|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
4.07e-156 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 434.32 E-value: 4.07e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 1 MTRNPFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMG 80
Cdd:MTH00141 1 MTRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 81 MILFITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQS 160
Cdd:MTH00141 81 FILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 161 MILTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYW 240
Cdd:MTH00141 161 LGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYW 240
|
250
....*....|....*....
gi 212725627 241 HFVDVVWLILYTCIYWWGS 259
Cdd:MTH00141 241 HFVDVVWLFLYLSIYWWGS 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
16-257 |
9.74e-119 |
|
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: 339.11 E-value: 9.74e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 16 LTGSLGAMFLTVGLTSWFHN-HGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMGMILFITSEICFFFA 94
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGyGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 95 FFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILTIILGVYFTVL 174
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 175 QAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVDVVWLILYTCI 254
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 212725627 255 YWW 257
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
5-259 |
2.09e-115 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 331.30 E-value: 2.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 5 PFHLVEFSPWPLTGSLGAMFLTVGLTSWFH--NHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMGMI 82
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 83 LFITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQSMI 162
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 163 LTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHF 242
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*..
gi 212725627 243 VDVVWLILYTCIYWWGS 259
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
69-257 |
7.85e-44 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 146.53 E-value: 7.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 69 HTMKVSLGMRMGMILFITSEICF-FFAFFWAYFHSSLAPNtevgacWPPIHIHPlnPFQVPLLNTAILLASGVTVTWAHH 147
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAPD------WPAGAELL--DLPLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 148 SLMCGNHKEATQSMILTIILGVYFTVLQAQEYME---TSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHH 224
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 212725627 225 FSTNHHLGFEAAAWYWHFVDVVWLILYTCIYWW 257
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
129-258 |
2.81e-12 |
|
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: 63.72 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 129 LLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILTIILGVYFTVLQAQE---YMETSFSISDSIYGSTFFVATGFHGLH 205
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 212725627 206 VMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVDVVWLILYTCIYWWG 258
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
4.07e-156 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 434.32 E-value: 4.07e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 1 MTRNPFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMG 80
Cdd:MTH00141 1 MTRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 81 MILFITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQS 160
Cdd:MTH00141 81 FILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 161 MILTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYW 240
Cdd:MTH00141 161 LGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYW 240
|
250
....*....|....*....
gi 212725627 241 HFVDVVWLILYTCIYWWGS 259
Cdd:MTH00141 241 HFVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
1.98e-141 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 397.40 E-value: 1.98e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 5 PFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMGMILF 84
Cdd:MTH00118 7 PYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 85 ITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILT 164
Cdd:MTH00118 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 165 IILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVD 244
Cdd:MTH00118 167 ILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVD 246
|
250
....*....|....*
gi 212725627 245 VVWLILYTCIYWWGS 259
Cdd:MTH00118 247 VVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
1-255 |
6.18e-139 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 390.70 E-value: 6.18e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 1 MTRNPFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMG 80
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 81 MILFITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQS 160
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 161 MILTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYW 240
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 212725627 241 HFVDVVWLILYTCIY 255
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
3.76e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 388.95 E-value: 3.76e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 1 MTRNPFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMG 80
Cdd:MTH00189 2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 81 MILFITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQS 160
Cdd:MTH00189 82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 161 MILTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYW 240
Cdd:MTH00189 162 LTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYW 241
|
250
....*....|....*....
gi 212725627 241 HFVDVVWLILYTCIYWWGS 259
Cdd:MTH00189 242 HFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
2.93e-131 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 371.43 E-value: 2.93e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 1 MTRNPFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMG 80
Cdd:MTH00219 4 FQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 81 MILFITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQS 160
Cdd:MTH00219 84 MILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 161 MILTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYW 240
Cdd:MTH00219 164 LLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYW 243
|
250
....*....|....*....
gi 212725627 241 HFVDVVWLILYTCIYWWGS 259
Cdd:MTH00219 244 HFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
1-259 |
2.57e-127 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 361.46 E-value: 2.57e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 1 MTRNPFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMG 80
Cdd:MTH00009 1 MIRQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 81 MILFITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQS 160
Cdd:MTH00009 81 MILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 161 MILTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYW 240
Cdd:MTH00009 161 LILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYW 240
|
250
....*....|....*....
