cd Length: 147 Bit Score: 192.40 E-value: 8.81e-64
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Name | Accession | Description | Interval | E-value | ||||
YciE | COG3685 | Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism]; |
3-163 | 8.71e-73 | ||||
Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism]; Pssm-ID: 442901 Cd Length: 165 Bit Score: 215.85 E-value: 8.71e-73
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DUF892 | pfam05974 | Domain of unknown function (DUF892); This family consists of several hypothetical bacterial ... |
8-162 | 8.78e-64 | ||||
Domain of unknown function (DUF892); This family consists of several hypothetical bacterial proteins of unknown function. Pssm-ID: 428701 Cd Length: 156 Bit Score: 192.43 E-value: 8.78e-64
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YciF | cd07909 | YciF bacterial stress response protein, ferritin-like iron-binding domain; YciF is a bacterial ... |
9-154 | 8.81e-64 | ||||
YciF bacterial stress response protein, ferritin-like iron-binding domain; YciF is a bacterial protein of unknown function that is up-regulated when bacteria experience stress conditions, and is highly conserved in a broad range of bacterial species. YciF has a ferritin-like domain. 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: 153118 Cd Length: 147 Bit Score: 192.40 E-value: 8.81e-64
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Blast search parameters | ||||
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