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Conserved domains on  [gi|2235262570|ref|YP_010373085|]
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cytochrome c oxidase subunit III (mitochondrion) [Teredorus hainanensis]

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
 5-259 5.87e-145

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 406.10  E-value: 5.87e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   5 NYNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  85 MILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQS 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 165 LLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2235262570 245 HFVDVIWLFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 5.87e-145

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 406.10  E-value: 5.87e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   5 NYNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  85 MILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQS 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 165 LLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2235262570 245 HFVDVIWLFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 4.87e-114

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 327.83  E-value: 4.87e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWF--YSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFhgYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  86 ILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 166 LFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 2235262570 246 FVDVIWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 1.14e-111

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: 321.39  E-value: 1.14e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  20 LTGAMGGMIMTTGLAKWF-YSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMILFITSEVLFFMS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMhGYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  99 FFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLFTVILGIYFTML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 179 QAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFVDVIWLFLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2235262570 259 YWW 261
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 6.69e-48

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 157.32  E-value: 6.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  72 LHTMNVSKGLRWGMILFITSEVLFFMSFFWAFFNSSLSSNielglmWPPKGVQPFNPiNIPLLNTIILLSSGITVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 152 SLMESNKTQANQSLLFTVILGIYFTMLQAYEYMEAQ---FSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLH 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2235262570 229 FSSKHHLGFETAAWYWHFVDVIWLFLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-259 5.87e-145

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 406.10  E-value: 5.87e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   5 NYNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWG 84
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  85 MILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQS 164
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 165 LLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYW 244
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 2235262570 245 HFVDVIWLFLYISIY 259
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 4-263 8.00e-133

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 375.44  E-value: 8.00e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   4 TNYNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRW 83
Cdd:MTH00118    2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  84 GMILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQ 163
Cdd:MTH00118   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 164 SLLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWY 243
Cdd:MTH00118  162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 2235262570 244 WHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00118  242 WHFVDVVWLFLYISIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 8-263 2.15e-129

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 366.99  E-value: 2.15e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00189    5 HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLF 167
Cdd:MTH00189   85 FITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00189  165 TVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFV 244

                         250
                  ....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00189  245 DVVWLFLYVSIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 8-263 1.31e-122

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 349.57  E-value: 1.31e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLF 167
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 5-263 2.97e-121

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 346.33  E-value: 2.97e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   5 NYNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWG 84
Cdd:MTH00039    2 THQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  85 MILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQS 164
Cdd:MTH00039   82 MILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 165 LLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYW 244
Cdd:MTH00039  162 LFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYW 241

                         250
                  ....*....|....*....
gi 2235262570 245 HFVDVIWLFLYISIYWWGS 263
Cdd:MTH00039  242 HFVDVVWLFLYVCIYWWGS 260
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 8-263 7.55e-120

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 342.92  E-value: 7.55e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00219    7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLF 167
Cdd:MTH00219   87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00219  167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246

                         250
                  ....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00219  247 DVVWLFLYVSIYWWGS 262
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 8-263 1.08e-118

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 339.80  E-value: 1.08e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00075    6 HAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLF 167
Cdd:MTH00075   86 FITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00075  166 TIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00075  246 DVVWLFLYVSIYWWGS 261
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 4-263 6.25e-118

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 337.85  E-value: 6.25e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   4 TNYNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRW 83
Cdd:MTH00099    2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  84 GMILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQ 163
Cdd:MTH00099   82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 164 SLLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWY 243
Cdd:MTH00099  162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241

                         250       260
                  ....*....|....*....|
gi 2235262570 244 WHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00099  242 WHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 8-263 8.84e-118

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 337.51  E-value: 8.84e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00130    6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLF 167
Cdd:MTH00130   86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00130  166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00130  246 DVVWLFLYISIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
8-263 4.87e-114

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 327.83  E-value: 4.87e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWF--YSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGM 85
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFhgYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  86 ILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSL 165
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 166 LFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 2235262570 246 FVDVIWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 20-261 1.14e-111

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: 321.39  E-value: 1.14e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  20 LTGAMGGMIMTTGLAKWF-YSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMILFITSEVLFFMS 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMhGYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  99 FFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLFTVILGIYFTML 178
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 179 QAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFVDVIWLFLYISI 258
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 2235262570 259 YWW 261
Cdd:cd01665   241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 8-263 4.41e-109

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 315.62  E-value: 4.41e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLF 167
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00009  244 DVVWIFLYLCIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 4-263 9.17e-108

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 312.07  E-value: 9.17e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   4 TNYNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRW 83
Cdd:MTH00024    2 SKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  84 GMILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQ 163
Cdd:MTH00024   82 GMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAIL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 164 SLLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWY 243
Cdd:MTH00024  162 GLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWY 241

