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Conserved domains on  [gi|733111454|gb|AIZ95290|]
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cytochrome oxidase subunit 3, partial (mitochondrion) [Sargassum polyceratium]

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 ...
 1-142 4.29e-62

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: 190.42  E-value: 4.29e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEAL 80
Cdd:cd01665   65 LGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAI 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733111454  81 LGLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:cd01665  145 LGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRL 206
 
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 ...
 1-142 4.29e-62

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: 190.42  E-value: 4.29e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEAL 80
Cdd:cd01665   65 LGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAI 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733111454  81 LGLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:cd01665  145 LGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRL 206
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-142 7.41e-60

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 185.00  E-value: 7.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEAL 80
Cdd:MTH00155  79 WGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQAT 158

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733111454  81 LGLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:MTH00155 159 QSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRH 220
COX3 pfam00510
Cytochrome c oxidase subunit III;
2-142 5.54e-56

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 175.29  E-value: 5.54e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454    2 GMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEALL 81
Cdd:pfam00510  79 GMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQ 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733111454   82 GLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:pfam00510 159 GLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRL 219
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
1-142 8.47e-29

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 103.78  E-value: 8.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSpvfniGGVWPpAGIEAISPWgLPLLNTIILLSSGASVTWAHHAIVGGFKKEAL 80
Cdd:COG1845   18 LGMWLFLASEVMLFAALFAAYFVLRAS-----APDWP-AGAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKGLR 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733111454  81 LGLVITIIFAVIFTGLQGFEY---INAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:COG1845   91 LWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRA 155
 
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 ...
 1-142 4.29e-62

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: 190.42  E-value: 4.29e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEAL 80
Cdd:cd01665   65 LGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAI 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733111454  81 LGLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:cd01665  145 LGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRL 206
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-142 7.41e-60

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 185.00  E-value: 7.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEAL 80
Cdd:MTH00155  79 WGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQAT 158

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733111454  81 LGLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:MTH00155 159 QSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRH 220
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 2-142 8.72e-59

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 182.64  E-value: 8.72e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   2 GMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEALL 81
Cdd:MTH00024  82 GMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAIL 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733111454  82 GLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:MTH00024 162 GLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRL 222
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-141 3.40e-57

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 178.63  E-value: 3.40e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEAL 80
Cdd:MTH00189  80 YGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAI 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733111454  81 LGLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFR 141
Cdd:MTH00189 160 QALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLR 220
COX3 pfam00510
Cytochrome c oxidase subunit III;
2-142 5.54e-56

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 175.29  E-value: 5.54e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454    2 GMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEALL 81
Cdd:pfam00510  79 GMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQ 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733111454   82 GLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:pfam00510 159 GLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRL 219
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 2-142 6.86e-56

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 175.14  E-value: 6.86e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   2 GMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEALL 81
Cdd:MTH00118  82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733111454  82 GLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRL 222
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 2-142 1.07e-55

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 174.98  E-value: 1.07e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   2 GMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEALL 81
Cdd:MTH00052  83 GMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAII 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733111454  82 GLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:MTH00052 163 GLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRL 223
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-142 3.90e-54

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 170.84  E-value: 3.90e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEAL 80
Cdd:MTH00141  79 WGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSAL 158

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733111454  81 LGLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:MTH00141 159 QGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRL 220
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 2-142 5.73e-54

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 170.29  E-value: 5.73e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   2 GMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEALL 81
Cdd:MTH00039  81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733111454  82 GLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:MTH00039 161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRL 221
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 2-141 1.34e-48

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 156.81  E-value: 1.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   2 GMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEALL 81
Cdd:MTH00099  82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454  82 GLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFR 141
Cdd:MTH00099 162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLR 221
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 2-141 5.00e-48

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 155.31  E-value: 5.00e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   2 GMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEALL 81
Cdd:MTH00130  82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454  82 GLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFR 141
Cdd:MTH00130 162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLR 221
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-142 6.42e-48

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 154.94  E-value: 6.42e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEAL 80
Cdd:MTH00219  82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733111454  81 LGLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRG 223
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-142 3.47e-47

