|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
2.14e-153 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 427.29 E-value: 2.14e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 5 NSNQPFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 85 MILFITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMS 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 165 LIMTIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2458278088 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
9-263 |
1.86e-121 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 346.71 E-value: 1.86e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 9 PFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYE--MDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMI 86
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSgnMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 87 LFITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLI 166
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 167 MTIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHF 246
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*..
gi 2458278088 247 VDVVWLFLYISIYWWGS 263
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
1.98e-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: 343.34 E-value: 1.98e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 20 LTSALGTMIMAAGLTKWFNMYEMDLI-ILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMILFITSEVLFFMS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLlFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 99 FFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIMTIMLGIYFTIL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 179 QAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2458278088 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
4.12e-56 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 178.12 E-value: 4.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 72 LHTNNVVKGMKMGMILFITSEVLFFMSFFWAYFNSSLAPNveigmmWPPEGIKSFNPmNIPLLNTVVLLTSGISVTWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 152 SMMESNYSQGNMSLIMTIMLGIYFTILQAYEY---WESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2458278088 229 FSSKHHMGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
82-262 |
5.25e-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: 57.56 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 82 KMGMILFITSEVLFFMSFFWAYFnsSLAPNVEIGMMWPPEGIKsfnpMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQG 161
Cdd:TIGR02897 11 ILGFWIFLGAEIALFATLFATYL--VLQHGGDYAGKMPAELFE----LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 162 NMSLIMTIMLGIYFTILQAYE---YWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFE 238
Cdd:TIGR02897 85 MFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVF 164
|
170 180
....*....|....*....|....
gi 2458278088 239 AAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 165 IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
2.14e-153 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 427.29 E-value: 2.14e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 5 NSNQPFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 85 MILFITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMS 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 165 LIMTIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2458278088 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
9-263 |
1.72e-140 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 395.09 E-value: 1.72e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 9 PFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMILF 88
Cdd:MTH00118 7 PYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 89 ITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIMT 168
Cdd:MTH00118 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 169 IMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFVD 248
Cdd:MTH00118 167 ILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVD 246
|
250
....*....|....*
gi 2458278088 249 VVWLFLYISIYWWGS 263
Cdd:MTH00118 247 VVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
9-263 |
7.70e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 388.18 E-value: 7.70e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 9 PFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMILF 88
Cdd:MTH00189 6 PFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 89 ITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIMT 168
Cdd:MTH00189 86 ITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 169 IMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFVD 248
Cdd:MTH00189 166 VILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVD 245
|
250
....*....|....*
gi 2458278088 249 VVWLFLYISIYWWGS 263
Cdd:MTH00189 246 VVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.07e-136 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 385.40 E-value: 1.07e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 8 QPFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMIL 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 88 FITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIM 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 168 TIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 2458278088 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
4-263 |
1.12e-130 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 370.21 E-value: 1.12e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 4 LNSNQPFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKM 83
Cdd:MTH00039 1 MTHQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 84 GMILFITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNM 163
Cdd:MTH00039 81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 164 SLIMTIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWY 243
Cdd:MTH00039 161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 2458278088 244 WHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00039 241 WHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
4.63e-129 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 366.03 E-value: 4.63e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 8 QPFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMIL 87
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 88 FITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIM 167
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 168 TIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFV 247
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 2458278088 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00219 247 DVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
9-263 |
3.69e-128 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 363.66 E-value: 3.69e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 9 PFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMILF 88
Cdd:MTH00099 7 AYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 89 ITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIMT 168
Cdd:MTH00099 87 IISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 169 IMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFVD 248
Cdd:MTH00099 167 ILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVD 246
|
250
....*....|....*
gi 2458278088 249 VVWLFLYISIYWWGS 263
Cdd:MTH00099 247 VVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
9-263 |
9.09e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 360.23 E-value: 9.09e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 9 PFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMILF 88
Cdd:MTH00130 7 AYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 89 ITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIMT 168
Cdd:MTH00130 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 169 IMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFVD 248
Cdd:MTH00130 167 ILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVD 246
|
250
....*....|....*
gi 2458278088 249 VVWLFLYISIYWWGS 263
Cdd:MTH00130 247 VVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
10-263 |
9.44e-125 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 355.21 E-value: 9.44e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 10 FHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMILFI 89
Cdd:MTH00075 8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 90 TSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIMTI 169
Cdd:MTH00075 88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 170 MLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFVDV 249
Cdd:MTH00075 168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247
|
250
....*....|....
