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Conserved domains on  [gi|169649033|gb|ACA62600|]
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cytochrome c oxidase subunit III, partial (mitochondrion) [Zaprionus badyi]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10009592)

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
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-194 2.96e-123

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 348.32  E-value: 2.96e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00155  62 EGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVT 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00155 142 VTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHL 221

                        170       180       190
                 ....*....|....*....|....*....|....
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIY 194
Cdd:MTH00155 222 NNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-194 2.96e-123

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 348.32  E-value: 2.96e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00155  62 EGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVT 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00155 142 VTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHL 221

                        170       180       190
                 ....*....|....*....|....*....|....
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIY 194
Cdd:MTH00155 222 NNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-196 1.50e-103

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: 297.89  E-value: 1.50e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:cd01665   48 ESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGAT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:cd01665  128 VTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLL 207

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:cd01665  208 KGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYWW 243
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-197 2.62e-99

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 287.77  E-value: 2.62e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033    1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:pfam00510  61 EGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:pfam00510 141 VTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLL 220

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 169649033  161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:pfam00510 221 KYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWWG 257
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
14-196 5.18e-49

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 157.70  E-value: 5.18e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  14 IGLRWGMILFILSEILFFVSFFWAFFHSSLSpaielgASWPPAGIISFNPFqIPLLNTAILLASGVTVTWAHHSLMEGNH 93
Cdd:COG1845   14 SPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  94 SQTSQGLFFTVLLGIYFSILQAYEY---IEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHLNNHFSKTHHF 170
Cdd:COG1845   87 KGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHT 166

                        170       180
                 ....*....|....*....|....*.
gi 169649033 171 GFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:COG1845  167 GVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 68-197 1.82e-09

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: 54.86  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   68 LLNTAILLASGVTVTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYE---YIEAPFTIADSVYGSTFFMATGFHGIH 144
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 169649033  145 VLIGTTFLLTCLLRHLNNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-194 2.96e-123

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 348.32  E-value: 2.96e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00155  62 EGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVT 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00155 142 VTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHL 221

                        170       180       190
                 ....*....|....*....|....*....|....
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIY 194
Cdd:MTH00155 222 NNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-197 1.06e-108

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 311.89  E-value: 1.06e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00118  64 ESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVT 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00118 144 VTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLI 223

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00118 224 KFHFTTNHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 260
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-197 1.05e-104

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 301.51  E-value: 1.05e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00189  63 ESTFQGFHTPPVQKGLRYGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVT 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00189 143 VTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQI 222

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00189 223 QGHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 259
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-196 1.50e-103

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: 297.89  E-value: 1.50e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:cd01665   48 ESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGAT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:cd01665  128 VTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLL 207

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:cd01665  208 KGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYWW 243
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-198 2.04e-102

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 295.65  E-value: 2.04e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00141  62 ESTFQGFHTSKVQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVT 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00141 142 VTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLL 221

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWGG 198
Cdd:MTH00141 222 LGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLSIYWWGS 259
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-198 5.27e-102

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 294.71  E-value: 5.27e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00039  63 EATFQGMHTLIVINGLRYGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVT 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00039 143 ITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLI 222

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWGG 198
Cdd:MTH00039 223 NHHFSNNHHFGFEAAAWYWHFVDVVWLFLYVCIYWWGS 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-197 1.99e-99

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 288.16  E-value: 1.99e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00099  64 ESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVS 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00099 144 ITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQL 223

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00099 224 KFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-197 2.62e-99

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 287.77  E-value: 2.62e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033    1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:pfam00510  61 EGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:pfam00510 141 VTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLL 220

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 169649033  161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:pfam00510 221 KYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWWG 257
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-197 1.63e-98

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 285.91  E-value: 1.63e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00219  65 ESTFMGLHTSKVSTGLRIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVT 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00219 145 VTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGL 224

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00219 225 MLHFSKNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-197 8.15e-98

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 284.35  E-value: 8.15e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00130  64 EGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVT 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00130 144 VTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQI 223

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00130 224 QYHFTSEHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 260
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-197 5.92e-97

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 282.02  E-value: 5.92e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00075  64 EGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVT 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00075 144 VTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQI 223

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00075 224 NFHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-197 8.88e-93

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 271.63  E-value: 8.88e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00024  64 ESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGAT 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00024 144 VTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLL 223

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00024 224 SNQFTRRQHVGFEAASWYWHFVDVVWLFLYLCIYWWG 260
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-197 2.23e-91

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 267.86  E-value: 2.23e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00009  62 EGTYMGHHTSYVTKGLRWGMILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVT 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00009 142 VTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTW 221

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00009 222 SHHFSTGHHFGFEAAAWYWHFVDVVWIFLYLCIYWWG 258
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-197 5.12e-86

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 254.33  E-value: 5.12e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00052  65 ESTYQGHHTLIVKQGLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGAT 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:MTH00052 145 VTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLI 224

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00052 225 NHQFTRHHHFGFEAAAWYWHFVDVVWLFLFIFMYWWG 261
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-197 3.82e-74

