|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
2-261 |
2.42e-134 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 379.32 E-value: 2.42e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 2 LVRKNPFHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRI 81
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 82 GMMLFIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLM 161
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 162 GLVWTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWY 241
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 270267404 242 WHFVDVVWIFLYVSIYWWGS 261
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
18-259 |
3.43e-101 |
|
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: 294.81 E-value: 3.43e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 18 IVAGGVALLLTMGLVLWMHSKT-FVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRIGMMLFIVSEVFFFLG 96
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGgPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 97 FFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLVWTLALGFFFTLL 176
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 177 QLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHFVDVVWIFLYVSI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 270267404 257 YWW 259
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-261 |
1.15e-100 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 293.93 E-value: 1.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 7 PFHLVDSSPWPIVAGGVALLLTMGLVLWMH--SKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRIGMM 84
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 85 LFIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLV 164
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 165 WTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHF 244
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*..
gi 270267404 245 VDVVWIFLYVSIYWWGS 261
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-259 |
1.21e-41 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 141.14 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 71 HGVMVQKGLRIGMMLFIVSEVFFFLGFFwaffhSSLSVLADISEEWPPvGLEPMDPmGVPLLNTVVLLSSGVTVTYCHYS 150
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALF-----AAYFVLRASAPDWPA-GAELLDL-PLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 151 VLTDSFGGGLMGLVWTLALGFFFTLLQLLEY---VESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHF 227
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 270267404 228 SSTQHVGLECAIWYWHFVDVVWIFLYVSIYWW 259
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
131-262 |
2.88e-07 |
|
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: 49.47 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 131 LLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLVWTLALG---FFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFH 207
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGagfVGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 270267404 208 VIVG---SLFLLVCLLRMGVGHFSSTQhvgLECAIWYWHFVDVVWIFLYVSIYWWGSV 262
Cdd:TIGR02897 136 VTLGivwAICLLIQIQRRGLTPYTAPK---VFIVSLYWHFLDVVWVFIFTAVYLIGMV 190
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
2-261 |
2.42e-134 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 379.32 E-value: 2.42e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 2 LVRKNPFHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRI 81
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 82 GMMLFIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLM 161
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 162 GLVWTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWY 241
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 270267404 242 WHFVDVVWIFLYVSIYWWGS 261
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-257 |
1.89e-110 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 318.66 E-value: 1.89e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 6 NPFHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRIGMML 85
Cdd:MTH00155 4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 86 FIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLVW 165
Cdd:MTH00155 84 FIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 166 TLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHFV 245
Cdd:MTH00155 164 TIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFV 243
|
250
....*....|..
gi 270267404 246 DVVWIFLYVSIY 257
Cdd:MTH00155 244 DVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
7-261 |
1.46e-109 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 316.51 E-value: 1.46e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 7 PFHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRIGMMLF 86
Cdd:MTH00118 7 PYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 87 IVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLVWT 166
Cdd:MTH00118 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 167 LALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHFVD 246
Cdd:MTH00118 167 ILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVD 246
|
250
....*....|....*
gi 270267404 247 VVWIFLYVSIYWWGS 261
Cdd:MTH00118 247 VVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
5-261 |
2.68e-109 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 316.06 E-value: 2.68e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 5 KNPFHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRIGMM 84
Cdd:MTH00141 3 RNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 85 LFIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLV 164
Cdd:MTH00141 83 LFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 165 WTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHF 244
Cdd:MTH00141 163 LTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHF 242
|
250
....*....|....*..
gi 270267404 245 VDVVWIFLYVSIYWWGS 261
Cdd:MTH00141 243 VDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
5-261 |
3.88e-104 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 302.80 E-value: 3.88e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 5 KNPFHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRIGMM 84
Cdd:MTH00039 4 QHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 85 LFIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLV 164
Cdd:MTH00039 84 LFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 165 WTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHF 244
Cdd:MTH00039 164 LTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHF 243
|
250
....*....|....*..
gi 270267404 245 VDVVWIFLYVSIYWWGS 261
Cdd:MTH00039 244 VDVVWLFLYVCIYWWGS 260
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
18-259 |
3.43e-101 |
|
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: 294.81 E-value: 3.43e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 18 IVAGGVALLLTMGLVLWMHSKT-FVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRIGMMLFIVSEVFFFLG 96
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGgPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 97 FFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLVWTLALGFFFTLL 176
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 177 QLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHFVDVVWIFLYVSI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 270267404 257 YWW 259
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-261 |
1.15e-100 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 293.93 E-value: 1.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 7 PFHLVDSSPWPIVAGGVALLLTMGLVLWMH--SKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRIGMM 84
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 85 LFIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLV 164
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 165 WTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHF 244
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*..
