|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
1.96e-152 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 424.98 E-value: 1.96e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 5 NSNHPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 85 MIMFIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQSTQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 165 LFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 1707765440 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
6.74e-120 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 342.85 E-value: 6.74e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 8 HPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNN--LLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 86 IMFIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQSTQGL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 166 FFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1707765440 246 FVDVVWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
2.21e-115 |
|
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: 330.63 E-value: 2.21e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 20 ITGAIGAMSLTSGLAKWFHQFDNN-LLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLRWGMIMFIASEVLFFIS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 99 FFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQSTQGLFFTMIMGIYFTML 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 179 QAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1707765440 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
73-261 |
3.00e-47 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 155.78 E-value: 3.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 73 HTKFVSVGLRWGMIMFIASEVLFFISFFWAFFsssiipTIELGTTWPPMGIQSFNPmQIPLLNTMILLASGVTVTWAHHS 152
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 153 LIESNYSQSTQGLFFTMIMGIYFTMLQAYEY---WEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQF 229
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 1707765440 230 SPNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
133-262 |
7.35e-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: 59.87 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 133 LLNTMILLASGVTVTWAHHSLIESNYSQSTQGLFFTMIMGIYFTMLQAYE---YWEAPFTIADAIYGSSFFVATGFHGLH 209
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1707765440 210 VMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
1.96e-152 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 424.98 E-value: 1.96e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 5 NSNHPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 85 MIMFIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQSTQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 165 LFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 1707765440 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
3-263 |
8.10e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 388.16 E-value: 8.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 3 MTNSNHPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLR 82
Cdd:MTH00118 1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 83 WGMIMFIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQST 162
Cdd:MTH00118 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 163 QGLFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAW 242
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1707765440 243 YWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
5.64e-132 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 373.54 E-value: 5.64e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 8 HPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLRWGMIM 87
Cdd:MTH00189 5 HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 88 FIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQSTQGLFF 167
Cdd:MTH00189 85 FITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 168 TMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00189 165 TVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 1707765440 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00189 245 DVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
8-263 |
1.40e-127 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 362.51 E-value: 1.40e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 8 HPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLRWGMIM 87
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 88 FIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQSTQGLFF 167
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 168 TMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 1707765440 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
2.39e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 361.52 E-value: 2.39e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 8 HPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLRWGMIM 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 88 FIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQSTQGLFF 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 168 TMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1707765440 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
2-263 |
4.03e-124 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 353.71 E-value: 4.03e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 2 MMTNSNHPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGL 81
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 82 RWGMIMFIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQS 161
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 162 TQGLFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAA 241
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 1707765440 242 WYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
3-263 |
1.44e-122 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 349.81 E-value: 1.44e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 3 MTNSNHPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLR 82
Cdd:MTH00075 1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 83 WGMIMFIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQST 162
Cdd:MTH00075 81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 163 QGLFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAW 242
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1707765440 243 YWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
3-263 |
2.13e-122 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 349.41 E-value: 2.13e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 3 MTNSNHPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLR 82
Cdd:MTH00099 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 83 WGMIMFIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQST 162
Cdd:MTH00099 81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 163 QGLFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAW 242
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1707765440 243 YWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
3-263 |
2.85e-122 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 349.06 E-value: 2.85e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 3 MTNSNHPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLR 82
Cdd:MTH00130 1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 83 WGMIMFIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQST 162
Cdd:MTH00130 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 163 QGLFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAW 242
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1707765440 243 YWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
6.74e-120 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 342.85 E-value: 6.74e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 8 HPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNN--LLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 86 IMFIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQSTQGL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 166 FFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1707765440 246 FVDVVWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-263 |
1.59e-116 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 334.50 E-value: 1.59e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 8 HPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLRWGMIM 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 88 FIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQSTQGLFF 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 168 TMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1707765440 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
2.21e-115 |
|
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: 330.63 E-value: 2.21e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 20 ITGAIGAMSLTSGLAKWFHQFDNN-LLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLRWGMIMFIASEVLFFIS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 99 FFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQSTQGLFFTMIMGIYFTML 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 179 QAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1707765440 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
3-263 |
1.25e-109 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 317.08 E-value: 1.25e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 3 MTNSNHPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLR 82
Cdd:MTH00024 1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 83 WGMIMFIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQST 162
Cdd:MTH00024 81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 163 QGLFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAW 242
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240
|
250 260
....*....|....*....|.
