|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
3.30e-159 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 441.93 E-value: 3.30e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 4 HKNHPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWG 83
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 84 MILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQG 163
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 164 LTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2049950112 244 HFVDVVWLFLYISIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
1.51e-122 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 349.40 E-value: 1.51e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 7 HPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNN--LFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 85 ILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 165 TLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 2049950112 245 FVDVVWLFLYISIYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
9.38e-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: 9.38e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 19 ITGALAAMITMTGIIKWFHFYNNN-LFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWGMILFITSEVFFFIS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 98 FFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGLTLTVLLGIYFTML 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 178 QAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFVDVVWLFLYISI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2049950112 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
81-260 |
1.41e-47 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 156.55 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 81 RWGMILFITSEVFF-FISFFWGFFHSSLTPsielgmmWPPKGITPFNPLqIPLLNTLILLTSGLTVTWAHHSLMENNYTM 159
Cdd:COG1845 17 KLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 160 TTQGLTLTVLLGIYFTMLQAYEY---IEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGF 236
Cdd:COG1845 89 LRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGV 168
|
170 180
....*....|....*....|....
gi 2049950112 237 EAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:COG1845 169 EAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
128-261 |
5.09e-11 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131943 Cd Length: 190 Bit Score: 60.25 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 128 LQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGLTLTVLLGIYFTMLQAYE---YIEAPFTIADTVYGSSFFMATGF 204
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2049950112 205 HGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:TIGR02897 132 HGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
3.30e-159 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 441.93 E-value: 3.30e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 4 HKNHPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWG 83
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 84 MILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQG 163
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 164 LTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2049950112 244 HFVDVVWLFLYISIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
4-262 |
2.82e-140 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 394.32 E-value: 2.82e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 4 HKNHPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWG 83
Cdd:MTH00118 3 HQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 84 MILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQG 163
Cdd:MTH00118 83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 164 LTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYW 243
Cdd:MTH00118 163 LTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 2049950112 244 HFVDVVWLFLYISIYWWGS 262
Cdd:MTH00118 243 HFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
6.06e-137 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 385.87 E-value: 6.06e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 3 MHKNHPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRW 82
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 83 GMILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQ 162
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 163 GLTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWY 242
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 2049950112 243 WHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
3-262 |
1.20e-130 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 370.21 E-value: 1.20e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 3 MHKNHPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRW 82
Cdd:MTH00039 1 MTHQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 83 GMILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQ 162
Cdd:MTH00039 81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 163 GLTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWY 242
Cdd:MTH00039 161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 2049950112 243 WHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00039 241 WHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
5-262 |
6.18e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 363.06 E-value: 6.18e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 5 KNHPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWGM 84
Cdd:MTH00141 2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 85 ILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGL 164
Cdd:MTH00141 82 ILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 165 TLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWH 244
Cdd:MTH00141 162 GLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWH 241
|
250
....*....|....*...
gi 2049950112 245 FVDVVWLFLYISIYWWGS 262
Cdd:MTH00141 242 FVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
4-262 |
7.61e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 362.93 E-value: 7.61e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 4 HKNHPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWG 83
Cdd:MTH00130 3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 84 MILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQG 163
Cdd:MTH00130 83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 164 LTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYW 243
Cdd:MTH00130 163 LTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 2049950112 244 HFVDVVWLFLYISIYWWGS 262
Cdd:MTH00130 243 HFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
4-262 |
3.10e-127 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 361.35 E-value: 3.10e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 4 HKNHPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWG 83
Cdd:MTH00099 3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 84 MILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQG 163
Cdd:MTH00099 83 MILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 164 LTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYW 243
Cdd:MTH00099 163 LFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 2049950112 244 HFVDVVWLFLYISIYWWGS 262
Cdd:MTH00099 243 HFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
4-262 |
1.36e-124 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 354.82 E-value: 1.36e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 4 HKNHPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWG 83
Cdd:MTH00075 3 HQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 84 MILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQG 163
Cdd:MTH00075 83 MILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 164 LTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYW 243
Cdd:MTH00075 163 LALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 2049950112 244 HFVDVVWLFLYISIYWWGS 262
Cdd:MTH00075 243 HFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
1.32e-123 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 352.17 E-value: 1.32e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 7 HPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWGMIL 86
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 87 FITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGLTL 166
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 167 TVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFV 246
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 2049950112 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00219 247 DVVWLFLYVSIYWWGS 262
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
1.51e-122 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 349.40 E-value: 1.51e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 7 HPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNN--LFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 85 ILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 165 TLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 2049950112 245 FVDVVWLFLYISIYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
9.38e-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: 9.38e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 19 ITGALAAMITMTGIIKWFHFYNNN-LFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWGMILFITSEVFFFIS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 98 FFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGLTLTVLLGIYFTML 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 178 QAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFVDVVWLFLYISI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2049950112 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
7-262 |
2.44e-113 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 326.41 E-value: 2.44e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 7 HPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWGMIL 86
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 87 FITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGLTL 166
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 167 TVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFV 246
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 2049950112 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
7-262 |
5.98e-112 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 322.86 E-value: 5.98e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 7 HPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWGMIL 86
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 87 FITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGLTL 166
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 167 TVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFV 246
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*.
