|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-257 |
7.22e-161 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 446.16 E-value: 7.22e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 5 NHPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLRWGMI 84
Cdd:MTH00155 3 NHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 85 LFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTKHSLL 164
Cdd:MTH00155 83 LFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 165 ITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHF 244
Cdd:MTH00155 163 FTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHF 242
|
250
....*....|...
gi 2018119586 245 VDVVWLFLYISIY 257
Cdd:MTH00155 243 VDVVWLFLYISIY 255
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
18-259 |
6.71e-122 |
|
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: 347.20 E-value: 6.71e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 18 LTGAIGTMTFVTGLIKWFHNF-NMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLRWGMILFIVSEIFFFIS 96
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 97 FFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTKHSLLITILLGIYFTIL 176
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 177 QAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFVDVVWLFLYISI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2018119586 257 YWW 259
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-260 |
3.36e-121 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 345.93 E-value: 3.36e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 6 HPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNF--NMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLRWGM 83
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 84 ILFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTKHSL 163
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 164 LITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 2018119586 244 FVDVVWLFLYISIYWWG 260
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-259 |
2.03e-52 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 168.87 E-value: 2.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 71 HTLSVSKGLRWGMILFIVSEIFFFISFFWAFFHSSLSpnieiGAMWPPSnINPFNPFqIPLLNTIILITSGVTVTWAHHA 150
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPAG-AELLDLP-LPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 151 LMENNFSQTKHSLLITILLGIYFTILQAYEYYE---APFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHF 227
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 2018119586 228 SNKHHFGFEAAAWYWHFVDVVWLFLYISIYWW 259
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
131-260 |
1.14e-09 |
|
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: 56.40 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 131 LLNTIILITSGVTVTWAHHALMENNFSQTKHSLLITILLGIYFTILQAYE---YYEAPFTIADSIYGSTFFMATGFHGLH 207
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2018119586 208 VIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 260
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-257 |
7.22e-161 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 446.16 E-value: 7.22e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 5 NHPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLRWGMI 84
Cdd:MTH00155 3 NHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 85 LFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTKHSLL 164
Cdd:MTH00155 83 LFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 165 ITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHF 244
Cdd:MTH00155 163 FTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHF 242
|
250
....*....|...
gi 2018119586 245 VDVVWLFLYISIY 257
Cdd:MTH00155 243 VDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
1-260 |
5.08e-141 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 396.24 E-value: 5.08e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 1 MSTYNHPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLR 80
Cdd:MTH00118 1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 81 WGMILFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTK 160
Cdd:MTH00118 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 161 HSLLITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240
|
250 260
....*....|....*....|
gi 2018119586 241 YWHFVDVVWLFLYISIYWWG 260
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
6-260 |
3.30e-137 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 386.64 E-value: 3.30e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 6 HPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLRWGMIL 85
Cdd:MTH00189 5 HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 86 FIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTKHSLLI 165
Cdd:MTH00189 85 FITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 166 TILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFV 245
Cdd:MTH00189 165 TVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFV 244
|
250
....*....|....*
gi 2018119586 246 DVVWLFLYISIYWWG 260
Cdd:MTH00189 245 DVVWLFLYVSIYWWG 259
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
6-261 |
5.08e-134 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 378.46 E-value: 5.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 6 HPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLRWGMIL 85
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 86 FIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTKHSLLI 165
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 166 TILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFV 245
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 2018119586 246 DVVWLFLYISIYWWGN 261
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
1.56e-132 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 374.89 E-value: 1.56e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 1 MSTYNHPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLR 80
Cdd:MTH00219 2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 81 WGMILFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTK 160
Cdd:MTH00219 82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 161 HSLLITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAW 240
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241
|
250 260
....*....|....*....|.
gi 2018119586 241 YWHFVDVVWLFLYISIYWWGN 261
Cdd:MTH00219 242 YWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
3-260 |
1.90e-131 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 372.14 E-value: 1.90e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 3 TYNHPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLRWG 82
Cdd:MTH00039 2 THQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 83 MILFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTKHS 162
Cdd:MTH00039 82 MILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 163 LLITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYW 242
Cdd:MTH00039 162 LFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYW 241
|
250
....*....|....*...
