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Conserved domains on  [gi|2064310045|gb|QXI86635|]
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cytochrome c oxidase subunit 3 (mitochondrion) [Koutabatermes spinifer]

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
 2-256 8.80e-173

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 476.21  E-value: 8.80e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   2 HENHPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWG 81
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  82 MILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQG 161
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 162 LFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYW 241
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2064310045 242 HFVDVVWLFLYISIY 256
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 2-256 8.80e-173

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 476.21  E-value: 8.80e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   2 HENHPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWG 81
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  82 MILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQG 161
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 162 LFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYW 241
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2064310045 242 HFVDVVWLFLYISIY 256
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
5-260 4.35e-135

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 380.99  E-value: 4.35e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   5 HPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDD--TLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWGM 82
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGnmTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  83 ILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQGL 162
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 163 FFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYWH 242
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 2064310045 243 FVDVVWLFLYISIYWWGS 260
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 17-258 5.37e-135

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: 380.32  E-value: 5.37e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  17 LTGAIGAMTMLMGLIKWFHQYD-DTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWGMILFIVSEILFFVS 95
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGgPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  96 FFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQGLFFTVLLGIYFTAL 175
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 176 QAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYWHFVDVVWLFLYISI 255
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2064310045 256 YWW 258
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
79-258 7.99e-58

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 182.74  E-value: 7.99e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  79 RWGMILFIVSEILFFVSFFWAYFHSSLSptielgSTWPPTGIQPFNPmQVPLLNTAILLASGVTVTWAHHSLLENNATQA 158
Cdd:COG1845    17 KLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVRAARRGDRKGL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 159 TQGLFFTVLLGIYFTALQAYEY---VEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFE 235
Cdd:COG1845    90 RLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVE 169

                         170       180
                  ....*....|....*....|...
gi 2064310045 236 AAAWYWHFVDVVWLFLYISIYWW 258
Cdd:COG1845   170 AAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 81-259 6.96e-11

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: 59.87  E-value: 6.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  81 GMILFIVSEILFFVSFFWAYFHSSlsptiELGSTWPPTGIQPFNpMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQ 160
Cdd:TIGR02897  13 GFWIFLGAEIALFATLFATYLVLQ-----HGGDYAGKMPAELFE-LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 161 GLFFTVLLGIYFTALQAYE---YVEAPFTIADSAYGSTFFMATGFHGLHVIIGTtFLITCLLRQTTLH-FSSNHHFGFEA 236
Cdd:TIGR02897  87 WMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGI-VWAICLLIQIQRRgLTPYTAPKVFI 165

                         170       180
                  ....*....|....*....|...
gi 2064310045 237 AAWYWHFVDVVWLFLYISIYWWG 259
Cdd:TIGR02897 166 VSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 2-256 8.80e-173

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 476.21  E-value: 8.80e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   2 HENHPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWG 81
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  82 MILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQG 161
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 162 LFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYW 241
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2064310045 242 HFVDVVWLFLYISIY 256
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 2-260 6.92e-158

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 439.00  E-value: 6.92e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   2 HENHPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWG 81
Cdd:MTH00118    3 HQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  82 MILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQG 161
Cdd:MTH00118   83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 162 LFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYW 241
Cdd:MTH00118  163 LTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYW 242

                         250
                  ....*....|....*....
gi 2064310045 242 HFVDVVWLFLYISIYWWGS 260
Cdd:MTH00118  243 HFVDVVWLFLYISIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-260 1.84e-154

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 430.16  E-value: 1.84e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   1 MHENHPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRW 80
Cdd:MTH00189    1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  81 GMILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQ 160
Cdd:MTH00189   81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 161 GLFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWY 240
Cdd:MTH00189  161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240

                         250       260
                  ....*....|....*....|
gi 2064310045 241 WHFVDVVWLFLYISIYWWGS 260
Cdd:MTH00189  241 WHFVDVVWLFLYVSIYWWGS 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-260 1.50e-144

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 405.27  E-value: 1.50e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   1 MHENHPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRW 80
Cdd:MTH00039    1 MTHQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  81 GMILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQ 160
Cdd:MTH00039   81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 161 GLFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWY 240
Cdd:MTH00039  161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWY 240

