|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
6.55e-158 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 438.85 E-value: 6.55e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 5 HSNHPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 85 MILFIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 165 LTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 306960096 245 HFVDVVWLFLYLSIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-262 |
3.63e-121 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 345.93 E-value: 3.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 8 HPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGIS--ITLLTMVQWWRDITREGTFQGLHTLKVSLGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIAlfSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 86 ILFIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 166 TLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 306960096 246 FVDVVWLFLYLSIYWWG 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
8.42e-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: 336.80 E-value: 8.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 20 LSGAIGALILTSGLTKWFHLFDISLLL-VGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRWGMILFIVSEVFFFIS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLfLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 99 FFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGLTLTVILGLYFTAL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 179 QAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWHFVDVVWLFLYLSI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 306960096 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
4.89e-48 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 157.70 E-value: 4.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 72 LHTLKVSLGLRWGMILFIVSEVFFFISFFWAFFhsslapTIELGTMWPPQGIYPFNPlHIPLLNTAILLASGVTITWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 152 ELMEGNHSQCTQGLTLTVILGLYFTALQAYEY---IEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQ 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 306960096 229 FSQTHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
129-262 |
3.50e-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: 60.64 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 129 LHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGLTLTVILGLYFTALQAYE---YIEAPFSIADSIYGSSFFMATGF 205
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 206 HGLHV---IIGSTFLLICLTRHIKNQFSQTHHFgfeAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:TIGR02897 132 HGCHVtlgIVWAICLLIQIQRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
6.55e-158 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 438.85 E-value: 6.55e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 5 HSNHPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 85 MILFIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 165 LTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 306960096 245 HFVDVVWLFLYLSIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
4-262 |
1.07e-143 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 403.18 E-value: 1.07e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 4 THSNHPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRW 83
Cdd:MTH00118 2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 84 GMILFIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQ 163
Cdd:MTH00118 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 164 GLTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWY 243
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241
|
250
....*....|....*....
gi 306960096 244 WHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
4-262 |
3.41e-137 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 386.64 E-value: 3.41e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 4 THSNHPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRW 83
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 84 GMILFIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQ 163
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 164 GLTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWY 243
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250
....*....|....*....
gi 306960096 244 WHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWG 259
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.57e-133 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 377.31 E-value: 1.57e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 8 HPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRWGMIL 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 88 FIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGLTL 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 168 TVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 306960096 248 DVVWLFLYLSIYWWGG 263
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
4-262 |
9.25e-131 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 370.60 E-value: 9.25e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 4 THSNHPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRW 83
Cdd:MTH00099 2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 84 GMILFIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQ 163
Cdd:MTH00099 82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 164 GLTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWY 243
Cdd:MTH00099 162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241
|
250
....*....|....*....
gi 306960096 244 WHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00099 242 WHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
8-263 |
1.59e-129 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 367.13 E-value: 1.59e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 8 HPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRWGMIL 87
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 88 FIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGLTL 167
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 168 TVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWHFV 247
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 306960096 248 DVVWLFLYLSIYWWGG 263
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
4-262 |
5.59e-129 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 366.01 E-value: 5.59e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 4 THSNHPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRW 83
Cdd:MTH00130 2 AHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 84 GMILFIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQ 163
Cdd:MTH00130 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 164 GLTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWY 243
Cdd:MTH00130 162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241
|
250
....*....|....*....
gi 306960096 244 WHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00130 242 WHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
4-262 |
1.01e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 365.22 E-value: 1.01e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 4 THSNHPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRW 83
Cdd:MTH00075 2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 84 GMILFIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQ 163
Cdd:MTH00075 82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 164 GLTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWY 243
Cdd:MTH00075 162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241
|
250
....*....|....*....
gi 306960096 244 WHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00075 242 WHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
2-262 |
1.03e-126 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 360.26 E-value: 1.03e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 2 MTTHSNHPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGL 81
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 82 RWGMILFIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQC 161
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 162 TQGLTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAA 241
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|.
gi 306960096 242 WYWHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWWG 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-262 |
3.63e-121 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 345.93 E-value: 3.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 8 HPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGIS--ITLLTMVQWWRDITREGTFQGLHTLKVSLGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIAlfSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 86 ILFIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 166 TLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 306960096 246 FVDVVWLFLYLSIYWWG 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-262 |
2.20e-120 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 344.13 E-value: 2.20e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 8 HPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRWGMIL 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 88 FIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGLTL 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 168 TVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*
gi 306960096 248 DVVWLFLYLSIYWWG 262
Cdd:MTH00009 244 DVVWIFLYLCIYWWG 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
8.42e-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: 336.80 E-value: 8.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 20 LSGAIGALILTSGLTKWFHLFDISLLL-VGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRWGMILFIVSEVFFFIS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLfLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 99 FFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGLTLTVILGLYFTAL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 179 QAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWHFVDVVWLFLYLSI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 306960096 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
8-262 |
7.28e-115 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 330.18 E-value: 7.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 8 HPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRWGMIL 87
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 88 FIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGLTL 167
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 168 TVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWHFV 247
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*
gi 306960096 248 DVVWLFLYLSIYWWG 262
Cdd:MTH00024 246 DVVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
2-262 |
1.77e-111 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 321.74 E-value: 1.77e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 2 MTTHSNHPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGL 81
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 82 RWGMILFIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHSQC 161
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 162 TQGLTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAA 241
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|.
