|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-258 |
1.45e-156 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 435.38 E-value: 1.45e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 6 NHPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGMI 85
Cdd:MTH00155 3 NHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 86 LFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGLL 165
Cdd:MTH00155 83 LFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 166 LTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHF 245
Cdd:MTH00155 163 FTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHF 242
|
250
....*....|...
gi 50812165 246 VDVVWLFLYISIY 258
Cdd:MTH00155 243 VDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-261 |
1.50e-120 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 344.39 E-value: 1.50e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 7 HPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPS--LFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 85 ILFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 165 LLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 50812165 245 FVDVVWLFLYISIYWWG 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
7.67e-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: 336.80 E-value: 7.67e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 19 LTGALGALITTTGLTKWFHQYD-PSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGMILFIISEVFFFVS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGgPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 98 FFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGLLLTILLGLYFTAL 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 178 QAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHFVDVVWLFLYISI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 50812165 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
2.00e-42 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 143.07 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 71 LHTMQVTLGLRWGMILFIISEVFFFVSFFWAFFHSSLAptveigSFWPPAGIVPFNPmHIPLLNTAILLASGVTVTWAHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 151 SLMEGNHTQATQGLLLTILLGLYFTALQAYEYYE---APFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSH 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 50812165 228 FSPTHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
132-261 |
1.75e-07 |
|
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: 50.24 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 132 LLNTAILLASGVTVTWAHHSLMEGNHTQATQGLLLTILLGLYFTALQAYE---YYEAPFTIADAVYGSTFFMATGFHGLH 208
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 50812165 209 VIIGsTFLATCLLRHLLSH-FSPTHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:TIGR02897 136 VTLG-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-258 |
1.45e-156 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 435.38 E-value: 1.45e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 6 NHPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGMI 85
Cdd:MTH00155 3 NHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 86 LFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGLL 165
Cdd:MTH00155 83 LFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 166 LTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHF 245
Cdd:MTH00155 163 FTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHF 242
|
250
....*....|...
gi 50812165 246 VDVVWLFLYISIY 258
Cdd:MTH00155 243 VDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
5-261 |
2.11e-141 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 397.40 E-value: 2.11e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 5 QNHPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGM 84
Cdd:MTH00118 4 QAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 85 ILFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGL 164
Cdd:MTH00118 84 ILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 165 LLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWH 244
Cdd:MTH00118 164 TLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWH 243
|
250
....*....|....*..
gi 50812165 245 FVDVVWLFLYISIYWWG 261
Cdd:MTH00118 244 FVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
5-261 |
4.10e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 388.95 E-value: 4.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 5 QNHPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGM 84
Cdd:MTH00189 3 QAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 85 ILFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGL 164
Cdd:MTH00189 83 ILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 165 LLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWH 244
Cdd:MTH00189 163 TLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWH 242
|
250
....*....|....*..
gi 50812165 245 FVDVVWLFLYISIYWWG 261
Cdd:MTH00189 243 FVDVVWLFLYVSIYWWG 259
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
5-262 |
1.16e-132 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 375.00 E-value: 1.16e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 5 QNHPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGM 84
Cdd:MTH00141 2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 85 ILFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGL 164
Cdd:MTH00141 82 ILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 165 LLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWH 244
Cdd:MTH00141 162 GLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWH 241
|
250
....*....|....*...
gi 50812165 245 FVDVVWLFLYISIYWWGG 262
Cdd:MTH00141 242 FVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
5-261 |
1.39e-130 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 369.83 E-value: 1.39e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 5 QNHPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGM 84
Cdd:MTH00099 4 QTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 85 ILFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGL 164
Cdd:MTH00099 84 ILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 165 LLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWH 244
Cdd:MTH00099 164 FITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWH 243
|
250
....*....|....*..
