|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
4.05e-160 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 444.24 E-value: 4.05e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 5 NYNHPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 85 MVMFITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 165 LTLTVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2473932266 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
9.66e-128 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 362.50 E-value: 9.66e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 8 HPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFE--MNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSgnMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 86 VMFITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 166 TLTVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 2473932266 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 |
1.20e-123 |
|
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: 351.82 E-value: 1.20e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 20 LTGAIGTMTMVTGMAKWFHLFE-MNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGMVMFITSEVLFFMS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGgPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 99 FFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGLTLTVMLGAYFTLL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 179 QSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2473932266 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
1.48e-54 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 174.27 E-value: 1.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 72 LHTKTVTNGLRLGMVMFITSEVLFFMSFFWAYFNSSLSptmeigMIWPPMGIEVFNPmQIPLLNTVVLLSSGITVTWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 152 SLMEHKFKQSDQGLTLTVMLGAYFTLLQSYEYWEAM---FTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2473932266 229 FSSTHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
83-262 |
1.67e-11 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131943 Cd Length: 190 Bit Score: 61.41 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 83 LGMVMFITSEVLFFMSFFWAYFNSSLSPTMEigmiwPPMGIEVFNpMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSD 162
Cdd:TIGR02897 12 LGFWIFLGAEIALFATLFATYLVLQHGGDYA-----GKMPAELFE-LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 163 QGLTLTVMLGAYFTLLQSYE---YWEAMFTMADSVYGSTFFMATGFHGIHV---IIGTTFLLICLMRHKSNHFSSTHHFg 236
Cdd:TIGR02897 86 FWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVtlgIVWAICLLIQIQRRGLTPYTAPKVF- 164
|
170 180
....*....|....*....|....*.
gi 2473932266 237 feAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 165 --IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
4.05e-160 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 444.24 E-value: 4.05e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 5 NYNHPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 85 MVMFITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 165 LTLTVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2473932266 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
2.84e-145 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 407.03 E-value: 2.84e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 8 HPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGMVM 87
Cdd:MTH00118 6 HPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 88 FITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGLTL 167
Cdd:MTH00118 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 168 TVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFV 247
Cdd:MTH00118 166 TILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 2473932266 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00118 246 DVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
3.53e-142 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 399.35 E-value: 3.53e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 8 HPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGMVM 87
Cdd:MTH00189 5 HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 88 FITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGLTL 167
Cdd:MTH00189 85 FITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 168 TVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFV 247
Cdd:MTH00189 165 TVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 2473932266 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00189 245 DVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
5-263 |
9.27e-137 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 385.62 E-value: 9.27e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 5 NYNHPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLG 84
Cdd:MTH00039 2 THQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 85 MVMFITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQG 164
Cdd:MTH00039 82 MILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 165 LTLTVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYW 244
Cdd:MTH00039 162 LFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYW 241
|
250
....*....|....*....
gi 2473932266 245 HFVDVVWLFLYISIYWWGS 263
Cdd:MTH00039 242 HFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
2.22e-135 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 381.93 E-value: 2.22e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 8 HPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGMVM 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 88 FITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGLTL 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 168 TVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 2473932266 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
5.13e-133 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 376.03 E-value: 5.13e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 8 HPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGMVM 87
Cdd:MTH00130 6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 88 FITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGLTL 167
Cdd:MTH00130 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 168 TVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFV 247
Cdd:MTH00130 166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 2473932266 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00130 246 DVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
2.65e-132 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 374.51 E-value: 2.65e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 8 HPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGMVM 87
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 88 FITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGLTL 167
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 168 TVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFV 247
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 2473932266 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00219 247 DVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
8-263 |
3.47e-129 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 366.36 E-value: 3.47e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 8 HPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGMVM 87
Cdd:MTH00099 6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 88 FITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGLTL 167
Cdd:MTH00099 86 FIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 168 TVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFV 247
Cdd:MTH00099 166 TILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 2473932266 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00099 246 DVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.89e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 364.45 E-value: 1.89e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 8 HPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGMVM 87
Cdd:MTH00075 6 HAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 88 FITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGLTL 167
Cdd:MTH00075 86 FITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 168 TVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFV 247
Cdd:MTH00075 166 TIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 2473932266 248 DVVWLFLYISIYWWGS 263
Cdd:MTH00075 246 DVVWLFLYVSIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
8-263 |
9.66e-128 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 362.50 E-value: 9.66e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 8 HPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFE--MNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGM 85
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSgnMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 86 VMFITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGL 165
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 166 TLTVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWH 245
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 2473932266 246 FVDVVWLFLYISIYWWGS 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-263 |
4.71e-124 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 353.37 E-value: 4.71e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 8 HPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGMVM 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 88 FITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGLTL 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 168 TVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 2473932266 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 |
1.20e-123 |
|
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: 351.82 E-value: 1.20e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 20 LTGAIGTMTMVTGMAKWFHLFE-MNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGMVMFITSEVLFFMS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGgPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 99 FFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGLTLTVMLGAYFTLL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 179 QSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2473932266 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
6-263 |
1.81e-119 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 341.73 E-value: 1.81e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 6 YNHPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGM 85
Cdd:MTH00024 4 LYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 86 VMFITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGL 165
Cdd:MTH00024 84 LLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 166 TLTVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWH 245
Cdd:MTH00024 164 FLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWH 243
|
250
....*....|....*...