gi 306960096 242 WYWHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWG 261
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
5.31e-95 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 281.18 E-value: 5.31e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 8 HPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSLGLRWGMIL 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 88 FIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNH--------- 158
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 159 ---------------------------SQCTQGLTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVI 211
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 306960096 212 IGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
2-263 |
1.31e-84 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 253.43 E-value: 1.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 2 MTTHSNHPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFD--ISLLLVGISITLLTMVQWWRDITREGTFQGLHTLKVSL 79
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 80 GLRWGMILFIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHS 159
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 160 QCTQGLTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEA 239
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|....
gi 306960096 240 AAWYWHFVDVVWLFLYLSIYWWGG 263
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWGG 264
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
3.36e-69 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 214.05 E-value: 3.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 8 HPFHLVDFSPWPLSGAIGALILTSGLTKWFHLFDISLLLVGISITLLTMVQWWRDITREGtFQGLHTLKVSLGLRWGMIL 87
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 88 FIVSEVFFFISFFWAFFHSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNhSQCTQGLTL 167
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 168 TVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWHFV 247
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*
gi 306960096 248 DVVWLFLYLSIYWWG 262
Cdd:MTH00083 241 DVVWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
73-261 |
1.03e-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: 194.73 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 73 HTLKVSLGLRWGMILFIVSEVFFFISFFWAFFHSSLAPTIELGTmwppqgiyPFNPLHIPLLNTAILLASGVTITWAHHE 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 153 LM--EGNHSQCTQGLTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 306960096 231 QTHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
4.89e-48 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 157.70 E-value: 4.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 72 LHTLKVSLGLRWGMILFIVSEVFFFISFFWAFFhsslapTIELGTMWPPQGIYPFNPlHIPLLNTAILLASGVTITWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 152 ELMEGNHSQCTQGLTLTVILGLYFTALQAYEY---IEAPFSIADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQ 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 306960096 229 FSQTHHFGFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
129-259 |
7.59e-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: 92.30 E-value: 7.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 129 LHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGLTLTVILGLYFTALQAYEY---IEAPFSIADSIYGSSFFMATGF 205
Cdd:cd02862 51 LLLGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGF 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 306960096 206 HGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWHFVDVVWLFLYLSIY 259
Cdd:cd02862 131 HLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
80-261 |
7.51e-18 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239216 Cd Length: 184 Bit Score: 78.95 E-value: 7.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 80 GLRWGMILFIVSEVFFFIsffwaffhSSLAPTIELGTMWPPQGIYPFNPLHIPLLNTAILLASGVTITWAHHELMEGNHS 159
Cdd:cd02865 8 PGWWGLWVFMAVEGTLFA--------LLISAYFMRMTSGDWQPGAPLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 160 QCTQGLTLTVILGLYFTALQAYEYIEAPFSI---ADSIYGSSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHFG 236
Cdd:cd02865 80 LARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLP 159
|
170 180
....*....|....*....|....*
gi 306960096 237 FEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:cd02865 160 VELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
129-259 |
8.38e-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: 76.12 E-value: 8.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 129 LHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGLTLTVILGLYFTALQAYE---YIEAPFSIADSIYGSSFFMATGF 205
Cdd:cd02863 50 LPLVFIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGT 129
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 306960096 206 HGLHVIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWHFVDVVWLFLYLSIY 259
Cdd:cd02863 130 HGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
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|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
128-259 |
3.04e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 74.95 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 128 PLHIPLLNTAILLASGVTITWAHHELmegNHSQCTQGLTLTVILGLYFTALQAYEYIEAPFSIADSIYGSSFFMATGFHG 207
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 306960096 208 LHVIIGStFLLICLTRHIKNQFSQTHHfgfEAAAWYWHFVDVVWLFLYLSIY 259
Cdd:MTH00049 166 SHVVLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
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|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
128-261 |
6.29e-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: 71.38 E-value: 6.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 128 PLHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGLTLTVILGLYFTALQAYEY-----------IEAPFSIAdsIYG 196
Cdd:cd02864 59 PLVLIAIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFG 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306960096 197 SSFFMATGFHGLHVIIGSTFLLICLTRHIKNQFSQTHHF-GFEAAAWYWHFVDVVWLFLYLSIYWW 261
Cdd:cd02864 137 ASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
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| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
129-262 |
3.50e-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: 60.64 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 129 LHIPLLNTAILLASGVTITWAHHELMEGNHSQCTQGLTLTVILGLYFTALQAYE---YIEAPFSIADSIYGSSFFMATGF 205
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 206 HGLHV---IIGSTFLLICLTRHIKNQFSQTHHFgfeAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:TIGR02897 132 HGCHVtlgIVWAICLLIQIQRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
133-262 |
1.16e-10 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 59.41 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306960096 133 LLNTAILLASGVTITWAHHELMEGNHSQCTQGLTLTVILGLYFTALQAYEY---IEAPFSIADSIYGSSFFMATGFHGLH 209
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 306960096 210 VIIGSTFLLICLTRHIKNQFSQTHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 262
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
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