|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
1.99e-164 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 455.41 E-value: 1.99e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 4 HSNHPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRWG 83
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 84 MILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQS 163
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 164 LFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 953244491 244 HFVDIVWLFLYVSIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-261 |
4.23e-128 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 363.65 E-value: 4.23e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 7 HPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQY--NMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 85 ILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQSL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 165 FFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 953244491 245 FVDIVWLFLYVSIYWWG 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 |
1.57e-124 |
|
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: 353.74 E-value: 1.57e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 19 LTASIGAMTTVAGMVKWFHQYNMS-LFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRWGMILFILSEVLFFVS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 98 FFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQSLFFTVTLGIYFTIL 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 178 QAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFVDIVWLFLYVSI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 953244491 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
2.17e-49 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 161.17 E-value: 2.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 71 LHTEAVTTGLRWGMILFILSEVLFFVSFFWAFFHSSLSpsielgAIWPPMGITPFNPFqIPLLNTVILLTSGITVTWAHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 151 SLMEGNHSQATQSLFFTVTLGIYFTILQAYEY---IEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNH 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 953244491 228 FSKNHHFGFEAAAWYWHFVDIVWLFLYVSIYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
128-261 |
1.22e-07 |
|
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131889 Cd Length: 180 Bit Score: 50.33 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 128 FQIP--LLNTVILLTSGITVTWAHHSLMEGNHSQATQSLFFTVTLGIYFTILQAYEY---IEAPFTIADSVYGSTFFMAT 202
Cdd:TIGR02842 40 FDLPfvLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAITFLLGLGFIGMEIYEFyhlIAEGNGPDRSAFLSAFFTLV 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 953244491 203 GFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFVDIVWLFLYVSIYWWG 261
Cdd:TIGR02842 120 GTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFWHFLDIVWICVFTFVYLLG 178
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
1.99e-164 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 455.41 E-value: 1.99e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 4 HSNHPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRWG 83
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 84 MILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQS 163
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 164 LFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 953244491 244 HFVDIVWLFLYVSIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
3-261 |
1.02e-141 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 398.17 E-value: 1.02e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 3 THSNHPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRW 82
Cdd:MTH00118 2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 83 GMILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQ 162
Cdd:MTH00118 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 163 SLFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWY 242
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241
|
250
....*....|....*....
gi 953244491 243 WHFVDIVWLFLYVSIYWWG 261
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
3-261 |
1.05e-140 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 395.50 E-value: 1.05e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 3 THSNHPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRW 82
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 83 GMILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQ 162
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 163 SLFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWY 242
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250
....*....|....*....
gi 953244491 243 WHFVDIVWLFLYVSIYWWG 261
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWG 259
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
1.19e-135 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 382.70 E-value: 1.19e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 7 HPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRWGMIL 86
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 87 FILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQSLFF 166
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 167 TVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFV 246
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 953244491 247 DIVWLFLYVSIYWWGG 262
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
7-262 |
3.28e-132 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 374.06 E-value: 3.28e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 7 HPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRWGMIL 86
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 87 FILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQSLFF 166
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 167 TVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFV 246
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 953244491 247 DIVWLFLYVSIYWWGG 262
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
1.72e-129 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 367.19 E-value: 1.72e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 1 MSTHSNHPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGL 80
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 81 RWGMILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQA 160
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 161 TQSLFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAA 240
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|.
gi 953244491 241 WYWHFVDIVWLFLYVSIYWWG 261
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWWG 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-261 |
4.23e-128 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 363.65 E-value: 4.23e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 7 HPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQY--NMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 85 ILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQSL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 165 FFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 953244491 245 FVDIVWLFLYVSIYWWG 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
3-261 |
2.19e-127 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 361.74 E-value: 2.19e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 3 THSNHPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRW 82
Cdd:MTH00099 2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 83 GMILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQ 162
Cdd:MTH00099 82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 163 SLFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWY 242
Cdd:MTH00099 162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241
|
250
....*....|....*....
