|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
3.47e-139 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 391.47 E-value: 3.47e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 6 NNHPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGM 85
Cdd:MTH00155 2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 86 ILFIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKAL 165
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 166 IMTILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWH 245
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 2041232742 246 FVDVVWLFLYISIY 259
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
1.08e-109 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 317.04 E-value: 1.08e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFH--STNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 86 ILFIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKAL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 166 IMTILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 2041232742 246 FVDVVWLFLYISIYWWGY 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
1.95e-108 |
|
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: 313.30 E-value: 1.95e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 20 ITGAMGAMTLTSGMLKWFHSTNSD-LFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMILFIISEVLFFFS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 99 FFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIMTILLGVYFTMT 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 179 QSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2041232742 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
6.26e-49 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 160.01 E-value: 6.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 72 AHTSMVYNGMRWGMILFIISEVLFFFSFFWAFFNSSLApnmelgFNWPPKGVEPFNPlHIPLLNTIILLASGVTVTWTHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 152 AMMKSNHSQAQKALIMTILLGVYFTMTQSYEY---LEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2041232742 229 FNSKHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
129-262 |
2.52e-10 |
|
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: 58.33 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 129 LHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIMTILLGVYFTMTQSYE---YLEAPFTLSDSIYGTTFFVTTGF 205
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2041232742 206 HGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 132 HGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
3.47e-139 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 391.47 E-value: 3.47e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 6 NNHPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGM 85
Cdd:MTH00155 2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 86 ILFIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKAL 165
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 166 IMTILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWH 245
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 2041232742 246 FVDVVWLFLYISIY 259
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
5.94e-126 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 358.11 E-value: 5.94e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00118 6 HPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIM 167
Cdd:MTH00118 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 168 TILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFV 247
Cdd:MTH00118 166 TILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFV 245
|
250
....*....|....*
gi 2041232742 248 DVVWLFLYISIYWWG 262
Cdd:MTH00118 246 DVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
5.30e-121 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 345.81 E-value: 5.30e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00189 5 HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIM 167
Cdd:MTH00189 85 FITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 168 TILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFV 247
Cdd:MTH00189 165 TVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 2041232742 248 DVVWLFLYISIYWWGY 263
Cdd:MTH00189 245 DVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
1.43e-118 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 339.46 E-value: 1.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIM 167
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 168 TILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFV 247
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....*
gi 2041232742 248 DVVWLFLYISIYWWG 262
Cdd:MTH00219 247 DVVWLFLYVSIYWWG 261
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
5.12e-118 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 338.02 E-value: 5.12e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIM 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 168 TILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 2041232742 248 DVVWLFLYISIYWWGY 263
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
8-262 |
5.78e-114 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 327.84 E-value: 5.78e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIM 167
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 168 TILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFV 247
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*
gi 2041232742 248 DVVWLFLYISIYWWG 262
Cdd:MTH00039 245 DVVWLFLYVCIYWWG 259
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
8-262 |
1.21e-112 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 324.37 E-value: 1.21e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00099 6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIM 167
Cdd:MTH00099 86 FIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 168 TILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFV 247
Cdd:MTH00099 166 TILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFV 245
|
250
....*....|....*
gi 2041232742 248 DVVWLFLYISIYWWG 262
Cdd:MTH00099 246 DVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
3.97e-110 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 318.25 E-value: 3.97e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00130 6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIM 167
Cdd:MTH00130 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 168 TILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFV 247
Cdd:MTH00130 166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245
|
250
....*....|....*
gi 2041232742 248 DVVWLFLYISIYWWG 262
Cdd:MTH00130 246 DVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
4.34e-110 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 318.23 E-value: 4.34e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00075 6 HAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIM 167
Cdd:MTH00075 86 FITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 168 TILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFV 247
Cdd:MTH00075 166 TIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFV 245
|
250
....*....|....*
gi 2041232742 248 DVVWLFLYISIYWWG 262
Cdd:MTH00075 246 DVVWLFLYVSIYWWG 260
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
1.08e-109 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 317.04 E-value: 1.08e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFH--STNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 86 ILFIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKAL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 166 IMTILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 2041232742 246 FVDVVWLFLYISIYWWGY 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
1.95e-108 |
|
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: 313.30 E-value: 1.95e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 20 ITGAMGAMTLTSGMLKWFHSTNSD-LFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMILFIISEVLFFFS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 99 FFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIMTILLGVYFTMT 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 179 QSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2041232742 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
8-262 |
1.89e-107 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 311.30 E-value: 1.89e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIM 167
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 168 TILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFV 247
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*
gi 2041232742 248 DVVWLFLYISIYWWG 262
Cdd:MTH00024 246 DVVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-262 |
1.07e-102 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 299.44 E-value: 1.07e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIM 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 168 TILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*
gi 2041232742 248 DVVWLFLYISIYWWG 262
Cdd:MTH00009 244 DVVWIFLYLCIYWWG 258
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
1.30e-98 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 289.00 E-value: 1.30e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00052 7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIM 167
Cdd:MTH00052 87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 168 TILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFV 247
Cdd:MTH00052 167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246
|
250
....*....|....*
gi 2041232742 248 DVVWLFLYISIYWWG 262
Cdd:MTH00052 247 DVVWLFLFIFMYWWG 261
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
6.66e-85 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 255.38 E-value: 6.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNH--------- 158
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 159 ---------------------------SQAQKALIMTILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVI 211
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2041232742 212 IGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
8-262 |
1.06e-78 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 238.41 E-value: 1.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFH--STNSDLFMLGMMIIIMTMMQWWRDITREATFTGAHTSMVYNGMRWGM 85
Cdd:PLN02194 7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 86 ILFIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKAL 165
Cdd:PLN02194 87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 166 IMTILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWH 245
Cdd:PLN02194 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246
|
250
....*....|....*..