gi 212725627 241 HFVDVVWLILYTCIYWWGS 259
Cdd:MTH00009 241 HFVDVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
5-259 |
2.91e-127 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 361.35 E-value: 2.91e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 5 PFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMGMILF 84
Cdd:MTH00039 6 PYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 85 ITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILT 164
Cdd:MTH00039 86 ITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 165 IILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVD 244
Cdd:MTH00039 166 VLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVD 245
|
250
....*....|....*
gi 212725627 245 VVWLILYTCIYWWGS 259
Cdd:MTH00039 246 VVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
8.19e-126 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 357.92 E-value: 8.19e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 5 PFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMGMILF 84
Cdd:MTH00130 7 AYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 85 ITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILT 164
Cdd:MTH00130 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 165 IILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVD 244
Cdd:MTH00130 167 ILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVD 246
|
250
....*....|....*
gi 212725627 245 VVWLILYTCIYWWGS 259
Cdd:MTH00130 247 VVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
1.19e-125 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 357.52 E-value: 1.19e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 6 FHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMGMILFI 85
Cdd:MTH00075 8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 86 TSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILTI 165
Cdd:MTH00075 88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 166 ILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVDV 245
Cdd:MTH00075 168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247
|
250
....*....|....
gi 212725627 246 VWLILYTCIYWWGS 259
Cdd:MTH00075 248 VWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
5-259 |
7.59e-125 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 355.19 E-value: 7.59e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 5 PFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMGMILF 84
Cdd:MTH00099 7 AYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 85 ITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILT 164
Cdd:MTH00099 87 IISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 165 IILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVD 244
Cdd:MTH00099 167 ILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVD 246
|
250
....*....|....*
gi 212725627 245 VVWLILYTCIYWWGS 259
Cdd:MTH00099 247 VVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
5-259 |
2.41e-119 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 341.35 E-value: 2.41e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 5 PFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMGMILF 84
Cdd:MTH00024 7 PYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 85 ITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILT 164
Cdd:MTH00024 87 ILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 165 IILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVD 244
Cdd:MTH00024 167 VFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVD 246
|
250
....*....|....*
gi 212725627 245 VVWLILYTCIYWWGS 259
Cdd:MTH00024 247 VVWLFLYLCIYWWGS 261
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
16-257 |
9.74e-119 |
|
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: 339.11 E-value: 9.74e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 16 LTGSLGAMFLTVGLTSWFHN-HGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMGMILFITSEICFFFA 94
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGyGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 95 FFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILTIILGVYFTVL 174
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 175 QAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVDVVWLILYTCI 254
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 212725627 255 YWW 257
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
5-259 |
2.09e-115 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 331.30 E-value: 2.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 5 PFHLVEFSPWPLTGSLGAMFLTVGLTSWFH--NHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMGMI 82
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 83 LFITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQSMI 162
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 163 LTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHF 242
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*..
gi 212725627 243 VDVVWLILYTCIYWWGS 259
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
2-259 |
4.48e-113 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 325.59 E-value: 4.48e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 2 TRNPFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMGM 81
Cdd:MTH00052 5 YYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 82 ILFITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQSM 161
Cdd:MTH00052 85 ILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 162 ILTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWH 241
Cdd:MTH00052 165 ALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWH 244
|
250
....*....|....*...
gi 212725627 242 FVDVVWLILYTCIYWWGS 259
Cdd:MTH00052 245 FVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
4-259 |
9.55e-92 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 272.71 E-value: 9.55e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 4 NPFHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMGMIL 83
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 84 FITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHK-------- 155
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNPaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 156 ----------------------------EATQSMILTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVM 207
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrtNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 212725627 208 IGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVDVVWLILYTCIYWWGS 259
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
3-258 |
7.95e-84 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 251.51 E-value: 7.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 3 RNPFHLVEFSPWPLTGSLGAMFLTVGLTSWFH--NHGIITMSLGLFLITMTMFQWWRDIIRESTFQGYHTMKVSLGMRMG 80
Cdd:PLN02194 6 RHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 81 MILFITSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQS 160
Cdd:PLN02194 86 SILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 161 MILTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYW 240
Cdd:PLN02194 166 LVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYW 245
|
250
....*....|....*...
gi 212725627 241 HFVDVVWLILYTCIYWWG 258
Cdd:PLN02194 246 HFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
9.34e-76 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 230.61 E-value: 9.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 6 FHLVEFSPWPLTGSLGAMFLTVGLTSWFHNHGIITMSLGLFLITMTMFQWWRDIIREStFQGYHTMKVSLGMRMGMILFI 85
Cdd:MTH00083 5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 86 TSEICFFFAFFWAYFHSSLAPNTEVGACWPPIHIHPLNPFQVPLLNTAILLASGVTVTWAHHSLMCGNhKEATQSMILTI 165
Cdd:MTH00083 84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 166 ILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVDV 245
Cdd:MTH00083 163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242
|
250
....*....|....
