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Conserved domains on  [gi|213511034|ref|NP_001134372|]
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Ubiquinone biosynthesis protein COQ7 homolog [Salmo salar]

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 ...
55-222 3.78e-93

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: 270.14  E-value: 3.78e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034   55 ALLHSMLRVDHAGEYGANRIYAGQMAVLGR-SQTGPLIQEMWDQEKKHLAKFNEILAENRVRPTLLLPLWNVAGFLLGAG 133
Cdd:pfam03232   1 ALLDRILRVDHAGELGAVRIYAGQLAVLRRdPELRPLIKHMWDQEKEHLATFNELLAEHRVRPTLLLPLWKVAGFALGAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034  134 TALLGKEGAMACTVAVEESISEHYNSQIRALMEEDPDRyvELLKLIKEFRDDEMEHHDTGLEHDAESLPGYKLLKSAIQL 213
Cdd:pfam03232  81 TALLGKEAAMACTEAVETVIGEHYNDQLRELPEKEEDK--ELRAIIEQFRDDELEHLDTAVENGAEEAPAYPLLTNVIKA 158

                  ....*....
gi 213511034  214 GCTAAIFVS 222
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 ...
55-222 3.78e-93

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: 270.14  E-value: 3.78e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034   55 ALLHSMLRVDHAGEYGANRIYAGQMAVLGR-SQTGPLIQEMWDQEKKHLAKFNEILAENRVRPTLLLPLWNVAGFLLGAG 133
Cdd:pfam03232   1 ALLDRILRVDHAGELGAVRIYAGQLAVLRRdPELRPLIKHMWDQEKEHLATFNELLAEHRVRPTLLLPLWKVAGFALGAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034  134 TALLGKEGAMACTVAVEESISEHYNSQIRALMEEDPDRyvELLKLIKEFRDDEMEHHDTGLEHDAESLPGYKLLKSAIQL 213
Cdd:pfam03232  81 TALLGKEAAMACTEAVETVIGEHYNDQLRELPEKEEDK--ELRAIIEQFRDDELEHLDTAVENGAEEAPAYPLLTNVIKA 158

                  ....*....
gi 213511034  214 GCTAAIFVS 222
Cdd:pfam03232 159 GCRVAIWLA 167
DMQH cd01042
Demethoxyubiquinone hydroxylase, ferritin-like diiron-binding domain; Demethoxyubiquinone ...
57-224 1.03e-84

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: 248.60  E-value: 1.03e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034  57 LHSMLRVDHAGEYGANRIYAGQMAVLGRSQTGPLIQEMWDQEKKHLAKFNEILAENRVRPTLLLPLWNVAGFLLGAGTAL 136
Cdd:cd01042    1 LARILRVNHAGEVGAVRIYRGQLAVARDPAVRPLIKEMLDEEKDHLAWFEELLPELGVRPSLLLPLWYVAGFALGALTAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034 137 LGKEGAMACTVAVEESISEHYNSQIRALMEEdpdRYVELLKLIKEFRDDEMEHHDTGLEHDAESLPGYKLLKSAIQLGCT 216
Cdd:cd01042   81 LGKKAAMACTAAVETVVEEHYNDQLRELPAQ---PDKELRAIIEQFRDDELEHADIAEELGAEKAPLYALLKALIKAGCK 157

                 ....*...
gi 213511034 217 AAIFVSQR 224
Cdd:cd01042  158 VAIWLAKR 165
Coq7 COG2941
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme ...
31-225 1.90e-59

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: 185.81  E-value: 1.90e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034  31 RALPvqlnsrAYSVIPPPRDEAEKALLHSMLRVDHAGEYGANRIYAGQMAVLGRSQTGPLIQEMWDQEKKHLAKFNEILA 110
Cdd:COG2941   26 RPRP------AAGVPEAELSAAERRHAAGLMRVNHAGEVCAQALYQGQALTARDPEVRAALEEAAAEETDHLAWCEERLR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034 111 ENRVRPTLLLPLWNVAGFLLGAGTALLGKEGAMACTVAVEESISEHYNSQIRALMEEDPdryvELLKLIKEFRDDEMEHH 190
Cdd:COG2941  100 ELGSRPSLLNPLWYAGSFALGALAGLLGDKWSLGFVAATERQVEAHLDSHLARLPAQDP----KSRAILEQMREDEAEHA 175
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 213511034 191 DTGLEHDAESLPgyKLLKSAIQLGCTAAIFVSQRL 225
Cdd:COG2941  176 DIALEAGAAELP--APLRGAMKAGSKVMTWTAYRI 208
DMQ_monoox_COQ7 NF033656
2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone monooxygenase;
50-202 1.79e-15

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


Pssm-ID: 468131  Cd Length: 205  Bit Score: 71.89  E-value: 1.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034  50 DEAEKALLHSMLRVDHAGEYGANRIYAGQMAVLGRSQTGPLIQEMWDQEKKHLAKFNEILAENRVRPTLLLPLWNVAGFL 129
Cdd:NF033656  36 SDAERRHAAGLMRVNHVGEVCAQALYQGQALTARDAAVREALEEAAREETDHLAWCEERLRELGSRPSLLNPLWYAGSFA 115
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213511034 130 LGAGTALLGKEGAMACTVAVEESISEHYNSQIRALMEEDpdryVELLKLIKEFRDDEMEHHDTGLEHDAESLP 202
Cdd:NF033656 116 LGALAGRLGDKWSLGFVAETERQVEAHLDSHLERLPEQD----ARSRAIVEQMRDDEARHAAAALAAGGAELP 184
 
