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Conserved domains on  [gi|1635577185|ref|NP_001357424|]
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5-demethoxyubiquinone hydroxylase, mitochondrial isoform 6 [Homo sapiens]

Protein Classification

demethoxyubiquinone hydroxylase family protein( domain architecture ID 11141550)

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

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 ...
 9-153 1.19e-76

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: 225.08  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185   9 AAVDRIIRVDHAGEYGANRIYAGQMAVLGR-TSVGPVIQKMWDQEKDHLKKFNELMVTFRVRPTVLMPLWNVLGFALGAG 87
Cdd:pfam03232   1 ALLDRILRVDHAGELGAVRIYAGQLAVLRRdPELRPLIKHMWDQEKEHLATFNELLAEHRVRPTLLLPLWKVAGFALGAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185  88 TALLGKEGAMACTVAVEESIAHHYNNQIRTLMEEDPEKY----------EEL-----------LQAPAYAVLKSIIQAGC 146
Cdd:pfam03232  81 TALLGKEAAMACTEAVETVIGEHYNDQLRELPEKEEDKElraiieqfrdDELehldtavengaEEAPAYPLLTNVIKAGC 160


                  ....*..
gi 1635577185 147 RVAIYLS 153
Cdd:pfam03232 161 RVAIWLA 167
 
Name Accession Description Interval E-value
COQ7 pfam03232
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
 9-153 1.19e-76

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: 225.08  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185   9 AAVDRIIRVDHAGEYGANRIYAGQMAVLGR-TSVGPVIQKMWDQEKDHLKKFNELMVTFRVRPTVLMPLWNVLGFALGAG 87
Cdd:pfam03232   1 ALLDRILRVDHAGELGAVRIYAGQLAVLRRdPELRPLIKHMWDQEKEHLATFNELLAEHRVRPTLLLPLWKVAGFALGAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185  88 TALLGKEGAMACTVAVEESIAHHYNNQIRTLMEEDPEKY----------EEL-----------LQAPAYAVLKSIIQAGC 146
Cdd:pfam03232  81 TALLGKEAAMACTEAVETVIGEHYNDQLRELPEKEEDKElraiieqfrdDELehldtavengaEEAPAYPLLTNVIKAGC 160


                  ....*..
gi 1635577185 147 RVAIYLS 153
Cdd:pfam03232 161 RVAIWLA 167
DMQH cd01042
Demethoxyubiquinone hydroxylase, ferritin-like diiron-binding domain; Demethoxyubiquinone ...
 11-155 1.26e-72

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: 215.08  E-value: 1.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185  11 VDRIIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKDHLKKFNELMVTFRVRPTVLMPLWNVLGFALGAGTAL 90
Cdd:cd01042     1 LARILRVNHAGEVGAVRIYRGQLAVARDPAVRPLIKEMLDEEKDHLAWFEELLPELGVRPSLLLPLWYVAGFALGALTAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185  91 LGKEGAMACTVAVEESIAHHYNNQIRTLMEEDPEKYEELLQ--------------------APAYAVLKSIIQAGCRVAI 150
Cdd:cd01042    81 LGKKAAMACTAAVETVVEEHYNDQLRELPAQPDKELRAIIEqfrddelehadiaeelgaekAPLYALLKALIKAGCKVAI 160


                  ....*
gi 1635577185 151 YLSER 155
Cdd:cd01042   161 WLAKR 165
Coq7 COG2941
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme ...
 8-156 1.44e-47

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: 153.06  E-value: 1.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185   8 RAAVDRIIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKDHLKKFNELMVTFRVRPTVLMPLWNVLGFALGAG 87
Cdd:COG2941    43 RRHAAGLMRVNHAGEVCAQALYQGQALTARDPEVRAALEEAAAEETDHLAWCEERLRELGSRPSLLNPLWYAGSFALGAL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185  88 TALLGKEGAMACTVAVEESIAHHYNNQIRTLMEEDPE--------KYEELLQA---------PAYAVLKSIIQAGCRVAI 150
Cdd:COG2941   123 AGLLGDKWSLGFVAATERQVEAHLDSHLARLPAQDPKsraileqmREDEAEHAdialeagaaELPAPLRGAMKAGSKVMT 202


                  ....*.
gi 1635577185 151 YLSERL 156
Cdd:COG2941   203 WTAYRI 208
DMQ_monoox_COQ7 NF033656
2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone monooxygenase;
16-122 9.29e-09

2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone monooxygenase;


Pssm-ID: 468131  Cd Length: 205  Bit Score: 51.86  E-value: 9.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185  16 RVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKDHL----KKFNELmvtfRVRPTVLMPLWNVLGFALGAGTALL 91
Cdd:NF033656   48 RVNHVGEVCAQALYQGQALTARDAAVREALEEAAREETDHLawceERLREL----GSRPSLLNPLWYAGSFALGALAGRL 123

