ferritin-3, chloroplastic-like [Hibiscus syriacus]
Protein Classification
ferritin( domain architecture ID 10099405)
ferritin is the primary iron storage protein of most living organisms and belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins. The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms.
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| Euk_Ferritin | cd01056 | eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ... |
87-249 | 3.89e-65 | ||||
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary iron storage proteins of most living organisms and members of a broad superfamily of ferritin-like diiron-carboxylate proteins. The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains arranged in 432 symmetry. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms. In vertebrates, two types of chains (subunits) have been characterized, H or M (fast) and L (slow), which differ in rates of iron uptake and mineralization. Fe(II) oxidation in the H/M subunits take place initially at the ferroxidase center, a carboxylate-bridged diiron center, located within the subunit four-helix bundle. In a complementary role, negatively charged residues on the protein shell inner surface of the L subunits promote ferrihydrite nucleation. Most plant ferritins combine both oxidase and nucleation functions in one chain: they have four interior glutamate residues as well as seven ferroxidase center residues. : Pssm-ID: 153114 Cd Length: 161 Bit Score: 200.08 E-value: 3.89e-65
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| Name | Accession | Description | Interval | E-value | ||||
| Euk_Ferritin | cd01056 | eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ... |
87-249 | 3.89e-65 | ||||
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary iron storage proteins of most living organisms and members of a broad superfamily of ferritin-like diiron-carboxylate proteins. The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains arranged in 432 symmetry. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms. In vertebrates, two types of chains (subunits) have been characterized, H or M (fast) and L (slow), which differ in rates of iron uptake and mineralization. Fe(II) oxidation in the H/M subunits take place initially at the ferroxidase center, a carboxylate-bridged diiron center, located within the subunit four-helix bundle. In a complementary role, negatively charged residues on the protein shell inner surface of the L subunits promote ferrihydrite nucleation. Most plant ferritins combine both oxidase and nucleation functions in one chain: they have four interior glutamate residues as well as seven ferroxidase center residues. Pssm-ID: 153114 Cd Length: 161 Bit Score: 200.08 E-value: 3.89e-65
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| Ferritin | pfam00210 | Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ... |
90-237 | 7.64e-19 | ||||
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: 80.02 E-value: 7.64e-19
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| FtnA | COG1528 | Ferritin [Inorganic ion transport and metabolism]; |
90-251 | 1.22e-18 | ||||
Ferritin [Inorganic ion transport and metabolism]; Pssm-ID: 441137 Cd Length: 158 Bit Score: 80.17 E-value: 1.22e-18
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| Name | Accession | Description | Interval | E-value | ||||
| Euk_Ferritin | cd01056 | eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ... |
87-249 | 3.89e-65 | ||||
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary iron storage proteins of most living organisms and members of a broad superfamily of ferritin-like diiron-carboxylate proteins. The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains arranged in 432 symmetry. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms. In vertebrates, two types of chains (subunits) have been characterized, H or M (fast) and L (slow), which differ in rates of iron uptake and mineralization. Fe(II) oxidation in the H/M subunits take place initially at the ferroxidase center, a carboxylate-bridged diiron center, located within the subunit four-helix bundle. In a complementary role, negatively charged residues on the protein shell inner surface of the L subunits promote ferrihydrite nucleation. Most plant ferritins combine both oxidase and nucleation functions in one chain: they have four interior glutamate residues as well as seven ferroxidase center residues. Pssm-ID: 153114 Cd Length: 161 Bit Score: 200.08 E-value: 3.89e-65
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| Ferritin | cd00904 | Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living ... |
88-249 | 2.55e-41 | ||||
Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living organisms and members of a broad superfamily of ferritin-like diiron-carboxylate proteins. The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains arranged in 432 symmetry. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms. In vertebrates, two types of chains (subunits) have been characterized, H or M (fast) and L (slow), which differ in rates of iron uptake and mineralization. Bacterial non-heme ferritins are composed only of H chains. Fe(II) oxidation in the H/M subunits take place initially at the ferroxidase center, a carboxylate-bridged diiron center, located within the subunit four-helix bundle. In a complementary role, negatively charged residues on the protein shell inner surface of the L subunits promote ferrihydrite nucleation. Most plant ferritins combine both oxidase and nucleation functions in one chain: they have four interior glutamate residues as well as seven ferroxidase center residues. Pssm-ID: 153098 Cd Length: 160 Bit Score: 139.32 E-value: 2.55e-41
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| Nonheme_Ferritin | cd01055 | nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ... |
90-251 | 4.88e-20 | ||||
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The ferritin protein shell is composed of 24 protein subunits arranged in 432 symmetry. Each protein subunit, a four-helix bundle with a fifth short terminal helix, contains a dinuclear ferroxidase center (H type). Unique to this group of proteins is a third metal site in the ferroxidase center. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite. Pssm-ID: 153113 Cd Length: 156 Bit Score: 83.69 E-value: 4.88e-20
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| Ferritin | pfam00210 | Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ... |
90-237 | 7.64e-19 | ||||
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: 80.02 E-value: 7.64e-19
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| FtnA | COG1528 | Ferritin [Inorganic ion transport and metabolism]; |
90-251 | 1.22e-18 | ||||
Ferritin [Inorganic ion transport and metabolism]; Pssm-ID: 441137 Cd Length: 158 Bit Score: 80.17 E-value: 1.22e-18
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