gi 2458278088 250 VWLFLYISIYWWGS 263
Cdd:MTH00075 248 VWLFLYVSIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
9-263 |
1.86e-121 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 346.71 E-value: 1.86e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 9 PFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYE--MDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMI 86
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSgnMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 87 LFITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLI 166
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 167 MTIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHF 246
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*..
gi 2458278088 247 VDVVWLFLYISIYWWGS 263
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
1.98e-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: 343.34 E-value: 1.98e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 20 LTSALGTMIMAAGLTKWFNMYEMDLI-ILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMILFITSEVLFFMS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLlFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 99 FFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIMTIMLGIYFTIL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 179 QAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2458278088 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-263 |
7.34e-118 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 337.58 E-value: 7.34e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 8 QPFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMIL 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 88 FITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIM 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 168 TIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 2458278088 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
9-263 |
1.60e-114 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 329.41 E-value: 1.60e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 9 PFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMILF 88
Cdd:MTH00024 7 PYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 89 ITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIMT 168
Cdd:MTH00024 87 ILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 169 IMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFVD 248
Cdd:MTH00024 167 VFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVD 246
|
250
....*....|....*
gi 2458278088 249 VVWLFLYISIYWWGS 263
Cdd:MTH00024 247 VVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
3.74e-107 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 310.57 E-value: 3.74e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 8 QPFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMIL 87
Cdd:MTH00052 7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 88 FITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIM 167
Cdd:MTH00052 87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 168 TIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFV 247
Cdd:MTH00052 167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 2458278088 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00052 247 DVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.50e-98 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 290.04 E-value: 1.50e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 8 QPFHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMIL 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 88 FITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMES----------- 156
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTgnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 157 -----NYSQGN--------------------MSLIMTIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVI 211
Cdd:MTH00028 166 giegpNPSNGAppdpqkgptfllsdfrtnavIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2458278088 212 IGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
10-262 |
3.79e-87 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 259.98 E-value: 3.79e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 10 FHLVDFSPWPLTSALGTMIMAAGLTKWFNMYE--MDLIILGLTINLMTMFQWWRDVTRESTFQGLHTNNVVKGMKMGMIL 87
Cdd:PLN02194 9 YHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 88 FITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIM 167
Cdd:PLN02194 89 FIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 168 TIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFV 247
Cdd:PLN02194 169 TVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFV 248
|
250
....*....|....*
gi 2458278088 248 DVVWLFLYISIYWWG 262
Cdd:PLN02194 249 DVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
10-263 |
5.89e-71 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 218.29 E-value: 5.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 10 FHLVDFSPWPLTSALGTMIMAAGLTKWFNMYEMDLIILGLTINLMTMFQWWRDVTREStFQGLHTNNVVKGMKMGMILFI 89
Cdd:MTH00083 5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 90 TSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNPMNIPLLNTVVLLTSGISVTWAHHSMMESNySQGNMSLIMTI 169
Cdd:MTH00083 84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 170 MLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFVDV 249
Cdd:MTH00083 163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242
|
250
....*....|....
gi 2458278088 250 VWLFLYISIYWWGS 263
Cdd:MTH00083 243 VWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
73-261 |
2.56e-68 |
|
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: 208.98 E-value: 2.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 73 HTNNVVKGMKMGMILFITSEVLFFMSFFWAYFNSSLAPNVEIGMmwppegikSFNPMNIPLLNTVVLLTSGISVTWAHHS 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 153 MM--ESNYSQGNMSLIMTIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 2458278088 231 SKHHMGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
4.12e-56 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 178.12 E-value: 4.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 72 LHTNNVVKGMKMGMILFITSEVLFFMSFFWAYFNSSLAPNveigmmWPPEGIKSFNPmNIPLLNTVVLLTSGISVTWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 152 SMMESNYSQGNMSLIMTIMLGIYFTILQAYEY---WESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2458278088 229 FSSKHHMGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
82-259 |
3.36e-27 |
|
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: 103.47 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 82 KMGMILFITSEVLFFMSFFWAYFnsslapnveIGMMWPPE----GIKSFNPmNIPLLNTVVLLTSGISVTWAHHSMMESN 157
Cdd:cd02862 10 KLGMWVFILSELLAFGALFIAYA---------VYRALYPElfaaGSAHLDL-LLGALNTLVLLTSSFTVALAVRAARAGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 158 YSQGNMSLIMTIMLGIYFTILQAYEYwESQFTLADSIYGSTFFMA----TGFHGIHVIIGTSFLLICMIRHLINHFSSKH 233
Cdd:cd02862 80 RRRARRWLAAAVLLGLVFLVIKYFEY-AHKIAAGIDPDAGLFFTLyfllTGFHLLHVLIGLGILLWVAWRARRGRYSARD 158
|
170 180
....*....|....*....|....*.
