|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
1-194 |
4.25e-123 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 347.94 E-value: 4.25e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00155 62 EGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00155 142 VTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHL 221
|
170 180 190
....*....|....*....|....*....|....
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIY 194
Cdd:MTH00155 222 NNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-196 |
1.85e-104 |
|
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: 300.20 E-value: 1.85e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:cd01665 48 ESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGAT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:cd01665 128 VTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLL 207
|
170 180 190
....*....|....*....|....*....|....*.
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:cd01665 208 KGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
1-197 |
3.60e-99 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 287.38 E-value: 3.60e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:pfam00510 61 EGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:pfam00510 141 VTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLL 220
|
170 180 190
....*....|....*....|....*....|....*..
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:pfam00510 221 KYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWWG 257
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
14-196 |
1.32e-49 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 159.24 E-value: 1.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 14 IGLRWGMILFILSEILFFVSFFWAFFHSSLSpaielGASWPPlGIISFNPFqIPLLNTAILLTSGVTVTWAHHSLMENNH 93
Cdd:COG1845 14 SPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 94 SQTTQGLFFTVLLGIYFSILQAYEY---IEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHLNHHFSKNHHF 170
Cdd:COG1845 87 KGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHT 166
|
170 180
....*....|....*....|....*.
gi 169648653 171 GFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:COG1845 167 GVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
68-197 |
5.39e-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: 56.40 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 68 LLNTAILLTSGVTVTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYE---YIEAPFTIADSIYGSTFFMATGFHGIH 144
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 169648653 145 VLIGTTFLLVCLLRHLNHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
1-194 |
4.25e-123 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 347.94 E-value: 4.25e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00155 62 EGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00155 142 VTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHL 221
|
170 180 190
....*....|....*....|....*....|....
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIY 194
Cdd:MTH00155 222 NNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
1-197 |
1.01e-107 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 309.19 E-value: 1.01e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00118 64 ESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00118 144 VTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLI 223
|
170 180 190
....*....|....*....|....*....|....*..
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00118 224 KFHFTTNHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
1-197 |
6.57e-105 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 302.28 E-value: 6.57e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00189 63 ESTFQGFHTPPVQKGLRYGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00189 143 VTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQI 222
|
170 180 190
....*....|....*....|....*....|....*..
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00189 223 QGHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-196 |
1.85e-104 |
|
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: 300.20 E-value: 1.85e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:cd01665 48 ESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGAT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:cd01665 128 VTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLL 207
|
170 180 190
....*....|....*....|....*....|....*.
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:cd01665 208 KGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYWW 243
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
1-198 |
7.52e-103 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 296.80 E-value: 7.52e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00141 62 ESTFQGFHTSKVQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00141 142 VTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLL 221
|
170 180 190
....*....|....*....|....*....|....*...
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWGG 198
Cdd:MTH00141 222 LGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
1-198 |
8.86e-103 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 296.64 E-value: 8.86e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00039 63 EATFQGMHTLIVINGLRYGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00039 143 ITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLI 222
|
170 180 190
....*....|....*....|....*....|....*...
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWGG 198
Cdd:MTH00039 223 NHHFSNNHHFGFEAAAWYWHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
1-197 |
2.31e-99 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 288.16 E-value: 2.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00099 64 ESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00099 144 ITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQL 223
|
170 180 190
....*....|....*....|....*....|....*..
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00099 224 KFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
1-197 |
3.60e-99 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 287.38 E-value: 3.60e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:pfam00510 61 EGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:pfam00510 141 VTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLL 220
|
170 180 190
....*....|....*....|....*....|....*..
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:pfam00510 221 KYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-197 |
1.31e-97 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 283.60 E-value: 1.31e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00219 65 ESTFMGLHTSKVSTGLRIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00219 145 VTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGL 224
|
170 180 190
....*....|....*....|....*....|....*..
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00219 225 MLHFSKNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
1-197 |
2.16e-97 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 283.19 E-value: 2.16e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00130 64 EGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00130 144 VTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQI 223
|
170 180 190
....*....|....*....|....*....|....*..
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00130 224 QYHFTSEHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
1-197 |
1.20e-96 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 281.25 E-value: 1.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00075 64 EGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00075 144 VTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQI 223
|
170 180 190
....*....|....*....|....*....|....*..
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00075 224 NFHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
1-197 |
1.52e-92 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 270.86 E-value: 1.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00024 64 ESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGAT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00024 144 VTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLL 223
|
170 180 190
....*....|....*....|....*....|....*..
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00024 224 SNQFTRRQHVGFEAASWYWHFVDVVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
1-197 |
1.09e-91 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 268.63 E-value: 1.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00009 62 EGTYMGHHTSYVTKGLRWGMILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00009 142 VTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTW 221
|
170 180 190
....*....|....*....|....*....|....*..
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00009 222 SHHFSTGHHFGFEAAAWYWHFVDVVWIFLYLCIYWWG 258
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-197 |
6.78e-87 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 256.64 E-value: 6.78e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00052 65 ESTYQGHHTLIVKQGLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGAT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:MTH00052 145 VTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLI 224
|
170 180 190
....*....|....*....|....*....|....*..
