|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
5.07e-151 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 421.51 E-value: 5.07e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 6 SNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGM 85
Cdd:MTH00155 2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 86 IMFILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSL 165
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 166 TLTVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWH 245
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 1896069749 246 FVDVVWLFLYISIY 259
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
1.07e-119 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 342.47 E-value: 1.07e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFH--TSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 86 IMFILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 166 TLTVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1896069749 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 |
6.73e-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: 337.18 E-value: 6.73e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 20 LTGAIGGMMMTSGLAQWFH-TSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGMIMFILSEVLFFMS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 99 FFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTLTVMLGIYFTML 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 179 QAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1896069749 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
82-261 |
8.05e-47 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 154.62 E-value: 8.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 82 RWGMIMFILSEVLFFMSFFwaffnSSLAVNVELGTMWPPmGIEPFNPmNIPLLNTIILLSSGITVTWCHHSLMESNKTQT 161
Cdd:COG1845 17 KLGMWLFLASEVMLFAALF-----AAYFVLRASAPDWPA-GAELLDL-PLPLINTLLLLLSSFTVALAVRAARRGDRKGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 162 MQSLTLTVMLGIYFTMLQAYEYMEAQ---FSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFE 238
Cdd:COG1845 90 RLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVE 169
|
170 180
....*....|....*....|...
gi 1896069749 239 AAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 170 AAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
133-262 |
1.69e-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: 53.32 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 133 LLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTLTVMLGIYFTMLQAYE---YMEAQFSIADSVYGTTFFMATGFHGIH 209
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1896069749 210 V---IIGTTFLLICLMRHIWEHFSASHHIgfeAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VtlgIVWAICLLIQIQRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
5.07e-151 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 421.51 E-value: 5.07e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 6 SNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGM 85
Cdd:MTH00155 2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 86 IMFILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSL 165
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 166 TLTVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWH 245
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 1896069749 246 FVDVVWLFLYISIY 259
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
2.64e-141 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 397.40 E-value: 2.64e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGMIM 87
Cdd:MTH00118 6 HPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 88 FILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTL 167
Cdd:MTH00118 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 168 TVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00118 166 TILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 1896069749 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00118 246 DVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
5-263 |
6.68e-139 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 391.26 E-value: 6.68e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 5 YSNHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWG 84
Cdd:MTH00189 2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 85 MIMFILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQS 164
Cdd:MTH00189 82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 165 LTLTVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYW 244
Cdd:MTH00189 162 LTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYW 241
|
250
....*....|....*....
gi 1896069749 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00189 242 HFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
3.37e-129 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 366.52 E-value: 3.37e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGMIM 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 88 FILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTL 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 168 TVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1896069749 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
8-263 |
6.27e-128 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 363.28 E-value: 6.27e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGMIM 87
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 88 FILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTL 167
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 168 TVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 1896069749 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.72e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 362.54 E-value: 1.72e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGMIM 87
Cdd:MTH00130 6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 88 FILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTL 167
Cdd:MTH00130 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 168 TVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00130 166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 1896069749 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00130 246 DVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
3.51e-125 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 356.36 E-value: 3.51e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGMIM 87
Cdd:MTH00075 6 HAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 88 FILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTL 167
Cdd:MTH00075 86 FITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 168 TVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00075 166 TIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 1896069749 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00075 246 DVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
6.64e-124 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 353.32 E-value: 6.64e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGMIM 87
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 88 FILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTL 167
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 168 TVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 1896069749 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00219 247 DVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
8-263 |
2.13e-123 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 352.11 E-value: 2.13e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGMIM 87
Cdd:MTH00099 6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 88 FILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTL 167
Cdd:MTH00099 86 FIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 168 TVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00099 166 TILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 1896069749 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00099 246 DVVWLFLYVSIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
1.07e-119 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 342.47 E-value: 1.07e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFH--TSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 86 IMFILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 166 TLTVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1896069749 246 FVDVVWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-263 |
2.80e-119 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 341.43 E-value: 2.80e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGMIM 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 88 FILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTL 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 168 TVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1896069749 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
6.73e-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: 337.18 E-value: 6.73e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 20 LTGAIGGMMMTSGLAQWFH-TSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGMIMFILSEVLFFMS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 99 FFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTLTVMLGIYFTML 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 179 QAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1896069749 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
1-263 |
3.86e-116 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 333.64 E-value: 3.86e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 1 MTKSYsnHPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTG 80
Cdd:MTH00024 1 MSKLY--HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 81 LRWGMIMFILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQ 160
Cdd:MTH00024 79 LKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 161 TMQSLTLTVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAA 240
Cdd:MTH00024 159 AILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAA 238
|
250 260
....*....|....*....|...
