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Conserved domains on  [gi|2125669188|gb|UDP51675|]
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cytochrome c oxidase subunit 3, partial (mitochondrion) [Padina tetrastromatica]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10108868)

cytochrome c oxidase subunit 3 is one of main transmembrane subunits of cytochrome c oxidase, the last enzyme in the respiratory electron transport chain of mitochondria or bacteria located in the mitochondrial or bacterial membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 7-217 1.76e-80

Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, 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. 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. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


:

Pssm-ID: 238834  Cd Length: 243  Bit Score: 240.50  E-value: 1.76e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   7 LVASIGALSLTFGGVMFMHNYSGGGqLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVSEVMFFF 86
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPL-LLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  87 AFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTFAIYFTT 166
Cdd:cd01665    80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2125669188 167 FQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:cd01665   160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGH 210
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 7-217 1.76e-80

Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, 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. 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. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 240.50  E-value: 1.76e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   7 LVASIGALSLTFGGVMFMHNYSGGGqLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVSEVMFFF 86
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPL-LLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  87 AFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTFAIYFTT 166
Cdd:cd01665    80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2125669188 167 FQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:cd01665   160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGH 210
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-217 1.60e-79

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 238.16  E-value: 1.60e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYSGggQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00155   10 DYSPWPLTGSIGAMTLTSGLIKWFHQFNM--NLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00155   88 EVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIIL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:MTH00155  168 GIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNH 224
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-217 1.99e-78

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 235.77  E-value: 1.99e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYSGGGQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:pfam00510   7 SPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIIS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:pfam00510  87 EVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:pfam00510 167 AVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYH 223
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
59-217 2.57e-22

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 89.52  E-value: 2.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  59 EGQHTSAVQDGLRLGMILFIVSEVMFFFAFfwaffTSSLAPVFNIGGVWPPAGLEVisPWGLPLLNTVLLLSSGATVTWA 138
Cdd:COG1845     5 EAPHAPERRSPGKLGMWLFLASEVMLFAAL-----FAAYFVLRASAPDWPAGAELL--DLPLPLINTLLLLLSSFTVALA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188 139 HHAIVGGLKREAQTGLYLTLTFAIYFTTFQFLEY---VEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYL 215
Cdd:COG1845    78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR 157


                  ..
gi 2125669188 216 DH 217
Cdd:COG1845   158 GG 159
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 7-217 1.76e-80

Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, 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. 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. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 240.50  E-value: 1.76e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   7 LVASIGALSLTFGGVMFMHNYSGGGqLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVSEVMFFF 86
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPL-LLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  87 AFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTFAIYFTT 166
Cdd:cd01665    80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2125669188 167 FQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:cd01665   160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGH 210
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-217 1.60e-79

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 238.16  E-value: 1.60e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYSGggQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00155   10 DYSPWPLTGSIGAMTLTSGLIKWFHQFNM--NLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00155   88 EVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIIL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:MTH00155  168 GIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNH 224
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-217 1.62e-78

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 236.02  E-value: 1.62e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYSGGgqLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00189   11 DPSPWPLTGAIAALLLTSGLAMWFHYNSFI--LLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFITS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00189   89 EVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVIL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:MTH00189  169 GVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGH 225
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-217 1.99e-78

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 235.77  E-value: 1.99e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYSGGGQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:pfam00510   7 SPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIIS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:pfam00510  87 EVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:pfam00510 167 AVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYH 223
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-217 6.70e-77

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 231.76  E-value: 6.70e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYSGggQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00118   12 DPSPWPLTGAMAALLLTSGLAMWFHYNST--TLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00118   90 EVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:MTH00118  170 GLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFH 226
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-217 1.71e-75

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 228.48  E-value: 1.71e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHnySGGGQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00024   12 EPSPWPFLGAGGAFFITVGSVVYFH--YGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00024   90 EVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:MTH00024  170 GVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQ 226
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-217 2.92e-75

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 227.47  E-value: 2.92e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYSGggQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00141   10 EFSPWPLTGSIGALFLTVGLVSWFHGGSF--LLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00141   88 EVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIIL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:MTH00141  168 GVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGH 224
PLN02194 PLN02194
cytochrome-c oxidase
 1-217 4.44e-72

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 219.92  E-value: 4.44e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYSGGGQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:PLN02194   13 DPSPWPISGSLGALATTVGGVMYMHPFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSILFIVS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:PLN02194   93 EVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:PLN02194  173 ALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGH 229
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-217 2.00e-71

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 218.06  E-value: 2.00e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYSGggQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00039   11 DQSPWPLTAAIGALIMTSGLVLWFHGDSI--LLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFITS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00039   89 EVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:MTH00039  169 GLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHH 225
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-213 2.73e-71

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 217.74  E-value: 2.73e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHnySGGGQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00052   13 DPSPWPYIGGCGALFTTVGGVMYFH--YSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILFIVS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00052   91 EVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVAL 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQI 213
Cdd:MTH00052  171 GLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRL 223
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-217 9.38e-69

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 211.18  E-value: 9.38e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYSGggQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00219   13 DYSPWPLTGSLGALMLTSGLVAWFHHYNL--DLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFIVS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00219   91 EILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILL 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:MTH00219  171 GLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLH 227
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-209 1.56e-68