gi 2458278088 234 HMGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862 159 YEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
75-259 |
5.72e-18 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 79.96 E-value: 5.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 75 NNVVKGMKMGMILFITSEVLFFMSFFWAYFnsslapnveIGMMWPPEGIKSfnPMNIPLLNTVVLLTSGISVTWAHHSMm 154
Cdd:MTH00049 47 VQVKHHYESAFWLFILSEVIIFGSLLVCCL---------WFDDWSYISLSS--SLEIPFVGCFLLLGSSITVTAYHHLL- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 155 esNYSQGNMSLIMTIMLGIYFTILQAYEYWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHH 234
Cdd:MTH00049 115 --GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLSTLLLVGSSSFGVYRST 192
|
170 180
....*....|....*....|....*
gi 2458278088 235 MgfeaAAWYWHFVDVVWLFLYISIY 259
Cdd:MTH00049 193 V----LTWYWHFVDYIWLLVYLIVY 213
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
73-259 |
3.16e-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: 77.28 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 73 HTNNVVKGMKMGMILFITSEVLFFMSFFWAYFnsSLAPNVEIGmmwpPEGIKSFNpMNIPLLNTVVLLTSGISVTWAHHS 152
Cdd:cd02863 1 HHTNTGSKKILGFWIYLMSDCILFATLFATYA--VLSGNTAGG----PPGHELFE-LPLVFIETFLLLLSSFTCGLAMIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 153 MMESNYSQGNMSLIMTIMLGIYFTILQAYE---YWESQFTLADSIYGSTFFMATGFHGIHVIIGTsFLLICMIRHLINH- 228
Cdd:cd02863 74 MNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGL-IWILVMIIQLKKRg 152
|
170 180 190
....*....|....*....|....*....|.
gi 2458278088 229 FSSKHHMGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863 153 LTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
80-261 |
1.06e-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: 75.87 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 80 GMKMGMILFITSEVLFFMSFFWAYFNSSLAPNVeigmmWPPEGIKSfnpMNIPLLNTVVLLTSGISVTWAHHSMMESNYS 159
Cdd:cd02865 8 PGWWGLWVFMAVEGTLFALLISAYFMRMTSGDW-----QPGAPLPL---PNLLSLNTAVLAASSVAMQWARRAARRNRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 160 QGNMSLIMTIMLGIYFTILQAYEY---WESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMG 236
Cdd:cd02865 80 LARLGLALAGALALAFLAGQLLAWhalNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLP 159
|
170 180
....*....|....*....|....*
gi 2458278088 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 ... |
82-261 |
1.26e-16 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239215 Cd Length: 202 Bit Score: 76.00 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 82 KMGMILFITSEVLFFMSFFWAYFNSSLAPNVEIGMMWPPEGIKSFNpMNIPL----LNTVVLLTSGISVTWAHHSMMESN 157
Cdd:cd02864 10 KAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFALRIGH-FNIPLvliaIMTFILITSSGTMAMAVNFGYRGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 158 YSQGNMSLIMTIMLGIYFTILQAYEYWE---------SQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINH 228
Cdd:cd02864 89 RKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168
|
170 180 190
....*....|....*....|....*....|....
gi 2458278088 229 FSSK-HHMGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864 169 YQRIgRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
82-262 |
5.25e-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: 57.56 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 82 KMGMILFITSEVLFFMSFFWAYFnsSLAPNVEIGMMWPPEGIKsfnpMNIPLLNTVVLLTSGISVTWAHHSMMESNYSQG 161
Cdd:TIGR02897 11 ILGFWIFLGAEIALFATLFATYL--VLQHGGDYAGKMPAELFE----LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 162 NMSLIMTIMLGIYFTILQAYE---YWESQFTLADSIYGSTFFMATGFHGIHVIIGTSFLLICMIRHLINHFSSKHHMGFE 238
Cdd:TIGR02897 85 MFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVF 164
|
170 180
....*....|....*....|....
gi 2458278088 239 AAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 165 IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
129-263 |
2.44e-09 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 55.56 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278088 129 MNIPLLNTVVLLTSGISVTWAHHSMMESNYSQGNMSLIMTIMLGIYFTILQAYEYW---ESQFTLADSIYGSTFFMATGF 205
Cdd:PRK10663 66 LPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGT 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2458278088 206 HGIHVIIGTSFLLICMIRHLINHFSSKHHMGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:PRK10663 146 HGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