gi 50812165 245 FVDVVWLFLYISIYWWG 261
Cdd:MTH00099 244 FVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
7-262 |
5.73e-128 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 363.28 E-value: 5.73e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 7 HPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGMIL 86
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 87 FIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGLLL 166
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 167 TILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHFV 246
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 50812165 247 DVVWLFLYISIYWWGG 262
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
3-261 |
1.45e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 362.16 E-value: 1.45e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 3 APQNHPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRW 82
Cdd:MTH00130 2 AHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 83 GMILFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQ 162
Cdd:MTH00130 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 163 GLLLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWY 242
Cdd:MTH00130 162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241
|
250
....*....|....*....
gi 50812165 243 WHFVDVVWLFLYISIYWWG 261
Cdd:MTH00130 242 WHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
5-261 |
2.46e-125 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 356.79 E-value: 2.46e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 5 QNHPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGM 84
Cdd:MTH00219 5 QTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 85 ILFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGL 164
Cdd:MTH00219 85 ILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 165 LLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWH 244
Cdd:MTH00219 165 LFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWH 244
|
250
....*....|....*..
gi 50812165 245 FVDVVWLFLYISIYWWG 261
Cdd:MTH00219 245 FVDVVWLFLYVSIYWWG 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
3-261 |
1.95e-124 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 354.44 E-value: 1.95e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 3 APQNHPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRW 82
Cdd:MTH00075 2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 83 GMILFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQ 162
Cdd:MTH00075 82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 163 GLLLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWY 242
Cdd:MTH00075 162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241
|
250
....*....|....*....
gi 50812165 243 WHFVDVVWLFLYISIYWWG 261
Cdd:MTH00075 242 WHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-261 |
1.50e-120 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 344.39 E-value: 1.50e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 7 HPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPS--LFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 85 ILFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 165 LLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 50812165 245 FVDVVWLFLYISIYWWG 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
7.67e-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: 336.80 E-value: 7.67e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 19 LTGALGALITTTGLTKWFHQYD-PSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGMILFIISEVFFFVS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGgPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 98 FFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGLLLTILLGLYFTAL 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 178 QAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHFVDVVWLFLYISI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 50812165 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
7-261 |
9.93e-116 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 332.19 E-value: 9.93e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 7 HPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGMIL 86
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 87 FIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGLLL 166
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 167 TILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHFV 246
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*
gi 50812165 247 DVVWLFLYISIYWWG 261
Cdd:MTH00009 244 DVVWIFLYLCIYWWG 258
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
7-261 |
2.69e-112 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 323.63 E-value: 2.69e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 7 HPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGMIL 86
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 87 FIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQATQGLLL 166
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 167 TILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHFV 246
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*
gi 50812165 247 DVVWLFLYISIYWWG 261
Cdd:MTH00024 246 DVVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
2.84e-106 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 308.26 E-value: 2.84e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 1 MSAPQNHPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 81 RWGMILFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHTQA 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 161 TQGLLLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAA 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|.
gi 50812165 241 WYWHFVDVVWLFLYISIYWWG 261
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWG 261
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
7-261 |
4.19e-89 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 266.16 E-value: 4.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 7 HPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTLGLRWGMIL 86
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 87 FIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNH--------- 157
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 158 ---------------------------TQATQGLLLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVI 210
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 50812165 211 IGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
1-262 |
2.60e-86 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 258.05 E-value: 2.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 1 MSAPQNHPYHLVDQSPWPLTGALGALITTTGLTKWFHQYD--PSLFFLGMLITLLTMIQWWRDVTREGTYQGLHTMQVTL 78
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 79 GLRWGMILFIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNHT 158
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 159 QATQGLLLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEA 238
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|....
