demethoxyubiquinone hydroxylase (DMQH) family protein which is a member of the ferritin-like, diiron-carboxylate family of diiron-containing oxidases/hydroxylases; binds iron in the diiron center
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
9-176
1.02e-95
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 amino acids, that contains two conserved motifs. One of these DXEXXH may be part of an enzyme active site.
:
Pssm-ID: 460854 Cd Length: 167 Bit Score: 274.38 E-value: 1.02e-95
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
9-176
1.02e-95
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 amino acids, that contains two conserved motifs. One of these DXEXXH may be part of an enzyme active site.
Pssm-ID: 460854 Cd Length: 167 Bit Score: 274.38 E-value: 1.02e-95
Demethoxyubiquinone hydroxylase, ferritin-like diiron-binding domain; Demethoxyubiquinone hydroxylases (DMQH) are members of the ferritin-like, diiron-carboxylate family which are present in eukaryotes (the CLK-1/CAT5 family) and prokaryotes (the Coq7 family). DMQH participates in one of the last steps of ubiquinone biosysnthesis and is responsible for DMQ hydroxylation, resulting in the formation of hydroxyubiquinone, a precursor of ubiquinone. CLK-1 is a mitochondrial inner membrane protein and Coq7 is a proposed interfacial integral membrane protein. Mutations in the Caenorhabditis elegans gene clk-1 affect biological timing and extend longevity. The conserved residues of a diiron center are present in this domain.
Pssm-ID: 153101 Cd Length: 165 Bit Score: 257.84 E-value: 3.23e-89
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme ...
8-179
5.48e-58
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme transport and metabolism]; Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 442184 Cd Length: 208 Bit Score: 180.41 E-value: 5.48e-58
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
9-176
1.02e-95
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 amino acids, that contains two conserved motifs. One of these DXEXXH may be part of an enzyme active site.
Pssm-ID: 460854 Cd Length: 167 Bit Score: 274.38 E-value: 1.02e-95
Demethoxyubiquinone hydroxylase, ferritin-like diiron-binding domain; Demethoxyubiquinone hydroxylases (DMQH) are members of the ferritin-like, diiron-carboxylate family which are present in eukaryotes (the CLK-1/CAT5 family) and prokaryotes (the Coq7 family). DMQH participates in one of the last steps of ubiquinone biosysnthesis and is responsible for DMQ hydroxylation, resulting in the formation of hydroxyubiquinone, a precursor of ubiquinone. CLK-1 is a mitochondrial inner membrane protein and Coq7 is a proposed interfacial integral membrane protein. Mutations in the Caenorhabditis elegans gene clk-1 affect biological timing and extend longevity. The conserved residues of a diiron center are present in this domain.
Pssm-ID: 153101 Cd Length: 165 Bit Score: 257.84 E-value: 3.23e-89
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme ...
8-179
5.48e-58
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme transport and metabolism]; Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 442184 Cd Length: 208 Bit Score: 180.41 E-value: 5.48e-58
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
13-150
1.13e-08
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: 50.96 E-value: 1.13e-08
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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