|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
1.82e-159 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 442.70 E-value: 1.82e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 85 MILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 1128272596 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
2.05e-126 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 359.42 E-value: 2.05e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLF--NINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 86 ILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQGL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 166 FFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1128272596 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 |
6.60e-120 |
|
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: 342.19 E-value: 6.60e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 20 LTGAIGAMVLVSGLAKWFHLF-NINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWGMILFIASEVLFFMS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 99 IFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQGLFFTVLLGIYFTML 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 179 QAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1128272596 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
5.05e-47 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 155.01 E-value: 5.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 72 LHTGFVSIGLRWGMILFIASEVLFFMSIFWAFFSSMLAptielgMLWPPMGIQPVNPmQIPLLNKAILLASGVTVNWTHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 152 SLMESNHIQALQGLFFTVLLGIYFTMLQAYEY---WEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQ 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1128272596 229 FSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
84-262 |
9.27e-08 |
|
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: 51.01 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 84 GMILFIASEVLFFMSIFWAFFSSMLAPTIElgmlwppmGIQPVNPMQIPLL--NKAILLASGVTVNWTHHSLMESNHIQA 161
Cdd:TIGR02897 13 GFWIFLGAEIALFATLFATYLVLQHGGDYA--------GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 162 LQGLFFTVLLGIYFTMLQAYE---YWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFE 238
Cdd:TIGR02897 85 MFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVF 164
|
170 180
....*....|....*....|....
gi 1128272596 239 AAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 165 IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
1.82e-159 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 442.70 E-value: 1.82e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 85 MILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 1128272596 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
5-263 |
2.18e-145 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 407.41 E-value: 2.18e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00118 3 HQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 85 MILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQG 164
Cdd:MTH00118 83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00118 163 LTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 1128272596 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00118 243 HFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
4-263 |
9.95e-140 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 393.18 E-value: 9.95e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 4 MHSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRW 83
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 84 GMILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQ 163
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 164 GLFFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWY 243
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 1128272596 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
4-263 |
1.66e-136 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 384.85 E-value: 1.66e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 4 MHSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRW 83
Cdd:MTH00039 1 MTHQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 84 GMILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQ 163
Cdd:MTH00039 81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 164 GLFFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWY 243
Cdd:MTH00039 161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 1128272596 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00039 241 WHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.29e-133 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 377.69 E-value: 1.29e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 88 FIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQGLFF 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 168 TVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1128272596 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
5-263 |
1.08e-132 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 375.26 E-value: 1.08e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00130 3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 85 MILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQG 164
Cdd:MTH00130 83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00130 163 LTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 1128272596 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00130 243 HFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
5-263 |
4.40e-132 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 373.70 E-value: 4.40e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00075 3 HQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 85 MILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQG 164
Cdd:MTH00075 83 MILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00075 163 LALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 1128272596 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00075 243 HFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
5-263 |
6.37e-131 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 370.98 E-value: 6.37e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 5 HSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWG 84
Cdd:MTH00099 3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 85 MILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQG 164
Cdd:MTH00099 83 MILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 165 LFFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYW 244
Cdd:MTH00099 163 LFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 1128272596 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00099 243 HFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
5.78e-130 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 368.35 E-value: 5.78e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 88 FIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQGLFF 167
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 168 TVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 1128272596 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00219 247 DVVWLFLYVSIYWWGS 262
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
2.05e-126 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 359.42 E-value: 2.05e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLF--NINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 86 ILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQGL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 166 FFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1128272596 246 FVDVVWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-263 |
1.85e-123 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 351.83 E-value: 1.85e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 88 FIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQGLFF 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 168 TVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1128272596 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 |
6.60e-120 |
|
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: 342.19 E-value: 6.60e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 20 LTGAIGAMVLVSGLAKWFHLF-NINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWGMILFIASEVLFFMS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 99 IFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQGLFFTVLLGIYFTML 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 179 QAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1128272596 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
8-263 |
6.97e-113 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 325.17 E-value: 6.97e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 88 FIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQGLFF 167
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 168 TVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*.
gi 1128272596 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00024 246 DVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
2-263 |
1.38e-110 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 319.43 E-value: 1.38e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 2 LTMHSNHPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGL 81
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 82 RWGMILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQA 161
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 162 LQGLFFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAA 241
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 1128272596 242 WYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
4.04e-94 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 278.87 E-value: 4.04e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 88 FIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNH--------- 158
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 159 ---------------------------IQALQGLFFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVI 211
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1128272596 212 IGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
8-262 |
7.03e-82 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 246.50 E-value: 7.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFN--INLFMIGMGITLLTMIQWWRDVVREGTYQGLHTGFVSIGLRWGM 85
Cdd:PLN02194 7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 86 ILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHIQALQGL 165
Cdd:PLN02194 87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 166 FFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWH 245
Cdd:PLN02194 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246
|
250
....*....|....*..
