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Conserved domains on  [gi|1824661656|ref|YP_009734782|]
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cytochrome c oxidase subunit III (mitochondrion) [Tetrix ruyuanensis]

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
 5-258 3.15e-153

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 214439  Cd Length: 255  Bit Score: 426.90  E-value: 3.15e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   5 SNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGM 84
Cdd:MTH00155    2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  85 IMFIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSL 164
Cdd:MTH00155   82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 165 TLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWH 244
Cdd:MTH00155  162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241

                         250
                  ....*....|....
gi 1824661656 245 FVDVVWLFLYISIY 258
Cdd:MTH00155  242 FVDVVWLFLYISIY 255
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-258 3.15e-153

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 426.90  E-value: 3.15e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   5 SNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGM 84
Cdd:MTH00155    2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  85 IMFIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSL 164
Cdd:MTH00155   82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 165 TLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWH 244
Cdd:MTH00155  162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241

                         250
                  ....*....|....
gi 1824661656 245 FVDVVWLFLYISIY 258
Cdd:MTH00155  242 FVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-262 5.01e-121

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 345.55  E-value: 5.01e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   7 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFH--TTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGM 84
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  85 IMFIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSL 164
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 165 TLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1824661656 245 FVDVVWLFLYISIYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-260 2.11e-118

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: 338.34  E-value: 2.11e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  19 LTGAIGGMMMTSGLAQWFHTTNAS-LMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIMFIVSEVLFFMS 97
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  98 FFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTML 177
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 178 QAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISI 257
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1824661656 258 YWW 260
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-260 3.62e-47

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 155.39  E-value: 3.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  72 HTKNVSTGLRWGMIMFIVSEVLFFMSFFWAFFNSSLAANvelgtmWPPMGIEPFNPmNIPLLNTIILLSSGITVTWCHHS 151
Cdd:COG1845     8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 152 LMESNKTQAMQSLTLTVILGIYFTMLQAYEYMEAQ---FSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHF 228
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1824661656 229 SASHHIGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:COG1845   161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 132-261 6.20e-08

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: 51.39  E-value: 6.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 132 LLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYE---YMEAQFSIADSVYGTTFFMATGFHGIH 208
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1824661656 209 VIIGTtFLATCLTRHIWEH-FSASHHIGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:TIGR02897 136 VTLGI-VWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-258 3.15e-153

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 426.90  E-value: 3.15e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   5 SNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGM 84
Cdd:MTH00155    2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  85 IMFIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSL 164
Cdd:MTH00155   82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 165 TLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWH 244
Cdd:MTH00155  162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241

                         250
                  ....*....|....
gi 1824661656 245 FVDVVWLFLYISIY 258
Cdd:MTH00155  242 FVDVVWLFLYISIY 255
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 7-262 2.68e-141

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 397.01  E-value: 2.68e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   7 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 86
Cdd:MTH00118    6 HPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  87 FIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 166
Cdd:MTH00118   86 FITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 167 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 246
Cdd:MTH00118  166 TILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*.
gi 1824661656 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00118  246 DVVWLFLYISIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 4-262 6.02e-139

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 390.87  E-value: 6.02e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   4 YSNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWG 83
Cdd:MTH00189    2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  84 MIMFIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQS 163
Cdd:MTH00189   82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 164 LTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYW 243
Cdd:MTH00189  162 LTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYW 241

                         250
                  ....*....|....*....
gi 1824661656 244 HFVDVVWLFLYISIYWWGS 262
Cdd:MTH00189  242 HFVDVVWLFLYVSIYWWGS 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 7-262 2.08e-130

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 369.44  E-value: 2.08e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   7 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 86
Cdd:MTH00039    5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  87 FIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 166
Cdd:MTH00039   85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 167 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 246
Cdd:MTH00039  165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244

                         250
                  ....*....|....*.
gi 1824661656 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00039  245 DVVWLFLYVCIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 7-262 2.51e-130

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 369.22  E-value: 2.51e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   7 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 86
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  87 FIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 166
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 167 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 246
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1824661656 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 7-262 3.15e-129

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 366.40  E-value: 3.15e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   7 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 86
Cdd:MTH00130    6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  87 FIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 166
Cdd:MTH00130   86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 167 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 246
Cdd:MTH00130  166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*.
gi 1824661656 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00130  246 DVVWLFLYISIYWWGS 261
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-262 7.56e-127

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 360.64  E-value: 7.56e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   1 MKSYSNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGL 80
Cdd:MTH00219    1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  81 RWGMIMFIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQA 160
Cdd:MTH00219   81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 161 MQSLTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAA 240
Cdd:MTH00219  161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240

                         250       260
                  ....*....|....*....|..
gi 1824661656 241 WYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00219  241 WYWHFVDVVWLFLYVSIYWWGS 262
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 7-262 1.82e-125

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 357.13  E-value: 1.82e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   7 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 86
Cdd:MTH00075    6 HAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  87 FIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 166
Cdd:MTH00075   86 FITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 167 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 246
Cdd:MTH00075  166 TIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*.
gi 1824661656 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00075  246 DVVWLFLYVSIYWWGS 261
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 7-262 8.00e-123

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 350.18  E-value: 8.00e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   7 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 86
Cdd:MTH00099    6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  87 FIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 166
Cdd:MTH00099   86 FIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 167 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 246
Cdd:MTH00099  166 TILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFV 245

                         250
                  ....*....|....*.
gi 1824661656 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00099  246 DVVWLFLYVSIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-262 5.01e-121

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 345.55  E-value: 5.01e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   7 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFH--TTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGM 84
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  85 IMFIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSL 164
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 165 TLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1824661656 245 FVDVVWLFLYISIYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-260 2.11e-118