gi 2049950112 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00024 246 DVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
4.87e-108 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 312.88 E-value: 4.87e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 1 MSMHKNHPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 81 RWGMILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMT 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 161 TQGLTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAA 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 2049950112 241 WYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
8.53e-94 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 278.10 E-value: 8.53e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 7 HPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTMGLRWGMIL 86
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 87 FITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHH---------------- 150
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHaiigtgnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 151 --------------------SLMENNYTMTTQGLTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVI 210
Cdd:MTH00028 166 giegpnpsngappdpqkgptFLLSDFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2049950112 211 IGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
1-261 |
2.00e-82 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 248.04 E-value: 2.00e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 1 MSMHKNHPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNN--LFLFGVTIMLLIMYQWWRDISREGTFQGLHTYSVTM 78
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGarLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 79 GLRWGMILFITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYT 158
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 159 MTTQGLTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEA 238
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|...
gi 2049950112 239 AAWYWHFVDVVWLFLYISIYWWG 261
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
2.67e-67 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 209.04 E-value: 2.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 7 HPYHLVDISPWPITGALAAMITMTGIIKWFHFYNNNLFLFGVTIMLLIMYQWWRDISREGtFQGLHTYSVTMGLRWGMIL 86
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 87 FITSEVFFFISFFWGFFHSSLTPSIELGMMWPPKGITPFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTqGLTL 166
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 167 TVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFV 246
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 2049950112 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00083 241 DVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
72-260 |
5.19e-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: 193.19 E-value: 5.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 72 HTYSVTMGLRWGMILFITSEVFFFISFFWGFFHSSLTPSIELGMmwppkgitPFNPLQIPLLNTLILLTSGLTVTWAHHS 151
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 152 LM--ENNYTMTTQGLTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFS 229
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 2049950112 230 CIHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
81-260 |
1.41e-47 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 156.55 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 81 RWGMILFITSEVFF-FISFFWGFFHSSLTPsielgmmWPPKGITPFNPLqIPLLNTLILLTSGLTVTWAHHSLMENNYTM 159
Cdd:COG1845 17 KLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 160 TTQGLTLTVLLGIYFTMLQAYEY---IEAPFTIADTVYGSSFFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGF 236
Cdd:COG1845 89 LRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGV 168
|
170 180
....*....|....*....|....
gi 2049950112 237 EAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:COG1845 169 EAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
128-258 |
4.35e-23 |
|
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.
Pssm-ID: 239213 Cd Length: 186 Bit Score: 92.68 E-value: 4.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 128 LQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGLTLTVLLGIYFTMLQAYEY---IEAPFTIADTVYGSSFFMATGF 204
Cdd:cd02862 51 LLLGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGF 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2049950112 205 HGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFVDVVWLFLYISIY 258
Cdd:cd02862 131 HLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
124-260 |
2.68e-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: 74.71 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 124 PFNPLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGLTLTVLLGIYFTMLQAYEYIEAPF---TIADTVYGSSFFM 200
Cdd:cd02865 45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYL 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 201 ATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd02865 125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
127-258 |
1.71e-15 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 73.03 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 127 PLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTtqgLTLTVLLGIYFTMLQAYEYIEAPFTIADTVYGSSFFMATGFHG 206
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLLGWKYCDLF---LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2049950112 207 LHVIIGTtFLLVCLLRHLNNHFSCIHHfgfEAAAWYWHFVDVVWLFLYISIY 258
Cdd:MTH00049 166 SHVVLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
127-260 |
2.10e-15 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239215 Cd Length: 202 Bit Score: 72.53 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 127 PLQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGLTLTVLLGIYFTMLQAYEYIEAPFTIADT---------VYGSS 197
Cdd:cd02864 59 PLVLIAIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQFGAS 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2049950112 198 FFMATGFHGLHVIIGTTFLLVCLLRHLNNHFSCIHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd02864 139 FFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
132-258 |
2.94e-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: 71.89 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 132 LLNTLILLTSGLTVTWAHHSLMENNYTMTTQGLTLTVLLGIYFTMLQAYE---YIEAPFTIADTVYGSSFFMATGFHGLH 208
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2049950112 209 VIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFVDVVWLFLYISIY 258
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
128-261 |
5.09e-11 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131943 Cd Length: 190 Bit Score: 60.25 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 128 LQIPLLNTLILLTSGLTVTWAHHSLMENNYTMTTQGLTLTVLLGIYFTMLQAYE---YIEAPFTIADTVYGSSFFMATGF 204
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2049950112 205 HGLHVIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:TIGR02897 132 HGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
132-262 |
2.37e-07 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 49.78 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049950112 132 LLNTLILLTSGLTVTWAHHSLMENNYTMTTQGLTLTVLLGIYFTMLQAYEY---IEAPFTIADTVYGSSFFMATGFHGLH 208
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2049950112 209 VIIGTTFLLVCLLRHLNNHFSCIHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 262
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
