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Conserved domains on  [gi|564330617|ref|XP_006230170|]
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5-demethoxyubiquinone hydroxylase, mitochondrial isoform X3 [Rattus norvegicus]

Protein Classification

demethoxyubiquinone hydroxylase family protein( domain architecture ID 11141550)

demethoxyubiquinone hydroxylase (DMQH) family protein is a member of the ferritin-like, diiron-carboxylate family of diiron-containing oxidases/hydroxylases; binds iron in the diiron center; similar to human mitochondrial 5-demethoxyubiquinone hydroxylase

EC:  1.14.-.-
Gene Ontology:  GO:0008199|GO:0046872|GO:0016705|GO:0006744
PubMed:  11435415|8621692|8749363

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COQ7 pfam03232
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
 67-234 4.29e-96

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: 277.85  E-value: 4.29e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617   67 AAVDQIIRVDHAGEYGANRIYAGQMAVLGR-TSVGPVIQKMWDQEKNHLKKFNELMVAFRVRPTVLMPLWNVAGFALGAG 145
Cdd:pfam03232   1 ALLDRILRVDHAGELGAVRIYAGQLAVLRRdPELRPLIKHMWDQEKEHLATFNELLAEHRVRPTLLLPLWKVAGFALGAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617  146 TALLGKEGAMACTVAVEESIAHHYNNQIRMLMEEDAEKyeELLQVIKQFRDEELEHHDTGLEHDAELAPAYTLLKRLIQA 225
Cdd:pfam03232  81 TALLGKEAAMACTEAVETVIGEHYNDQLRELPEKEEDK--ELRAIIEQFRDDELEHLDTAVENGAEEAPAYPLLTNVIKA 158


                  ....*....
gi 564330617  226 GCSAAIYLS 234
Cdd:pfam03232 159 GCRVAIWLA 167
 
Name Accession Description Interval E-value
COQ7 pfam03232
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
 67-234 4.29e-96

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: 277.85  E-value: 4.29e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617   67 AAVDQIIRVDHAGEYGANRIYAGQMAVLGR-TSVGPVIQKMWDQEKNHLKKFNELMVAFRVRPTVLMPLWNVAGFALGAG 145
Cdd:pfam03232   1 ALLDRILRVDHAGELGAVRIYAGQLAVLRRdPELRPLIKHMWDQEKEHLATFNELLAEHRVRPTLLLPLWKVAGFALGAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617  146 TALLGKEGAMACTVAVEESIAHHYNNQIRMLMEEDAEKyeELLQVIKQFRDEELEHHDTGLEHDAELAPAYTLLKRLIQA 225
Cdd:pfam03232  81 TALLGKEAAMACTEAVETVIGEHYNDQLRELPEKEEDK--ELRAIIEQFRDDELEHLDTAVENGAEEAPAYPLLTNVIKA 158


                  ....*....
gi 564330617  226 GCSAAIYLS 234
Cdd:pfam03232 159 GCRVAIWLA 167
DMQH cd01042
Demethoxyubiquinone hydroxylase, ferritin-like diiron-binding domain; Demethoxyubiquinone ...
 69-236 1.02e-87

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: 256.69  E-value: 1.02e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617  69 VDQIIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKNHLKKFNELMVAFRVRPTVLMPLWNVAGFALGAGTAL 148
Cdd:cd01042    1 LARILRVNHAGEVGAVRIYRGQLAVARDPAVRPLIKEMLDEEKDHLAWFEELLPELGVRPSLLLPLWYVAGFALGALTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617 149 LGKEGAMACTVAVEESIAHHYNNQIRMLMEedaEKYEELLQVIKQFRDEELEHHDTGLEHDAELAPAYTLLKRLIQAGCS 228
Cdd:cd01042   81 LGKKAAMACTAAVETVVEEHYNDQLRELPA---QPDKELRAIIEQFRDDELEHADIAEELGAEKAPLYALLKALIKAGCK 157


                 ....*...
gi 564330617 229 AAIYLSER 236
Cdd:cd01042  158 VAIWLAKR 165
Coq7 COG2941
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme ...
 66-237 3.03e-56

