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Conserved domains on  [gi|499837730|ref|WP_011518464|]
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bb3-type cytochrome oxidase subunit III [Cupriavidus metallidurans]

Protein Classification

Heme_Cu_Oxidase_III_2 domain-containing protein( domain architecture ID 10120728)

Heme_Cu_Oxidase_III_2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 33-210 1.06e-57

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: 180.64  E-value: 1.06e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  33 HGHGARTPGSLGLWVFMGVVTALFTLFLAAYIMRMDSPDWQ---RIALPWQVWLSTAVLAAACVAMEIARRAAHSGRMVR 109
Cdd:cd02865    1 YVAGARSPGWWGLWVFMAVEGTLFALLISAYFMRMTSGDWQpgaPLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730 110 ARHAFRLGGMGAVAFVGVQLWAWQALYALHVVPANNPAGSFFYLLTAMHGLHMLGGLVAFAFVAVDRGSGT---RTVTRI 186
Cdd:cd02865   81 ARLGLALAGALALAFLAGQLLAWHALNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHygpRRRLPV 160

                        170       180
                 ....*....|....*....|....
gi 499837730 187 GLCARYWHFLLAVWVVLLGALGWL 210
Cdd:cd02865  161 ELCALYWHFLLLVWLVLLALLYGT 184
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 33-210 1.06e-57

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: 180.64  E-value: 1.06e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  33 HGHGARTPGSLGLWVFMGVVTALFTLFLAAYIMRMDSPDWQ---RIALPWQVWLSTAVLAAACVAMEIARRAAHSGRMVR 109
Cdd:cd02865    1 YVAGARSPGWWGLWVFMAVEGTLFALLISAYFMRMTSGDWQpgaPLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730 110 ARHAFRLGGMGAVAFVGVQLWAWQALYALHVVPANNPAGSFFYLLTAMHGLHMLGGLVAFAFVAVDRGSGT---RTVTRI 186
Cdd:cd02865   81 ARLGLALAGALALAFLAGQLLAWHALNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHygpRRRLPV 160

                        170       180
                 ....*....|....*....|....
gi 499837730 187 GLCARYWHFLLAVWVVLLGALGWL 210
Cdd:cd02865  161 ELCALYWHFLLLVWLVLLALLYGT 184
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
30-210 2.51e-39

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 133.82  E-value: 2.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  30 DALHGHGARTPGSLGLWVFMGVVTALFTLFLAAYIM-RMDSPDWQRIAL---PWQVWLSTAVLAAACVAMEIARRAAHSG 105
Cdd:COG1845    5 EAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVlRASAPDWPAGAElldLPLPLINTLLLLLSSFTVALAVRAARRG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730 106 RMVRARHAFRLGGMGAVAFVGVQLWAWQALYALHVVPANNPAGSFFYLLTAMHGLHMLGGLVAFAFVAV---DRGSGTRT 182
Cdd:COG1845   85 DRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVralRGGFTPEN 164

                        170       180
                 ....*....|....*....|....*...
gi 499837730 183 VTRIGLCARYWHFLLAVWVVLLGALGWL 210
Cdd:COG1845  165 HTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 43-207 6.79e-06

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 45.23  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730   43 LGLWVFMGVVTALF-TLFLAAYIMR----MDSPDWQRIALPWQVWLSTAVLAAACVAMEIARRAAHSGRMVRARHAFRLG 117
Cdd:TIGR02897  12 LGFWIFLGAEIALFaTLFATYLVLQhggdYAGKMPAELFELPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIIT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  118 GMGAVAFVGVQLWAWQALYALHVVPANNPAGSFFYLLTAMHGLHMLGGLVAFAFVAVD---RGSGTRTVTRIGLCARYWH 194
Cdd:TIGR02897  92 LLLGAGFVGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQiqrRGLTPYTAPKVFIVSLYWH 171

                         170
                  ....*....|...
gi 499837730  195 FLLAVWVVLLGAL 207
Cdd:TIGR02897 172 FLDVVWVFIFTAV 184
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 33-207 9.14e-06

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 44.77  E-value: 9.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  33 HGHGARTPGS---LGLWVFMGVVTALFTLFLAAYIMRMDS----PDWQRI-ALPWqVWLSTAVLAAACVAMEIARRAAHS 104
Cdd:PRK10663  14 HEHGHHDAGAtkvFGFWIYLMSDCILFSILFATYAVLVNGtaggPTGKDIfELPF-VLVETFLLLFSSITYGMAAIAMYK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730 105 GRMVRARHAFRLGGMGAVAFVGVQLWAWQALYALHVVPANNPAGSFFYLLTAMHGLHMLGGLVAFAFVAVD---RGSGTR 181
Cdd:PRK10663  93 NNKSQVISWLALTFLFGAGFIGMEIYEFHHLIVEGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQvarRGLTST 172

                        170       180       190
                 ....*....|....*....|....*....|..
gi 499837730 182 TVTRIGLCARYWHFLLAVW------VVLLGAL 207
Cdd:PRK10663 173 NRTRIMCLSLFWHFLDVVWicvftvVYLMGAM 204
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 33-210 1.06e-57