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 210.78  E-value: 1.56e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYSGggQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00130   12 DPSPWPLTGAVAALLMTSGLAIWFHFHST--TLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00130   90 EVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILL 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAIC 209
Cdd:MTH00130  170 GFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVC 218
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-217 1.84e-68

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 210.35  E-value: 1.84e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYSGggQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00099   12 NPSPWPLTGALSALLMTSGLIMWFHFNST--TLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIIS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00099   90 EVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:MTH00099  170 GLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFH 226
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-212 8.02e-67

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 206.13  E-value: 8.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHnySGGGQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00075   12 DPSPWPLTGAIAALLLTSGLAMWFH--FGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00075   90 EVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIIL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQ 212
Cdd:MTH00075  170 GLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLR 221
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-217 4.11e-63

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 196.60  E-value: 4.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHNYsgGGQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00009   10 EYSPWPLTGSIGAFTLTVGLASWFHGY--GTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFIAS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKREAQTGLYLTLTF 160
Cdd:MTH00009   88 EVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2125669188 161 AIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:MTH00009  168 GAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHH 224
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-213 1.97e-55

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 178.34  E-value: 1.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   1 DPSPWPLVASIGALSLTFGGVMFMHnYSGGgQLLCLGVVTVLYVMLTWWRDIIREASFEGQHTSAVQDGLRLGMILFIVS 80
Cdd:MTH00028   12 DPSPWPFVGASGAFLFTSGAVILFH-YSDY-RLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFILS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  81 EVMFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGG--------------- 145
Cdd:MTH00028   90 EVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTgnpaslekgtqgieg 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188 146 ---------------------LKREAQTGLYLTLTFAIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTI 204
Cdd:MTH00028  170 pnpsngappdpqkgptfllsdFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTT 249


                  ....*....
gi 2125669188 205 FLAICAIQI 213
Cdd:MTH00028  250 FLIVCFIRL 258
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 3-217 4.66e-43

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 145.10  E-value: 4.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188   3 SPWPLVASIGALSLTFGGVMFMHNYSGGGQLLCLgvVTVLYVMLTWWRDIIREaSFEGQHTSAVQDGLRLGMILFIVSEV 82
Cdd:MTH00083   11 SSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSL--LYLLFISFLWGKDISME-GLSGYHNFFVMDGFKFGMILFIFSEF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  83 MFFFAFFWAFFTSSLAPVFNIGGVWPPAGLEVISPWGLPLLNTVLLLSSGATVTWAHHAIVGGLKrEAQTGLYLTLTFAI 162
Cdd:MTH00083   88 MFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNK-SCTNSLLLTCFLGL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2125669188 163 YFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:MTH00083  167 YFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSH 221
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 62-217 7.83e-34

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: 119.23  E-value: 7.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  62 HTSAVQDGLRLGMILFIVSEVMFFFAFFWAFFTSSLAPVfniggVWPPAGlevISPWGLPLLNTVLLLSSGATVTWAHHA 141
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPP-----VEFGAG---LDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2125669188 142 IVGGL--KREAQTGLYLTLTFAIYFTTFQFLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYLDH 217
Cdd:cd00386    73 LAARRgnRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGH 150
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
59-217 2.57e-22

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 89.52  E-value: 2.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188  59 EGQHTSAVQDGLRLGMILFIVSEVMFFFAFfwaffTSSLAPVFNIGGVWPPAGLEVisPWGLPLLNTVLLLSSGATVTWA 138
Cdd:COG1845     5 EAPHAPERRSPGKLGMWLFLASEVMLFAAL-----FAAYFVLRASAPDWPAGAELL--DLPLPLINTLLLLLSSFTVALA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188 139 HHAIVGGLKREAQTGLYLTLTFAIYFTTFQFLEY---VEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIYL 215
Cdd:COG1845    78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR 157


                  ..
gi 2125669188 216 DH 217
Cdd:COG1845   158 GG 159
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 130-213 1.65e-06

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: 46.84  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188 130 SSGATVTWAHHAIVGGLKREAQTGLYLTLTFAIYFTTFQFLEY---VEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFL 206
Cdd:cd02862    63 TSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLHVLIGLGIL 142


                  ....*..
gi 2125669188 207 AICAIQI 213
Cdd:cd02862   143 LWVAWRA 149
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 130-210 7.11e-06

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: 45.18  E-value: 7.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188 130 SSGATVTWAHHAIVGGLKREAQTGLYLTLTFAIYFTTFQFLEY-------VEAPFSMSDGV--YGSTFFMATGFHGFHVL 200
Cdd:cd02864    72 TSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveeGVRPWGNPWGAaqFGASFFMITGFHGTHVT 151

                          90
                  ....*....|
gi 2125669188 201 IGTIFLAICA 210
Cdd:cd02864   152 IGVIYLIIIA 161
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 138-214 7.23e-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: 41.84  E-value: 7.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125669188 138 AHHAIVGGLKREAQTGLYLTLTFAIYFTTFQ---FLEYVEAPFSMSDGVYGSTFFMATGFHGFHVLIGTIFLAICAIQIY 214
Cdd:cd02863    70 AMIAMNKNNKKKVILWLIITFLLGLGFVGMEiyeFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLK 149
 
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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