gi 1707765440 243 YWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
2-263 |
4.11e-105 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 305.56 E-value: 4.11e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 2 MMTNSNHPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGL 81
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 82 RWGMIMFIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQS 161
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 162 TQGLFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAA 241
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 1707765440 242 WYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
5.17e-93 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 276.18 E-value: 5.17e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 8 HPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSVGLRWGMIM 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 88 FIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYSQSTQ---- 163
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNPASLEkgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 164 --------------------------------GLFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVM 211
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrtnaviGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1707765440 212 IGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
2-262 |
1.25e-81 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 246.11 E-value: 1.25e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 2 MMTNSNHPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNN--LLIMGLSITILTMIQWWRDVIREGTYQGMHTKFVSV 79
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGarLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 80 GLRWGMIMFIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNYS 159
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 160 QSTQGLFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEA 239
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|...
gi 1707765440 240 AAWYWHFVDVVWLFLYISIYWWG 262
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.77e-62 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 196.72 E-value: 1.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 8 HPFHLVDFSPWPITGAIGAMSLTSGLAKWFHQFDNNLLIMGLSITILTMIQWWRDVIREGtYQGMHTKFVSVGLRWGMIM 87
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 88 FIASEVLFFISFFWAFFSSSIIPTIELGTTWPPMGIQSFNPMQIPLLNTMILLASGVTVTWAHHSLIESNySQSTQGLFF 167
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 168 TMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 1707765440 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00083 241 DVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
73-261 |
3.39e-59 |
|
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: 185.87 E-value: 3.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 73 HTKFVSVGLRWGMIMFIASEVLFFISFFWAFFSSSIIPTIELGttwppmgiQSFNPMQIPLLNTMILLASGVTVTWAHHS 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 153 LI--ESNYSQSTQGLFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 1707765440 231 PNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
73-261 |
3.00e-47 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 155.78 E-value: 3.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 73 HTKFVSVGLRWGMIMFIASEVLFFISFFWAFFsssiipTIELGTTWPPMGIQSFNPmQIPLLNTMILLASGVTVTWAHHS 152
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 153 LIESNYSQSTQGLFFTMIMGIYFTMLQAYEY---WEAPFTIADAIYGSSFFVATGFHGLHVMIGTMFLLTCLIRHLMNQF 229
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 1707765440 230 SPNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
133-259 |
9.59e-20 |
|
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: 83.82 E-value: 9.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 133 LLNTMILLASGVTVTWAHHSLIESNYSQSTQGLFFTMIMGIYFTMLQAYEYWE---APFTIADAIYGSSFFVATGFHGLH 209
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1707765440 210 VMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
133-259 |
6.20e-15 |
|
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.
Pssm-ID: 239214 Cd Length: 186 Bit Score: 70.73 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 133 LLNTMILLASGVTVTWAHHSLIESNYSQSTQGLFFTMIMGIYFTMLQAYE---YWEAPFTIADAIYGSSFFVATGFHGLH 209
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1707765440 210 VMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
128-259 |
1.01e-14 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 71.10 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 128 PMQIPLLNTMILLASGVTVTwAHHSLIESNYSQSTqgLFFTMIMGIYFTMLQAYEYWEAPFTIADAIYGSSFFVATGFHG 207
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1707765440 208 LHVMIGTMFLLTCLIRHLMNqfspnhhFGF---EAAAWYWHFVDVVWLFLYISIY 259
Cdd:MTH00049 166 SHVVLGVVGLSTLLLVGSSS-------FGVyrsTVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
132-261 |
9.96e-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: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 132 PLLNTMILLASGVTVTWAHHSLIESNYSQSTQGLFFTMIMGIYFTMLQAYEYWEAPF---TIADAIYGSSFFVATGFHGL 208
Cdd:cd02865 52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1707765440 209 HVMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
136-261 |
2.21e-13 |
|
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: 67.14 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 136 TMILLASGVTVTWAHHSLIESNYSQSTQGLFFTMIMGIYFTMLQAYEY-----------WEAPFTIAdaIYGSSFFVATG 204
Cdd:cd02864 67 TFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITG 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1707765440 205 FHGLHVMIGTMFLLTCLIRHLMNQFSPNHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864 145 FHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
133-262 |
7.35e-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: 59.87 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 133 LLNTMILLASGVTVTWAHHSLIESNYSQSTQGLFFTMIMGIYFTMLQAYE---YWEAPFTIADAIYGSSFFVATGFHGLH 209
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1707765440 210 VMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
133-263 |
8.45e-08 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 51.32 E-value: 8.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765440 133 LLNTMILLASGVTVTWAHHSLIESNYSQSTQGLFFTMIMGIYFTMLQAYEYW---EAPFTIADAIYGSSFFVATGFHGLH 209
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1707765440 210 VMIGTMFLLTCLIRHLMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
|