|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
2-256 |
2.31e-153 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 427.29 E-value: 2.31e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 2 HKNHPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWG 81
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 82 MILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQG 161
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 162 LMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYW 241
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 769829438 242 HFVDVVWLFLYITIY 256
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
5-260 |
1.90e-119 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 341.70 E-value: 1.90e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 5 HPYHLVDISPWPILSSLSAMVMMSGLIKWFHMF--DSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWGM 82
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 83 ILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQGL 162
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 163 MLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWH 242
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 769829438 243 FVDVVWLFLYITIYWWGS 260
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
17-258 |
1.55e-118 |
|
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: 338.72 E-value: 1.55e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 17 ILSSLSAMVMMSGLIKWFHMFDSSLMM-IGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWGMILFITSEVFFFLS 95
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLfLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 96 FFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQGLMLTVILGLYFTIL 175
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 176 QGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFVDVVWLFLYITI 255
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 769829438 256 YWW 258
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
69-258 |
5.42e-51 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 165.02 E-value: 5.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 69 QHTFTVTLGLKWGMILFITSEVFFFLSFFWGFFHNSLAPAidigmmWPPKGIETFNPIqIPLLNTLILLTSGLTVTWAHH 148
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 149 SLMENNFKQTSQGLMLTVILGLYFTILQGYEY---IESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNH 225
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 769829438 226 FSPIHHFGFEAAAWYWHFVDVVWLFLYITIYWW 258
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
130-259 |
6.07e-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: 62.95 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 130 LLNTLILLTSGLTVTWAHHSLMENNFKQTSQGLMLTVILGLYFTILQGYE---YIESPFTISDAAYGSSFFMATGFHGIH 206
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 769829438 207 VIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 259
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
2-256 |
2.31e-153 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 427.29 E-value: 2.31e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 2 HKNHPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWG 81
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 82 MILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQG 161
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 162 LMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYW 241
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 769829438 242 HFVDVVWLFLYITIY 256
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
2-260 |
7.80e-135 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 380.45 E-value: 7.80e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 2 HKNHPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWG 81
Cdd:MTH00118 3 HQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 82 MILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQG 161
Cdd:MTH00118 83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 162 LMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYW 241
Cdd:MTH00118 163 LTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 769829438 242 HFVDVVWLFLYITIYWWGS 260
Cdd:MTH00118 243 HFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
1-260 |
6.43e-131 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 370.46 E-value: 6.43e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 1 MHKNHPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKW 80
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 81 GMILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQ 160
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 161 GLMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWY 240
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 769829438 241 WHFVDVVWLFLYITIYWWGS 260
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
3-260 |
5.70e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 360.75 E-value: 5.70e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 3 KNHPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWGM 82
Cdd:MTH00141 2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 83 ILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQGL 162
Cdd:MTH00141 82 ILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 163 MLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWH 242
Cdd:MTH00141 162 GLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWH 241
|
250
....*....|....*...
