|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
4.23e-162 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 449.25 E-value: 4.23e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 5 HTNHPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 85 MILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 165 LSLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 938339405 245 HFVDVVWLFLYLSIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-262 |
5.97e-125 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 355.56 E-value: 5.97e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 8 HPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTF--NMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 86 ILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQGL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 166 SLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 938339405 246 FVDVVWLFLYLSIYWWG 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
1.17e-122 |
|
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: 349.12 E-value: 1.17e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 20 LTGAIGALVLTSGLTKWFHTF-NMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWGMILFIISEVFFFIS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 99 FFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQGLSLTIILGVYFTIL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 179 QAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWHFVDVVWLFLYLSI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 938339405 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
3.81e-47 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 155.39 E-value: 3.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 72 LHTSKVTLGLRWGMILFIISEVFFFISFFWAFFHSSLSptveigTNWPPLGISPFNPmQIPLLNTAILLASGVTITWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 152 SIMENNHTQCSQGLSLTIILGVYFTILQAYEY---IEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 938339405 229 FSSIHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
133-262 |
1.76e-09 |
|
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: 56.02 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 133 LLNTAILLASGVTITWAHHSIMENNHTQCSQGLSLTIILGVYFTILQAYE---YIEAPFTIADAVYGSTFFMATGFHGLH 209
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 938339405 210 V---IIGSSFLMVCLMRHLLNHFSSIHHFgfeAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:TIGR02897 136 VtlgIVWAICLLIQIQRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
4.23e-162 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 449.25 E-value: 4.23e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 5 HTNHPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 85 MILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 165 LSLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 938339405 245 HFVDVVWLFLYLSIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
4-262 |
1.07e-146 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 410.88 E-value: 1.07e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 4 THTNHPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRW 83
Cdd:MTH00118 2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 84 GMILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQ 163
Cdd:MTH00118 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 164 GLSLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWY 243
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241
|
250
....*....|....*....
gi 938339405 244 WHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
4-262 |
4.88e-140 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 393.96 E-value: 4.88e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 4 THTNHPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRW 83
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 84 GMILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQ 163
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 164 GLSLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWY 243
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250
....*....|....*....
gi 938339405 244 WHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWG 259
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
6-263 |
1.69e-137 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 387.32 E-value: 1.69e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 6 TNHPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWGM 85
Cdd:MTH00141 2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 86 ILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQGL 165
Cdd:MTH00141 82 ILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 166 SLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWH 245
Cdd:MTH00141 162 GLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWH 241
|
250
....*....|....*...
gi 938339405 246 FVDVVWLFLYLSIYWWGN 263
Cdd:MTH00141 242 FVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
4-262 |
5.58e-134 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 378.69 E-value: 5.58e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 4 THTNHPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRW 83
Cdd:MTH00099 2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 84 GMILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQ 163
Cdd:MTH00099 82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 164 GLSLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWY 243
Cdd:MTH00099 162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241
|
250
....*....|....*....
gi 938339405 244 WHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00099 242 WHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
3.88e-132 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 374.12 E-value: 3.88e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 8 HPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWGMIL 87
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 88 FIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQGLSL 167
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 168 TIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWHFV 247
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 938339405 248 DVVWLFLYLSIYWWGN 263
Cdd:MTH00219 247 DVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
8-262 |
4.69e-132 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 373.68 E-value: 4.69e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 8 HPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWGMIL 87
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 88 FIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQGLSL 167
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 168 TIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWHFV 247
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*
gi 938339405 248 DVVWLFLYLSIYWWG 262
Cdd:MTH00039 245 DVVWLFLYVCIYWWG 259
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
4-263 |
5.12e-132 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 373.71 E-value: 5.12e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 4 THTNHPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRW 83
Cdd:MTH00130 2 AHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 84 GMILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQ 163
Cdd:MTH00130 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 164 GLSLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWY 243
Cdd:MTH00130 162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 938339405 244 WHFVDVVWLFLYLSIYWWGN 263
Cdd:MTH00130 242 WHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
4-262 |
6.59e-132 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 373.31 E-value: 6.59e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 4 THTNHPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRW 83
Cdd:MTH00075 2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 84 GMILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQ 163
Cdd:MTH00075 82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 164 GLSLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWY 243
Cdd:MTH00075 162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241
|
250
....*....|....*....
gi 938339405 244 WHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00075 242 WHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-262 |
5.97e-125 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 355.56 E-value: 5.97e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 8 HPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTF--NMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 86 ILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQGL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 166 SLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 938339405 246 FVDVVWLFLYLSIYWWG 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
6-262 |
1.67e-124 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 354.53 E-value: 1.67e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 6 TNHPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWGM 85
Cdd:MTH00009 2 IRQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 86 ILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQGL 165
Cdd:MTH00009 82 ILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 166 SLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWH 245
Cdd:MTH00009 162 ILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWH 241
|
250
....*....|....*..