gi 2018119586 243 HFVDVVWLFLYISIYWWG 260
Cdd:MTH00039 242 HFVDVVWLFLYVCIYWWG 259
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
1-260 |
4.76e-129 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 365.97 E-value: 4.76e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 1 MSTYNHPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLR 80
Cdd:MTH00099 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 81 WGMILFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTK 160
Cdd:MTH00099 81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 161 HSLLITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAW 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240
|
250 260
....*....|....*....|
gi 2018119586 241 YWHFVDVVWLFLYISIYWWG 260
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
4.79e-129 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 366.01 E-value: 4.79e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 1 MSTYNHPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLR 80
Cdd:MTH00130 1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 81 WGMILFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTK 160
Cdd:MTH00130 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 161 HSLLITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAW 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 2018119586 241 YWHFVDVVWLFLYISIYWWGN 261
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
1-260 |
2.44e-126 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 359.06 E-value: 2.44e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 1 MSTYNHPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLR 80
Cdd:MTH00075 1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 81 WGMILFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTK 160
Cdd:MTH00075 81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 161 HSLLITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAW 240
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240
|
250 260
....*....|....*....|
gi 2018119586 241 YWHFVDVVWLFLYISIYWWG 260
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWG 260
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
18-259 |
6.71e-122 |
|
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: 347.20 E-value: 6.71e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 18 LTGAIGTMTFVTGLIKWFHNF-NMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLRWGMILFIVSEIFFFIS 96
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 97 FFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTKHSLLITILLGIYFTIL 176
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 177 QAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFVDVVWLFLYISI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2018119586 257 YWW 259
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-260 |
3.36e-121 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 345.93 E-value: 3.36e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 6 HPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNF--NMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLRWGM 83
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 84 ILFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTKHSL 163
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 164 LITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 2018119586 244 FVDVVWLFLYISIYWWG 260
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
6-260 |
8.65e-118 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 337.58 E-value: 8.65e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 6 HPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLRWGMIL 85
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 86 FIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTKHSLLI 165
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 166 TILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFV 245
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*
gi 2018119586 246 DVVWLFLYISIYWWG 260
Cdd:MTH00009 244 DVVWIFLYLCIYWWG 258
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
1-260 |
4.70e-117 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 335.57 E-value: 4.70e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 1 MSTYNHPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLR 80
Cdd:MTH00024 1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 81 WGMILFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTK 160
Cdd:MTH00024 81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 161 HSLLITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAW 240
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240
|
250 260
....*....|....*....|
gi 2018119586 241 YWHFVDVVWLFLYISIYWWG 260
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
7.98e-109 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 314.81 E-value: 7.98e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 1 MSTYNHPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLR 80
Cdd:MTH00052 2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 81 WGMILFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQTK 160
Cdd:MTH00052 82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 161 HSLLITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAW 240
Cdd:MTH00052 162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241
|
250 260
....*....|....*....|.
gi 2018119586 241 YWHFVDVVWLFLYISIYWWGN 261
Cdd:MTH00052 242 YWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
5.28e-98 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 288.89 E-value: 5.28e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 1 MSTYNHPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKGLR 80
Cdd:MTH00028 1 MSLVYHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 81 WGMILFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALM-----ENN 155
Cdd:MTH00028 81 LGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIgtgnpASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 156 FSQTKHS-------------------------------LLITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFH 204
Cdd:MTH00028 161 EKGTQGIegpnpsngappdpqkgptfllsdfrtnavigLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTH 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2018119586 205 GLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFVDVVWLFLYISIYWWGN 261
Cdd:MTH00028 241 GLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
1-260 |
5.96e-88 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 261.91 E-value: 5.96e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 1 MSTYNHPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFN--MNLMILGYIIIILTMYQWWRDICREGTFQGKHTLSVSKG 78
Cdd:PLN02194 2 IESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 79 LRWGMILFIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNFSQ 158
Cdd:PLN02194 82 PRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 159 TKHSLLITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAA 238
Cdd:PLN02194 162 AVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAA 241
|
250 260
....*....|....*....|..
