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Conserved domains on  [gi|237875316|gb|ACR27649|]
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5-demethoxyubiquinone hydroxylase [Burkholderia glumae BGR1]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DMQ_monoox_COQ7 super family cl41368
2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone monooxygenase;
4-209 7.62e-121

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


The actual alignment was detected with superfamily member NF033656:

Pssm-ID: 468131  Cd Length: 205  Bit Score: 340.76  E-value: 7.62e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316   4 DELINEFDRGLRAVVGVSRMTRPLPePSADAPAAELSVEERRHAAGLMRVNHVGEVCAQALYQAQKLSTSSPSLKALFEA 83
Cdd:NF033656   1 DRLISEFDKALRTLFAPARASRPSP-AAALEAAGALSDAERRHAAGLMRVNHVGEVCAQALYQGQALTARDAAVREALEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316  84 SAREEEDHLAWTMHRLKSLDSRPSLLNPLWYSGALAIGLVAGRLGDRASLGFMAETERQVERHLDGHLAELPAADAASRA 163
Cdd:NF033656  80 AAREETDHLAWCEERLRELGSRPSLLNPLWYAGSFALGALAGRLGDKWSLGFVAETERQVEAHLDSHLERLPEQDARSRA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 237875316 164 IVEQMRDDEAKHGRTATDAGGTELPAPARWLMQAASKVMTRTAYYL 209
Cdd:NF033656 160 IVEQMRDDEARHAAAALAAGGAELPAPVRALMRAMSKVMTTTAYRI 205
 
Name Accession Description Interval E-value
DMQ_monoox_COQ7 NF033656
2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone monooxygenase;
4-209 7.62e-121

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


Pssm-ID: 468131  Cd Length: 205  Bit Score: 340.76  E-value: 7.62e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316   4 DELINEFDRGLRAVVGVSRMTRPLPePSADAPAAELSVEERRHAAGLMRVNHVGEVCAQALYQAQKLSTSSPSLKALFEA 83
Cdd:NF033656   1 DRLISEFDKALRTLFAPARASRPSP-AAALEAAGALSDAERRHAAGLMRVNHVGEVCAQALYQGQALTARDAAVREALEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316  84 SAREEEDHLAWTMHRLKSLDSRPSLLNPLWYSGALAIGLVAGRLGDRASLGFMAETERQVERHLDGHLAELPAADAASRA 163
Cdd:NF033656  80 AAREETDHLAWCEERLRELGSRPSLLNPLWYAGSFALGALAGRLGDKWSLGFVAETERQVEAHLDSHLERLPEQDARSRA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 237875316 164 IVEQMRDDEAKHGRTATDAGGTELPAPARWLMQAASKVMTRTAYYL 209
Cdd:NF033656 160 IVEQMRDDEARHAAAALAAGGAELPAPVRALMRAMSKVMTTTAYRI 205
Coq7 COG2941
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme ...
1-209 6.81e-102

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: 292.89  E-value: 6.81e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316   1 MLLDELINEFDRGLRAVVGVSRMTRPLPepSADAPAAELSVEERRHAAGLMRVNHVGEVCAQALYQAQKLSTSSPSLKAL 80
Cdd:COG2941    2 SFLDRLIIEFDRALRTLFGPARASRPRP--AAGVPEAELSAAERRHAAGLMRVNHAGEVCAQALYQGQALTARDPEVRAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316  81 FEASAREEEDHLAWTMHRLKSLDSRPSLLNPLWYSGALAIGLVAGRLGDRASLGFMAETERQVERHLDGHLAELPAADAA 160
Cdd:COG2941   80 LEEAAAEETDHLAWCEERLRELGSRPSLLNPLWYAGSFALGALAGLLGDKWSLGFVAATERQVEAHLDSHLARLPAQDPK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 237875316 161 SRAIVEQMRDDEAKHGRTATDAGGTELPAPARWLMQAASKVMTRTAYYL 209
Cdd:COG2941  160 SRAILEQMREDEAEHADIALEAGAAELPAPLRGAMKAGSKVMTWTAYRI 208
DMQH cd01042
Demethoxyubiquinone hydroxylase, ferritin-like diiron-binding domain; Demethoxyubiquinone ...
47-208 8.85e-64

