|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-258 |
5.47e-162 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 449.25 E-value: 5.47e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 6 NHPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRWGMI 85
Cdd:MTH00155 3 NHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 86 LFIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLF 165
Cdd:MTH00155 83 LFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 166 FTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHF 245
Cdd:MTH00155 163 FTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHF 242
|
250
....*....|...
gi 511347969 246 VDVVWLFLYISIY 258
Cdd:MTH00155 243 VDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
6.29e-126 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 357.88 E-value: 6.29e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 7 HPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNS--LLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 85 ILFIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 165 FFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 511347969 245 FVDVVWLFLYISIYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
7.37e-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: 347.20 E-value: 7.37e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 19 LTGAIGTLITVAGLTKWFHQYNNS-LLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRWGMILFIISEVFFFIS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 98 FFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFFTVILGAYFTVL 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 178 QAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFVDVVWLFLYISI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 511347969 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
2.49e-50 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 163.48 E-value: 2.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 71 LHTLPVTLGLRWGMILFIISEVFF-FISFFWAFFHSSLSPDielgvmwPPAGIHPFNPLqIPLLNTAILLASGVTVTWAH 149
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAPD-------WPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 150 HSLMEGNSSQTTQGLFFTVILGAYFTVLQAYEY---IEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFK 226
Cdd:COG1845 79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158
|
170 180 190
....*....|....*....|....*....|....
gi 511347969 227 HFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:COG1845 159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
128-261 |
1.21e-11 |
|
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: 61.79 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 128 LQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFFTVILGAYFTVLQAYE---YIEAPFTIADAIYGSTFFVATGF 204
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 511347969 205 HGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:TIGR02897 132 HGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-258 |
5.47e-162 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 449.25 E-value: 5.47e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 6 NHPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRWGMI 85
Cdd:MTH00155 3 NHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 86 LFIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLF 165
Cdd:MTH00155 83 LFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 166 FTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHF 245
Cdd:MTH00155 163 FTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHF 242
|
250
....*....|...
gi 511347969 246 VDVVWLFLYISIY 258
Cdd:MTH00155 243 VDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
5.51e-146 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 408.96 E-value: 5.51e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 3 TYANHPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRW 82
Cdd:MTH00118 2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 83 GMILFIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQ 162
Cdd:MTH00118 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 163 GLFFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWY 242
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 511347969 243 WHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
6.24e-140 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 393.57 E-value: 6.24e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 3 TYANHPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRW 82
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 83 GMILFIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQ 162
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 163 GLFFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWY 242
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 511347969 243 WHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
3-262 |
6.13e-135 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 381.00 E-value: 6.13e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 3 TYANHPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRW 82
Cdd:MTH00099 2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 83 GMILFIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQ 162
Cdd:MTH00099 82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 163 GLFFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWY 242
Cdd:MTH00099 162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 511347969 243 WHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00099 242 WHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
1.94e-133 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 376.92 E-value: 1.94e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 7 HPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRWGMIL 86
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 87 FIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFF 166
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 167 TVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFV 246
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 511347969 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
7-262 |
5.79e-131 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 370.98 E-value: 5.79e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 7 HPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRWGMIL 86
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 87 FIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFF 166
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 167 TVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFV 246
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 511347969 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
8.21e-131 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 370.63 E-value: 8.21e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 7 HPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRWGMIL 86
Cdd:MTH00130 6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 87 FIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFF 166
Cdd:MTH00130 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 167 TVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFV 246
Cdd:MTH00130 166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 511347969 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00130 246 DVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
2.24e-129 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 366.76 E-value: 2.24e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 3 TYANHPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRW 82
Cdd:MTH00075 2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 83 GMILFIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQ 162
Cdd:MTH00075 82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 163 GLFFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWY 242
Cdd:MTH00075 162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 511347969 243 WHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00075 242 WHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
1.57e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 364.88 E-value: 1.57e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 1 MTTYANHPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGL 80
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 81 RWGMILFIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQT 160
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 161 TQGLFFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAA 240
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 511347969 241 WYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
6.29e-126 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 357.88 E-value: 6.29e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 7 HPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNS--LLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 85 ILFIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 165 FFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 511347969 245 FVDVVWLFLYISIYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
7.37e-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: 347.20 E-value: 7.37e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 19 LTGAIGTLITVAGLTKWFHQYNNS-LLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRWGMILFIISEVFFFIS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 98 FFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFFTVILGAYFTVL 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 178 QAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFVDVVWLFLYISI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 511347969 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
7-262 |
4.27e-120 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 343.36 E-value: 4.27e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 7 HPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRWGMIL 86
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 87 FIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFF 166
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 167 TVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFV 246
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 511347969 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
7-262 |
1.68e-116 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 334.41 E-value: 1.68e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 7 HPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRWGMIL 86
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 87 FIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFF 166
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 167 TVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFV 246
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*.