gi 270267404 245 VDVVWIFLYVSIYWWGS 261
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
7.26e-98 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 287.04 E-value: 7.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 1 MLVRKNPFHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLR 80
Cdd:MTH00130 1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 81 IGMMLFIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGL 160
Cdd:MTH00130 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 161 MGLVWTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIW 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 270267404 241 YWHFVDVVWIFLYVSIYWWGS 261
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
1.93e-97 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 285.91 E-value: 1.93e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 1 MLVRKNPFHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLR 80
Cdd:MTH00219 2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 81 IGMMLFIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGL 160
Cdd:MTH00219 82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 161 MGLVWTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIW 240
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241
|
250 260
....*....|....*....|.
gi 270267404 241 YWHFVDVVWIFLYVSIYWWGS 261
Cdd:MTH00219 242 YWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
8-261 |
3.11e-97 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 285.49 E-value: 3.11e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 8 FHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRIGMMLFI 87
Cdd:MTH00075 8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 88 VSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLVWTL 167
Cdd:MTH00075 88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 168 ALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHFVDV 247
Cdd:MTH00075 168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247
|
250
....*....|....
gi 270267404 248 VWIFLYVSIYWWGS 261
Cdd:MTH00075 248 VWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
1-261 |
2.01e-96 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 283.54 E-value: 2.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 1 MLVRKNPFHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLR 80
Cdd:MTH00099 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 81 IGMMLFIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGL 160
Cdd:MTH00099 81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 161 MGLVWTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIW 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 270267404 241 YWHFVDVVWIFLYVSIYWWGS 261
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
1-261 |
2.10e-91 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 270.47 E-value: 2.10e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 1 MLVRKNPFHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLR 80
Cdd:MTH00024 1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 81 IGMMLFIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGL 160
Cdd:MTH00024 81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 161 MGLVWTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIW 240
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240
|
250 260
....*....|....*....|.
gi 270267404 241 YWHFVDVVWIFLYVSIYWWGS 261
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
7-261 |
2.61e-86 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 257.80 E-value: 2.61e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 7 PFHLVDSSPWPIVAGGVALLLTMGLVLWMH-SKTFVFVGGSFFLMVFLVYsWWRDVVREGSYLGFHGVMVQKGLRIGMML 85
Cdd:MTH00052 8 PYHLVDPSPWPYIGGCGALFTTVGGVMYFHySQSWVLILGLITIIFTMVV-WWRDVIRESTYQGHHTLIVKQGLKYGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 86 FIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLVW 165
Cdd:MTH00052 87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 166 TLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHFV 245
Cdd:MTH00052 167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 270267404 246 DVVWIFLYVSIYWWGS 261
Cdd:MTH00052 247 DVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
5-261 |
2.64e-86 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 257.46 E-value: 2.64e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 5 KNPFHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRIGMM 84
Cdd:MTH00009 3 RQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 85 LFIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLV 164
Cdd:MTH00009 83 LFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 165 WTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHF 244
Cdd:MTH00009 163 LTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHF 242
|
250
....*....|....*..
gi 270267404 245 VDVVWIFLYVSIYWWGS 261
Cdd:MTH00009 243 VDVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
6-261 |
5.72e-82 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 248.06 E-value: 5.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 6 NPFHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGSYLGFHGVMVQKGLRIGMML 85
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 86 FIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVL------------- 152
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIgtgnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 153 -----------------------TDSFGGGLMGLVWTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVI 209
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllSDFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 270267404 210 VGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHFVDVVWIFLYVSIYWWGS 261
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
4-262 |
1.79e-68 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 212.60 E-value: 1.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 4 RKNPFHLVDSSPWPIVAGGVALLLTMGLVLWMHSktfvFVGGSFFL---MVFLVYS---WWRDVVREGSYLGFHGVMVQK 77
Cdd:PLN02194 5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHP----FQGGARLLslgLIFILYTmfvWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 78 GLRIGMMLFIVSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSFG 157
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 158 GGLMGLVWTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLEC 237
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|....*
gi 270267404 238 AIWYWHFVDVVWIFLYVSIYWWGSV 262
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWGGI 265
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
8-261 |
2.46e-61 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 193.63 E-value: 2.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 8 FHLVDSSPWPIVAGGVALLLTMGLVLWMHSKTFVFVGGSFFLMVFLVYSWWRDVVREGsYLGFHGVMVQKGLRIGMMLFI 87
Cdd:MTH00083 5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 88 VSEVFFFLGFFWAFFHSSLSVLADISEEWPPVGLEPMDPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSfGGGLMGLVWTL 167
Cdd:MTH00083 84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 168 ALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHFVDV 247
Cdd:MTH00083 163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242
|
250
....*....|....
