3-demethoxyubiquinol 3-hydroxylase catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol during ubiquinone biosynthesis; belongs to the ferritin-like, diiron-carboxylate family of diiron-containing oxidases/hydroxylases that bind iron in the diiron center
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme ...
4-211
8.56e-111
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: 315.62 E-value: 8.56e-111
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: 217.01 E-value: 1.82e-72
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
47-208
1.67e-57
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: 178.85 E-value: 1.67e-57
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme ...
4-211
8.56e-111
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: 315.62 E-value: 8.56e-111
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: 217.01 E-value: 1.82e-72
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
47-208
1.67e-57
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: 178.85 E-value: 1.67e-57
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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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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