gi 769829438 243 FVDVVWLFLYITIYWWGS 260
Cdd:MTH00141 242 FVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
1-260 |
5.11e-124 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 353.26 E-value: 5.11e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 1 MHKNHPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKW 80
Cdd:MTH00039 1 MTHQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 81 GMILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQ 160
Cdd:MTH00039 81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 161 GLMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWY 240
Cdd:MTH00039 161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 769829438 241 WHFVDVVWLFLYITIYWWGS 260
Cdd:MTH00039 241 WHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
2-260 |
2.67e-123 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 351.37 E-value: 2.67e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 2 HKNHPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWG 81
Cdd:MTH00130 3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 82 MILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQG 161
Cdd:MTH00130 83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 162 LMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYW 241
Cdd:MTH00130 163 LTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 769829438 242 HFVDVVWLFLYITIYWWGS 260
Cdd:MTH00130 243 HFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
2-260 |
3.48e-123 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 350.95 E-value: 3.48e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 2 HKNHPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWG 81
Cdd:MTH00099 3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 82 MILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQG 161
Cdd:MTH00099 83 MILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 162 LMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYW 241
Cdd:MTH00099 163 LFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 769829438 242 HFVDVVWLFLYITIYWWGS 260
Cdd:MTH00099 243 HFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
5-260 |
6.03e-120 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 342.92 E-value: 6.03e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 5 HPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWGMIL 84
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 85 FITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQGLML 164
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 165 TVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFV 244
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 769829438 245 DVVWLFLYITIYWWGS 260
Cdd:MTH00219 247 DVVWLFLYVSIYWWGS 262
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
5-260 |
1.90e-119 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 341.70 E-value: 1.90e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 5 HPYHLVDISPWPILSSLSAMVMMSGLIKWFHMF--DSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWGM 82
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 83 ILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQGL 162
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 163 MLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWH 242
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 769829438 243 FVDVVWLFLYITIYWWGS 260
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
17-258 |
1.55e-118 |
|
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: 338.72 E-value: 1.55e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 17 ILSSLSAMVMMSGLIKWFHMFDSSLMM-IGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWGMILFITSEVFFFLS 95
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLfLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 96 FFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQGLMLTVILGLYFTIL 175
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 176 QGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFVDVVWLFLYITI 255
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 769829438 256 YWW 258
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
2-260 |
4.01e-118 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 338.26 E-value: 4.01e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 2 HKNHPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWG 81
Cdd:MTH00075 3 HQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 82 MILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQG 161
Cdd:MTH00075 83 MILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 162 LMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYW 241
Cdd:MTH00075 163 LALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 769829438 242 HFVDVVWLFLYITIYWWGS 260
Cdd:MTH00075 243 HFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
5-260 |
1.00e-110 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 319.39 E-value: 1.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 5 HPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWGMIL 84
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 85 FITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQGLML 164
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 165 TVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFV 244
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*.
gi 769829438 245 DVVWLFLYITIYWWGS 260
Cdd:MTH00024 246 DVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
5-260 |
1.86e-108 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 313.70 E-value: 1.86e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 5 HPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWGMIL 84
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 85 FITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQGLML 164
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 165 TVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFV 244
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 769829438 245 DVVWLFLYITIYWWGS 260
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-260 |
6.11e-106 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 307.49 E-value: 6.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 1 MHKNHPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKW 80
Cdd:MTH00052 3 QQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 81 GMILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQ 160
Cdd:MTH00052 83 GMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 161 GLMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWY 240
Cdd:MTH00052 163 GLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWY 242
|
250 260
....*....|....*....|
gi 769829438 241 WHFVDVVWLFLYITIYWWGS 260
Cdd:MTH00052 243 WHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
5-260 |
3.11e-91 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 271.55 E-value: 3.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 5 HPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKWGMIL 84
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 85 FITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLM------------- 151
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIgtgnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 152 ----------------------ENNFKQTSQ-GLMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVI 208
Cdd:MTH00028 166 giegpnpsngappdpqkgptflLSDFRTNAViGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 769829438 209 IGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFVDVVWLFLYITIYWWGS 260
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
3-259 |
7.53e-83 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 249.20 E-value: 7.53e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 3 KNHPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFD--SSLMMIGSISMILIMYQWWRDISREGTFQGQHTFTVTLGLKW 80
Cdd:PLN02194 5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 81 GMILFITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQ 160
Cdd:PLN02194 85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 161 GLMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWY 240
Cdd:PLN02194 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244
|
250
....*....|....*....
