|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
1.37e-163 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 453.48 E-value: 1.37e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 1 MMQQVYHPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 81 KYGMILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEA 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 161 IIGLVFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAV 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 63025101 241 WYWHFVDVVWLFLFIFMYWWGS 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-260 |
2.42e-117 |
|
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: 335.64 E-value: 2.42e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 20 IGGCGALLTTVGAIVYFHYSP-AWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLKYGMILFILSEVCLFFSF 98
Cdd:cd01665 2 LGSFGLLLLALGLVLWMHGYGgPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 99 FWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVFTVFLGILFTGLQ 178
Cdd:cd01665 82 FWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 179 AMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFVDVVWLFLFIFMY 258
Cdd:cd01665 162 AYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVY 241
|
..
gi 63025101 259 WW 260
Cdd:cd01665 242 WW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
6.58e-114 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 327.45 E-value: 6.58e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 7 HPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAW--VLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLKYGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 85 ILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAIIGL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 165 VFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 63025101 245 FVDVVWLFLFIFMYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
2.27e-46 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 153.47 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 71 HHTLIVKQGLKYGMILFILSEVCLFFSFFWAFFHSSLVptveiGAVWPPrGVDPLNPfSVPLLNTVVLLSSGATVTWTHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 151 AIISGKRKEAIIGLVFTVFLGILFTGLQAMEYYE---APFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQ 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 63025101 228 FTRHHHFGFEAAVWYWHFVDVVWLFLFIFMYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
132-261 |
7.32e-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: 56.79 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 132 LLNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVFTVFLGILFTGLQAME---YYEAPFTISDSVYGSTFFLTTGAHGAH 208
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 63025101 209 VLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFVDVVWLFLFIFMYWWG 261
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
1.37e-163 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 453.48 E-value: 1.37e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 1 MMQQVYHPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 81 KYGMILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEA 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 161 IIGLVFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAV 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 63025101 241 WYWHFVDVVWLFLFIFMYWWGS 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
2-262 |
2.50e-139 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 392.19 E-value: 2.50e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 2 MQQVYHPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLK 81
Cdd:MTH00024 1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 82 YGMILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAI 161
Cdd:MTH00024 81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 162 IGLVFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVW 241
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240
|
250 260
....*....|....*....|.
gi 63025101 242 YWHFVDVVWLFLFIFMYWWGS 262
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
1.98e-134 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 379.68 E-value: 1.98e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 7 HPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLKYGMIL 86
Cdd:MTH00118 6 HPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 87 FILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVF 166
Cdd:MTH00118 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 167 TVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFV 246
Cdd:MTH00118 166 TILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 63025101 247 DVVWLFLFIFMYWWGS 262
Cdd:MTH00118 246 DVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
1.65e-130 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 369.69 E-value: 1.65e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 1 MMQQvyHPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGL 80
Cdd:MTH00189 1 MHQA--HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 81 KYGMILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEA 160
Cdd:MTH00189 79 RYGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 161 IIGLVFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAV 240
Cdd:MTH00189 159 IQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAA 238
|
250 260
....*....|....*....|..
gi 63025101 241 WYWHFVDVVWLFLFIFMYWWGS 262
Cdd:MTH00189 239 WYWHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
7-258 |
2.34e-125 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 356.41 E-value: 2.34e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 7 HPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLKYGMIL 86
Cdd:MTH00155 4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 87 FILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVF 166
Cdd:MTH00155 84 FIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 167 TVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFV 246
Cdd:MTH00155 164 TIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFV 243
|
250
....*....|..
