|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
1.16e-144 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 405.33 E-value: 1.16e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 4 HWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWG 83
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 84 MILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQS 163
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 164 LFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2296408317 244 HFVDVVWLFLYVSIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-261 |
9.68e-119 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 339.77 E-value: 9.68e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHF--NSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 85 ILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 165 FVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 2296408317 245 FVDVVWLFLYVSIYWWG 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
9.37e-114 |
|
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: 326.39 E-value: 9.37e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 19 LTASIGALTLTVGLSYWFH-FNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMILFIVSEVFFFLS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 98 FFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTAL 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 178 QAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2296408317 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
2.85e-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: 2.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 71 LHSNMVMVNLRWGMILFIVSEVFFFLSFFWAFFHASLApsveigTQWPPVGIIPFNPFqIPLLNTAILLASGVTVTWSHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 151 SLMGGNHTQAMQSLFVTILLGMYFTALQAYEYME---APFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFH 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2296408317 228 FSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
121-261 |
1.91e-10 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131943 Cd Length: 190 Bit Score: 58.71 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 121 GIIPFNPFQIPLL--NTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYE---YMEAPFSISEAVYG 195
Cdd:TIGR02897 43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2296408317 196 STFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
1.16e-144 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 405.33 E-value: 1.16e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 4 HWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWG 83
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 84 MILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQS 163
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 164 LFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2296408317 244 HFVDVVWLFLYVSIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
3-261 |
2.16e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 389.70 E-value: 2.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 3 NHWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRW 82
Cdd:MTH00118 2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 83 GMILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQ 162
Cdd:MTH00118 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 163 SLFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWY 242
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241
|
250
....*....|....*....
gi 2296408317 243 WHFVDVVWLFLYVSIYWWG 261
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
7-261 |
1.95e-130 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 369.69 E-value: 1.95e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMIL 86
Cdd:MTH00189 5 HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 87 FIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFV 166
Cdd:MTH00189 85 FITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 167 TILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFV 246
Cdd:MTH00189 165 TVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFV 244
|
250
....*....|....*
gi 2296408317 247 DVVWLFLYVSIYWWG 261
Cdd:MTH00189 245 DVVWLFLYVSIYWWG 259
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
4.58e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 360.75 E-value: 4.58e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMIL 86
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 87 FIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFV 166
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 167 TILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFV 246
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 2296408317 247 DVVWLFLYVSIYWWGG 262
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
7-262 |
9.55e-124 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 352.49 E-value: 9.55e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMIL 86
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 87 FIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFV 166
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 167 TILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFV 246
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 2296408317 247 DVVWLFLYVSIYWWGG 262
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
4-261 |
4.87e-123 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 350.99 E-value: 4.87e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 4 HWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWG 83
Cdd:MTH00130 3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 84 MILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQS 163
Cdd:MTH00130 83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 164 LFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYW 243
Cdd:MTH00130 163 LTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYW 242
|
250
....*....|....*...
gi 2296408317 244 HFVDVVWLFLYVSIYWWG 261
Cdd:MTH00130 243 HFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
4-261 |
2.70e-122 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 349.02 E-value: 2.70e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 4 HWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWG 83
Cdd:MTH00099 3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 84 MILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQS 163
Cdd:MTH00099 83 MILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 164 LFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYW 243
Cdd:MTH00099 163 LFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYW 242
|
250
....*....|....*...
gi 2296408317 244 HFVDVVWLFLYVSIYWWG 261
Cdd:MTH00099 243 HFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
4-261 |
9.58e-122 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 347.50 E-value: 9.58e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 4 HWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWG 83
Cdd:MTH00075 3 HQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 84 MILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQS 163
Cdd:MTH00075 83 MILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 164 LFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYW 243
Cdd:MTH00075 163 LALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYW 242
|
250
....*....|....*...
gi 2296408317 244 HFVDVVWLFLYVSIYWWG 261
Cdd:MTH00075 243 HFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-261 |
9.68e-119 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 339.77 E-value: 9.68e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHF--NSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 85 ILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 165 FVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 2296408317 245 FVDVVWLFLYVSIYWWG 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
7-261 |
1.52e-118 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 339.46 E-value: 1.52e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMIL 86
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 87 FIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFV 166
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 167 TILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFV 246
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....*
gi 2296408317 247 DVVWLFLYVSIYWWG 261
Cdd:MTH00219 247 DVVWLFLYVSIYWWG 261
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
9.37e-114 |
|
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: 326.39 E-value: 9.37e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 19 LTASIGALTLTVGLSYWFH-FNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMILFIVSEVFFFLS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 98 FFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTAL 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 178 QAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2296408317 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
7-261 |
5.13e-108 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 312.54 E-value: 5.13e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMIL 86
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 87 FIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFV 166
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 167 TILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFV 246
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*
gi 2296408317 247 DVVWLFLYVSIYWWG 261
Cdd:MTH00009 244 DVVWIFLYLCIYWWG 258
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
6-261 |
8.39e-107 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 309.76 E-value: 8.39e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 6 HHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMI 85
Cdd:MTH00024 5 YHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGML 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 86 LFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLF 165
Cdd:MTH00024 85 LFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 166 VTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHF 245
Cdd:MTH00024 165 LTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHF 244
|
250
....*....|....*.
