|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
1-164 |
1.58e-88 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 258.88 E-value: 1.58e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 1 AVRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIA 80
Cdd:pfam00510 71 AVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 81 GNRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHV 160
Cdd:pfam00510 151 GNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHF 230
|
....
gi 1732629959 161 GYET 164
Cdd:pfam00510 231 GFEA 234
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-164 |
1.87e-77 |
|
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: 230.48 E-value: 1.87e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 1 AVRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIA 80
Cdd:cd01665 58 KVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 81 GNRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHV 160
Cdd:cd01665 138 GNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHL 217
|
....
gi 1732629959 161 GYET 164
Cdd:cd01665 218 GFEA 221
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
2-163 |
2.35e-59 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 184.61 E-value: 2.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00155 73 VTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMEN 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00155 153 NYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFG 232
|
..
gi 1732629959 162 YE 163
Cdd:MTH00155 233 FE 234
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
8-164 |
5.62e-33 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 115.33 E-value: 5.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 8 LGFLMFVLSEVLIFAGLFWAYF-HSAMSPDvtlgscWPPvGIEAVQPTeLPLLNTIILLSSGATVTYSHHALIAGNRNKA 86
Cdd:COG1845 18 LGMWLFLASEVMLFAALFAAYFvLRASAPD------WPA-GAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 87 LSGLLITFWLIVIFVSCQYIEYTNAA---FTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVGYE 163
Cdd:COG1845 90 RLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVE 169
|
.
gi 1732629959 164 T 164
Cdd:COG1845 170 A 170
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
1-164 |
1.58e-88 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 258.88 E-value: 1.58e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 1 AVRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIA 80
Cdd:pfam00510 71 AVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 81 GNRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHV 160
Cdd:pfam00510 151 GNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHF 230
|
....
gi 1732629959 161 GYET 164
Cdd:pfam00510 231 GFEA 234
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-164 |
1.87e-77 |
|
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: 230.48 E-value: 1.87e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 1 AVRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIA 80
Cdd:cd01665 58 KVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 81 GNRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHV 160
Cdd:cd01665 138 GNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHL 217
|
....
gi 1732629959 161 GYET 164
Cdd:cd01665 218 GFEA 221
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
2-163 |
2.35e-59 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 184.61 E-value: 2.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00155 73 VTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMEN 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00155 153 NYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFG 232
|
..
gi 1732629959 162 YE 163
Cdd:MTH00155 233 FE 234
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
2-163 |
9.19e-59 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 183.64 E-value: 9.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00189 74 VQKGLRYGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00189 154 NRKEAIQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFG 233
|
..
gi 1732629959 162 YE 163
Cdd:MTH00189 234 FE 235
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
2-163 |
3.14e-57 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 179.70 E-value: 3.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00141 73 VQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00141 153 DYKSALQGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFG 232
|
..
gi 1732629959 162 YE 163
Cdd:MTH00141 233 FE 234
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
2-163 |
2.57e-55 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 174.94 E-value: 2.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00024 75 VKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00024 155 KRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVG 234
|
..
gi 1732629959 162 YE 163
Cdd:MTH00024 235 FE 236
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
2-163 |
2.80e-55 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 174.75 E-value: 2.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00118 75 VQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00118 155 NRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFG 234
|
..
gi 1732629959 162 YE 163
Cdd:MTH00118 235 FE 236
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
2-163 |
1.78e-54 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 172.60 E-value: 1.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00039 74 VINGLRYGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00039 154 NRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFG 233
|
..
gi 1732629959 162 YE 163
Cdd:MTH00039 234 FE 235
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
2-163 |
3.75e-52 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 166.89 E-value: 3.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00052 76 VKQGLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00052 156 KRKEAIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFG 235
|
..
gi 1732629959 162 YE 163
Cdd:MTH00052 236 FE 237
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
2-163 |
6.65e-52 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 166.06 E-value: 6.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00099 75 VQKGLRYGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00099 155 NRKHMLQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFG 234
|
..
gi 1732629959 162 YE 163
Cdd:MTH00099 235 FE 236
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
2-163 |
4.28e-51 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 164.17 E-value: 4.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00130 75 VQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00130 155 ERKQAIQSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFG 234
|
..
gi 1732629959 162 YE 163
Cdd:MTH00130 235 FE 236
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
2-163 |
6.20e-49 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 158.41 E-value: 6.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00219 76 VSTGLRIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMES 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00219 156 NHKEAQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFG 235
|
..
gi 1732629959 162 YE 163
Cdd:MTH00219 236 FE 237
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
2-163 |
1.00e-48 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 157.98 E-value: 1.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00075 75 VQKGLRYGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00075 155 NRKEAIQSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFG 234
|
..
gi 1732629959 162 YE 163
Cdd:MTH00075 235 FE 236
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
2-164 |
1.59e-48 |
|
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: 155.05 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGscwppvgiEAVQPTELPLLNTIILLSSGATVTYSHHALIA- 80
Cdd:cd00386 5 VRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHASLAAr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 81 -GNRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHH 159
Cdd:cd00386 77 rGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFTPRHH 156
|
....*
gi 1732629959 160 VGYET 164
Cdd:cd00386 157 LGLEA 161
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
2-163 |
7.36e-46 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 150.49 E-value: 7.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00083 71 VMDGFKFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NrNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00083 151 N-KSCTNSLLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLG 229
|
..
gi 1732629959 162 YE 163
Cdd:MTH00083 230 LE 231
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
2-163 |
2.49e-45 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 150.22 E-value: 2.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00028 75 VVRGLKLGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 N------------------------------------RNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFY 125
Cdd:MTH00028 155 GnpaslekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFF 234
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732629959 126 AGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVGYE 163
Cdd:MTH00028 235 MLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLE 272
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
2-163 |
3.36e-43 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 143.82 E-value: 3.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:MTH00009 73 VTKGLRWGMILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:MTH00009 153 DRPEATQALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFG 232
|
..
gi 1732629959 162 YE 163
Cdd:MTH00009 233 FE 234
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
2-163 |
8.84e-37 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 127.47 E-value: 8.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 2 VRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGSCWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAG 81
Cdd:PLN02194 78 VQLGPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 82 NRNKALSGLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVG 161
Cdd:PLN02194 158 KEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVG 237
|
..
gi 1732629959 162 YE 163
Cdd:PLN02194 238 FE 239
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
8-164 |
5.62e-33 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 115.33 E-value: 5.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 8 LGFLMFVLSEVLIFAGLFWAYF-HSAMSPDvtlgscWPPvGIEAVQPTeLPLLNTIILLSSGATVTYSHHALIAGNRNKA 86
Cdd:COG1845 18 LGMWLFLASEVMLFAALFAAYFvLRASAPD------WPA-GAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 87 LSGLLITFWLIVIFVSCQYIEYTNAA---FTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRLRNYHLTAGHHVGYE 163
Cdd:COG1845 90 RLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVE 169
|
.
gi 1732629959 164 T 164
Cdd:COG1845 170 A 170
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
9-136 |
2.00e-07 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 48.76 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732629959 9 GFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGScwppvgieavqPTELPLLNTIILLSSGATVTYSHHaLIAGNRNKALs 88
Cdd:MTH00049 56 AFWLFILSEVIIFGSLLVCCLWFDDWSYISLSS-----------SLEIPFVGCFLLLGSSITVTAYHH-LLGWKYCDLF- 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1732629959 89 gLLITFWLIVIFVSCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMV 136
Cdd:MTH00049 123 -LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVV 169
|
|
|