gi 270267404 248 VWIFLYVSIYWWGS 261
Cdd:MTH00083 243 VWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
71-259 |
7.85e-53 |
|
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: 169.69 E-value: 7.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 71 HGVMVQKGLRIGMMLFIVSEVFFFLGFFWAFFHSSLSVLADISEewppvglePMDPMGVPLLNTVVLLSSGVTVTYCHYS 150
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 151 VL--TDSFGGGLMGLVWTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHFS 228
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 270267404 229 STQHVGLECAIWYWHFVDVVWIFLYVSIYWW 259
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-259 |
1.21e-41 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 141.14 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 71 HGVMVQKGLRIGMMLFIVSEVFFFLGFFwaffhSSLSVLADISEEWPPvGLEPMDPmGVPLLNTVVLLSSGVTVTYCHYS 150
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALF-----AAYFVLRASAPDWPA-GAELLDL-PLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 151 VLTDSFGGGLMGLVWTLALGFFFTLLQLLEY---VESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHF 227
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 270267404 228 SSTQHVGLECAIWYWHFVDVVWIFLYVSIYWW 259
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
131-257 |
6.14e-19 |
|
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: 81.90 E-value: 6.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 131 LLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLVWTLALGFFFTLLQLLEYVESsFSIADSVYGSVFFMA----TGFHGF 206
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHK-IAAGIDPDAGLFFTLyfllTGFHLL 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 270267404 207 HVIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHFVDVVWIFLYVSIY 257
Cdd:cd02862 134 HVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
71-259 |
1.39e-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: 75.48 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 71 HGVMVQKGLRIGMMLFIVSEVFFFLGFFwaffhSSLSVLADISEEWPPvglEPMDPMGVPLLNTVVLLSSGVTVTYCHYS 150
Cdd:cd02865 1 YVAGARSPGWWGLWVFMAVEGTLFALLI-----SAYFMRMTSGDWQPG---APLPLPNLLSLNTAVLAASSVAMQWARRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 151 VLTDSFGGGLMGLVWTLALGFFFTLLQLLEY---VESSFSIADSVYGSVFFMATGFHGFHVIVGSLFLLVCLLRMGVGHF 227
Cdd:cd02865 73 ARRNRRVLARLGLALAGALALAFLAGQLLAWhalNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHY 152
|
170 180 190
....*....|....*....|....*....|..
gi 270267404 228 SSTQHVGLECAIWYWHFVDVVWIFLYVSIYWW 259
Cdd:cd02865 153 GPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
125-257 |
5.54e-14 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 68.79 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 125 DPMGVPLLNTVVLLSSGVTVTYCHYSVLTDSfggGLMGLVWTLALGFFFTLLQLLEYVESSFSIADSVYGSVFFMATGFH 204
Cdd:MTH00049 88 SSLEIPFVGCFLLLGSSITVTAYHHLLGWKY---CDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLH 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 270267404 205 GFHVIVGSlFLLVCLLRMGVghfSSTQHVGLECAIWYWHFVDVVWIFLYVSIY 257
Cdd:MTH00049 165 FSHVVLGV-VGLSTLLLVGS---SSFGVYRSTVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
131-257 |
2.93e-13 |
|
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: 66.49 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 131 LLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLVWTLALGFFFTLLQLLE---YVESSFSIADSVYGSVFFMATGFHGFH 207
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 270267404 208 VIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHFVDVVWIFLYVSIY 257
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
129-259 |
1.51e-10 |
|
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: 59.05 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 129 VPLLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMgLVWTLALGFFFTLLQLLEY----VESSFSIADSVYG-----SVFFM 199
Cdd:cd02864 63 IAIMTFILITSSGTMAMAVNFGYRGNRKAAARL-MLATALLGATFVGMQAFEWtkliVEEGVRPWGNPWGaaqfgASFFM 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 270267404 200 ATGFHGFHVIVGSLFLLVCLLRMGVGHFSST-QHVGLECAIWYWHFVDVVWIFLYVSIYWW 259
Cdd:cd02864 142 ITGFHGTHVTIGVIYLIIIARKVWRGKYQRIgRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
131-262 |
2.88e-07 |
|
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: 49.47 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 131 LLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLVWTLALG---FFFTLLQLLEYVESSFSIADSVYGSVFFMATGFHGFH 207
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGagfVGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 270267404 208 VIVG---SLFLLVCLLRMGVGHFSSTQhvgLECAIWYWHFVDVVWIFLYVSIYWWGSV 262
Cdd:TIGR02897 136 VTLGivwAICLLIQIQRRGLTPYTAPK---VFIVSLYWHFLDVVWVFIFTAVYLIGMV 190
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
131-262 |
6.44e-07 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 48.62 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 131 LLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLVWTLALGFFFTLLQLLEY---VESSFSIADSVYGSVFFMATGFHGFH 207
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 270267404 208 VIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHFVDVVWIFLYVSIYWWGSV 262
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
131-262 |
1.32e-06 |
|
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131889 Cd Length: 180 Bit Score: 47.25 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267404 131 LLNTVVLLSSGVTVTYCHYSVLTDSFGGGLMGLVWTLALGFFFTLLQLLEYVE---SSFSIADSVYGSVFFMATGFHGFH 207
Cdd:TIGR02842 46 LVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAITFLLGLGFIGMEIYEFYHliaEGNGPDRSAFLSAFFTLVGTHGLH 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 270267404 208 VIVGSLFLLVCLLRMGVGHFSSTQHVGLECAIWYWHFVDVVWIFLYVSIYWWGSV 262
Cdd:TIGR02842 126 VTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFWHFLDIVWICVFTFVYLLGVL 180
|
|
| |