gi 1896069749 241 AWYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00024 239 SWYWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
6.38e-105 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 305.18 E-value: 6.38e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGMIM 87
Cdd:MTH00052 7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 88 FILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTL 167
Cdd:MTH00052 87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 168 TVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00052 167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 1896069749 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00052 247 DVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
3.04e-95 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 281.96 E-value: 3.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGMIM 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 88 FILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESN---------- 157
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 158 --------------------------KTQTMQSLTLTVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVI 211
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1896069749 212 IGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
8-262 |
2.80e-80 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 242.65 E-value: 2.80e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFH--TSSPTLMYMGVTVLMLTMIQWWRDITREGTYQGMHTKYVSTGLRWGM 85
Cdd:PLN02194 7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 86 IMFILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSL 165
Cdd:PLN02194 87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 166 TLTVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWH 245
Cdd:PLN02194 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246
|
250
....*....|....*..
gi 1896069749 246 FVDVVWLFLYISIYWWG 262
Cdd:PLN02194 247 FVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
3.38e-65 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 204.03 E-value: 3.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 8 HPFHLVDYSPWPLTGAIGGMMMTSGLAQWFHTSSPTLMYMGVTVLMLTMIQWWRDITREGtYQGMHTKYVSTGLRWGMIM 87
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 88 FILSEVLFFMSFFWAFFNSSLAVNVELGTMWPPMGIEPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMqSLTL 167
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 168 TVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFV 247
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 1896069749 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 |
9.59e-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: 192.42 E-value: 9.59e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 73 HTKYVSTGLRWGMIMFILSEVLFFMSFFWAFFNSSLAVNVELGtmwppmgiEPFNPMNIPLLNTIILLSSGITVTWCHHS 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 153 LM--ESNKTQTMQSLTLTVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 1896069749 231 ASHHIGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
82-261 |
8.05e-47 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 154.62 E-value: 8.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 82 RWGMIMFILSEVLFFMSFFwaffnSSLAVNVELGTMWPPmGIEPFNPmNIPLLNTIILLSSGITVTWCHHSLMESNKTQT 161
Cdd:COG1845 17 KLGMWLFLASEVMLFAALF-----AAYFVLRASAPDWPA-GAELLDL-PLPLINTLLLLLSSFTVALAVRAARRGDRKGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 162 MQSLTLTVMLGIYFTMLQAYEYMEAQ---FSIADSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFE 238
Cdd:COG1845 90 RLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVE 169
|
170 180
....*....|....*....|...
gi 1896069749 239 AAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 170 AAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
133-259 |
3.83e-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: 95.76 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 133 LLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTLTVMLGIYFTMLQAYEY---MEAQFSIADSVYGTTFFMATGFHGIH 209
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1896069749 210 VIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
120-259 |
1.63e-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: 72.66 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 120 PMGIEPFNpMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTLTVMLGIYFTMLQAYE---YMEAQFSIADSVYG 196
Cdd:cd02863 42 PPGHELFE-LPLVFIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069749 197 TTFFMATGFHGIHVIIGtTFLLICLMRHIWEH-FSASHHIGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863 121 SAFFTLVGTHGLHVTFG-LIWILVMIIQLKKRgLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
124-261 |
2.24e-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: 72.02 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 124 EPFNPMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTLTVMLGIYFTMLQAYEYMEAQFSI---ADSVYGTTFF 200
Cdd:cd02865 44 APLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFY 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896069749 201 MATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865 124 LLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
131-259 |
5.91e-15 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 71.87 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 131 IPLLNTIILLSSGITVTwCHHSLMESNKTQTMqsLTLTVMLGIYFTMLQAYEYMEAQFSIADSVYGTTFFMATGFHGIHV 210
Cdd:MTH00049 92 IPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHV 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1896069749 211 IIGTtFLLICLMRHIWEHFSASHHigfEAAAWYWHFVDVVWLFLYISIY 259
Cdd:MTH00049 169 VLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
125-261 |
2.23e-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: 69.84 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 125 PFNPMNIPL----LNTIILLSSGITVTWCHHSLMESNKTQTMQSLTLTVMLGIYFTMLQAYEYME---------AQFSIA 191
Cdd:cd02864 52 RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWG 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896069749 192 DSVYGTTFFMATGFHGIHVIIGTTFLLIcLMRHIWEHFSASH--HIGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864 132 AAQFGASFFMITGFHGTHVTIGVIYLII-IARKVWRGKYQRIgrYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
115-263 |
1.53e-08 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 53.63 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 115 GTMWPPMGIEPFNpMNIPLLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTLTVMLGIYFTMLQAYEY---MEAQFSIA 191
Cdd:PRK10663 53 GTAGGPTGKDIFE-LPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPD 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896069749 192 DSVYGTTFFMATGFHGIHVIIGTTFLLICLMRHIWEHFSASHHIGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:PRK10663 132 RSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
133-262 |
1.69e-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: 53.32 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069749 133 LLNTIILLSSGITVTWCHHSLMESNKTQTMQSLTLTVMLGIYFTMLQAYE---YMEAQFSIADSVYGTTFFMATGFHGIH 209
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1896069749 210 V---IIGTTFLLICLMRHIWEHFSASHHIgfeAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VtlgIVWAICLLIQIQRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
|