|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
4.36e-153 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 426.52 E-value: 4.36e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 5 NSNHPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 85 MILFITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 165 LFFTVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 1707765531 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
6.85e-121 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 345.16 E-value: 6.85e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 8 HPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTF--NMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 86 ILFITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQGL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 166 FFTVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1707765531 246 FVDVVWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
1.96e-115 |
|
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: 331.02 E-value: 1.96e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 20 LTGAIGVLTLTSGLTKWFHTF-NMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGMILFITSEVLFFIS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 99 FFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQGLFFTVILGMYFTIL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 179 QAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1707765531 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
1.41e-48 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 158.86 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 72 LHTEFVSIGLRWGMILFITSEVLFFISFFWAFFsssiipTIELGMMWPPNGIQPFNPIqIPLLNTAILLASGITVTWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 152 SMMESNHSQTMQGLFFTVILGMYFTILQAYEY---WEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQ 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1707765531 229 FSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
133-262 |
1.07e-10 |
|
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: 59.48 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 133 LLNTAILLASGITVTWAHHSMMESNHSQTMQGLFFTVILGMYFTILQAYE---YWEAPFTIADAIYGSSFFMATGFHGLH 209
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1707765531 210 VIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
4.36e-153 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 426.52 E-value: 4.36e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 5 NSNHPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 85 MILFITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 165 LFFTVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 1707765531 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
4-263 |
2.41e-139 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 392.01 E-value: 2.41e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 4 ANSNHPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRW 83
Cdd:MTH00118 2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 84 GMILFITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQ 163
Cdd:MTH00118 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 164 GLFFTVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWY 243
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 1707765531 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
4.48e-132 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 373.54 E-value: 4.48e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 8 HPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGMIL 87
Cdd:MTH00189 5 HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 88 FITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQGLFF 167
Cdd:MTH00189 85 FITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 168 TVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00189 165 TVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 1707765531 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00189 245 DVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
9.15e-129 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 365.37 E-value: 9.15e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 8 HPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGMIL 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 88 FITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQGLFF 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 168 TVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1707765531 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
8-263 |
1.45e-127 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 362.12 E-value: 1.45e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 8 HPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGMIL 87
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 88 FITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQGLFF 167
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 168 TVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 1707765531 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
6.57e-126 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 358.33 E-value: 6.57e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 8 HPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGMIL 87
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 88 FITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQGLFF 167
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 168 TVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 1707765531 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00219 247 DVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
4-263 |
4.64e-125 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 355.98 E-value: 4.64e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 4 ANSNHPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRW 83
Cdd:MTH00075 2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 84 GMILFITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQ 163
Cdd:MTH00075 82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 164 GLFFTVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWY 243
Cdd:MTH00075 162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 1707765531 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00075 242 WHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
8-263 |
1.51e-124 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 354.80 E-value: 1.51e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 8 HPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGMIL 87
Cdd:MTH00099 6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 88 FITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQGLFF 167
Cdd:MTH00099 86 FIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 168 TVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00099 166 TILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 1707765531 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00099 246 DVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
4-263 |
7.06e-124 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 352.91 E-value: 7.06e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 4 ANSNHPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRW 83
Cdd:MTH00130 2 AHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 84 GMILFITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQ 163
Cdd:MTH00130 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 164 GLFFTVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWY 243
Cdd:MTH00130 162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 1707765531 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00130 242 WHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
6.85e-121 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 345.16 E-value: 6.85e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 8 HPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTF--NMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 86 ILFITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQGL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 166 FFTVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1707765531 246 FVDVVWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-263 |
1.52e-116 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 334.50 E-value: 1.52e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 8 HPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGMIL 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 88 FITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQGLFF 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 168 TVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1707765531 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
1.96e-115 |
|
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: 331.02 E-value: 1.96e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 20 LTGAIGVLTLTSGLTKWFHTF-NMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGMILFITSEVLFFIS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 99 FFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQGLFFTVILGMYFTIL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 179 QAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1707765531 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
8-263 |
3.01e-108 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 313.23 E-value: 3.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 8 HPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGMIL 87
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 88 FITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQGLFF 167
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 168 TVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*.