gi 953244491 243 WHFVDIVWLFLYVSIYWWG 261
Cdd:MTH00099 242 WHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
3-261 |
2.93e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 361.39 E-value: 2.93e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 3 THSNHPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRW 82
Cdd:MTH00130 2 AHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 83 GMILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQ 162
Cdd:MTH00130 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 163 SLFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWY 242
Cdd:MTH00130 162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241
|
250
....*....|....*....
gi 953244491 243 WHFVDIVWLFLYVSIYWWG 261
Cdd:MTH00130 242 WHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
3-261 |
4.58e-126 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 358.67 E-value: 4.58e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 3 THSNHPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRW 82
Cdd:MTH00075 2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 83 GMILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQ 162
Cdd:MTH00075 82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 163 SLFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWY 242
Cdd:MTH00075 162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241
|
250
....*....|....*....
gi 953244491 243 WHFVDIVWLFLYVSIYWWG 261
Cdd:MTH00075 242 WHFVDVVWLFLYVSIYWWG 260
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
1.57e-124 |
|
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: 353.74 E-value: 1.57e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 19 LTASIGAMTTVAGMVKWFHQYNMS-LFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRWGMILFILSEVLFFVS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 98 FFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQSLFFTVTLGIYFTIL 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 178 QAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFVDIVWLFLYVSI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 953244491 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
7-261 |
1.94e-120 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 344.13 E-value: 1.94e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 7 HPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRWGMIL 86
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 87 FILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQSLFF 166
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 167 TVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFV 246
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*
gi 953244491 247 DIVWLFLYVSIYWWG 261
Cdd:MTH00009 244 DVVWIFLYLCIYWWG 258
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
7-261 |
3.33e-115 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 330.95 E-value: 3.33e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 7 HPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRWGMIL 86
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 87 FILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQATQSLFF 166
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 167 TVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFV 246
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*
gi 953244491 247 DIVWLFLYVSIYWWG 261
Cdd:MTH00024 246 DVVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
2.48e-110 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 318.66 E-value: 2.48e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 1 MSTHSNHPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 81 RWGMILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHSQA 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 161 TQSLFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAA 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|.
gi 953244491 241 WYWHFVDIVWLFLYVSIYWWG 261
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWG 261
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
7-261 |
1.65e-95 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 282.34 E-value: 1.65e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 7 HPFHLVDYSPWPLTASIGAMTTVAGMVKWFHQYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTTGLRWGMIL 86
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 87 FILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNH--------- 157
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 158 ---------------------------SQATQSLFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVL 210
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 953244491 211 IGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFVDIVWLFLYVSIYWWG 261
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
1-262 |
4.54e-87 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 259.98 E-value: 4.54e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 1 MSTHSNHPFHLVDYSPWPLTASIGAMTTVAGMVKWFH--QYNMSLFLLGNIITILTVYQWWRDVSREGTFQGLHTEAVTT 78
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 79 GLRWGMILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNHS 158
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 159 QATQSLFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEA 238
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|....
gi 953244491 239 AAWYWHFVDIVWLFLYVSIYWWGG 262
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWGG 264
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
7-261 |
1.23e-66 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 207.50 E-value: 1.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 7 HPFHLVDYSPWPLTASIGAMTTVAGMVKWFhQYNMSLFLLGNIITILTV-YQWWRDVSREGtFQGLHTEAVTTGLRWGMI 85
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFF-KYGLFYSFFFSLLYLLFIsFLWGKDISMEG-LSGYHNFFVMDGFKFGMI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 86 LFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGITPFNPFQIPLLNTVILLTSGITVTWAHHSLMEGNhSQATQSLF 165
Cdd:MTH00083 81 LFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 166 FTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHF 245
Cdd:MTH00083 160 LTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHF 239
|
250
....*....|....*.