gi 2296408317 246 VDVVWLFLYVSIYWWG 261
Cdd:MTH00024 245 VDVVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
1.32e-100 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 294.01 E-value: 1.32e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 1 MKNHWHHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 81 RWGMILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQA 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 161 MQSLFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAA 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|.
gi 2296408317 241 WYWHFVDVVWLFLYVSIYWWG 261
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWG 261
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
6-261 |
2.27e-89 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 266.93 E-value: 2.27e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 6 HHPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGMI 85
Cdd:MTH00028 5 YHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGML 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 86 LFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNH-------- 157
Cdd:MTH00028 85 LFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgt 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 158 ----------------------------TQAMQSLFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHV 209
Cdd:MTH00028 165 qgiegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2296408317 210 IIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
Cdd:MTH00028 245 LVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
7-262 |
4.21e-78 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 236.87 E-value: 4.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFH--FNSMLILLLGLAIIIISSYQWWRDISREGTLQGLHSNMVMVNLRWGM 84
Cdd:PLN02194 7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 85 ILFIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSL 164
Cdd:PLN02194 87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 165 FVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWH 244
Cdd:PLN02194 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246
|
250
....*....|....*...
gi 2296408317 245 FVDVVWLFLYVSIYWWGG 262
Cdd:PLN02194 247 FVDVVWLFLFVSIYWWGG 264
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
7-261 |
1.04e-66 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 207.50 E-value: 1.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 7 HPFHMVDMSPWPLTASIGALTLTVGLSYWFHFNSMLILLLGLAIIIISSYQWWRDISREGtLQGLHSNMVMVNLRWGMIL 86
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 87 FIVSEVFFFLSFFWAFFHASLAPSVEIGTQWPPVGIIPFNPFQIPLLNTAILLASGVTVTWSHHSLMGGNHTQAMqSLFV 166
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 167 TILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFV 246
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*
gi 2296408317 247 DVVWLFLYVSIYWWG 261
Cdd:MTH00083 241 DVVWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
72-260 |
3.23e-63 |
|
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: 196.27 E-value: 3.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 72 HSNMVMVNLRWGMILFIVSEVFFFLSFFWAFFHASLAPSVEIGtqwppvgiIPFNPFQIPLLNTAILLASGVTVTWSHHS 151
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 152 LM--GGNHTQAMQSLFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFS 229
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 2296408317 230 PAHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
2.85e-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: 2.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 71 LHSNMVMVNLRWGMILFIVSEVFFFLSFFWAFFHASLApsveigTQWPPVGIIPFNPFqIPLLNTAILLASGVTVTWSHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 151 SLMGGNHTQAMQSLFVTILLGMYFTALQAYEYME---APFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFH 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2296408317 228 FSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
132-258 |
1.70e-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: 91.14 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 132 LLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYEY---MEAPFSISEAVYGSTFFVATGFHGLH 208
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2296408317 209 VIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIY 258
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
131-260 |
8.78e-18 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239216 Cd Length: 184 Bit Score: 78.57 E-value: 8.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 131 PLLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYEYMEAPFSI---SEAVYGSTFFVATGFHGL 207
Cdd:cd02865 52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYLLTGLHGL 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2296408317 208 HVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
128-258 |
1.80e-17 |
|
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: 77.67 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 128 FQIPL--LNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYE---YMEAPFSISEAVYGSTFFVAT 202
Cdd:cd02863 48 FELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLV 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2296408317 203 GFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIY 258
Cdd:cd02863 128 GTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
115-260 |
6.08e-17 |
|
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: 76.77 E-value: 6.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 115 TQWPP---VGIIPFNPFQIPL----LNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYEYME--- 184
Cdd:cd02864 40 EPWPLpsdVFALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKliv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 185 ------APFSISEAVYGSTFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHF-GFEAAAWYWHFVDVVWLFLYVSI 257
Cdd:cd02864 120 eegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFF 199
|
...
gi 2296408317 258 YWW 260
Cdd:cd02864 200 YLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
127-258 |
6.24e-14 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 68.79 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 127 PFQIPLLNTAILLASGVTVTwSHHSLMGGNHTQAMqsLFVTILLGMYFTALQAYEYMEAPFSISEAVYGSTFFVATGFHG 206
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2296408317 207 LHVIIGTTFLL-ICFYRLSKFHFSPAhhfgfEAAAWYWHFVDVVWLFLYVSIY 258
Cdd:MTH00049 166 SHVVLGVVGLStLLLVGSSSFGVYRS-----TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
121-261 |
1.91e-10 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131943 Cd Length: 190 Bit Score: 58.71 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 121 GIIPFNPFQIPLL--NTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYE---YMEAPFSISEAVYG 195
Cdd:TIGR02897 43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2296408317 196 STFFVATGFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
128-261 |
5.90e-10 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 57.48 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296408317 128 FQIP--LLNTAILLASGVTVTWSHHSLMGGNHTQAMQSLFVTILLGMYFTALQAYEY---MEAPFSISEAVYGSTFFVAT 202
Cdd:PRK10663 64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALV 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2296408317 203 GFHGLHVIIGTTFLLICFYRLSKFHFSPAHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
Cdd:PRK10663 144 GTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
|
|
|