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 225.33  E-value: 3.82e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:MTH00028  64 EGTHQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGAT 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNH-------SQTSQ-----------------------------GLFFTVLLGIYFSILQAYEYIEAPFT 124
Cdd:MTH00028 144 VTWAHHAIIGTGNpaslekgTQGIEgpnpsngappdpqkgptfllsdfrtnaviGLLMTILLGIIFTGLQAFEYKEASFA 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169649033 125 IADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHLNNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00028 224 ISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
PLN02194 PLN02194
cytochrome-c oxidase
 1-198 1.21e-66

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 205.28  E-value: 1.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVT 80
Cdd:PLN02194  67 ESTLEGHHTKVVQLGPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAA 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  81 VTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:PLN02194 147 VTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQY 226

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 169649033 161 NNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWGG 198
Cdd:PLN02194 227 LGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWWGG 264
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 8-196 7.15e-63

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: 192.80  E-value: 7.15e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   8 HTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASwppagiisFNPFQIPLLNTAILLASGVTVTWAHHS 87
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGAG--------LDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  88 LM--EGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHLNNHFS 165
Cdd:cd00386   73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 169649033 166 KTHHFGFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:cd00386  153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 4-197 5.71e-62

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 192.86  E-value: 5.71e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   4 YQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPAGIISFNPFQIPLLNTAILLASGVTVTW 83
Cdd:MTH00083  63 LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTW 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  84 AHHSLMEGNhSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHLNNH 163
Cdd:MTH00083 143 SHHSLCLSN-KSCTNSLLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSH 221

                        170       180       190
                 ....*....|....*....|....*....|....
gi 169649033 164 FSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00083 222 FNYNHHLGLEFAILYWHFVDVVWLFLFVFVYWWS 255
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
14-196 5.18e-49

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 157.70  E-value: 5.18e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  14 IGLRWGMILFILSEILFFVSFFWAFFHSSLSpaielgASWPPAGIISFNPFqIPLLNTAILLASGVTVTWAHHSLMEGNH 93
Cdd:COG1845   14 SPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  94 SQTSQGLFFTVLLGIYFSILQAYEY---IEAPFTIADSVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHLNNHFSKTHHF 170
Cdd:COG1845   87 KGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHT 166

                        170       180
                 ....*....|....*....|....*.
gi 169649033 171 GFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:COG1845  167 GVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 68-194 3.19e-21

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: 86.13  E-value: 3.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  68 LLNTAILLASGVTVTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEY---IEAPFTIADSVYGSTFFMATGFHGIH 144
Cdd:cd02862   55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 169649033 145 VLIGTTFLLTCLLRHLNNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIY 194
Cdd:cd02862  135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 63-194 8.49e-17

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 74.95  E-value: 8.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  63 PFQIPLLNTAILLASGVTVTWAHHSLmegNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPFTIADSVYGSTFFMATGFHG 142
Cdd:MTH00049  89 SLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169649033 143 IHVLIGTTFLLTCLLRHLNNhFSKTHHfgfEAAAWYWHFVDVVWLFLYITIY 194
Cdd:MTH00049 166 SHVVLGVVGLSTLLLVGSSS-FGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 19-196 1.63e-16

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: 74.07  E-value: 1.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  19 GMILFILSEILFFVSFFWAFFHSSLSPAIelgaSWPPAG---IISFNPFQIPL----LNTAILLASGVTVTWAHHSLMEG 91
Cdd:cd02864   12 MMWFFLLSDAFIFSSFLIAYMTARISTTE----PWPLPSdvfALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  92 NHSQTSQGLFFTVLLGIYFSILQAYEY-----------IEAPFTIAdsVYGSTFFMATGFHGIHVLIGTTFLLTCLLRHL 160
Cdd:cd02864   88 NRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVW 165

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169649033 161 NNHFSKTHHF-GFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:cd02864  166 RGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 67-196 9.40e-16

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: 71.63  E-value: 9.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  67 PLLNTAILLASGVTVTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEYIEAPF---TIADSVYGSTFFMATGFHGI 143
Cdd:cd02865   52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169649033 144 HVLIGTTFLLTCLLRHLNNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:cd02865  132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 64-194 9.98e-15

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: 68.81  E-value: 9.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  64 FQIPL--LNTAILLASGVTVTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYE---YIEAPFTIADSVYGSTFFMAT 138
Cdd:cd02863   48 FELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLV 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169649033 139 GFHGIHVLIGTTFLLTCLLRHLNNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIY 194
Cdd:cd02863  128 GTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 64-197 9.94e-10

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 55.56  E-value: 9.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033  64 FQIP--LLNTAILLASGVTVTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYEY---IEAPFTIADSVYGSTFFMAT 138
Cdd:PRK10663  64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALV 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169649033 139 GFHGIHVLIGTTFLLTCLLRHLNNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:PRK10663 144 GTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 68-197 1.82e-09

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: 54.86  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169649033   68 LLNTAILLASGVTVTWAHHSLMEGNHSQTSQGLFFTVLLGIYFSILQAYE---YIEAPFTIADSVYGSTFFMATGFHGIH 144
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 169649033  145 VLIGTTFLLTCLLRHLNNHFSKTHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
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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