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1635577185  92 GKEGAMACTVAVEESIAHHYNNQIRTLMEED 122
Cdd:NF033656  124 GDKWSLGFVAETERQVEAHLDSHLERLPEQD 154
 
Name Accession Description Interval E-value
COQ7 pfam03232
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
 9-153 1.19e-76

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: 225.08  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185   9 AAVDRIIRVDHAGEYGANRIYAGQMAVLGR-TSVGPVIQKMWDQEKDHLKKFNELMVTFRVRPTVLMPLWNVLGFALGAG 87
Cdd:pfam03232   1 ALLDRILRVDHAGELGAVRIYAGQLAVLRRdPELRPLIKHMWDQEKEHLATFNELLAEHRVRPTLLLPLWKVAGFALGAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185  88 TALLGKEGAMACTVAVEESIAHHYNNQIRTLMEEDPEKY----------EEL-----------LQAPAYAVLKSIIQAGC 146
Cdd:pfam03232  81 TALLGKEAAMACTEAVETVIGEHYNDQLRELPEKEEDKElraiieqfrdDELehldtavengaEEAPAYPLLTNVIKAGC 160


                  ....*..
gi 1635577185 147 RVAIYLS 153
Cdd:pfam03232 161 RVAIWLA 167
DMQH cd01042
Demethoxyubiquinone hydroxylase, ferritin-like diiron-binding domain; Demethoxyubiquinone ...
 11-155 1.26e-72

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: 215.08  E-value: 1.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185  11 VDRIIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKDHLKKFNELMVTFRVRPTVLMPLWNVLGFALGAGTAL 90
Cdd:cd01042     1 LARILRVNHAGEVGAVRIYRGQLAVARDPAVRPLIKEMLDEEKDHLAWFEELLPELGVRPSLLLPLWYVAGFALGALTAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185  91 LGKEGAMACTVAVEESIAHHYNNQIRTLMEEDPEKYEELLQ--------------------APAYAVLKSIIQAGCRVAI 150
Cdd:cd01042    81 LGKKAAMACTAAVETVVEEHYNDQLRELPAQPDKELRAIIEqfrddelehadiaeelgaekAPLYALLKALIKAGCKVAI 160


                  ....*
gi 1635577185 151 YLSER 155
Cdd:cd01042   161 WLAKR 165
Coq7 COG2941
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme ...
 8-156 1.44e-47

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: 153.06  E-value: 1.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185   8 RAAVDRIIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKDHLKKFNELMVTFRVRPTVLMPLWNVLGFALGAG 87
Cdd:COG2941    43 RRHAAGLMRVNHAGEVCAQALYQGQALTARDPEVRAALEEAAAEETDHLAWCEERLRELGSRPSLLNPLWYAGSFALGAL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185  88 TALLGKEGAMACTVAVEESIAHHYNNQIRTLMEEDPE--------KYEELLQA---------PAYAVLKSIIQAGCRVAI 150
Cdd:COG2941   123 AGLLGDKWSLGFVAATERQVEAHLDSHLARLPAQDPKsraileqmREDEAEHAdialeagaaELPAPLRGAMKAGSKVMT 202


                  ....*.
gi 1635577185 151 YLSERL 156
Cdd:COG2941   203 WTAYRI 208
DMQ_monoox_COQ7 NF033656
2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone monooxygenase;
16-122 9.29e-09

2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone monooxygenase;


Pssm-ID: 468131  Cd Length: 205  Bit Score: 51.86  E-value: 9.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185  16 RVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKDHL----KKFNELmvtfRVRPTVLMPLWNVLGFALGAGTALL 91
Cdd:NF033656   48 RVNHVGEVCAQALYQGQALTARDAAVREALEEAAREETDHLawceERLREL----GSRPSLLNPLWYAGSFALGALAGRL 123

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1635577185  92 GKEGAMACTVAVEESIAHHYNNQIRTLMEED 122
Cdd:NF033656  124 GDKWSLGFVAETERQVEAHLDSHLERLPEQD 154
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 13-122 8.60e-07

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: 45.56  E-value: 8.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577185  13 RIIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKDHLKKFNELMVTFRVRPTVLMPLwnvLGFALGAGTALLG 92
Cdd:cd00657     1 RLLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAH---LLAAYALPKTSDD 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1635577185  93 KEGAMACTVAVEESIAHHYNNQIRTLMEED 122
Cdd:cd00657    78 PAEALRAALEVEARAIAAYRELIEQADDPE 107
 
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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