                         250       260
                  ....*....|....*....|
gi 2064310045 241 WHFVDVVWLFLYISIYWWGS 260
Cdd:MTH00039  241 WHFVDVVWLFLYVCIYWWGS 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 2-260 3.19e-143

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 401.80  E-value: 3.19e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   2 HENHPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWG 81
Cdd:MTH00099    3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  82 MILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQG 161
Cdd:MTH00099   83 MILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 162 LFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYW 241
Cdd:MTH00099  163 LFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYW 242

                         250
                  ....*....|....*....
gi 2064310045 242 HFVDVVWLFLYISIYWWGS 260
Cdd:MTH00099  243 HFVDVVWLFLYVSIYWWGS 261
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 5-260 4.46e-143

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 401.19  E-value: 4.46e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   5 HPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWGMIL 84
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  85 FIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQGLFF 164
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 165 TVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYWHFV 244
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 2064310045 245 DVVWLFLYISIYWWGS 260
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 2-260 9.44e-139

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 390.66  E-value: 9.44e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   2 HENHPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWG 81
Cdd:MTH00130    3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  82 MILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQG 161
Cdd:MTH00130   83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 162 LFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYW 241
Cdd:MTH00130  163 LTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYW 242

                         250
                  ....*....|....*....
gi 2064310045 242 HFVDVVWLFLYISIYWWGS 260
Cdd:MTH00130  243 HFVDVVWLFLYISIYWWGS 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 2-260 1.05e-137

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 387.95  E-value: 1.05e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   2 HENHPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWG 81
Cdd:MTH00075    3 HQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  82 MILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQG 161
Cdd:MTH00075   83 MILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 162 LFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYW 241
Cdd:MTH00075  163 LALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYW 242

                         250
                  ....*....|....*....
gi 2064310045 242 HFVDVVWLFLYISIYWWGS 260
Cdd:MTH00075  243 HFVDVVWLFLYVSIYWWGS 261
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 5-260 1.13e-137

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 387.99  E-value: 1.13e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   5 HPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWGMIL 84
Cdd:MTH00219    7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  85 FIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQGLFF 164
Cdd:MTH00219   87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 165 TVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYWHFV 244
Cdd:MTH00219  167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*.
gi 2064310045 245 DVVWLFLYISIYWWGS 260
Cdd:MTH00219  247 DVVWLFLYVSIYWWGS 262
COX3 pfam00510
Cytochrome c oxidase subunit III;
5-260 4.35e-135

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 380.99  E-value: 4.35e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   5 HPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDD--TLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWGM 82
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGnmTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  83 ILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQGL 162
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 163 FFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYWH 242
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 2064310045 243 FVDVVWLFLYISIYWWGS 260
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 17-258 5.37e-135

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: 380.32  E-value: 5.37e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  17 LTGAIGAMTMLMGLIKWFHQYD-DTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWGMILFIVSEILFFVS 95
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGgPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  96 FFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQGLFFTVLLGIYFTAL 175
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 176 QAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYWHFVDVVWLFLYISI 255
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2064310045 256 YWW 258
Cdd:cd01665   241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 5-260 1.19e-128

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 364.93  E-value: 1.19e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   5 HPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWGMIL 84
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  85 FIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQGLFF 164
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 165 TVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYWHFV 244
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 2064310045 245 DVVWLFLYISIYWWGS 260
Cdd:MTH00009  244 DVVWIFLYLCIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 5-260 2.33e-126

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 359.07  E-value: 2.33e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   5 HPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWGMIL 84
Cdd:MTH00024    6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  85 FIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQGLFF 164
Cdd:MTH00024   86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 165 TVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYWHFV 244
Cdd:MTH00024  166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245

                         250
                  ....*....|....*.
gi 2064310045 245 DVVWLFLYISIYWWGS 260
Cdd:MTH00024  246 DVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-260 7.24e-118

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 337.54  E-value: 7.24e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   1 MHENHPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRW 80
Cdd:MTH00052    3 QQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  81 GMILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQ 160
Cdd:MTH00052   83 GMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAII 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 161 GLFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWY 240
Cdd:MTH00052  163 GLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWY 242

                         250       260
                  ....*....|....*....|
gi 2064310045 241 WHFVDVVWLFLYISIYWWGS 260
Cdd:MTH00052  243 WHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 5-260 3.25e-102