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 154.07  E-value: 3.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGG------ 74
Cdd:MTH00028  81 LGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTgnpasl 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454  75 ------------------------------FKKEALLGLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFH 124
Cdd:MTH00028 161 ekgtqgiegpnpsngappdpqkgptfllsdFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTH 240

                        170
                 ....*....|....*...
gi 733111454 125 GFHVIIGTIFLSICAFRL 142
Cdd:MTH00028 241 GLHVLVGTTFLIVCFIRL 258
PLN02194 PLN02194
cytochrome-c oxidase
 2-141 5.71e-47

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 152.90  E-value: 5.71e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   2 GMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEALL 81
Cdd:PLN02194  85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454  82 GLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFR 141
Cdd:PLN02194 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIR 224
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 2-141 7.13e-47

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 152.21  E-value: 7.13e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   2 GMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEALL 81
Cdd:MTH00075  82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454  82 GLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFR 141
Cdd:MTH00075 162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLR 221
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 2-141 3.22e-42

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 140.36  E-value: 3.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   2 GMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGFKKEALL 81
Cdd:MTH00009  80 GMILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQ 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454  82 GLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFR 141
Cdd:MTH00009 160 ALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLR 219
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 1-142 1.90e-37

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 127.76  E-value: 1.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSPVFNIGGVWPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIVGGfKKEAL 80
Cdd:MTH00083  77 FGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLS-NKSCT 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733111454  81 LGLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:MTH00083 156 NSLLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRL 217
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 1-142 7.33e-37

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: 124.24  E-value: 7.33e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSPvfniggvwPPAGIEAISPWGLPLLNTIILLSSGASVTWAHHAIV--GGFKKE 78
Cdd:cd00386   11 LGMWLFILSEVMLFGSFFWAYFHSRLSP--------PVEFGAGLDPLDLPLLNTNTLLLSGSSVTWAHASLAarRGNRKK 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 733111454  79 ALLGLVITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:cd00386   83 ARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRL 146
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
1-142 8.47e-29

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 103.78  E-value: 8.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   1 MGMVLFIVSEVMFFFAFFWAFFTSSLSpvfniGGVWPpAGIEAISPWgLPLLNTIILLSSGASVTWAHHAIVGGFKKEAL 80
Cdd:COG1845   18 LGMWLFLASEVMLFAALFAAYFVLRAS-----APDWP-AGAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKGLR 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733111454  81 LGLVITIIFAVIFTGLQGFEY---INAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSICAFRL 142
Cdd:COG1845   91 LWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRA 155
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 48-142 3.94e-09

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: 52.24  E-value: 3.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454  48 GLPLLNTIILLSSGASVTWAHHAIVGGFKKEALLGLVITIIFAVIFTGLQGFE---YINAPFAMSDSVYGSVFFMATGFH 124
Cdd:cd02863   51 PLVFIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTH 130

                         90
                 ....*....|....*...
gi 733111454 125 GFHVIIGTIFLSICAFRL 142
Cdd:cd02863  131 GLHVTFGLIWILVMIIQL 148
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 54-142 5.36e-08

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: 49.42  E-value: 5.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454  54 TIILLSSGASVTWAHHAIVGGFKKEALLGLVITIIFAVIFTGLQGFEYINAPFAMSD---------SVYGSVFFMATGFH 124
Cdd:cd02864   67 TFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVrpwgnpwgaAQFGASFFMITGFH 146

                         90
                 ....*....|....*...
gi 733111454 125 GFHVIIGTIFLSICAFRL 142
Cdd:cd02864  147 GTHVTIGVIYLIIIARKV 164
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 5-137 2.13e-06

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 45.29  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733111454   5 LFIVSEVMFFFAFFWAFFTSSLSPVFNIGgvwppagieaiSPWGLPLLNTIILLSSGASVTWAHHAIVggfKKEALLGLV 84
Cdd:MTH00049  59 LFILSEVIIFGSLLVCCLWFDDWSYISLS-----------SSLEIPFVGCFLLLGSSITVTAYHHLLG---WKYCDLFLY 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 733111454  85 ITIIFAVIFTGLQGFEYINAPFAMSDSVYGSVFFMATGFHGFHVIIGTIFLSI 137
Cdd:MTH00049 125 LTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLST 177
 
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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