gi 2041232742 246 FVDVVWLFLYISIYWWG 262
Cdd:PLN02194 247 FVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
3.69e-64 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 200.95 E-value: 3.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 8 HPYHLVDISPWPITGAMGAMTLTSGMLKWFHSTNSDLFMLGMMIIIMTMMQWWRDITREAtFTGAHTSMVYNGMRWGMIL 87
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 88 FIISEVLFFFSFFWAFFNSSLAPNMELGFNWPPKGVEPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNhSQAQKALIM 167
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 168 TILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFV 247
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 2041232742 248 DVVWLFLYISIYWWGY 263
Cdd:MTH00083 241 DVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
73-261 |
2.96e-61 |
|
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: 191.26 E-value: 2.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 73 HTSMVYNGMRWGMILFIISEVLFFFSFFWAFFNSSLAPNMELGfnwppkgvEPFNPLHIPLLNTIILLASGVTVTWTHHA 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 153 MM--KSNHSQAQKALIMTILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFN 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 2041232742 231 SKHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
6.26e-49 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 160.01 E-value: 6.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 72 AHTSMVYNGMRWGMILFIISEVLFFFSFFWAFFNSSLApnmelgFNWPPKGVEPFNPlHIPLLNTIILLASGVTVTWTHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 152 AMMKSNHSQAQKALIMTILLGVYFTMTQSYEY---LEAPFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2041232742 229 FNSKHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
129-259 |
8.77e-22 |
|
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.
Pssm-ID: 239213 Cd Length: 186 Bit Score: 89.22 E-value: 8.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 129 LHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIMTILLGVYFTMTQSYEY---LEAPFTLSDSIYGTTFFVTTGF 205
Cdd:cd02862 51 LLLGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGF 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2041232742 206 HGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862 131 HLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
120-259 |
3.38e-20 |
|
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: 84.98 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 120 PKGVEPFNpLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIMTILLGVYFTMTQSYE---YLEAPFTLSDSIYG 196
Cdd:cd02863 42 PPGHELFE-LPLVFIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041232742 197 TTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863 121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
124-261 |
1.92e-18 |
|
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: 80.49 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 124 EPFNPLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIMTILLGVYFTMTQSYEYLEAPF---TLSDSIYGTTFF 200
Cdd:cd02865 44 APLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFY 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041232742 201 VTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865 124 LLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
128-259 |
6.33e-18 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 79.57 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 128 PLHIPLLNTIILLASGVTVTWTHHaMMKSNHSQAQkaLIMTILLGVYFTMTQSYEYLEAPFTLSDSIYGTTFFVTTGFHG 207
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHH-LLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2041232742 208 IHVIIGTIFLSTsmtrLYYMHFNSKHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:MTH00049 166 SHVVLGVVGLST----LLLVGSSSFGVYRSTVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
84-261 |
4.51e-16 |
|
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: 74.46 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 84 GMILFIISEVLFFFSFFWAFFNSSLA-----PNMELGFNWPPKGVEPfnPLHIPLLNTIILLASGVTVTWTHHAMMKSNH 158
Cdd:cd02864 12 MMWFFLLSDAFIFSSFLIAYMTARISttepwPLPSDVFALRIGHFNI--PLVLIAIMTFILITSSGTMAMAVNFGYRGNR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 159 SQAQKALIMTILLGVYFTMTQSYEYLE---------APFTLSDSIYGTTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHF 229
Cdd:cd02864 90 KAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKY 169
|
170 180 190
....*....|....*....|....*....|...
gi 2041232742 230 NSKHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864 170 QRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
120-262 |
2.32e-10 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 58.64 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 120 PKGVEPFNpLHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIMTILLGVYFTMTQSYEY---LEAPFTLSDSIYG 196
Cdd:PRK10663 58 PTGKDIFE-LPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFL 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041232742 197 TTFFVTTGFHGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:PRK10663 137 SAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
129-262 |
2.52e-10 |
|
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: 58.33 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041232742 129 LHIPLLNTIILLASGVTVTWTHHAMMKSNHSQAQKALIMTILLGVYFTMTQSYE---YLEAPFTLSDSIYGTTFFVTTGF 205
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2041232742 206 HGIHVIIGTIFLSTSMTRLYYMHFNSKHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 132 HGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