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: 194.67  E-value: 8.85e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316  47 AAGLMRVNHVGEVCAQALYQAQKLSTSSPSLKALFEASAREEEDHLAWTMHRLKSLDSRPSLLNPLWYSGALAIGLVAGR 126
Cdd:cd01042    1 LARILRVNHAGEVGAVRIYRGQLAVARDPAVRPLIKEMLDEEKDHLAWFEELLPELGVRPSLLLPLWYVAGFALGALTAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316 127 LGDRASLGFMAETERQVERHLDGHLAELPA-ADAASRAIVEQMRDDEAKHGRTATDAGGT--ELPAPARWLMQAASKVMT 203
Cdd:cd01042   81 LGKKAAMACTAAVETVVEEHYNDQLRELPAqPDKELRAIIEQFRDDELEHADIAEELGAEkaPLYALLKALIKAGCKVAI 160

                 ....*
gi 237875316 204 RTAYY 208
Cdd:cd01042  161 WLAKR 165
COQ7 pfam03232
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
45-206 2.86e-58

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: 180.78  E-value: 2.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316   45 RHAAGLMRVNHVGEVCAQALYQAQKLSTSS-PSLKALFEASAREEEDHLAWTMHRLKSLDSRPSLLNPLWYSGALAIGLV 123
Cdd:pfam03232   1 ALLDRILRVDHAGELGAVRIYAGQLAVLRRdPELRPLIKHMWDQEKEHLATFNELLAEHRVRPTLLLPLWKVAGFALGAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316  124 AGRLGDRASLGFMAETERQVERHLDGHLAELPA--ADAASRAIVEQMRDDEAKHGRTATDAGGTELPA--PARWLMQAAS 199
Cdd:pfam03232  81 TALLGKEAAMACTEAVETVIGEHYNDQLRELPEkeEDKELRAIIEQFRDDELEHLDTAVENGAEEAPAypLLTNVIKAGC 160

                  ....*..
gi 237875316  200 KVMTRTA 206
Cdd:pfam03232 161 RVAIWLA 167
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
38-175 2.21e-03

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 38.38  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316   38 ELSVEERRH---AAGL--MRVNHVGEVCAQALYQAQKLSTSSPSLKALFEASAREEEDHLAWTMHRLKSLDSRPSLLNPL 112
Cdd:PRK12775  847 KLQALDRRKvedAAALeaIRTAFEIELGGMAFYARAAKETSDPVLKELFLKFAGMEQEHMATLARRYHAAAPSPTEGFKI 926
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237875316  113 wYSGALAIGlVAGRLGDRASLGFMA-ETERQVERHLDGHLAELPAAdAASRAIVEQMRDDEAKH 175
Cdd:PRK12775  927 -ERAAIMAG-VKGRPDDPGNLFRIAiEFERRAVKFFKERVAETPDG-SVERQLYKELAAEEREH 987
 
Name Accession Description Interval E-value
DMQ_monoox_COQ7 NF033656
2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone monooxygenase;
4-209 7.62e-121

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


Pssm-ID: 468131  Cd Length: 205  Bit Score: 340.76  E-value: 7.62e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316   4 DELINEFDRGLRAVVGVSRMTRPLPePSADAPAAELSVEERRHAAGLMRVNHVGEVCAQALYQAQKLSTSSPSLKALFEA 83
Cdd:NF033656   1 DRLISEFDKALRTLFAPARASRPSP-AAALEAAGALSDAERRHAAGLMRVNHVGEVCAQALYQGQALTARDAAVREALEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316  84 SAREEEDHLAWTMHRLKSLDSRPSLLNPLWYSGALAIGLVAGRLGDRASLGFMAETERQVERHLDGHLAELPAADAASRA 163
Cdd:NF033656  80 AAREETDHLAWCEERLRELGSRPSLLNPLWYAGSFALGALAGRLGDKWSLGFVAETERQVEAHLDSHLERLPEQDARSRA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 237875316 164 IVEQMRDDEAKHGRTATDAGGTELPAPARWLMQAASKVMTRTAYYL 209
Cdd:NF033656 160 IVEQMRDDEARHAAAALAAGGAELPAPVRALMRAMSKVMTTTAYRI 205
Coq7 COG2941
Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme ...
1-209 6.81e-102

