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Conserved domains on  [gi|2153798588|ref|WP_229207863|]
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heme-copper oxidase subunit III [Dyadobacter beijingensis]

Protein Classification

heme-copper oxidase subunit III( domain architecture ID 10004778)

heme-copper oxidase subunit III is a member of a diverse family that differs in terms of electron donors, subunit composition, and heme types and includes cytochrome c and ubiquinol oxidases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
14-210 3.87e-26

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


:

Pssm-ID: 441450  Cd Length: 192  Bit Score: 99.54  E-value: 3.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2153798588  14 TTKQTENPFTKRREPLGFMLWLGVAGSSVLFTSIFVIFL-LRAHHETGHLVAL---PDMFWLSTLVILFSSITLHEANLA 89
Cdd:COG1845     1 AHDVEAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFvLRASAPDWPAGAElldLPLPLINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2153798588  90 FTNERFLHYRVFLGATLLLGFIFILLQAGGWMEMVNSGVFSGVNTSEGFIYLLTGLHLLHMIGGVLYLSYLFRKAVKnss 169
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2153798588 170 yvdsfvYSVNPPNRLRIKLFTRYWHFTGALWLVVFIFLIVL 210
Cdd:COG1845   158 ------GGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
 
Name Accession Description Interval E-value
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
14-210 3.87e-26

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 99.54  E-value: 3.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2153798588  14 TTKQTENPFTKRREPLGFMLWLGVAGSSVLFTSIFVIFL-LRAHHETGHLVAL---PDMFWLSTLVILFSSITLHEANLA 89
Cdd:COG1845     1 AHDVEAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFvLRASAPDWPAGAElldLPLPLINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2153798588  90 FTNERFLHYRVFLGATLLLGFIFILLQAGGWMEMVNSGVFSGVNTSEGFIYLLTGLHLLHMIGGVLYLSYLFRKAVKnss 169
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2153798588 170 yvdsfvYSVNPPNRLRIKLFTRYWHFTGALWLVVFIFLIVL 210
Cdd:COG1845   158 ------GGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 25-207 6.62e-17

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239216  Cd Length: 184  Bit Score: 75.10  E-value: 6.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2153798588  25 RREPLGFMLWLGVAGSSVLFTS-IFVIFLLRAHHETGHLVALPD--MFWLSTLVILFSSITLHEANLAFTNERFLHYRVF 101
Cdd:cd02865     5 ARSPGWWGLWVFMAVEGTLFALlISAYFMRMTSGDWQPGAPLPLpnLLSLNTAVLAASSVAMQWARRAARRNRRVLARLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2153798588 102 LGATLLLGFIFILLQAGGWMEMVNSGVFSGVNTSEGFIYLLTGLHLLHMIGGVLYLSYLFrkavknssyVDSFVYSVNPP 181
Cdd:cd02865    85 LALAGALALAFLAGQLLAWHALNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVL---------AGLIRGHYGPR 155

                         170       180
                  ....*....|....*....|....*.
gi 2153798588 182 NRLRIKLFTRYWHFTGALWLVVFIFL 207
Cdd:cd02865   156 RRLPVELCALYWHFLLLVWLVLLALL 181
 
Name Accession Description Interval E-value
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
14-210 3.87e-26

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 99.54  E-value: 3.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2153798588  14 TTKQTENPFTKRREPLGFMLWLGVAGSSVLFTSIFVIFL-LRAHHETGHLVAL---PDMFWLSTLVILFSSITLHEANLA 89
Cdd:COG1845     1 AHDVEAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFvLRASAPDWPAGAElldLPLPLINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2153798588  90 FTNERFLHYRVFLGATLLLGFIFILLQAGGWMEMVNSGVFSGVNTSEGFIYLLTGLHLLHMIGGVLYLSYLFRKAVKnss 169
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2153798588 170 yvdsfvYSVNPPNRLRIKLFTRYWHFTGALWLVVFIFLIVL 210
Cdd:COG1845   158 ------GGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 25-207 6.62e-17

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239216  Cd Length: 184  Bit Score: 75.10  E-value: 6.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2153798588  25 RREPLGFMLWLGVAGSSVLFTS-IFVIFLLRAHHETGHLVALPD--MFWLSTLVILFSSITLHEANLAFTNERFLHYRVF 101
Cdd:cd02865     5 ARSPGWWGLWVFMAVEGTLFALlISAYFMRMTSGDWQPGAPLPLpnLLSLNTAVLAASSVAMQWARRAARRNRRVLARLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2153798588 102 LGATLLLGFIFILLQAGGWMEMVNSGVFSGVNTSEGFIYLLTGLHLLHMIGGVLYLSYLFrkavknssyVDSFVYSVNPP 181
Cdd:cd02865    85 LALAGALALAFLAGQLLAWHALNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVL---------AGLIRGHYGPR 155

                         170       180
                  ....*....|....*....|....*.
gi 2153798588 182 NRLRIKLFTRYWHFTGALWLVVFIFL 207
Cdd:cd02865   156 RRLPVELCALYWHFLLLVWLVLLALL 181
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 23-207 3.18e-13

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 65.30  E-value: 3.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2153798588  23 TKRREPLGFMLWLGVAGSSVLFTSIFVIFLLRAHHETGHLVALPDMF-----WLSTLVILFSSITLHEANLAFTNERFLH 97
Cdd:cd00386     3 ASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGAGLDPLdlpllNTNTLLLSGSSVTWAHASLAARRGNRKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2153798588  98 YRVFLGATLLLGFIFILLQAggwMEMVNSGVFSGVNTSEGFIYLLTGLHLLHMIGGVLYLSYLFRKAVKnssyvdsfvYS 177
Cdd:cd00386    83 ARLWLLLTILLGLAFLGLQA---YEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRR---------GH 150

                         170       180       190
                  ....*....|....*....|....*....|
gi 2153798588 178 VNPPNRLRIKLFTRYWHFTGALWLVVFIFL 207
Cdd:cd00386   151 FTPRHHLGLEAAALYWHFVDVVWLFLFPLV 180
 
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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