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 299.29  E-value: 3.25e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   5 HPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRWGMIL 84
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  85 FIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHH---------------- 148
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHaiigtgnpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 149 --------------------SLLENNATQATQGLFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVI 208
Cdd:MTH00028  166 giegpnpsngappdpqkgptFLLSDFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2064310045 209 IGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 260
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 3-259 1.68e-90

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 268.46  E-value: 1.68e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   3 ENHPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDD--TLLGIGAIITVLTMIQWWRDVTREGTYQGLHTKMVTTGLRW 80
Cdd:PLN02194    5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGgaRLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  81 GMILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQ 160
Cdd:PLN02194   85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 161 GLFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWY 240
Cdd:PLN02194  165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244

                         250
                  ....*....|....*....
gi 2064310045 241 WHFVDVVWLFLYISIYWWG 259
Cdd:PLN02194  245 WHFVDVVWLFLFVSIYWWG 263
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 70-258 1.05e-73

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: 222.85  E-value: 1.05e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  70 HTKMVTTGLRWGMILFIVSEILFFVSFFWAYFHSSLSPTIELGstwpptgiQPFNPMQVPLLNTAILLASGVTVTWAHHS 149
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 150 LL--ENNATQATQGLFFTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFS 227
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2064310045 228 SNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 258
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 5-260 8.69e-73

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 222.91  E-value: 8.69e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045   5 HPFHMVNKSPWPLTGAIGAMTMLMGLIKWFHQYDDTLLGIGAIITVLTMIQWWRDVTREGtYQGLHTKMVTTGLRWGMIL 84
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  85 FIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIQPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNaTQATQGLFF 164
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 165 TVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAAAWYWHFV 244
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*.
gi 2064310045 245 DVVWLFLYISIYWWGS 260
Cdd:MTH00083  241 DVVWLFLFVFVYWWSY 256
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
79-258 7.99e-58

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 182.74  E-value: 7.99e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  79 RWGMILFIVSEILFFVSFFWAYFHSSLSptielgSTWPPTGIQPFNPmQVPLLNTAILLASGVTVTWAHHSLLENNATQA 158
Cdd:COG1845    17 KLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVRAARRGDRKGL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 159 TQGLFFTVLLGIYFTALQAYEY---VEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFE 235
Cdd:COG1845    90 RLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVE 169

                         170       180
                  ....*....|....*....|...
gi 2064310045 236 AAAWYWHFVDVVWLFLYISIYWW 258
Cdd:COG1845   170 AAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 81-256 1.59e-23

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: 93.84  E-value: 1.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  81 GMILFIVSEILFFVSFFWAYF-HSSLSP---TIELGSTWPPTGiqpfnpmqvpLLNTAILLASGVTVTWAHHSLLENNAT 156
Cdd:cd02862    12 GMWVFILSELLAFGALFIAYAvYRALYPelfAAGSAHLDLLLG----------ALNTLVLLTSSFTVALAVRAARAGRRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 157 QATQGLFFTVLLGIYFTALQAYEYVEApFTIADSAYGSTFFMA----TGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHF 232
Cdd:cd02862    82 RARRWLAAAVLLGLVFLVIKYFEYAHK-IAAGIDPDAGLFFTLyfllTGFHLLHVLIGLGILLWVAWRARRGRYSARDYE 160

                         170       180
                  ....*....|....*....|....
gi 2064310045 233 GFEAAAWYWHFVDVVWLFLYISIY 256
Cdd:cd02862   161 GVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 76-258 2.26e-20

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: 85.50  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  76 TGLRWGMILFIVSEILFFVSFFWAYFHSSLSPTIELGStwpptgiqPFNPMQVPLLNTAILLASGVTVTWAHHSLLENNA 155
Cdd:cd02865     7 SPGWWGLWVFMAVEGTLFALLISAYFMRMTSGDWQPGA--------PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 156 TQATQGLFFTVLLGIYFTALQAYEY---VEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHF 232
Cdd:cd02865    79 VLARLGLALAGALALAFLAGQLLAWhalNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRL 158