gi 769829438 241 WHFVDVVWLFLYITIYWWG 259
Cdd:PLN02194 245 WHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
5-260 |
1.67e-68 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 212.12 E-value: 1.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 5 HPYHLVDISPWPILSSLSAMVMMSGLIKWFHMFDSSLMMIGSISMILIMYQWWRDISREGtFQGQHTFTVTLGLKWGMIL 84
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 85 FITSEVFFFLSFFWGFFHNSLAPAIDIGMMWPPKGIETFNPIQIPLLNTLILLTSGLTVTWAHHSLMENNfKQTSQGLML 164
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 165 TVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFV 244
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 769829438 245 DVVWLFLYITIYWWGS 260
Cdd:MTH00083 241 DVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
70-258 |
1.27e-62 |
|
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: 194.34 E-value: 1.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 70 HTFTVTLGLKWGMILFITSEVFFFLSFFWGFFHNSLAPAIDIGmmwppkgiETFNPIQIPLLNTLILLTSGLTVTWAHHS 149
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 150 LM--ENNFKQTSQGLMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNHFS 227
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 769829438 228 PIHHFGFEAAAWYWHFVDVVWLFLYITIYWW 258
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
69-258 |
5.42e-51 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 165.02 E-value: 5.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 69 QHTFTVTLGLKWGMILFITSEVFFFLSFFWGFFHNSLAPAidigmmWPPKGIETFNPIqIPLLNTLILLTSGLTVTWAHH 148
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 149 SLMENNFKQTSQGLMLTVILGLYFTILQGYEY---IESPFTISDAAYGSSFFMATGFHGIHVIIGTTFLAICLARHLNNH 225
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 769829438 226 FSPIHHFGFEAAAWYWHFVDVVWLFLYITIYWW 258
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
130-256 |
1.21e-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: 94.22 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 130 LLNTLILLTSGLTVTWAHHSLMENNFKQTSQGLMLTVILGLYFTILQGYEYIESpFTISDAAYGSSFFMA----TGFHGI 205
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHK-IAAGIDPDAGLFFTLyfllTGFHLL 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 769829438 206 HVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFVDVVWLFLYITIY 256
Cdd:cd02862 134 HVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
117-256 |
1.11e-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: 78.44 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 117 PKGIETFNpIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQGLMLTVILGLYFTILQGYE---YIESPFTISDAAYG 193
Cdd:cd02863 42 PPGHELFE-LPLVFIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 769829438 194 SSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFVDVVWLFLYITIY 256
Cdd:cd02863 121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
125-256 |
2.81e-17 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 78.03 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 125 PIQIPLLNTLILLTSGLTVTWAHHSLmenNFKQTSQGLMLTVILGLYFTILQGYEYIESPFTISDAAYGSSFFMATGFHG 204
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 769829438 205 IHVIIGTTFLAICLARHLNNhFSPIHHfgfEAAAWYWHFVDVVWLFLYITIY 256
Cdd:MTH00049 166 SHVVLGVVGLSTLLLVGSSS-FGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
129-258 |
4.68e-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: 239216 Cd Length: 184 Bit Score: 76.64 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 129 PLLNTLILLTSGLTVTWAHHSLMENNFKQTSQGLMLTVILGLYFTILQGYEYIESPF---TISDAAYGSSFFMATGFHGI 205
Cdd:cd02865 52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 769829438 206 HVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFVDVVWLFLYITIYWW 258
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
125-258 |
2.72e-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: 72.15 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 125 PIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQGLMLTVILGLYFTILQGYEY-----------IESPFTIsdAAYG 193
Cdd:cd02864 59 PLVLIAIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGA--AQFG 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 769829438 194 SSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFG-FEAAAWYWHFVDVVWLFLYITIYWW 258
Cdd:cd02864 137 ASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
130-259 |
6.07e-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: 62.95 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 130 LLNTLILLTSGLTVTWAHHSLMENNFKQTSQGLMLTVILGLYFTILQGYE---YIESPFTISDAAYGSSFFMATGFHGIH 206
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 769829438 207 VIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 259
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
117-260 |
2.79e-09 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 55.56 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769829438 117 PKGIETFNpIQIPLLNTLILLTSGLTVTWAHHSLMENNFKQTSQGLMLTVILGLYFTILQGYEY---IESPFTISDAAYG 193
Cdd:PRK10663 58 PTGKDIFE-LPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFL 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 769829438 194 SSFFMATGFHGIHVIIGTTFLAICLARHLNNHFSPIHHFGFEAAAWYWHFVDVVWLFLYITIYWWGS 260
Cdd:PRK10663 137 SAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