gi 511347969 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00024 246 DVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
5.27e-110 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 317.89 E-value: 5.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 1 MTTYANHPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 81 RWGMILFIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQT 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 161 TQGLFFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAA 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 511347969 241 WYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
9.23e-91 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 270.40 E-value: 9.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 7 HPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNSLLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTLGLRWGMIL 86
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 87 FIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQ---- 162
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNPASLEkgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 163 --------------------------------GLFFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVI 210
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrtnaviGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 511347969 211 IGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
1-261 |
3.96e-84 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 252.28 E-value: 3.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 1 MTTYANHPYHLVNPSPWPLTGAIGTLITVAGLTKWFHQYNNS--LLTLGGLITILTMIQWWRDITREGTYQGLHTLPVTL 78
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGarLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 79 GLRWGMILFIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSS 158
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 159 QTTQGLFFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEA 238
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|...
gi 511347969 239 AAWYWHFVDVVWLFLYISIYWWG 261
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
52-262 |
4.79e-66 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 205.96 E-value: 4.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 52 ILTMIQWWRDITREGtYQGLHTLPVTLGLRWGMILFIISEVFFFISFFWAFFHSSLSPDIELGVMWPPAGIHPFNPLQIP 131
Cdd:MTH00083 48 LFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 132 LLNTAILLASGVTVTWAHHSLMEGNSSqTTQGLFFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVII 211
Cdd:MTH00083 127 LLNTIILLSSGVSVTWSHHSLCLSNKS-CTNSLLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLC 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 511347969 212 GTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00083 206 GGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
72-260 |
5.70e-65 |
|
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: 200.51 E-value: 5.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 72 HTLPVTLGLRWGMILFIISEVFFFISFFWAFFHSSLSPDIELGvmwppagiHPFNPLQIPLLNTAILLASGVTVTWAHHS 151
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 152 LM--EGNSSQTTQGLFFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFKHFS 229
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 511347969 230 PSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
2.49e-50 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 163.48 E-value: 2.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 71 LHTLPVTLGLRWGMILFIISEVFF-FISFFWAFFHSSLSPDielgvmwPPAGIHPFNPLqIPLLNTAILLASGVTVTWAH 149
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAPD-------WPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 150 HSLMEGNSSQTTQGLFFTVILGAYFTVLQAYEY---IEAPFTIADAIYGSTFFVATGFHGLHVIIGTTFLLTCLLRHLFK 226
Cdd:COG1845 79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158
|
170 180 190
....*....|....*....|....*....|....
gi 511347969 227 HFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:COG1845 159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
128-258 |
6.69e-23 |
|
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.
Pssm-ID: 239213 Cd Length: 186 Bit Score: 92.30 E-value: 6.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 128 LQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFFTVILGAYFTVLQAYEY---IEAPFTIADAIYGSTFFVATGF 204
Cdd:cd02862 51 LLLGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGF 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 511347969 205 HGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFVDVVWLFLYISIY 258
Cdd:cd02862 131 HLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
132-258 |
3.01e-17 |
|
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: 77.28 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 132 LLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFFTVILGAYFTVLQAYE---YIEAPFTIADAIYGSTFFVATGFHGLH 208
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 511347969 209 VIIGtTFLLTCLLRHLFKH-FSPSHHFGFEAAAWYWHFVDVVWLFLYISIY 258
Cdd:cd02863 134 VTFG-LIWILVMIIQLKKRgLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
124-260 |
3.05e-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: 77.02 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 124 PFNPLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFFTVILGAYFTVLQAYEYIEAPF---TIADAIYGSTFFV 200
Cdd:cd02865 45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYL 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 201 ATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd02865 125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
127-258 |
1.59e-15 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 73.03 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 127 PLQIPLLNTAILLASGVTVTWAHHSLmegNSSQTTQGLFFTVILGAYFTVLQAYEYIEAPFTIADAIYGSTFFVATGFHG 206
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 511347969 207 LHVIIGTTFLLTCLLRHLFKhFSPSHHfgfEAAAWYWHFVDVVWLFLYISIY 258
Cdd:MTH00049 166 SHVVLGVVGLSTLLLVGSSS-FGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
127-260 |
7.06e-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: 70.99 E-value: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 127 PLQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFFTVILGAYFTVLQAYEYIE---------APFTIADAIYGST 197
Cdd:cd02864 59 PLVLIAIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGAS 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511347969 198 FFVATGFHGLHVIIGTTFLLTCLLRHLFKHFSPSHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd02864 139 FFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
128-261 |
1.21e-11 |
|
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: 61.79 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 128 LQIPLLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFFTVILGAYFTVLQAYE---YIEAPFTIADAIYGSTFFVATGF 204
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 511347969 205 HGLHVIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:TIGR02897 132 HGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
132-262 |
3.05e-09 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 55.56 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511347969 132 LLNTAILLASGVTVTWAHHSLMEGNSSQTTQGLFFTVILGAYFTVLQAYEY---IEAPFTIADAIYGSTFFVATGFHGLH 208
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 511347969 209 VIIGTTFLLTCLLRHLFKHFSPSHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 262
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
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