                         170       180
                  ....*....|....*....|....*.
gi 2064310045 233 GFEAAAWYWHFVDVVWLFLYISIYWW 258
Cdd:cd02865   159 PVELCALYWHFLLLVWLVLLALLYGT 184
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 81-258 3.14e-19

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: 82.93  E-value: 3.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  81 GMILFIVSEILFFVSFFWAYFHSSLSPTIELGSTWPPTGIqPFNPMQVPL----LNTAILLASGVTVTWAHHSLLENNAT 156
Cdd:cd02864    12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 157 QATQGLFFTVLLGIYFTALQAYEY----VEAPFTIADSAYG-----STFFMATGFHGLHVIIGTTFLITCLLRQTTLHFS 227
Cdd:cd02864    91 AAARLMLATALLGATFVGMQAFEWtkliVEEGVRPWGNPWGaaqfgASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQ 170

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2064310045 228 SNHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 258
Cdd:cd02864   171 RIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 81-256 8.11e-18

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: 78.82  E-value: 8.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  81 GMILFIVSEILFFVSFFWAYFhsslspTIELGSTWPPTGIQPFNPMQVpLLNTAILLASGVTVTWAHHSLLENNATQATQ 160
Cdd:cd02863    12 GFWIYLMSDCILFATLFATYA------VLSGNTAGGPPGHELFELPLV-FIETFLLLLSSFTCGLAMIAMNKNNKKKVIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 161 GLFFTVLLGIYFTALQAYE---YVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEAA 237
Cdd:cd02863    85 WLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCL 164

                         170
                  ....*....|....*....
gi 2064310045 238 AWYWHFVDVVWLFLYISIY 256
Cdd:cd02863   165 SLFWHFLDIVWIFVFTVVY 183
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 84-256 9.25e-17

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 76.49  E-value: 9.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  84 LFIVSEILFFVSFFWAYFHSSLSPTIELGStwpptgiqpfnPMQVPLLNTAILLASGVTVTWAHHSLLENNATQAtqgLF 163
Cdd:MTH00049   59 LFILSEVIIFGSLLVCCLWFDDWSYISLSS-----------SLEIPFVGCFLLLGSSITVTAYHHLLGWKYCDLF---LY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 164 FTVLLGIYFTALQAYEYVEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFgfeaAAWYWHF 243
Cdd:MTH00049  125 LTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLSTLLLVGSSSFGVYRSTV----LTWYWHF 200

                         170
                  ....*....|...
gi 2064310045 244 VDVVWLFLYISIY 256
Cdd:MTH00049  201 VDYIWLLVYLIVY 213
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 81-259 6.96e-11

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: 59.87  E-value: 6.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  81 GMILFIVSEILFFVSFFWAYFHSSlsptiELGSTWPPTGIQPFNpMQVPLLNTAILLASGVTVTWAHHSLLENNATQATQ 160
Cdd:TIGR02897  13 GFWIFLGAEIALFATLFATYLVLQ-----HGGDYAGKMPAELFE-LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 161 GLFFTVLLGIYFTALQAYE---YVEAPFTIADSAYGSTFFMATGFHGLHVIIGTtFLITCLLRQTTLH-FSSNHHFGFEA 236
Cdd:TIGR02897  87 WMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGI-VWAICLLIQIQRRgLTPYTAPKVFI 165

                         170       180
                  ....*....|....*....|...
gi 2064310045 237 AAWYWHFVDVVWLFLYISIYWWG 259
Cdd:TIGR02897 166 VSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 80-260 1.08e-10

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 59.41  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045  80 WGMILFIVSEILFFVSFFWAYfhsslsPTIELGSTWPPTGIQPFNpMQVPLLNTAILLASGVTVTWAHHSLLENNATQAT 159
Cdd:PRK10663   27 FGFWIYLMSDCILFSILFATY------AVLVNGTAGGPTGKDIFE-LPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064310045 160 QGLFFTVLLGIYFTALQAYEY---VEAPFTIADSAYGSTFFMATGFHGLHVIIGTTFLITCLLRQTTLHFSSNHHFGFEA 236
Cdd:PRK10663  100 SWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMC 179

                         170       180
                  ....*....|....*....|....
gi 2064310045 237 AAWYWHFVDVVWLFLYISIYWWGS 260
Cdd:PRK10663  180 LSLFWHFLDVVWICVFTVVYLMGA 203
 
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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