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00052 225 NHQFTRHHHFGFEAAAWYWHFVDVVWLFLFIFMYWWG 261
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
1-197 |
5.84e-74 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 224.95 E-value: 5.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:MTH00028 64 EGTHQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGAT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHH------------------------------------SLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFT 124
Cdd:MTH00028 144 VTWAHHaiigtgnpaslekgtqgiegpnpsngappdpqkgptFLLSDFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFA 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169648653 125 IADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHLNHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00028 224 ISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
1-198 |
2.13e-66 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 204.51 E-value: 2.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 1 EGTYQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVT 80
Cdd:PLN02194 67 ESTLEGHHTKVVQLGPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 81 VTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:PLN02194 147 VTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQY 226
|
170 180 190
....*....|....*....|....*....|....*...
gi 169648653 161 NHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWGG 198
Cdd:PLN02194 227 LGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWWGG 264
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
4-197 |
1.46e-63 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 197.10 E-value: 1.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 4 YQGLHTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASWPPLGIISFNPFQIPLLNTAILLTSGVTVTW 83
Cdd:MTH00083 63 LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTW 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 84 AHHSLMENNhSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHLNHH 163
Cdd:MTH00083 143 SHHSLCLSN-KSCTNSLLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSH 221
|
170 180 190
....*....|....*....|....*....|....
gi 169648653 164 FSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:MTH00083 222 FNYNHHLGLEFAILYWHFVDVVWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
8-196 |
5.63e-63 |
|
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.
Pssm-ID: 238227 Cd Length: 183 Bit Score: 192.80 E-value: 5.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 8 HTYAVTIGLRWGMILFILSEILFFVSFFWAFFHSSLSPAIELGASwpplgiisFNPFQIPLLNTAILLTSGVTVTWAHHS 87
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGAG--------LDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 88 LM--ENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHLNHHFS 165
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 169648653 166 KNHHFGFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
14-196 |
1.32e-49 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 159.24 E-value: 1.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 14 IGLRWGMILFILSEILFFVSFFWAFFHSSLSpaielGASWPPlGIISFNPFqIPLLNTAILLTSGVTVTWAHHSLMENNH 93
Cdd:COG1845 14 SPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 94 SQTTQGLFFTVLLGIYFSILQAYEY---IEAPFTIADSIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHLNHHFSKNHHF 170
Cdd:COG1845 87 KGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHT 166
|
170 180
....*....|....*....|....*.
gi 169648653 171 GFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:COG1845 167 GVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
68-194 |
8.04e-22 |
|
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: 87.68 E-value: 8.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 68 LLNTAILLTSGVTVTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEY---IEAPFTIADSIYGSTFFMATGFHGIH 144
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 169648653 145 VLIGTTFLLVCLLRHLNHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIY 194
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
19-196 |
1.04e-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: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 19 GMILFILSEILFFVSFFWAFFHSSLSPAIelgaSWPPLG---IISFNPFQIPL----LNTAILLTSGVTVTWAHHSLMEN 91
Cdd:cd02864 12 MMWFFLLSDAFIFSSFLIAYMTARISTTE----PWPLPSdvfALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 92 NHSQTTQGLFFTVLLGIYFSILQAYEY-----------IEAPFTIAdsIYGSTFFMATGFHGIHVLIGTTFLLVCLLRHL 160
Cdd:cd02864 88 NRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVW 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 169648653 161 NHHF-SKNHHFGFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:cd02864 166 RGKYqRIGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
67-196 |
3.88e-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: 72.79 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 67 PLLNTAILLTSGVTVTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEYIEAPF---TIADSIYGSTFFMATGFHGI 143
Cdd:cd02865 52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 169648653 144 HVLIGTTFLLVCLLRHLNHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWW 196
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
63-194 |
7.77e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 72.64 E-value: 7.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 63 PFQIPLLNTAILLTSGVTVTWAHHSL-MENNHSQttqgLFFTVLLGIYFSILQAYEYIEAPFTIADSIYGSTFFMATGFH 141
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLLgWKYCDLF----LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLH 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 169648653 142 GIHVLIGTtFLLVCLLRHLNHHFSKNHHfgfEAAAWYWHFVDVVWLFLYITIY 194
Cdd:MTH00049 165 FSHVVLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
64-194 |
3.50e-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: 69.96 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 64 FQIPL--LNTAILLTSGVTVTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYE---YIEAPFTIADSIYGSTFFMAT 138
Cdd:cd02863 48 FELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLV 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 169648653 139 GFHGIHVLIGTTFLLVCLLRHLNHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIY 194
Cdd:cd02863 128 GTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
68-197 |
5.39e-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: 56.40 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 68 LLNTAILLTSGVTVTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYE---YIEAPFTIADSIYGSTFFMATGFHGIH 144
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 169648653 145 VLIGTTFLLVCLLRHLNHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
64-197 |
1.37e-09 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 55.17 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169648653 64 FQIP--LLNTAILLTSGVTVTWAHHSLMENNHSQTTQGLFFTVLLGIYFSILQAYEY---IEAPFTIADSIYGSTFFMAT 138
Cdd:PRK10663 64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALV 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 169648653 139 GFHGIHVLIGTTFLLVCLLRHLNHHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWG 197
Cdd:PRK10663 144 GTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
|
|
|