|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
6.96e-150 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 418.43 E-value: 6.96e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 6 SNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGM 85
Cdd:MTH00155 2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 86 IMFIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSL 165
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 166 TLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWH 245
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 1275874104 246 FVDVVWLFLYISIY 259
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
1.50e-119 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 342.08 E-value: 1.50e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWF--YTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFhgYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 86 IMFIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 166 TLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1275874104 246 FVDVVWLFLYISIYWWGS 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 |
4.88e-116 |
|
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: 332.56 E-value: 4.88e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 20 LTGAIGGMMMTSGLAQWF-YTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIMFIVSEVLFFMS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMhGYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 99 FFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTML 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 179 QAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1275874104 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
73-261 |
4.52e-46 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 152.70 E-value: 4.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 73 HTKNVSTGLRWGMIMFIVSEVLFFMSFFwaffnSSLAVNVELGTMWPPvGIESFNPmNIPLLNTIILLSSGITVTWCHHS 152
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALF-----AAYFVLRASAPDWPA-GAELLDL-PLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 153 LMESNKTQAMQSLTLTVILGIYFTMLQAYEYMEAQ---FSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHF 229
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 1275874104 230 SASHHIGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
133-262 |
7.72e-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: 51.01 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 133 LLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYE---YMEAQFSIADSVYGTTFFMATGFHGIH 209
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1275874104 210 VMIGTtFLATCLTRHIWEH-FSASHHIGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VTLGI-VWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
6.96e-150 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 418.43 E-value: 6.96e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 6 SNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGM 85
Cdd:MTH00155 2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 86 IMFIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSL 165
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 166 TLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWH 245
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 1275874104 246 FVDVVWLFLYISIY 259
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
2.43e-139 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 392.01 E-value: 2.43e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 87
Cdd:MTH00118 6 HPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 88 FIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 167
Cdd:MTH00118 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 168 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00118 166 TILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 1275874104 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00118 246 DVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
5-263 |
1.67e-136 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 384.71 E-value: 1.67e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 5 YSNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWG 84
Cdd:MTH00189 2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 85 MIMFIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQS 164
Cdd:MTH00189 82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 165 LTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYW 244
Cdd:MTH00189 162 LTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYW 241
|
250
....*....|....*....
gi 1275874104 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00189 242 HFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
8-263 |
2.86e-128 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 364.05 E-value: 2.86e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 87
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 88 FIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 167
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 168 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 1275874104 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
6.08e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 363.06 E-value: 6.08e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 88 FIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 168 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1275874104 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
2.61e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 361.77 E-value: 2.61e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 87
Cdd:MTH00130 6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 88 FIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 167
Cdd:MTH00130 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 168 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00130 166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 1275874104 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00130 246 DVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
2-263 |
4.27e-125 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 356.02 E-value: 4.27e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 2 MKSYSNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGL 81
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 82 RWGMIMFIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQA 161
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 162 MQSLTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAA 241
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 1275874104 242 WYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.79e-122 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 349.43 E-value: 1.79e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 87
Cdd:MTH00075 6 HAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 88 FIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 167
Cdd:MTH00075 86 FITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 168 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00075 166 TIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 1275874104 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00075 246 DVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
8-263 |
2.78e-120 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 344.02 E-value: 2.78e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 87
Cdd:MTH00099 6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 88 FIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 167
Cdd:MTH00099 86 FIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 168 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00099 166 TILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 1275874104 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00099 246 DVVWLFLYVSIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
1.50e-119 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 342.08 E-value: 1.50e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWF--YTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFhgYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 86 IMFIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 166 TLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1275874104 246 FVDVVWLFLYISIYWWGS 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 |
4.88e-116 |
|
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: 332.56 E-value: 4.88e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 20 LTGAIGGMMMTSGLAQWF-YTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIMFIVSEVLFFMS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMhGYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 99 FFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTML 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 179 QAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1275874104 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-263 |
1.82e-115 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 331.80 E-value: 1.82e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 88 FIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 168 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1275874104 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
8-263 |
1.69e-114 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 329.41 E-value: 1.69e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 87
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 88 FIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTL 167
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 168 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*.
gi 1275874104 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00024 246 DVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-263 |
2.24e-103 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 300.94 E-value: 2.24e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 1 MMKSYsnHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTG 80
Cdd:MTH00052 2 MQQYY--HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 81 LRWGMIMFIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQ 160
Cdd:MTH00052 80 LKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 161 AMQSLTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAA 240
Cdd:MTH00052 160 AIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAA 239
|
250 260
....*....|....*....|...