gi 2473932266 246 FVDVVWLFLYISIYWWGS 263
Cdd:MTH00024 244 FVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
2-263 |
1.10e-111 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 322.13 E-value: 1.10e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 2 LTKNYNHPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGL 81
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 82 RLGMVMFITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQS 161
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 162 DQGLTLTVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAA 241
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 2473932266 242 WYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.62e-100 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 295.05 E-value: 1.62e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 8 HPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTNGLRLGMVM 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 88 FITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQ---- 163
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNPASLEkgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 164 --------------------------------GLTLTVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVI 211
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrtnaviGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2473932266 212 IGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
2-262 |
2.59e-87 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 260.37 E-value: 2.59e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 2 LTKNYNHPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFE--MNLFITGMMINLLTMIQWWRDVIREGTFQGLHTKTVTN 79
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 80 GLRLGMVMFITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKFK 159
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 160 QSDQGLTLTVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEA 239
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|...
gi 2473932266 240 AAWYWHFVDVVWLFLYISIYWWG 262
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
4.76e-68 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 210.97 E-value: 4.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 8 HPFHMVDYSPWPLTGAIGTMTMVTGMAKWFHLFEMNLFITGMMINLLTMIQWWRDVIREGtFQGLHTKTVTNGLRLGMVM 87
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 88 FITSEVLFFMSFFWAYFNSSLSPTMEIGMIWPPMGIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLMEHKfKQSDQGLTL 167
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 168 TVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFV 247
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 2473932266 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 |
2.55e-67 |
|
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.
Pssm-ID: 238227 Cd Length: 183 Bit Score: 206.67 E-value: 2.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 73 HTKTVTNGLRLGMVMFITSEVLFFMSFFWAYFNSSLSPTMEIGmiwppmgiEVFNPMQIPLLNTVVLLSSGITVTWAHHS 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 153 LM--EHKFKQSDQGLTLTVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 2473932266 231 STHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
1.48e-54 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 174.27 E-value: 1.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 72 LHTKTVTNGLRLGMVMFITSEVLFFMSFFWAYFNSSLSptmeigMIWPPMGIEVFNPmQIPLLNTVVLLSSGITVTWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 152 SLMEHKFKQSDQGLTLTVMLGAYFTLLQSYEYWEAM---FTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2473932266 229 FSSTHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
82-259 |
3.25e-25 |
|
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: 98.46 E-value: 3.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 82 RLGMVMFITSEVLFFMSFFWAYF-NSSLSPtmeigmiwppmgiEVFNPMQ------IPLLNTVVLLSSGITVTWAHHSLM 154
Cdd:cd02862 10 KLGMWVFILSELLAFGALFIAYAvYRALYP-------------ELFAAGSahldllLGALNTLVLLTSSFTVALAVRAAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 155 EHKFKQSDQGLTLTVMLGAYFTLLQSYEY-WEamFTMADSVYGSTFFMA----TGFHGIHVIIGTTFLLICLMRHKSNHF 229
Cdd:cd02862 77 AGRRRRARRWLAAAVLLGLVFLVIKYFEYaHK--IAAGIDPDAGLFFTLyfllTGFHLLHVLIGLGILLWVAWRARRGRY 154
|
170 180 190
....*....|....*....|....*....|
gi 2473932266 230 SSTHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862 155 SARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
79-261 |
8.51e-19 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239216 Cd Length: 184 Bit Score: 81.26 E-value: 8.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 79 NGLRLGMVMFITSEVLFFMSFFWAYFNSSLSPTMeigmiWPPMGIEVFNpmqIPLLNTVVLLSSGITVTWAHHSLMEHKF 158
Cdd:cd02865 7 SPGWWGLWVFMAVEGTLFALLISAYFMRMTSGDW-----QPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 159 KQSDQGLTLTVMLGAYFTLLQSYEY---WEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHF 235
Cdd:cd02865 79 VLARLGLALAGALALAFLAGQLLAWhalNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRL 158
|
170 180
....*....|....*....|....*.