gi 1128272596 246 FVDVVWLFLYISIYWWG 262
Cdd:PLN02194 247 FVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.89e-66 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 207.12 E-value: 1.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 8 HPFHLVDYSPWPLTGAIGAMVLVSGLAKWFHLFNINLFMIGMGITLLTMIQWWRDVVREGtYQGLHTGFVSIGLRWGMIL 87
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 88 FIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHiQALQGLFF 167
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNK-SCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 168 TVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFV 247
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 1128272596 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 |
6.09e-63 |
|
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: 195.50 E-value: 6.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 73 HTGFVSIGLRWGMILFIASEVLFFMSIFWAFFSSMLAPTIELGMlwppmgiqPVNPMQIPLLNKAILLASGVTVNWTHHS 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 153 LM--ESNHIQALQGLFFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 1128272596 231 PNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
5.05e-47 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 155.01 E-value: 5.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 72 LHTGFVSIGLRWGMILFIASEVLFFMSIFWAFFSSMLAptielgMLWPPMGIQPVNPmQIPLLNKAILLASGVTVNWTHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 152 SLMESNHIQALQGLFFTVLLGIYFTMLQAYEY---WEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQ 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1128272596 229 FSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
84-259 |
7.29e-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: 7.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 84 GMILFIASEVLFFMSIFwAFFSSMLAPTIEL-----GMLWPPMGiqpvnpmqipLLNKAILLASGVTVNWTHHSLMESNH 158
Cdd:cd02862 12 GMWVFILSELLAFGALF-IAYAVYRALYPELfaagsAHLDLLLG----------ALNTLVLLTSSFTVALAVRAARAGRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 159 IQALQGLFFTVLLGIYFTMLQAYEYWE---APFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHF 235
Cdd:cd02862 81 RRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLHVLIGLGILLWVAWRARRGRYSARDYE 160
|
170 180
....*....|....*....|....
gi 1128272596 236 GFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862 161 GVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
80-261 |
2.10e-15 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239216 Cd Length: 184 Bit Score: 72.02 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 80 GLRWGMILFIASEVLFFMSIFWAFFSSMLAPTIelgmlWPPmgiQPVNPMQIPLLNKAILLASGVTVNWTHHSLMESNHI 159
Cdd:cd02865 8 PGWWGLWVFMAVEGTLFALLISAYFMRMTSGDW-----QPG---APLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 160 QALQGLFFTVLLGIYFTMLQAYEYWEAPF---TIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFG 236
Cdd:cd02865 80 LARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLP 159
|
170 180
....*....|....*....|....*
gi 1128272596 237 FEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865 160 VELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
84-261 |
4.86e-13 |
|
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: 65.99 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 84 GMILFIASEVLFFMSIFWAFFSSMLAPTIELGMLWPPMGIqPVNPMQIPLLNKAI----LLASGVTVNWTHHSLMESNHI 159
Cdd:cd02864 12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLVLIAImtfiLITSSGTMAMAVNFGYRGNRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 160 QALQGLFFTVLLGIYFTMLQAYEY-----------WEAPFTIAdaIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQ 228
Cdd:cd02864 91 AAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168
|
170 180 190
....*....|....*....|....*....|....
gi 1128272596 229 FSPNHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864 169 YQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
87-259 |
3.16e-12 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 64.17 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 87 LFIASEVLFFMSIFWAFFSSMLAPTIELGmlwppmgiqpvNPMQIPLLNKAILLASGVTVNWTHHSL-MESNHIQalqgL 165
Cdd:MTH00049 59 LFILSEVIIFGSLLVCCLWFDDWSYISLS-----------SSLEIPFVGCFLLLGSSITVTAYHHLLgWKYCDLF----L 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 166 FFTVLLGIYFTMLQAYEYWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNqfspnhhFGF---EAAAW 242
Cdd:MTH00049 124 YLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLSTLLLVGSSS-------FGVyrsTVLTW 196
|
170
....*....|....*..
gi 1128272596 243 YWHFVDVVWLFLYISIY 259
Cdd:MTH00049 197 YWHFVDYIWLLVYLIVY 213
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
133-259 |
1.29e-11 |
|
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: 61.87 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 133 LLNKAILLASGVTVNWTHHSLMESNHIQALQGLFFTVLLGIYFTMLQAYE---YWEAPFTIADAIYGSTFFVATGFHSLH 209
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1128272596 210 VIIGSMFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
84-262 |
9.27e-08 |
|
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: 51.01 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 84 GMILFIASEVLFFMSIFWAFFSSMLAPTIElgmlwppmGIQPVNPMQIPLL--NKAILLASGVTVNWTHHSLMESNHIQA 161
Cdd:TIGR02897 13 GFWIFLGAEIALFATLFATYLVLQHGGDYA--------GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 162 LQGLFFTVLLGIYFTMLQAYE---YWEAPFTIADAIYGSTFFVATGFHSLHVIIGSMFLLTCLMRHSMNQFSPNHHFGFE 238
Cdd:TIGR02897 85 MFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVF 164
|
170 180
....*....|....*....|....
gi 1128272596 239 AAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 165 IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
138-263 |
1.67e-04 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 41.69 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128272596 138 ILLASGVTVNWTHHSLMESNHIQALQGLFFTVLLGIYFTMLQAYEYW---EAPFTIADAIYGSTFFVATGFHSLHVIIGS 214
Cdd:PRK10663 75 LLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLHVTSGL 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1128272596 215 MFLLTCLMRHSMNQFSPNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:PRK10663 155 IWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