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: 338.34  E-value: 2.11e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  19 LTGAIGGMMMTSGLAQWFHTTNAS-LMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIMFIVSEVLFFMS 97
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  98 FFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTML 177
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 178 QAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISI 257
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1824661656 258 YWW 260
Cdd:cd01665   241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 7-262 1.22e-117

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 337.19  E-value: 1.22e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   7 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 86
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  87 FIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 166
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 167 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 246
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1824661656 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00009  244 DVVWIFLYLCIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 7-262 1.60e-117

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 336.72  E-value: 1.60e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   7 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 86
Cdd:MTH00024    6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  87 FIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 166
Cdd:MTH00024   86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 167 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 246
Cdd:MTH00024  166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245

                         250
                  ....*....|....*.
gi 1824661656 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00024  246 DVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-262 4.70e-106

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 307.87  E-value: 4.70e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   1 MKSYSNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGL 80
Cdd:MTH00052    1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  81 RWGMIMFIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQA 160
Cdd:MTH00052   81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 161 MQSLTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAA 240
Cdd:MTH00052  161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240

                         250       260
                  ....*....|....*....|..
gi 1824661656 241 WYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00052  241 WYWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 7-262 2.44e-95

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 281.96  E-value: 2.44e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   7 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 86
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  87 FIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESN---------- 156
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 157 --------------------------KTQAMQSLTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVI 210
Cdd:MTH00028  166 giegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1824661656 211 IGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 1-261 5.16e-82

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 246.88  E-value: 5.16e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   1 MKSYSNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFH--TTNASLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVST 78
Cdd:PLN02194    1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  79 GLRWGMIMFIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKT 158
Cdd:PLN02194   81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 159 QAMQSLTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEA 238
Cdd:PLN02194  161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240

                         250       260
                  ....*....|....*....|...
gi 1824661656 239 AAWYWHFVDVVWLFLYISIYWWG 261
Cdd:PLN02194  241 AAWYWHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 7-262 4.35e-66

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 205.96  E-value: 4.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656   7 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTTNASLMYMGMMVLLLTMIQWWRDITREGtYQGMHTKNVSTGLRWGMIM 86
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  87 FIVSEVLFFMSFFWAFFNSSLAANVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMqSLTL 166
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 167 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 246
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*.
gi 1824661656 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00083  241 DVVWLFLFVFVYWWSY 256
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 72-260 5.36e-62

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 192.80  E-value: 5.36e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  72 HTKNVSTGLRWGMIMFIVSEVLFFMSFFWAFFNSSLAANVELGtmwppmgiEPFNPMNIPLLNTIILLSSGITVTWCHHS 151
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 152 LM--ESNKTQAMQSLTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFS 229
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1824661656 230 ASHHIGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
72-260 3.62e-47

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 155.39  E-value: 3.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656  72 HTKNVSTGLRWGMIMFIVSEVLFFMSFFWAFFNSSLAANvelgtmWPPMGIEPFNPmNIPLLNTIILLSSGITVTWCHHS 151
Cdd:COG1845     8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 152 LMESNKTQAMQSLTLTVILGIYFTMLQAYEYMEAQ---FSIADSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHF 228
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1824661656 229 SASHHIGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:COG1845   161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 132-258 5.80e-24

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: 94.99  E-value: 5.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 132 LLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYEY---MEAQFSIADSVYGTTFFMATGFHGIH 208
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1824661656 209 VIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIY 258
Cdd:cd02862   135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 123-260 6.73e-16

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239216  Cd Length: 184  Bit Score: 73.56  E-value: 6.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 123 EPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYEYMEAQFSI---ADSVYGTTFF 199
Cdd:cd02865    44 APLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFY 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1824661656 200 MATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd02865   124 LLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 130-258 8.75e-16

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 73.80  E-value: 8.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 130 IPLLNTIILLSSGITVTwCHHSLMESNKTQAMqsLTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHV 209
Cdd:MTH00049   92 IPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHV 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1824661656 210 IIGTTFLATCLtrhiweHFSASHHIGF--EAAAWYWHFVDVVWLFLYISIY 258
Cdd:MTH00049  169 VLGVVGLSTLL------LVGSSSFGVYrsTVLTWYWHFVDYIWLLVYLIVY 213
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 119-258 2.23e-15

Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.


Pssm-ID: 239214  Cd Length: 186  Bit Score: 72.27  E-value: 2.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 119 PMGIEPFNpMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYE---YMEAQFSIADSVYG 195
Cdd:cd02863    42 PPGHELFE-LPLVFIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1824661656 196 TTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIY 258
Cdd:cd02863   121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 124-260 8.15e-14

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: 68.30  E-value: 8.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 124 PFNPMNIPL----LNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYEYME---------AQFSIA 190
Cdd:cd02864    52 RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWG 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824661656 191 DSVYGTTFFMATGFHGIHVIIGTTFLATcLTRHIWEHFSASH--HIGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd02864   132 AAQFGASFFMITGFHGTHVTIGVIYLII-IARKVWRGKYQRIgrYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 132-261 6.20e-08

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: 51.39  E-value: 6.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 132 LLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYE---YMEAQFSIADSVYGTTFFMATGFHGIH 208
Cdd:TIGR02897  56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1824661656 209 VIIGTtFLATCLTRHIWEH-FSASHHIGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:TIGR02897 136 VTLGI-VWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 114-262 7.05e-08

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 51.32  E-value: 7.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661656 114 GTMWPPMGIEPFNpMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYEY---MEAQFSIA 190
Cdd:PRK10663   53 GTAGGPTGKDIFE-LPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPD 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824661656 191 DSVYGTTFFMATGFHGIHVIIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIYWWGS 262
Cdd:PRK10663  132 RSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 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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