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: 180.64  E-value: 1.06e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  33 HGHGARTPGSLGLWVFMGVVTALFTLFLAAYIMRMDSPDWQ---RIALPWQVWLSTAVLAAACVAMEIARRAAHSGRMVR 109
Cdd:cd02865    1 YVAGARSPGWWGLWVFMAVEGTLFALLISAYFMRMTSGDWQpgaPLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730 110 ARHAFRLGGMGAVAFVGVQLWAWQALYALHVVPANNPAGSFFYLLTAMHGLHMLGGLVAFAFVAVDRGSGT---RTVTRI 186
Cdd:cd02865   81 ARLGLALAGALALAFLAGQLLAWHALNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHygpRRRLPV 160

                        170       180
                 ....*....|....*....|....
gi 499837730 187 GLCARYWHFLLAVWVVLLGALGWL 210
Cdd:cd02865  161 ELCALYWHFLLLVWLVLLALLYGT 184
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
30-210 2.51e-39

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 133.82  E-value: 2.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  30 DALHGHGARTPGSLGLWVFMGVVTALFTLFLAAYIM-RMDSPDWQRIAL---PWQVWLSTAVLAAACVAMEIARRAAHSG 105
Cdd:COG1845    5 EAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVlRASAPDWPAGAElldLPLPLINTLLLLLSSFTVALAVRAARRG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730 106 RMVRARHAFRLGGMGAVAFVGVQLWAWQALYALHVVPANNPAGSFFYLLTAMHGLHMLGGLVAFAFVAV---DRGSGTRT 182
Cdd:COG1845   85 DRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVralRGGFTPEN 164

                        170       180
                 ....*....|....*....|....*...
gi 499837730 183 VTRIGLCARYWHFLLAVWVVLLGALGWL 210
Cdd:COG1845  165 HTGVEAAALYWHFVDVVWIFLFALVYLL 192
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 33-210 5.70e-32

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: 114.61  E-value: 5.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  33 HGHGARTPGSLGLWVFMGVVTALFTLFLAAYIMRMDSPDW-----QRIALPWQVWLSTAVLAAACVAMEIARRAAHSGRM 107
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVefgagLDPLDLPLLNTNTLLLSGSSVTWAHASLAARRGNR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730 108 VRARHAFRLGGMGAVAFVGVQLWAWQALYAlhvVPANNPAGSFFYLLTAMHGLHMLGGLVAFAFVAVDRGSG---TRTVT 184
Cdd:cd00386   81 KKARLWLLLTILLGLAFLGLQAYEYSHLIF---TISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGhftPRHHL 157

                        170       180
                 ....*....|....*....|....*.
gi 499837730 185 RIGLCARYWHFLLAVWVVLLGALGWL 210
Cdd:cd00386  158 GLEAAALYWHFVDVVWLFLFPLVYLW 183
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 38-203 1.47e-14

NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.


Pssm-ID: 239213  Cd Length: 186  Bit Score: 69.19  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  38 RTPGSLGLWVFMGVVTALFTLFLAAY-IMRMDSPDWQRIAL----PWQVWLSTAVLAAACVAMEIARRAAHSGRMVRARH 112
Cdd:cd02862    6 RLPGKLGMWVFILSELLAFGALFIAYaVYRALYPELFAAGSahldLLLGALNTLVLLTSSFTVALAVRAARAGRRRRARR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730 113 AFRLGGMGAVAFVGVQLWAWQALYALHVVPANNPAGSFFYLLTAMHGLHMLGGLVAFAFVAV---DRGSGTRTVTRIGLC 189
Cdd:cd02862   86 WLAAAVLLGLVFLVIKYFEYAHKIAAGIDPDAGLFFTLYFLLTGFHLLHVLIGLGILLWVAWrarRGRYSARDYEGVEAA 165

                        170
                 ....*....|....
gi 499837730 190 ARYWHFLLAVWVVL 203
Cdd:cd02862  166 ALYWHMVDLVWIVL 179
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 39-201 1.68e-10

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: 239215  Cd Length: 202  Bit Score: 58.28  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  39 TPGSLGLWVFMGVVTALFTLFLAAYI-MRMDSPDW-----QRIALPWQ--------VWLSTAVLAAACVAMEIARRAAHS 104
Cdd:cd02864    7 SWGKAMMWFFLLSDAFIFSSFLIAYMtARISTTEPwplpsDVFALRIGhfniplvlIAIMTFILITSSGTMAMAVNFGYR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730 105 GRMVRARHAFRLGGMGAVAFVGVQLWAWQALYA-LHVVPANNPAG-----SFFYLLTAMHGLHMLGGLVAFAFVA--VDR 176
Cdd:cd02864   87 GNRKAAARLMLATALLGATFVGMQAFEWTKLIVeEGVRPWGNPWGaaqfgASFFMITGFHGTHVTIGVIYLIIIArkVWR 166

                        170       180       190
                 ....*....|....*....|....*....|
gi 499837730 177 GSGTRT-----VTRIGLcarYWHFLLAVWV 201
Cdd:cd02864  167 GKYQRIgryeiVEIAGL---YWHFVDLVWV 193
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 43-207 6.79e-06