gi 2473932266 236 GFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865 159 PVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
87-259 |
6.16e-17 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 76.88 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 87 MFITSEVLFFMSFFWA--YFNSSLSptmeigmiwppmgIEVFNPMQIPLLNTVVLLSSGITVTWAHHSLmehKFKQSDQG 164
Cdd:MTH00049 59 LFILSEVIIFGSLLVCclWFDDWSY-------------ISLSSSLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 165 LTLTVMLGAYFTLLQSYEYWEAMFTMADSVYGSTFFMATGFHGIHVIIGTtFLLICLMRHKSNHFSSTHHfgfEAAAWYW 244
Cdd:MTH00049 123 LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYW 198
|
170
....*....|....*
gi 2473932266 245 HFVDVVWLFLYISIY 259
Cdd:MTH00049 199 HFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
82-261 |
4.24e-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: 74.46 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 82 RLGMVMFITSEVLFFMSFFWAYFNSSLSPTmeigmIWPPMGIEVFN--------PMQIPLLNTVVLLSSGITVTWAHHSL 153
Cdd:cd02864 10 KAMMWFFLLSDAFIFSSFLIAYMTARISTT-----EPWPLPSDVFAlrighfniPLVLIAIMTFILITSSGTMAMAVNFG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 154 MEHKFKQSDQGLTLTVMLGAYFTLLQSYEYWEAMFTMAD---------SVYGSTFFMATGFHGIHVIIGTTFLLICLMRH 224
Cdd:cd02864 85 YRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVrpwgnpwgaAQFGASFFMITGFHGTHVTIGVIYLIIIARKV 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 2473932266 225 KSNHFSSTHHFG-FEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864 165 WRGKYQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
83-259 |
6.02e-15 |
|
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: 71.12 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 83 LGMVMFITSEVLFFMSFFWAYFnsslspTMEIGMIWPPMGIEVFNpMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSD 162
Cdd:cd02863 11 LGFWIYLMSDCILFATLFATYA------VLSGNTAGGPPGHELFE-LPLVFIETFLLLLSSFTCGLAMIAMNKNNKKKVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 163 QGLTLTVMLGAYFTLLQSYE---YWEAMFTMADSVYGSTFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEA 239
Cdd:cd02863 84 LWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFC 163
|
170 180
....*....|....*....|
gi 2473932266 240 AAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863 164 LSLFWHFLDIVWIFVFTVVY 183
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
83-262 |
1.67e-11 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131943 Cd Length: 190 Bit Score: 61.41 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 83 LGMVMFITSEVLFFMSFFWAYFNSSLSPTMEigmiwPPMGIEVFNpMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSD 162
Cdd:TIGR02897 12 LGFWIFLGAEIALFATLFATYLVLQHGGDYA-----GKMPAELFE-LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 163 QGLTLTVMLGAYFTLLQSYE---YWEAMFTMADSVYGSTFFMATGFHGIHV---IIGTTFLLICLMRHKSNHFSSTHHFg 236
Cdd:TIGR02897 86 FWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVtlgIVWAICLLIQIQRRGLTPYTAPKVF- 164
|
170 180
....*....|....*....|....*.
gi 2473932266 237 feAAAWYWHFVDVVWLFLYISIYWWG 262
Cdd:TIGR02897 165 --IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
120-263 |
3.24e-08 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 52.48 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932266 120 PMGIEVFNpMQIPLLNTVVLLSSGITVTWAHHSLMEHKFKQSDQGLTLTVMLGAYFTLLQSYEYWEAM---FTMADSVYG 196
Cdd:PRK10663 58 PTGKDIFE-LPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHLIvegMGPDRSGFL 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2473932266 197 STFFMATGFHGIHVIIGTTFLLICLMRHKSNHFSSTHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 263
Cdd:PRK10663 137 SAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
