Filopodia upregulated, FAM65; PL48 is associated with cytotrophoblast and lineage-specific ...
118-530
4.94e-160
Filopodia upregulated, FAM65; PL48 is associated with cytotrophoblast and lineage-specific HL-60 cell differentiation. The N-terminal part of the family is found to induce the formation of filopodia. It is found in vertebrates.
The actual alignment was detected with superfamily member pfam15903:
Pssm-ID: 464930 Cd Length: 297 Bit Score: 480.74 E-value: 4.94e-160
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
1160-1304
4.27e-62
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).
The actual alignment was detected with superfamily member cd00904:
Pssm-ID: 469698 Cd Length: 160 Bit Score: 208.65 E-value: 4.27e-62
Filopodia upregulated, FAM65; PL48 is associated with cytotrophoblast and lineage-specific ...
118-530
4.94e-160
Filopodia upregulated, FAM65; PL48 is associated with cytotrophoblast and lineage-specific HL-60 cell differentiation. The N-terminal part of the family is found to induce the formation of filopodia. It is found in vertebrates.
Pssm-ID: 464930 Cd Length: 297 Bit Score: 480.74 E-value: 4.94e-160
Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living ...
1160-1304
4.27e-62
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: 208.65 E-value: 4.27e-62
Filopodia upregulated, FAM65; PL48 is associated with cytotrophoblast and lineage-specific ...
118-530
4.94e-160
Filopodia upregulated, FAM65; PL48 is associated with cytotrophoblast and lineage-specific HL-60 cell differentiation. The N-terminal part of the family is found to induce the formation of filopodia. It is found in vertebrates.
Pssm-ID: 464930 Cd Length: 297 Bit Score: 480.74 E-value: 4.94e-160
Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living ...
1160-1304
4.27e-62
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: 208.65 E-value: 4.27e-62
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
1160-1305
4.76e-57
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: 194.30 E-value: 4.76e-57
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
1160-1263
7.03e-09
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: 55.96 E-value: 7.03e-09
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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