gi 63025101 247 DVVWLFLFIFMY 258
Cdd:MTH00155 244 DVVWLFLYISIY 255
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
7-262 |
9.59e-125 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 355.19 E-value: 9.59e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 7 HPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLKYGMIL 86
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 87 FILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVF 166
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 167 TVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFV 246
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 63025101 247 DVVWLFLFIFMYWWGS 262
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
2.41e-120 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 343.80 E-value: 2.41e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 7 HPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLKYGMIL 86
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 87 FILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVF 166
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 167 TVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFV 246
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 63025101 247 DVVWLFLFIFMYWWGS 262
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
2-262 |
4.21e-119 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 340.95 E-value: 4.21e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 2 MQQVYHPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLK 81
Cdd:MTH00075 1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 82 YGMILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAI 161
Cdd:MTH00075 81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 162 IGLVFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVW 241
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 63025101 242 YWHFVDVVWLFLFIFMYWWGS 262
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
2-262 |
1.28e-117 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 337.12 E-value: 1.28e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 2 MQQVYHPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLK 81
Cdd:MTH00130 1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 82 YGMILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAI 161
Cdd:MTH00130 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 162 IGLVFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVW 241
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 63025101 242 YWHFVDVVWLFLFIFMYWWGS 262
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-260 |
2.42e-117 |
|
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: 335.64 E-value: 2.42e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 20 IGGCGALLTTVGAIVYFHYSP-AWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLKYGMILFILSEVCLFFSF 98
Cdd:cd01665 2 LGSFGLLLLALGLVLWMHGYGgPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 99 FWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVFTVFLGILFTGLQ 178
Cdd:cd01665 82 FWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 179 AMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFVDVVWLFLFIFMY 258
Cdd:cd01665 162 AYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVY 241
|
..
gi 63025101 259 WW 260
Cdd:cd01665 242 WW 243
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
2-262 |
4.26e-116 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 334.73 E-value: 4.26e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 2 MQQVYHPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLK 81
Cdd:MTH00028 1 MSLVYHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 82 YGMILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGK----- 156
Cdd:MTH00028 81 LGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpasl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 157 -------------------------------RKEAIIGLVFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAH 205
Cdd:MTH00028 161 ekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTH 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 63025101 206 GAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFVDVVWLFLFIFMYWWGS 262
Cdd:MTH00028 241 GLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
2-262 |
9.23e-116 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 332.46 E-value: 9.23e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 2 MQQVYHPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLK 81
Cdd:MTH00099 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 82 YGMILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAI 161
Cdd:MTH00099 81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 162 IGLVFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVW 241
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 63025101 242 YWHFVDVVWLFLFIFMYWWGS 262
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
6.58e-114 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 327.45 E-value: 6.58e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 7 HPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAW--VLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLKYGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 85 ILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAIIGL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 165 VFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 63025101 245 FVDVVWLFLFIFMYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
4.52e-111 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 320.58 E-value: 4.52e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 1 MMQQVYHPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGL 80
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 81 KYGMILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEA 160
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 161 IIGLVFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAV 240
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 63025101 241 WYWHFVDVVWLFLFIFMYWWGS 262
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
5-262 |
2.63e-103 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 300.60 E-value: 2.63e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 5 VYHPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQGLKYGM 84
Cdd:MTH00009 2 IRQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 85 ILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRKEAIIGL 164
Cdd:MTH00009 82 ILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 165 VFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWH 244
Cdd:MTH00009 162 ILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWH 241
|
250
....*....|....*...
gi 63025101 245 FVDVVWLFLFIFMYWWGS 262
Cdd:MTH00009 242 FVDVVWIFLYLCIYWWGS 259
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
1-261 |
3.15e-92 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 273.08 E-value: 3.15e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 1 MMQQVYHPYHLVKPSPWPYIGGCGALLTTVGAIVYFH--YSPAWVLSFGLVIIVVTMVVWWRDVIREATYQGHHTLIVKQ 78
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 79 GLKYGMILFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKRK 158
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 159 EAIIGLVFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEA 238
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|...
gi 63025101 239 AVWYWHFVDVVWLFLFIFMYWWG 261
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
6-262 |
4.35e-69 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 213.66 E-value: 4.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 6 YHPYHLVKPSPWPYIGGCGALLTTVGAIVYFHYSPAWVLSFGLVIIVVTMVVWWRDVIREAtYQGHHTLIVKQGLKYGMI 85
Cdd:MTH00083 2 FHNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 86 LFILSEVCLFFSFFWAFFHSSLVPTVEIGAVWPPRGVDPLNPFSVPLLNTVVLLSSGATVTWTHHAIISGKrKEAIIGLV 165
Cdd:MTH00083 81 LFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 166 FTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHF 245
Cdd:MTH00083 160 LTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHF 239
|
250
....*....|....*..