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: 292.89  E-value: 6.81e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316   1 MLLDELINEFDRGLRAVVGVSRMTRPLPepSADAPAAELSVEERRHAAGLMRVNHVGEVCAQALYQAQKLSTSSPSLKAL 80
Cdd:COG2941    2 SFLDRLIIEFDRALRTLFGPARASRPRP--AAGVPEAELSAAERRHAAGLMRVNHAGEVCAQALYQGQALTARDPEVRAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316  81 FEASAREEEDHLAWTMHRLKSLDSRPSLLNPLWYSGALAIGLVAGRLGDRASLGFMAETERQVERHLDGHLAELPAADAA 160
Cdd:COG2941   80 LEEAAAEETDHLAWCEERLRELGSRPSLLNPLWYAGSFALGALAGLLGDKWSLGFVAATERQVEAHLDSHLARLPAQDPK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 237875316 161 SRAIVEQMRDDEAKHGRTATDAGGTELPAPARWLMQAASKVMTRTAYYL 209
Cdd:COG2941  160 SRAILEQMREDEAEHADIALEAGAAELPAPLRGAMKAGSKVMTWTAYRI 208
DMQH cd01042
Demethoxyubiquinone hydroxylase, ferritin-like diiron-binding domain; Demethoxyubiquinone ...
47-208 8.85e-64

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: 194.67  E-value: 8.85e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316  47 AAGLMRVNHVGEVCAQALYQAQKLSTSSPSLKALFEASAREEEDHLAWTMHRLKSLDSRPSLLNPLWYSGALAIGLVAGR 126
Cdd:cd01042    1 LARILRVNHAGEVGAVRIYRGQLAVARDPAVRPLIKEMLDEEKDHLAWFEELLPELGVRPSLLLPLWYVAGFALGALTAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316 127 LGDRASLGFMAETERQVERHLDGHLAELPA-ADAASRAIVEQMRDDEAKHGRTATDAGGT--ELPAPARWLMQAASKVMT 203
Cdd:cd01042   81 LGKKAAMACTAAVETVVEEHYNDQLRELPAqPDKELRAIIEQFRDDELEHADIAEELGAEkaPLYALLKALIKAGCKVAI 160

                 ....*
gi 237875316 204 RTAYY 208
Cdd:cd01042  161 WLAKR 165
COQ7 pfam03232
Ubiquinone biosynthesis protein COQ7; Members of this family contain two repeats of about 90 ...
45-206 2.86e-58

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: 180.78  E-value: 2.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316   45 RHAAGLMRVNHVGEVCAQALYQAQKLSTSS-PSLKALFEASAREEEDHLAWTMHRLKSLDSRPSLLNPLWYSGALAIGLV 123
Cdd:pfam03232   1 ALLDRILRVDHAGELGAVRIYAGQLAVLRRdPELRPLIKHMWDQEKEHLATFNELLAEHRVRPTLLLPLWKVAGFALGAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316  124 AGRLGDRASLGFMAETERQVERHLDGHLAELPA--ADAASRAIVEQMRDDEAKHGRTATDAGGTELPA--PARWLMQAAS 199
Cdd:pfam03232  81 TALLGKEAAMACTEAVETVIGEHYNDQLRELPEkeEDKELRAIIEQFRDDELEHLDTAVENGAEEAPAypLLTNVIKAGC 160

                  ....*..
gi 237875316  200 KVMTRTA 206
Cdd:pfam03232 161 RVAIWLA 167
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
61-177 7.57e-04

Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];


Pssm-ID: 441240  Cd Length: 141  Bit Score: 38.55  E-value: 7.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316  61 AQALYQAQKLSTSSPSLKALFEASAREEEDHLAWTMHRLKSLDSRPSLLNPLWYSGALA--IGLVAGRLGDRASLGFMAE 138
Cdd:COG1633   16 AIEFYLELAEKAKDPELKKLFEELAEEEKKHAELLEKLYEKLGGKPVAPPEEESQPGLAelMDKLDGSVSDAEALELAIA 95
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 237875316 139 TERQVERHLDGHLAELPAADAasRAIVEQMRDDEAKHGR 177
Cdd:COG1633   96 TEKDAIEFYRELAAKVGDPEI--KKLFEELAADEKEHAA 132
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
38-175 2.21e-03

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 38.38  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237875316   38 ELSVEERRH---AAGL--MRVNHVGEVCAQALYQAQKLSTSSPSLKALFEASAREEEDHLAWTMHRLKSLDSRPSLLNPL 112
Cdd:PRK12775  847 KLQALDRRKvedAAALeaIRTAFEIELGGMAFYARAAKETSDPVLKELFLKFAGMEQEHMATLARRYHAAAPSPTEGFKI 926
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237875316  113 wYSGALAIGlVAGRLGDRASLGFMA-ETERQVERHLDGHLAELPAAdAASRAIVEQMRDDEAKH 175
Cdd:PRK12775  927 -ERAAIMAG-VKGRPDDPGNLFRIAiEFERRAVKFFKERVAETPDG-SVERQLYKELAAEEREH 987
 
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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