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 45.23  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730   43 LGLWVFMGVVTALF-TLFLAAYIMR----MDSPDWQRIALPWQVWLSTAVLAAACVAMEIARRAAHSGRMVRARHAFRLG 117
Cdd:TIGR02897  12 LGFWIFLGAEIALFaTLFATYLVLQhggdYAGKMPAELFELPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIIT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  118 GMGAVAFVGVQLWAWQALYALHVVPANNPAGSFFYLLTAMHGLHMLGGLVAFAFVAVD---RGSGTRTVTRIGLCARYWH 194
Cdd:TIGR02897  92 LLLGAGFVGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQiqrRGLTPYTAPKVFIVSLYWH 171

                         170
                  ....*....|...
gi 499837730  195 FLLAVWVVLLGAL 207
Cdd:TIGR02897 172 FLDVVWVFIFTAV 184
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 33-207 9.14e-06

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 44.77  E-value: 9.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  33 HGHGARTPGS---LGLWVFMGVVTALFTLFLAAYIMRMDS----PDWQRI-ALPWqVWLSTAVLAAACVAMEIARRAAHS 104
Cdd:PRK10663  14 HEHGHHDAGAtkvFGFWIYLMSDCILFSILFATYAVLVNGtaggPTGKDIfELPF-VLVETFLLLFSSITYGMAAIAMYK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730 105 GRMVRARHAFRLGGMGAVAFVGVQLWAWQALYALHVVPANNPAGSFFYLLTAMHGLHMLGGLVAFAFVAVD---RGSGTR 181
Cdd:PRK10663  93 NNKSQVISWLALTFLFGAGFIGMEIYEFHHLIVEGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQvarRGLTST 172

                        170       180       190
                 ....*....|....*....|....*....|..
gi 499837730 182 TVTRIGLCARYWHFLLAVW------VVLLGAL 207
Cdd:PRK10663 173 NRTRIMCLSLFWHFLDVVWicvftvVYLMGAM 204
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 33-203 2.89e-05

Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine 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 bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.


Pssm-ID: 239214  Cd Length: 186  Bit Score: 43.00  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  33 HGHGARTPGSLGLWVFMGVVTALFTLFLAAYIMRMDS-----PDWQRIALPWqVWLSTAVLAAACVAMEIARRAAHSGRM 107
Cdd:cd02863    1 HHTNTGSKKILGFWIYLMSDCILFATLFATYAVLSGNtaggpPGHELFELPL-VFIETFLLLLSSFTCGLAMIAMNKNNK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730 108 VRARH----AFRLGgmgaVAFVGVQLWAWQALYALHVVPANNPAGSFFYLLTAMHGLHMLGGL----VAFAFVAVdRGSG 179
Cdd:cd02863   80 KKVILwliiTFLLG----LGFVGMEIYEFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLiwilVMIIQLKK-RGLT 154

                        170       180
                 ....*....|....*....|....
gi 499837730 180 TRTVTRIGLCARYWHFLLAVWVVL 203
Cdd:cd02863  155 PDTARRLFCLSLFWHFLDIVWIFV 178
PLN02194 PLN02194
cytochrome-c oxidase
 78-209 4.90e-05

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 43.11  E-value: 4.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  78 PWQV-WLSTAVLAAACVAMEIARRAAHSGRMVRARHAFRLGGMGAVAFVGVQ-LWAWQALYALhvvpANNPAGSFFYLLT 155
Cdd:PLN02194 129 PWEIpFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQgMEYYQAPFTI----SDSIYGSTFFLAT 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499837730 156 AMHGLHMLGGLVAFAFVAVDRGSGTRTVTR-IGL--CARYWHFLLAVWVVLLGALGW 209
Cdd:PLN02194 205 GFHGFHVIIGTLFLIICGIRQYLGHLTKEHhVGFeaAAWYWHFVDVVWLFLFVSIYW 261
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 148-203 7.35e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 39.49  E-value: 7.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730 148 GSFFYLLTAMHGLHMLGGLVaFAFVAVDRGSGTRTVTR--IGL--CARYWHFLLAVWVVL 203
Cdd:MTH00141 192 GSTFFVLTGFHGLHVIIGTT-FLLVCLVRLLLGHFSTNhhFGFeaAAWYWHFVDVVWLFL 250
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 78-209 4.83e-03

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 37.01  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499837730  78 PWQV-WLSTAVLAAACVAMEIARRAAHSGRMVRARHAFRLGGMGAVAFVGVQLWA-WQALYALhvvpANNPAGSFFYLLT 155
Cdd:MTH00039 125 PFLVpLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEyYDAPFTI----ADSVYGSTFFVAT 200

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499837730 156 AMHGLHMLGGlVAFAFVAVDRGSGTRTVT--RIGL--CARYWHFLLAVWVVLLGALGW 209
Cdd:MTH00039 201 GFHGLHVIIG-TTFLAVCLFRLINHHFSNnhHFGFeaAAWYWHFVDVVWLFLYVCIYW 257
 
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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