gi 63025101 246 VDVVWLFLFIFMYWWGS 262
Cdd:MTH00083 240 VDVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
72-260 |
2.40e-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: 2.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 72 HTLIVKQGLKYGMILFILSEVCLFFSFFWAFFHSSLVPTVEIGAvwpprgvdPLNPFSVPLLNTVVLLSSGATVTWTHHA 151
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 152 II--SGKRKEAIIGLVFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFT 229
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 63025101 230 RHHHFGFEAAVWYWHFVDVVWLFLFIFMYWW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
2.27e-46 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 153.47 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 71 HHTLIVKQGLKYGMILFILSEVCLFFSFFWAFFHSSLVptveiGAVWPPrGVDPLNPfSVPLLNTVVLLSSGATVTWTHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 151 AIISGKRKEAIIGLVFTVFLGILFTGLQAMEYYE---APFTISDSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQ 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 63025101 228 FTRHHHFGFEAAVWYWHFVDVVWLFLFIFMYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
132-258 |
4.99e-23 |
|
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.
Pssm-ID: 239213 Cd Length: 186 Bit Score: 92.68 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 132 LLNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVFTVFLGILFTGLQAMEYYE---APFTISDSVYGSTFFLTTGAHGAH 208
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 63025101 209 VLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFVDVVWLFLFIFMY 258
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
132-258 |
2.33e-19 |
|
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: 82.67 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 132 LLNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVFTVFLGILFTGLQAME---YYEAPFTISDSVYGSTFFLTTGAHGAH 208
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 63025101 209 VLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFVDVVWLFLFIFMY 258
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
114-260 |
1.99e-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: 239216 Cd Length: 184 Bit Score: 75.10 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 114 GAVWPPRGVDPLNpfsVPLLNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVFTVFLGILFTGLQAMEYYEAPF---TIS 190
Cdd:cd02865 38 GDWQPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPT 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 191 DSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFVDVVWLFLFIFMYWW 260
Cdd:cd02865 115 SNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
127-258 |
4.09e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 74.57 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 127 PFSVPLLNTVVLLSSGATVTWTHHAIISgkrKEAIIGLVFTVFLGILFTGLQAMEYYEAPFTISDSVYGSTFFLTTGAHG 206
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLLGW---KYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 63025101 207 AHVLIGSsfllVCLIRLIYYQFTRHHHFGFEAAVWYWHFVDVVWLFLFIFMY 258
Cdd:MTH00049 166 SHVVLGV----VGLSTLLLVGSSSFGVYRSTVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
124-260 |
1.88e-15 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239215 Cd Length: 202 Bit Score: 72.53 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 124 PLNPFSVPL----LNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVFTVFLGILFTGLQAMEYYE---------APFTIS 190
Cdd:cd02864 52 RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWG 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63025101 191 DSVYGSTFFLTTGAHGAHVLIGSSFLLVCLIRLIYYQFTRHHHFG-FEAAVWYWHFVDVVWLFLFIFMYWW 260
Cdd:cd02864 132 AAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
132-261 |
7.32e-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: 56.79 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 132 LLNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVFTVFLGILFTGLQAME---YYEAPFTISDSVYGSTFFLTTGAHGAH 208
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 63025101 209 VLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFVDVVWLFLFIFMYWWG 261
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
132-262 |
9.60e-07 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 48.24 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025101 132 LLNTVVLLSSGATVTWTHHAIISGKRKEAIIGLVFTVFLGILFTglqAMEYYEAPFTISD------SVYGSTFFLTTGAH 205
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFI---GMEIYEFHHLIVEgmgpdrSGFLSAFFALVGTH 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 63025101 206 GAHVLIGSSFLLVCLIRLIYYQFTRHHHFGFEAAVWYWHFVDVVWLFLFIFMYWWGS 262
Cdd:PRK10663 147 GLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