gi 1275874104 241 AWYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00052 240 AWYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
2.64e-94 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 279.26 E-value: 2.64e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVSTGLRWGMIM 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 88 FIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESN---------- 157
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 158 --------------------------KTQAMQSLTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVM 211
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1275874104 212 IGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
2-262 |
3.01e-80 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 242.65 E-value: 3.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 2 MKSYSNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWF--YTTNTSLMYMGMMVLLLTMIQWWRDITREGTYQGMHTKNVST 79
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMhpFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 80 GLRWGMIMFIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKT 159
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 160 QAMQSLTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEA 239
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|...
gi 1275874104 240 AAWYWHFVDVVWLFLYISIYWWG 262
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.04e-65 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 205.19 E-value: 1.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFYTTNTSLMYMGMMVLLLTMIQWWRDITREGtYQGMHTKNVSTGLRWGMIM 87
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 88 FIVSEVLFFMSFFWAFFNSSLAVNVELGTMWPPVGIESFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMqSLTL 167
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 168 TVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 1275874104 248 DVVWLFLYISIYWWGS 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 |
3.26e-61 |
|
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: 190.88 E-value: 3.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 73 HTKNVSTGLRWGMIMFIVSEVLFFMSFFWAFFNSSLAVNVELGtmwppvgiESFNPMNIPLLNTIILLSSGITVTWCHHS 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 153 LM--ESNKTQAMQSLTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 1275874104 231 ASHHIGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
73-261 |
4.52e-46 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 152.70 E-value: 4.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 73 HTKNVSTGLRWGMIMFIVSEVLFFMSFFwaffnSSLAVNVELGTMWPPvGIESFNPmNIPLLNTIILLSSGITVTWCHHS 152
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALF-----AAYFVLRASAPDWPA-GAELLDL-PLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 153 LMESNKTQAMQSLTLTVILGIYFTMLQAYEYMEAQ---FSIADSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHF 229
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 1275874104 230 SASHHIGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
133-259 |
1.82e-23 |
|
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.
Pssm-ID: 239213 Cd Length: 186 Bit Score: 93.84 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 133 LLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYEY---MEAQFSIADSVYGTTFFMATGFHGIH 209
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1275874104 210 VMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
131-259 |
5.10e-15 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 71.87 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 131 IPLLNTIILLSSGITVTwCHHSLMESNKTQAMqsLTLTVILGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHV 210
Cdd:MTH00049 92 IPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHV 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1275874104 211 MIGTTFLATCLtrhiweHFSASHHIGF--EAAAWYWHFVDVVWLFLYISIY 259
Cdd:MTH00049 169 VLGVVGLSTLL------LVGSSSFGVYrsTVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
130-261 |
6.89e-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: 70.86 E-value: 6.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 130 NIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYEYMEAQFSI---ADSVYGTTFFMATGFH 206
Cdd:cd02865 50 NLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYLLTGLH 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1275874104 207 GIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865 130 GLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
120-259 |
8.24e-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: 70.73 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 120 PVGIESFNpMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYE---YMEAQFSIADSVYG 196
Cdd:cd02863 42 PPGHELFE-LPLVFIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1275874104 197 TTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863 121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
130-261 |
5.65e-13 |
|
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: 65.99 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 130 NIPL----LNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYEYME---------AQFSIADSVYG 196
Cdd:cd02864 57 NIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFG 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1275874104 197 TTFFMATGFHGIHVMIGTTFLATcLTRHIWEHFSASH--HIGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864 137 ASFFMITGFHGTHVTIGVIYLII-IARKVWRGKYQRIgrYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
115-263 |
6.46e-08 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 51.71 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 115 GTMWPPVGIESFNpMNIPLLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYEY---MEAQFSIA 191
Cdd:PRK10663 53 GTAGGPTGKDIFE-LPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPD 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1275874104 192 DSVYGTTFFMATGFHGIHVMIGTTFLATCLTRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:PRK10663 132 RSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
133-262 |
7.72e-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: 51.01 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275874104 133 LLNTIILLSSGITVTWCHHSLMESNKTQAMQSLTLTVILGIYFTMLQAYE---YMEAQFSIADSVYGTTFFMATGFHGIH 209
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1275874104 210 VMIGTtFLATCLTRHIWEH-FSASHHIGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VTLGI-VWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
