|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
5.87e-145 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 406.10 E-value: 5.87e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 5 NYNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 85 MILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQS 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 165 LLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2235262570 245 HFVDVIWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
4-263 |
8.00e-133 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 375.44 E-value: 8.00e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 4 TNYNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRW 83
Cdd:MTH00118 2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 84 GMILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQ 163
Cdd:MTH00118 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 164 SLLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWY 243
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 2235262570 244 WHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
2.15e-129 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 366.99 E-value: 2.15e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00189 5 HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLF 167
Cdd:MTH00189 85 FITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00189 165 TVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00189 245 DVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.31e-122 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 349.57 E-value: 1.31e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLF 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
5-263 |
2.97e-121 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 346.33 E-value: 2.97e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 5 NYNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWG 84
Cdd:MTH00039 2 THQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 85 MILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQS 164
Cdd:MTH00039 82 MILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 165 LLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYW 244
Cdd:MTH00039 162 LFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYW 241
|
250
....*....|....*....
gi 2235262570 245 HFVDVIWLFLYISIYWWGS 263
Cdd:MTH00039 242 HFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
7.55e-120 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 342.92 E-value: 7.55e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLF 167
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00219 247 DVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.08e-118 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 339.80 E-value: 1.08e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00075 6 HAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLF 167
Cdd:MTH00075 86 FITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00075 166 TIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00075 246 DVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
4-263 |
6.25e-118 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 337.85 E-value: 6.25e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 4 TNYNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRW 83
Cdd:MTH00099 2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 84 GMILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQ 163
Cdd:MTH00099 82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 164 SLLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWY 243
Cdd:MTH00099 162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 2235262570 244 WHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00099 242 WHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
8.84e-118 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 337.51 E-value: 8.84e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00130 6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLF 167
Cdd:MTH00130 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00130 166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00130 246 DVVWLFLYISIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
4.87e-114 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 327.83 E-value: 4.87e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWF--YSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFhgYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 86 ILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 166 LFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 2235262570 246 FVDVIWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
1.14e-111 |
|
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.
Pssm-ID: 238834 Cd Length: 243 Bit Score: 321.39 E-value: 1.14e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 20 LTGAMGGMIMTTGLAKWF-YSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMILFITSEVLFFMS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMhGYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 99 FFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLFTVILGIYFTML 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 179 QAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFVDVIWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2235262570 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-263 |
4.41e-109 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 315.62 E-value: 4.41e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLF 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
4-263 |
9.17e-108 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 312.07 E-value: 9.17e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 4 TNYNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRW 83
Cdd:MTH00024 2 SKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 84 GMILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQ 163
Cdd:MTH00024 82 GMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 164 SLLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWY 243
Cdd:MTH00024 162 GLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWY 241
|
250 260
....*....|....*....|
gi 2235262570 244 WHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00024 242 WHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
6-263 |
1.55e-98 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 289.00 E-value: 1.55e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 6 YNHPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGM 85
Cdd:MTH00052 5 YYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 86 ILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSL 165
Cdd:MTH00052 85 ILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 166 LFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWH 245
Cdd:MTH00052 165 ALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWH 244
|
250
....*....|....*...
gi 2235262570 246 FVDVIWLFLYISIYWWGS 263
Cdd:MTH00052 245 FVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
5.00e-89 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 266.16 E-value: 5.00e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESN---------- 157
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 158 --------------------------KTQANQSLLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVI 211
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2235262570 212 IGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFVDVIWLFLYISIYWWGS 263
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
8-262 |
3.62e-76 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 232.25 E-value: 3.62e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWF--YSSNMNLMLLGMMILLMTMFQWWRDVTREGTMQGLHTMNVSKGLRWGM 85
Cdd:PLN02194 7 HSYHLVDPSPWPISGSLGALATTVGGVMYMhpFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 86 ILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSL 165
Cdd:PLN02194 87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 166 LFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWH 245
Cdd:PLN02194 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246
|
250
....*....|....*..
gi 2235262570 246 FVDVIWLFLYISIYWWG 262
Cdd:PLN02194 247 FVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
5.90e-66 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 205.57 E-value: 5.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 8 HPFHLVDYSPWPLTGAMGGMIMTTGLAKWFYSSNMNLMLLGMMILLMTMFQWWRDVTREGtMQGLHTMNVSKGLRWGMIL 87
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 88 FITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVQPFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANqSLLF 167
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 168 TVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFV 247
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 2235262570 248 DVIWLFLYISIYWWGS 263
Cdd:MTH00083 241 DVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
73-261 |
2.17e-63 |
|
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.