gi 212725627 246 VWLILYTCIYWWGS 259
Cdd:MTH00083 243 VWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
69-257 |
4.22e-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: 190.49 E-value: 4.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 69 HTMKVSLGMRMGMILFITSEICFFFAFFWAYFHSSLAPNTEVGAcwppihihPLNPFQVPLLNTAILLASGVTVTWAHHS 148
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 149 LMC--GNHKEATQSMILTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFS 226
Cdd:cd00386 73 LAArrGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 212725627 227 TNHHLGFEAAAWYWHFVDVVWLILYTCIYWW 257
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
69-257 |
7.85e-44 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 146.53 E-value: 7.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 69 HTMKVSLGMRMGMILFITSEICF-FFAFFWAYFHSSLAPNtevgacWPPIHIHPlnPFQVPLLNTAILLASGVTVTWAHH 147
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAPD------WPAGAELL--DLPLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 148 SLMCGNHKEATQSMILTIILGVYFTVLQAQEYME---TSFSISDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHH 224
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 212725627 225 FSTNHHLGFEAAAWYWHFVDVVWLILYTCIYWW 257
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
129-255 |
4.58e-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: 89.99 E-value: 4.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 129 LLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILTIILGVYFTVLQAQEY---METSFSISDSIYGSTFFVATGFHGLH 205
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 212725627 206 VMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVDVVWLILYTCIY 255
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
110-257 |
1.87e-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: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 110 VGACWPPIHIHPLNpfqVPLLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILTIILGVYFTVLQAQEYMETSFSI--- 186
Cdd:cd02865 37 SGDWQPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygp 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212725627 187 SDSIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVDVVWLILYTCIYWW 257
Cdd:cd02865 114 TSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
114-257 |
3.81e-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: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 114 WPPIH---IHPLNPFQVPL----LNTAILLASGVTVTWAHHSLMCGNHKEATQSMILTIILGVYFTVLQAQEYMETSFSI 186
Cdd:cd02864 42 WPLPSdvfALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 187 SD---------SIYGSTFFVATGFHGLHVMIGSIFLFTCLMRILYHHF-STNHHLGFEAAAWYWHFVDVVWLILYTCIYW 256
Cdd:cd02864 122 GVrpwgnpwgaAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYqRIGRYEIVEIAGLYWHFVDLVWVFIFAFFYL 201
|
.
gi 212725627 257 W 257
Cdd:cd02864 202 W 202
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
125-255 |
1.84e-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: 72.27 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 125 FQVPL--LNTAILLASGVTVTWAHHSLMCGNHKEATQSMILTIILGVYFTVLQAQE---YMETSFSISDSIYGSTFFVAT 199
Cdd:cd02863 48 FELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLV 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 212725627 200 GFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVDVVWLILYTCIY 255
Cdd:cd02863 128 GTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
124-255 |
3.29e-15 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 72.26 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 124 PFQVPLLNTAILLASGVTVTWAHHSLmcgNHKEATQSMILTIILGVYFTVLQAQEYMETSFSISDSIYGSTFFVATGFHG 203
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 212725627 204 LHVMIGSIFLFTclmrILYHHFSTNHHLGFEAAAWYWHFVDVVWLILYTCIY 255
Cdd:MTH00049 166 SHVVLGVVGLST----LLLVGSSSFGVYRSTVLTWYWHFVDYIWLLVYLIVY 213
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
129-258 |
2.81e-12 |
|
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: 63.72 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 129 LLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILTIILGVYFTVLQAQE---YMETSFSISDSIYGSTFFVATGFHGLH 205
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 212725627 206 VMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVDVVWLILYTCIYWWG 258
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
125-259 |
2.08e-07 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 50.16 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 125 FQVP--LLNTAILLASGVTVTWAHHSLMCGNHKEATQSMILTIILGVYFTVLQAQEY---METSFSISDSIYGSTFFVAT 199
Cdd:PRK10663 64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALV 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 212725627 200 GFHGLHVMIGSIFLFTCLMRILYHHFSTNHHLGFEAAAWYWHFVDVVWLILYTCIYWWGS 259
Cdd:PRK10663 144 GTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