gi 2018119586 239 AWYWHFVDVVWLFLYISIYWWG 260
Cdd:PLN02194 242 AWYWHFVDVVWLFLFVSIYWWG 263
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
71-259 |
6.62e-67 |
|
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: 205.52 E-value: 6.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 71 HTLSVSKGLRWGMILFIVSEIFFFISFFWAFFHSSLSPNIEIGAmwppsninPFNPFQIPLLNTIILITSGVTVTWAHHA 150
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 151 LM--ENNFSQTKHSLLITILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFS 228
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 2018119586 229 NKHHFGFEAAAWYWHFVDVVWLFLYISIYWW 259
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
6-260 |
2.36e-66 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 206.73 E-value: 2.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 6 HPYHLVDYSPWPLTGAIGTMTFVTGLIKWFHNFNMNLMILGYIIIILTMYQWWRDICREGtFQGKHTLSVSKGLRWGMIL 85
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 86 FIVSEIFFFISFFWAFFHSSLSPNIEIGAMWPPSNINPFNPFQIPLLNTIILITSGVTVTWAHHALMENNfSQTKHSLLI 165
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 166 TILLGIYFTILQAYEYYEAPFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFV 245
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*
gi 2018119586 246 DVVWLFLYISIYWWG 260
Cdd:MTH00083 241 DVVWLFLFVFVYWWS 255
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-259 |
2.03e-52 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 168.87 E-value: 2.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 71 HTLSVSKGLRWGMILFIVSEIFFFISFFWAFFHSSLSpnieiGAMWPPSnINPFNPFqIPLLNTIILITSGVTVTWAHHA 150
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPAG-AELLDLP-LPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 151 LMENNFSQTKHSLLITILLGIYFTILQAYEYYE---APFTIADSIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHF 227
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 2018119586 228 SNKHHFGFEAAAWYWHFVDVVWLFLYISIYWW 259
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
131-257 |
3.50e-24 |
|
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: 95.76 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 131 LLNTIILITSGVTVTWAHHALMENNFSQTKHSLLITILLGIYFTILQAYEYYEApFTIADSIYGSTFFMA----TGFHGL 206
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHK-IAAGIDPDAGLFFTLyfllTGFHLL 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2018119586 207 HVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFVDVVWLFLYISIY 257
Cdd:cd02862 134 HVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
130-259 |
3.19e-19 |
|
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: 82.42 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 130 PLLNTIILITSGVTVTWAHHALMENNFSQTKHSLLITILLGIYFTILQAYEYYEAPF---TIADSIYGSTFFMATGFHGL 206
Cdd:cd02865 52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2018119586 207 HVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFVDVVWLFLYISIYWW 259
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
123-259 |
1.14e-17 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239215 Cd Length: 202 Bit Score: 78.70 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 123 PFNPFQIPL----LNTIILITSGVTVTWAHHALMENNFSQTKHSLLITILLGIYFTILQAYEY-----------YEAPFT 187
Cdd:cd02864 52 RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWG 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018119586 188 IAdsIYGSTFFMATGFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 259
Cdd:cd02864 132 AA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
119-257 |
2.21e-17 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 78.03 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 119 SNINPFNPFQIPLLNTIILITSGVTVTWAHHALmennfsQTKHS---LLITILLGIYFTILQAYEYYEAPFTIADSIYGS 195
Cdd:MTH00049 82 SYISLSSSLEIPFVGCFLLLGSSITVTAYHHLL------GWKYCdlfLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYA 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018119586 196 TFFMATGFHGLHVIIGTIFLFTCFIrhlFNHFSNKHHFGfEAAAWYWHFVDVVWLFLYISIY 257
Cdd:MTH00049 156 SCFCTVGLHFSHVVLGVVGLSTLLL---VGSSSFGVYRS-TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
127-257 |
1.23e-16 |
|
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: 75.35 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 127 FQIPL--LNTIILITSGVTVTWAHHALMENNFSQTKHSLLITILLGIYFTILQAYE---YYEAPFTIADSIYGSTFFMAT 201
Cdd:cd02863 48 FELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLV 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2018119586 202 GFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFVDVVWLFLYISIY 257
Cdd:cd02863 128 GTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
131-260 |
1.14e-09 |
|
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: 56.40 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 131 LLNTIILITSGVTVTWAHHALMENNFSQTKHSLLITILLGIYFTILQAYE---YYEAPFTIADSIYGSTFFMATGFHGLH 207
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2018119586 208 VIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 260
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
127-260 |
8.50e-09 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 54.02 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018119586 127 FQIP--LLNTIILITSGVTVTWAHHALMENNFSQTKHSLLITILLGIYFTILQAYEYY---EAPFTIADSIYGSTFFMAT 201
Cdd:PRK10663 64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALV 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2018119586 202 GFHGLHVIIGTIFLFTCFIRHLFNHFSNKHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 260
Cdd:PRK10663 144 GTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
|
|
| |