                         250       260
                  ....*....|....*....|
gi 2235262570 244 WHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00024  242 WHFVDVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 6-263 1.55e-98

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 289.00  E-value: 1.55e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   6 YNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGM 85
Cdd:MTH00052    5 YYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGM 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  86 ILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSL 165
Cdd:MTH00052   85 ILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 166 LFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWH 245
Cdd:MTH00052  165 ALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWH 244

                         250
                  ....*....|....*...
gi 2235262570 246 FVDVIWLFLYISIYWWGS 263
Cdd:MTH00052  245 FVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 8-263 5.00e-89

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 266.16  E-value: 5.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESN---------- 157
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 158 --------------------------KTQANQSLLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVI 211
Cdd:MTH00028  166 giegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2235262570 212 IGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 8-262 3.62e-76

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 232.25  E-value: 3.62e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWF--YSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGM 85
Cdd:PLN02194    7 HSYHLVDPSPWPISGSLGALATTVGGVMYMhpFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  86 ILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSL 165
Cdd:PLN02194   87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 166 LFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWH 245
Cdd:PLN02194  167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246

                         250
                  ....*....|....*..
gi 2235262570 246 FVDVIWLFLYISIYWWG 262
Cdd:PLN02194  247 FVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 8-263 5.90e-66

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 205.57  E-value: 5.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570   8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGtMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANqSLLF 167
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00083  241 DVVWLFLFVFVYWWSY 256
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 73-261 2.17e-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: 196.66  E-value: 2.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  73 HTMNVSKGLRWGMILFITSEVLFFMSFFWAFFNSSLSSNIELGlmwppkgvQPFNPINIPLLNTIILLSSGITVTWAHHS 152
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 153 LM--ESNKTQANQSLLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFS 230
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2235262570 231 SKHHLGFETAAWYWHFVDVIWLFLYISIYWW 261
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-261 6.69e-48

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 157.32  E-value: 6.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  72 LHTMNVSKGLRWGMILFITSEVLFFMSFFWAFFNSSLSSNielglmWPPKGVQPFNPiNIPLLNTIILLSSGITVTWAHH 151
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 152 SLMESNKTQANQSLLFTVILGIYFTMLQAYEYMEAQ---FSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLH 228
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2235262570 229 FSSKHHLGFETAAWYWHFVDVIWLFLYISIYWW 261
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 133-259 1.85e-22

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: 91.14  E-value: 1.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 133 LLNTIILLSSGITVTWAHHSLMESNKTQANQSLLFTVILGIYFTMLQAYEY---MEAQFSIADSIYGTVFFMATGFHGIH 209
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2235262570 210 VIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFVDVIWLFLYISIY 259
Cdd:cd02862   135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 84-261 1.06e-15

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: 73.30  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570  84 GMILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVqPFNPINIPL----LNTIILLSSGITVTWAHHSLMESNKT 159
Cdd:cd02864    12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 160 QANQSLLFTVILGIYFTMLQAYEYME---------AQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFS 230
Cdd:cd02864    91 AAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQ 170

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2235262570 231 SK-HHLGFETAAWYWHFVDVIWLFLYISIYWW 261
Cdd:cd02864   171 RIgRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 131-259 1.77e-15

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 73.03  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 131 IPLLNTIILLSSGITVTwAHHSLMESNKTQANqsLLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHV 210
Cdd:MTH00049   92 IPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHV 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2235262570 211 IIGTTFLFICLMRQLNLHFSSKHHLgfetAAWYWHFVDVIWLFLYISIY 259
Cdd:MTH00049  169 VLGVVGLSTLLLVGSSSFGVYRSTV----LTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 125-261 3.09e-15

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: 3.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 125 PFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLFTVILGIYFTMLQAYEYMEAQFSI---ADSIYGTVFFM 201
Cdd:cd02865    45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYL 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 202 ATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFVDVIWLFLYISIYWW 261
Cdd:cd02865   125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 133-259 3.37e-14

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: 3.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 133 LLNTIILLSSGITVTWAHHSLMESNKTQANQSLLFTVILGIYFTMLQAYE---YMEAQFSIADSIYGTVFFMATGFHGIH 209
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2235262570 210 VIIGtTFLFICLMRQLNLH-FSSKHHLGFETAAWYWHFVDVIWLFLYISIY 259
Cdd:cd02863   134 VTFG-LIWILVMIIQLKKRgLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 133-263 1.18e-08

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 53.63  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 133 LLNTIILLSSGITVTWAHHSLMESNKTQANQSLLFTVILGIYFTMLQAYEY---MEAQFSIADSIYGTVFFMATGFHGIH 209
Cdd:PRK10663   70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALVGTHGLH 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2235262570 210 VIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFVDVIWLFLYISIYWWGS 263
Cdd:PRK10663  150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 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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