gi 953244491 246 VDIVWLFLYVSIYWWG 261
Cdd:MTH00083 240 VDVVWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
72-260 |
4.49e-65 |
|
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: 200.89 E-value: 4.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 72 HTEAVTTGLRWGMILFILSEVLFFVSFFWAFFHSSLSPSIELGAiwppmgitPFNPFQIPLLNTVILLTSGITVTWAHHS 151
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 152 LM--EGNHSQATQSLFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNHFS 229
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 953244491 230 KNHHFGFEAAAWYWHFVDIVWLFLYVSIYWW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
2.17e-49 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 161.17 E-value: 2.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 71 LHTEAVTTGLRWGMILFILSEVLFFVSFFWAFFHSSLSpsielgAIWPPMGITPFNPFqIPLLNTVILLTSGITVTWAHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 151 SLMEGNHSQATQSLFFTVTLGIYFTILQAYEY---IEAPFTIADSVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNH 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 953244491 228 FSKNHHFGFEAAAWYWHFVDIVWLFLYVSIYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
132-258 |
1.17e-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: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 132 LLNTVILLTSGITVTWAHHSLMEGNHSQATQSLFFTVTLGIYFTILQAYEY---IEAPFTIADSVYGSTFFMATGFHGVH 208
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 953244491 209 VLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFVDIVWLFLYVSIY 258
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
83-260 |
5.22e-16 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239215 Cd Length: 202 Bit Score: 74.07 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 83 GMILFILSEVLFFVSFFWAFFHSSLSPSIELGAIWPPMGItPFNPFQIPL----LNTVILLTSGITVTWAHHSLMEGNHS 158
Cdd:cd02864 12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 159 QATQSLFFTVTLGIYFTILQAYEY-----------IEAPFTIAdsVYGSTFFMATGFHGVHVLIGTTFLLICLIRHLNNH 227
Cdd:cd02864 91 AAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168
|
170 180 190
....*....|....*....|....*....|....
gi 953244491 228 F-SKNHHFGFEAAAWYWHFVDIVWLFLYVSIYWW 260
Cdd:cd02864 169 YqRIGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
127-258 |
6.20e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 74.18 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 127 PFQIPLLNTVILLTSGITVTWAHHSL-MEGNHSQatqsLFFTVTLGIYFTILQAYEYIEAPFTIADSVYGSTFFMATGFH 205
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLLgWKYCDLF----LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLH 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 953244491 206 GVHVLIGTTFLLICLIRHLNNHFSKNHhfgfEAAAWYWHFVDIVWLFLYVSIY 258
Cdd:MTH00049 165 FSHVVLGVVGLSTLLLVGSSSFGVYRS----TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
121-258 |
1.70e-15 |
|
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.
Pssm-ID: 239214 Cd Length: 186 Bit Score: 72.27 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 121 GITPFNPFQIPL--LNTVILLTSGITVTWAHHSLMEGNHSQATQSLFFTVTLGIYFTILQAYE---YIEAPFTIADSVYG 195
Cdd:cd02863 41 GPPGHELFELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 953244491 196 STFFMATGFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFVDIVWLFLYVSIY 258
Cdd:cd02863 121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
131-260 |
8.06e-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: 239216 Cd Length: 184 Bit Score: 70.48 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 131 PLLNTVILLTSGITVTWAHHSLMEGNHSQATQSLFFTVTLGIYFTILQAYEYIEAPF---TIADSVYGSTFFMATGFHGV 207
Cdd:cd02865 52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 953244491 208 HVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFVDIVWLFLYVSIYWW 260
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
128-261 |
2.05e-09 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 55.94 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 128 FQIP--LLNTVILLTSGITVTWAHHSLMEGNHSQATQSLFFTVTLGIYFTILQAYEY---IEAPFTIADSVYGSTFFMAT 202
Cdd:PRK10663 64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALV 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 953244491 203 GFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFVDIVWLFLYVSIYWWG 261
Cdd:PRK10663 144 GTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
128-261 |
1.22e-07 |
|
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131889 Cd Length: 180 Bit Score: 50.33 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953244491 128 FQIP--LLNTVILLTSGITVTWAHHSLMEGNHSQATQSLFFTVTLGIYFTILQAYEY---IEAPFTIADSVYGSTFFMAT 202
Cdd:TIGR02842 40 FDLPfvLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAITFLLGLGFIGMEIYEFyhlIAEGNGPDRSAFLSAFFTLV 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 953244491 203 GFHGVHVLIGTTFLLICLIRHLNNHFSKNHHFGFEAAAWYWHFVDIVWLFLYVSIYWWG 261
Cdd:TIGR02842 120 GTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFWHFLDIVWICVFTFVYLLG 178
|
|
| |