Pssm-ID: 238227 Cd Length: 183 Bit Score: 196.66 E-value: 2.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 73 HTMNVSKGLRWGMILFITSEVLFFMSFFWAFFNSSLSSNIELGlmwppkgvQPFNPINIPLLNTIILLSSGITVTWAHHS 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 153 LM--ESNKTQANQSLLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 2235262570 231 SKHHLGFETAAWYWHFVDVIWLFLYISIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
6.69e-48 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 157.32 E-value: 6.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 72 LHTMNVSKGLRWGMILFITSEVLFFMSFFWAFFNSSLSSNielglmWPPKGVQPFNPiNIPLLNTIILLSSGITVTWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 152 SLMESNKTQANQSLLFTVILGIYFTMLQAYEYMEAQ---FSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2235262570 229 FSSKHHLGFETAAWYWHFVDVIWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
133-259 |
1.85e-22 |
|
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.
Pssm-ID: 239213 Cd Length: 186 Bit Score: 91.14 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 133 LLNTIILLSSGITVTWAHHSLMESNKTQANQSLLFTVILGIYFTMLQAYEY---MEAQFSIADSIYGTVFFMATGFHGIH 209
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2235262570 210 VIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFVDVIWLFLYISIY 259
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
84-261 |
1.06e-15 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239215 Cd Length: 202 Bit Score: 73.30 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 84 GMILFITSEVLFFMSFFWAFFNSSLSSNIELGLMWPPKGVqPFNPINIPL----LNTIILLSSGITVTWAHHSLMESNKT 159
Cdd:cd02864 12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 160 QANQSLLFTVILGIYFTMLQAYEYME---------AQFSIADSIYGTVFFMATGFHGIHVIIGTTFLFICLMRQLNLHFS 230
Cdd:cd02864 91 AAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQ 170
|
170 180 190
....*....|....*....|....*....|..
gi 2235262570 231 SK-HHLGFETAAWYWHFVDVIWLFLYISIYWW 261
Cdd:cd02864 171 RIgRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
131-259 |
1.77e-15 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 73.03 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 131 IPLLNTIILLSSGITVTwAHHSLMESNKTQANqsLLFTVILGIYFTMLQAYEYMEAQFSIADSIYGTVFFMATGFHGIHV 210
Cdd:MTH00049 92 IPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHV 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2235262570 211 IIGTTFLFICLMRQLNLHFSSKHHLgfetAAWYWHFVDVIWLFLYISIY 259
Cdd:MTH00049 169 VLGVVGLSTLLLVGSSSFGVYRSTV----LTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
125-261 |
3.09e-15 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239216 Cd Length: 184 Bit Score: 71.63 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 125 PFNPINIPLLNTIILLSSGITVTWAHHSLMESNKTQANQSLLFTVILGIYFTMLQAYEYMEAQFSI---ADSIYGTVFFM 201
Cdd:cd02865 45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYL 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 202 ATGFHGIHVIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFVDVIWLFLYISIYWW 261
Cdd:cd02865 125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
133-259 |
3.37e-14 |
|
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.
Pssm-ID: 239214 Cd Length: 186 Bit Score: 68.81 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 133 LLNTIILLSSGITVTWAHHSLMESNKTQANQSLLFTVILGIYFTMLQAYE---YMEAQFSIADSIYGTVFFMATGFHGIH 209
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2235262570 210 VIIGtTFLFICLMRQLNLH-FSSKHHLGFETAAWYWHFVDVIWLFLYISIY 259
Cdd:cd02863 134 VTFG-LIWILVMIIQLKKRgLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
133-263 |
1.18e-08 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 53.63 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2235262570 133 LLNTIILLSSGITVTWAHHSLMESNKTQANQSLLFTVILGIYFTMLQAYEY---MEAQFSIADSIYGTVFFMATGFHGIH 209
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2235262570 210 VIIGTTFLFICLMRQLNLHFSSKHHLGFETAAWYWHFVDVIWLFLYISIYWWGS 263
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
|