Name Accession Description Interval E-value
COQ7 pfam03232
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
55-222 3.78e-93

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: 270.14  E-value: 3.78e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034   55 ALLHSMLRVDHAGEYGANRIYAGQMAVLGR-SQTGPLIQEMWDQEKKHLAKFNEILAENRVRPTLLLPLWNVAGFLLGAG 133
Cdd:pfam03232   1 ALLDRILRVDHAGELGAVRIYAGQLAVLRRdPELRPLIKHMWDQEKEHLATFNELLAEHRVRPTLLLPLWKVAGFALGAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034  134 TALLGKEGAMACTVAVEESISEHYNSQIRALMEEDPDRyvELLKLIKEFRDDEMEHHDTGLEHDAESLPGYKLLKSAIQL 213
Cdd:pfam03232  81 TALLGKEAAMACTEAVETVIGEHYNDQLRELPEKEEDK--ELRAIIEQFRDDELEHLDTAVENGAEEAPAYPLLTNVIKA 158

                  ....*....
gi 213511034  214 GCTAAIFVS 222
Cdd:pfam03232 159 GCRVAIWLA 167
DMQH cd01042
Demethoxyubiquinone hydroxylase, ferritin-like diiron-binding domain; Demethoxyubiquinone ...
57-224 1.03e-84

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: 248.60  E-value: 1.03e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034  57 LHSMLRVDHAGEYGANRIYAGQMAVLGRSQTGPLIQEMWDQEKKHLAKFNEILAENRVRPTLLLPLWNVAGFLLGAGTAL 136
Cdd:cd01042    1 LARILRVNHAGEVGAVRIYRGQLAVARDPAVRPLIKEMLDEEKDHLAWFEELLPELGVRPSLLLPLWYVAGFALGALTAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034 137 LGKEGAMACTVAVEESISEHYNSQIRALMEEdpdRYVELLKLIKEFRDDEMEHHDTGLEHDAESLPGYKLLKSAIQLGCT 216
Cdd:cd01042   81 LGKKAAMACTAAVETVVEEHYNDQLRELPAQ---PDKELRAIIEQFRDDELEHADIAEELGAEKAPLYALLKALIKAGCK 157

                 ....*...
gi 213511034 217 AAIFVSQR 224
Cdd:cd01042  158 VAIWLAKR 165
Coq7 COG2941
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme ...
31-225 1.90e-59

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: 185.81  E-value: 1.90e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034  31 RALPvqlnsrAYSVIPPPRDEAEKALLHSMLRVDHAGEYGANRIYAGQMAVLGRSQTGPLIQEMWDQEKKHLAKFNEILA 110
Cdd:COG2941   26 RPRP------AAGVPEAELSAAERRHAAGLMRVNHAGEVCAQALYQGQALTARDPEVRAALEEAAAEETDHLAWCEERLR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034 111 ENRVRPTLLLPLWNVAGFLLGAGTALLGKEGAMACTVAVEESISEHYNSQIRALMEEDPdryvELLKLIKEFRDDEMEHH 190
Cdd:COG2941  100 ELGSRPSLLNPLWYAGSFALGALAGLLGDKWSLGFVAATERQVEAHLDSHLARLPAQDP----KSRAILEQMREDEAEHA 175
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 213511034 191 DTGLEHDAESLPgyKLLKSAIQLGCTAAIFVSQRL 225
Cdd:COG2941  176 DIALEAGAAELP--APLRGAMKAGSKVMTWTAYRI 208
DMQ_monoox_COQ7 NF033656
2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone monooxygenase;
50-202 1.79e-15

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


Pssm-ID: 468131  Cd Length: 205  Bit Score: 71.89  E-value: 1.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034  50 DEAEKALLHSMLRVDHAGEYGANRIYAGQMAVLGRSQTGPLIQEMWDQEKKHLAKFNEILAENRVRPTLLLPLWNVAGFL 129
Cdd:NF033656  36 SDAERRHAAGLMRVNHVGEVCAQALYQGQALTARDAAVREALEEAAREETDHLAWCEERLRELGSRPSLLNPLWYAGSFA 115
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213511034 130 LGAGTALLGKEGAMACTVAVEESISEHYNSQIRALMEEDpdryVELLKLIKEFRDDEMEHHDTGLEHDAESLP 202
Cdd:NF033656 116 LGALAGRLGDKWSLGFVAETERQVEAHLDSHLERLPEQD----ARSRAIVEQMRDDEARHAAAALAAGGAELP 184
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
60-196 2.30e-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: 48.26  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511034  60 MLRVDHAGEYGANRIYAGQMAVLGRSQTGPLIQEMWDQEKKHLAKFNEILAENRVRPTLLLPLwnvAGFLLGAGTALLGK 139
Cdd:cd00657    2 LLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAH---LLAAYALPKTSDDP 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 213511034 140 EGAMACTVAVEESISEHYNSQIRALMEEdpdryvELLKLIKEFRDDEMEHHDTGLEH 196
Cdd:cd00657   79 AEALRAALEVEARAIAAYRELIEQADDP------ELRRLLERILADEQRHAAWFRKL 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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