gi 50812165 239 AAWYWHFVDVVWLFLYISIYWWGG 262
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWGG 264
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
7-261 |
6.83e-64 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 200.18 E-value: 6.83e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 7 HPYHLVDQSPWPLTGALGALITTTGLTKWFHQYDPSLFFLGMLITLLTMIQWWRDVTREGtYQGLHTMQVTLGLRWGMIL 86
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 87 FIISEVFFFVSFFWAFFHSSLAPTVEIGSFWPPAGIVPFNPMHIPLLNTAILLASGVTVTWAHHSLMEGNhTQATQGLLL 166
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 167 TILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHFV 246
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*
gi 50812165 247 DVVWLFLYISIYWWG 261
Cdd:MTH00083 241 DVVWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
72-260 |
1.42e-58 |
|
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: 184.33 E-value: 1.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 72 HTMQVTLGLRWGMILFIISEVFFFVSFFWAFFHSSLAPTVEIGSfwppagivPFNPMHIPLLNTAILLASGVTVTWAHHS 151
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 152 LM--EGNHTQATQGLLLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSHFS 229
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 50812165 230 PTHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
2.00e-42 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 143.07 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 71 LHTMQVTLGLRWGMILFIISEVFFFVSFFWAFFHSSLAptveigSFWPPAGIVPFNPmHIPLLNTAILLASGVTVTWAHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 151 SLMEGNHTQATQGLLLTILLGLYFTALQAYEYYE---APFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLSH 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 50812165 228 FSPTHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
132-258 |
4.15e-18 |
|
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: 79.59 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 132 LLNTAILLASGVTVTWAHHSLMEGNHTQATQGLLLTILLGLYFTALQAYEYYEApFTIADAVYGSTFFMA----TGFHGL 207
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHK-IAAGIDPDAGLFFTLyfllTGFHLL 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 50812165 208 HVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHFVDVVWLFLYISIY 258
Cdd:cd02862 134 HVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
131-260 |
8.61e-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: 239216 Cd Length: 184 Bit Score: 67.78 E-value: 8.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 131 PLLNTAILLASGVTVTWAHHSLMEGNHTQATQGLLLTILLGLYFTALQAYEYYEAPF---TIADAVYGSTFFMATGFHGL 207
Cdd:cd02865 52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 50812165 208 HVIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
83-260 |
3.77e-12 |
|
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: 63.67 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 83 GMILFIISEVFFFVSFFWAFFHSSLAPTVeigsFWPPAGIV---PFNPMHIPL----LNTAILLASGVTVTWAHHSLMEG 155
Cdd:cd02864 12 MMWFFLLSDAFIFSSFLIAYMTARISTTE----PWPLPSDVfalRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 156 NHTQATQGLLLTILLGLYFTALQAYEYYE---------APFTIADAVYGSTFFMATGFHGLHVIIGSTFLATCLLRHLLS 226
Cdd:cd02864 88 NRKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRG 167
|
170 180 190
....*....|....*....|....*....|....*
gi 50812165 227 HFSPTHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd02864 168 KYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
130-258 |
2.82e-10 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 58.39 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 130 IPLLNTAILLASGVTVTWAHHSL-MEGNHTQatqgLLLTILLGLYFTALQAYEYYEAPFTIADAVYGSTFFMATGFHGLH 208
Cdd:MTH00049 92 IPFVGCFLLLGSSITVTAYHHLLgWKYCDLF----LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSH 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 50812165 209 VIIGSTFLATCLLRHLLShfspthhFGF---EAAAWYWHFVDVVWLFLYISIY 258
Cdd:MTH00049 168 VVLGVVGLSTLLLVGSSS-------FGVyrsTVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
132-258 |
4.46e-09 |
|
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: 54.55 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 132 LLNTAILLASGVTVTWAHHSLMEGNHTQATQGLLLTILLGLYFTALQAYE---YYEAPFTIADAVYGSTFFMATGFHGLH 208
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 50812165 209 VIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHFVDVVWLFLYISIY 258
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
132-261 |
1.75e-07 |
|
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: 50.24 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 132 LLNTAILLASGVTVTWAHHSLMEGNHTQATQGLLLTILLGLYFTALQAYE---YYEAPFTIADAVYGSTFFMATGFHGLH 208
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 50812165 209 VIIGsTFLATCLLRHLLSH-FSPTHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:TIGR02897 136 VTLG-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
132-261 |
5.95e-05 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 42.85 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812165 132 LLNTAILLASGVTVTWAHHSLMEGNHTQATQGLLLTILLGLYFTALQAYEYY---EAPFTIADAVYGSTFFMATGFHGLH 208
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 50812165 209 VIIGSTFLATCLLRHLLSHFSPTHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
|
|
| |