gi 938339405 246 FVDVVWLFLYLSIYWWG 262
Cdd:MTH00009 242 FVDVVWIFLYLCIYWWG 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
1.17e-122 |
|
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: 349.12 E-value: 1.17e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 20 LTGAIGALVLTSGLTKWFHTF-NMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWGMILFIISEVFFFIS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 99 FFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQGLSLTIILGVYFTIL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 179 QAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWHFVDVVWLFLYLSI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 938339405 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
8-262 |
1.64e-115 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 331.72 E-value: 1.64e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 8 HPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWGMIL 87
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 88 FIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQGLSL 167
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 168 TIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWHFV 247
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*
gi 938339405 248 DVVWLFLYLSIYWWG 262
Cdd:MTH00024 246 DVVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
2-263 |
2.83e-108 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 313.65 E-value: 2.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 2 LTTHTNHPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGL 81
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 82 RWGMILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQC 161
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 162 SQGLSLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAA 241
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 938339405 242 WYWHFVDVVWLFLYLSIYWWGN 263
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
4.50e-94 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 278.87 E-value: 4.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 8 HPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWGMIL 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 88 FIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIM------------- 154
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIgtgnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 155 -----------------------ENNHTQCSQGLSLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVI 211
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllSDFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 938339405 212 IGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWHFVDVVWLFLYLSIYWWGN 263
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
8-262 |
1.96e-84 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 253.05 E-value: 1.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 8 HPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFN--MNLLMIGFMITLLTMIQWWRDVAREGTFQGLHTSKVTLGLRWGM 85
Cdd:PLN02194 7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 86 ILFIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNHTQCSQGL 165
Cdd:PLN02194 87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 166 SLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWH 245
Cdd:PLN02194 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246
|
250
....*....|....*..
gi 938339405 246 FVDVVWLFLYLSIYWWG 262
Cdd:PLN02194 247 FVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
2.92e-67 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 209.04 E-value: 2.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 8 HPFHLVDYSPWPLTGAIGALVLTSGLTKWFHTFNMNLLMIGFMITLLTMIQWWRDVAREGtFQGLHTSKVTLGLRWGMIL 87
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 88 FIISEVFFFISFFWAFFHSSLSPTVEIGTNWPPLGISPFNPMQIPLLNTAILLASGVTITWAHHSIMENNhTQCSQGLSL 167
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 168 TIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWHFV 247
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*
gi 938339405 248 DVVWLFLYLSIYWWG 262
Cdd:MTH00083 241 DVVWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
73-261 |
8.26e-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: 195.11 E-value: 8.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 73 HTSKVTLGLRWGMILFIISEVFFFISFFWAFFHSSLSPTVEIGTnwpplgisPFNPMQIPLLNTAILLASGVTITWAHHS 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 153 IM--ENNHTQCSQGLSLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNHFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 938339405 231 SIHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
3.81e-47 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 155.39 E-value: 3.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 72 LHTSKVTLGLRWGMILFIISEVFFFISFFWAFFHSSLSptveigTNWPPLGISPFNPmQIPLLNTAILLASGVTITWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 152 SIMENNHTQCSQGLSLTIILGVYFTILQAYEY---IEAPFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLNH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 938339405 229 FSSIHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
133-259 |
1.53e-21 |
|
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: 88.83 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 133 LLNTAILLASGVTITWAHHSIMENNHTQCSQGLSLTIILGVYFTILQAYEY---IEAPFTIADAVYGSTFFMATGFHGLH 209
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 938339405 210 VIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWHFVDVVWLFLYLSIY 259
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
132-261 |
2.35e-17 |
|
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: 77.41 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 132 PLLNTAILLASGVTITWAHHSIMENNHTQCSQGLSLTIILGVYFTILQAYEYIEAPF---TIADAVYGSTFFMATGFHGL 208
Cdd:cd02865 52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 938339405 209 HVIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
128-259 |
2.17e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 75.34 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 128 PMQIPLLNTAILLASGVTITWAHHSIMENNhtqCSQGLSLTIILGVYFTILQAYEYIEAPFTIADAVYGSTFFMATGFHG 207
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLLGWKY---CDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 938339405 208 LHVIIGSsFLMVCLMRHLLNHFSSIHHfgfEAAAWYWHFVDVVWLFLYLSIY 259
Cdd:MTH00049 166 SHVVLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
133-259 |
1.22e-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: 69.96 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 133 LLNTAILLASGVTITWAHHSIMENNHTQCSQGLSLTIILGVYFTILQAYE---YIEAPFTIADAVYGSTFFMATGFHGLH 209
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 938339405 210 VIIGsSFLMVCLMRHLLNH-FSSIHHFGFEAAAWYWHFVDVVWLFLYLSIY 259
Cdd:cd02863 134 VTFG-LIWILVMIIQLKKRgLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
84-261 |
4.06e-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: 69.07 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 84 GMILFIISEVFFFISFFWAFFHSSLSPTveigTNWPPLG---ISPFNPMQIPL----LNTAILLASGVTITWAHHSIMEN 156
Cdd:cd02864 12 MMWFFLLSDAFIFSSFLIAYMTARISTT----EPWPLPSdvfALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 157 NHTQCSQGLSLTIILGVYFTILQAYEYIE---------APFTIADAVYGSTFFMATGFHGLHVIIGSSFLMVCLMRHLLN 227
Cdd:cd02864 88 NRKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRG 167
|
170 180 190
....*....|....*....|....*....|....*
gi 938339405 228 HFSSIHHFG-FEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:cd02864 168 KYQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
133-262 |
1.76e-09 |
|
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: 56.02 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 133 LLNTAILLASGVTITWAHHSIMENNHTQCSQGLSLTIILGVYFTILQAYE---YIEAPFTIADAVYGSTFFMATGFHGLH 209
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 938339405 210 V---IIGSSFLMVCLMRHLLNHFSSIHHFgfeAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:TIGR02897 136 VtlgIVWAICLLIQIQRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
133-262 |
3.71e-07 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 49.39 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339405 133 LLNTAILLASGVTITWAHHSIMENNHTQCSQGLSLTIILGVYFTILQAYEY---IEAPFTIADAVYGSTFFMATGFHGLH 209
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 938339405 210 VIIGSSFLMVCLMRHLLNHFSSIHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
|
|
| |