gi 1707765531 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00024 246 DVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
8.06e-103 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 299.79 E-value: 8.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 8 HPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGMIL 87
Cdd:MTH00052 7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 88 FITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMQGLFF 167
Cdd:MTH00052 87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 168 TVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00052 167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 1707765531 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00052 247 DVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
8.63e-89 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 265.39 E-value: 8.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 8 HPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSIGLRWGMIL 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 88 FITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMM------------- 154
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIgtgnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 155 ------ESNHSQTMQ-----------------GLFFTVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVI 211
Cdd:MTH00028 166 giegpnPSNGAPPDPqkgptfllsdfrtnaviGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1707765531 212 IGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
2-262 |
7.07e-81 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 244.19 E-value: 7.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 2 LTANSNHPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFN--MNLFSIGILITMLTMIQWWRDVIREGTYQGLHTEFVSI 79
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 80 GLRWGMILFITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHS 159
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 160 QTMQGLFFTVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEA 239
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|...
gi 1707765531 240 AAWYWHFVDVVWLFLYISIYWWG 262
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
3.48e-63 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 198.64 E-value: 3.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 8 HPFHLVDYSPWPLTGAIGVLTLTSGLTKWFHTFNMNLFSIGILITMLTMIQWWRDVIREGtYQGLHTEFVSIGLRWGMIL 87
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 88 FITSEVLFFISFFWAFFSSSIIPTIELGMMWPPNGIQPFNPIQIPLLNTAILLASGITVTWAHHSMMESNHSQTMqGLFF 167
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 168 TVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 1707765531 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00083 241 DVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
73-261 |
1.17e-59 |
|
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: 187.03 E-value: 1.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 73 HTEFVSIGLRWGMILFITSEVLFFISFFWAFFSSSIIPTIELGMmwppngiqPFNPIQIPLLNTAILLASGITVTWAHHS 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 153 MM--ESNHSQTMQGLFFTVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 1707765531 231 PNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
1.41e-48 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 158.86 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 72 LHTEFVSIGLRWGMILFITSEVLFFISFFWAFFsssiipTIELGMMWPPNGIQPFNPIqIPLLNTAILLASGITVTWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 152 SMMESNHSQTMQGLFFTVILGMYFTILQAYEY---WEAPFTIADAIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQ 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1707765531 229 FSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
133-259 |
7.36e-21 |
|
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: 86.91 E-value: 7.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 133 LLNTAILLASGITVTWAHHSMMESNHSQTMQGLFFTVILGMYFTILQAYEY-WEapFTIADAIYGSSFFMA----TGFHG 207
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYaHK--IAAGIDPDAGLFFTLyfllTGFHL 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1707765531 208 LHVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862 133 LHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
133-259 |
5.02e-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: 76.51 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 133 LLNTAILLASGITVTWAHHSMMESNHSQTMQGLFFTVILGMYFTILQAYE---YWEAPFTIADAIYGSSFFMATGFHGLH 209
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1707765531 210 VIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
132-261 |
1.91e-16 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239216 Cd Length: 184 Bit Score: 75.10 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 132 PLLNTAILLASGITVTWAHHSMMESNHSQTMQGLFFTVILGMYFTILQAYEYWEAPF---TIADAIYGSSFFMATGFHGL 208
Cdd:cd02865 52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1707765531 209 HVIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
128-259 |
6.43e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 74.18 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 128 PIQIPLLNTAILLASGITVTwAHHSMMESNHSQTMqgLFFTVILGMYFTILQAYEYWEAPFTIADAIYGSSFFMATGFHG 207
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1707765531 208 LHVIIGTIFLLTCLtrhLLKQFSPNHHFGfEAAAWYWHFVDVVWLFLYISIY 259
Cdd:MTH00049 166 SHVVLGVVGLSTLL---LVGSSSFGVYRS-TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
125-261 |
2.02e-15 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239215 Cd Length: 202 Bit Score: 72.53 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 125 PFNPIQIPL----LNTAILLASGITVTWAHHSMMESNHSQTMQGLFFTVILGMYFTILQAYEY-----------WEAPFT 189
Cdd:cd02864 52 RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWG 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1707765531 190 IAdaIYGSSFFMATGFHGLHVIIGTIFLLTCLTRHLLKQFSPNHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864 132 AA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
133-262 |
1.07e-10 |
|
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: 59.48 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 133 LLNTAILLASGITVTWAHHSMMESNHSQTMQGLFFTVILGMYFTILQAYE---YWEAPFTIADAIYGSSFFMATGFHGLH 209
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1707765531 210 VIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
133-263 |
4.00e-09 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 55.17 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765531 133 LLNTAILLASGITVTWAHHSMMESNHSQTMQGLFFTVILGMYFTILQAYEYW---EAPFTIADAIYGSSFFMATGFHGLH 209
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1707765531 210 VIIGTIFLLTCLTRHLLKQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