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: 178.10  E-value: 3.03e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617  66 RAAVDQIIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKNHLKKFNELMVAFRVRPTVLMPLWNVAGFALGAG 145
Cdd:COG2941   43 RRHAAGLMRVNHAGEVCAQALYQGQALTARDPEVRAALEEAAAEETDHLAWCEERLRELGSRPSLLNPLWYAGSFALGAL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617 146 TALLGKEGAMACTVAVEESIAHHYNNQIRMLMEEDAekyeELLQVIKQFRDEELEHHDTGLEHDAELAPAytLLKRLIQA 225
Cdd:COG2941  123 AGLLGDKWSLGFVAATERQVEAHLDSHLARLPAQDP----KSRAILEQMREDEAEHADIALEAGAAELPA--PLRGAMKA 196

                        170
                 ....*....|..
gi 564330617 226 GCSAAIYLSERF 237
Cdd:COG2941  197 GSKVMTWTAYRI 208
 
Name Accession Description Interval E-value
COQ7 pfam03232
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
 67-234 4.29e-96

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: 277.85  E-value: 4.29e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617   67 AAVDQIIRVDHAGEYGANRIYAGQMAVLGR-TSVGPVIQKMWDQEKNHLKKFNELMVAFRVRPTVLMPLWNVAGFALGAG 145
Cdd:pfam03232   1 ALLDRILRVDHAGELGAVRIYAGQLAVLRRdPELRPLIKHMWDQEKEHLATFNELLAEHRVRPTLLLPLWKVAGFALGAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617  146 TALLGKEGAMACTVAVEESIAHHYNNQIRMLMEEDAEKyeELLQVIKQFRDEELEHHDTGLEHDAELAPAYTLLKRLIQA 225
Cdd:pfam03232  81 TALLGKEAAMACTEAVETVIGEHYNDQLRELPEKEEDK--ELRAIIEQFRDDELEHLDTAVENGAEEAPAYPLLTNVIKA 158


                  ....*....
gi 564330617  226 GCSAAIYLS 234
Cdd:pfam03232 159 GCRVAIWLA 167
DMQH cd01042
Demethoxyubiquinone hydroxylase, ferritin-like diiron-binding domain; Demethoxyubiquinone ...
 69-236 1.02e-87

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: 256.69  E-value: 1.02e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617  69 VDQIIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKNHLKKFNELMVAFRVRPTVLMPLWNVAGFALGAGTAL 148
Cdd:cd01042    1 LARILRVNHAGEVGAVRIYRGQLAVARDPAVRPLIKEMLDEEKDHLAWFEELLPELGVRPSLLLPLWYVAGFALGALTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617 149 LGKEGAMACTVAVEESIAHHYNNQIRMLMEedaEKYEELLQVIKQFRDEELEHHDTGLEHDAELAPAYTLLKRLIQAGCS 228
Cdd:cd01042   81 LGKKAAMACTAAVETVVEEHYNDQLRELPA---QPDKELRAIIEQFRDDELEHADIAEELGAEKAPLYALLKALIKAGCK 157


                 ....*...
gi 564330617 229 AAIYLSER 236
Cdd:cd01042  158 VAIWLAKR 165
Coq7 COG2941
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme ...
 66-237 3.03e-56

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: 178.10  E-value: 3.03e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617  66 RAAVDQIIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKNHLKKFNELMVAFRVRPTVLMPLWNVAGFALGAG 145
Cdd:COG2941   43 RRHAAGLMRVNHAGEVCAQALYQGQALTARDPEVRAALEEAAAEETDHLAWCEERLRELGSRPSLLNPLWYAGSFALGAL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617 146 TALLGKEGAMACTVAVEESIAHHYNNQIRMLMEEDAekyeELLQVIKQFRDEELEHHDTGLEHDAELAPAytLLKRLIQA 225
Cdd:COG2941  123 AGLLGDKWSLGFVAATERQVEAHLDSHLARLPAQDP----KSRAILEQMREDEAEHADIALEAGAAELPA--PLRGAMKA 196

                        170
                 ....*....|..
gi 564330617 226 GCSAAIYLSERF 237
Cdd:COG2941  197 GSKVMTWTAYRI 208
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 72-208 4.00e-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: 50.57  E-value: 4.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330617  72 IIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKNHLKKFNELMVAFRVRPTVLMPLwnvAGFALGAGTALLGK 151
Cdd:cd00657    2 LLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAH---LLAAYALPKTSDDP 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564330617 152 EGAMACTVAVEESIAHHYNNQIRMLMEedaekyEELLQVIKQFRDEELEHHDTGLEH 208
Cdd:cd00657   79 AEALRAALEVEARAIAAYRELIEQADD------PELRRLLERILADEQRHAAWFRKL 129
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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