|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
7.21e-138 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 395.78 E-value: 7.21e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00153 24 SGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00153 104 PPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00153 184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-219 |
1.34e-121 |
|
Cytochrome C oxidase subunit I. 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. It 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, may play a role in assembly or oxygen delivery to the active site. 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 I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 353.33 E-value: 1.34e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:cd01663 17 SGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:cd01663 97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:cd01663 177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 235
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-219 |
1.24e-66 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 213.84 E-value: 1.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:COG0843 29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:COG0843 108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:COG0843 188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-219 |
5.29e-41 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 144.25 E-value: 5.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:pfam00115 13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSlveNGAGTGCTVYPPLSAniahagasVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLdQTPLFV 160
Cdd:pfam00115 92 VLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPNFNQHLFSFLGPREVY 219
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVY 212
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
7.21e-138 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 395.78 E-value: 7.21e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00153 24 SGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00153 104 PPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00153 184 WSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-219 |
1.34e-121 |
|
Cytochrome C oxidase subunit I. 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. It 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, may play a role in assembly or oxygen delivery to the active site. 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 I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 353.33 E-value: 1.34e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:cd01663 17 SGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:cd01663 97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:cd01663 177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 235
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
8.53e-119 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 347.05 E-value: 8.53e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00167 26 AGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00167 106 PPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00167 186 WSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
4.98e-118 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 345.54 E-value: 4.98e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00116 26 AGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00116 106 PPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00116 186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
3.76e-116 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 340.55 E-value: 3.76e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00142 24 AGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00142 104 PPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00142 184 WSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
3.46e-113 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 333.10 E-value: 3.46e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00223 23 SGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00223 103 PPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFV 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00223 183 WSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
1.38e-107 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 318.79 E-value: 1.38e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00183 26 AGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00183 106 PPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00183 186 WAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-219 |
3.78e-107 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 317.59 E-value: 3.78e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00103 26 AGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00103 106 PPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00103 186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
1.23e-106 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 316.50 E-value: 1.23e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00077 26 AGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00077 106 PPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00077 186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVY 244
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
2.59e-103 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 307.91 E-value: 2.59e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00037 26 AGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00037 106 PPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00037 186 WSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVY 244
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-219 |
8.23e-103 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 306.44 E-value: 8.23e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00007 23 GGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00007 103 PPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFV 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00007 183 WAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
6.82e-96 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 289.03 E-value: 6.82e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00182 28 AGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00182 108 PPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00182 188 WSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
1.51e-95 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 287.88 E-value: 1.51e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00184 28 AGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00184 108 PPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00184 188 WSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
8.57e-92 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 278.10 E-value: 8.57e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00079 27 SGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSaNIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00079 107 PTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00079 186 WTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVY 244
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
3.21e-85 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 261.87 E-value: 3.21e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00026 27 SGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:MTH00026 107 PPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00026 187 WSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-219 |
8.96e-78 |
|
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.
Pssm-ID: 238461 Cd Length: 463 Bit Score: 240.51 E-value: 8.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNcLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:cd00919 15 ALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGN-LLPPLIGARDLAFPRLNNLSFWLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:cd00919 94 PPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:cd00919 174 WSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVY 232
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-219 |
1.24e-66 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 213.84 E-value: 1.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:COG0843 29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFV 160
Cdd:COG0843 108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:COG0843 188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-219 |
1.64e-58 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 192.20 E-value: 1.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:MTH00048 27 SGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSLVenGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLdQTPLFV 160
Cdd:MTH00048 107 VPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIIL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:MTH00048 184 WSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVY 242
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
5-219 |
5.66e-54 |
|
Ubiquinol oxidase subunit I. 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. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.
Pssm-ID: 238832 Cd Length: 501 Bit Score: 180.08 E-value: 5.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 5 GTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNCLVPLMLGAPDMAFPRMNNMSFWLLPPSL 84
Cdd:cd01662 25 GGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 85 SLLLASSLVENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVCAVG 164
Cdd:cd01662 104 LLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1221394320 165 ITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:cd01662 184 VTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVY 238
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-219 |
5.29e-41 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 144.25 E-value: 5.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 1 AGMVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNCLVPLMLGAPDMAFPRMNNMSFWLL 80
Cdd:pfam00115 13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 81 PPSLSLLLASSlveNGAGTGCTVYPPLSAniahagasVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLdQTPLFV 160
Cdd:pfam00115 92 VLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221394320 161 CAVGITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPNFNQHLFSFLGPREVY 219
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVY 212
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
14-219 |
3.03e-32 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 123.12 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 14 AELGQPGYLigDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNCLVPLMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLV 93
Cdd:PRK15017 86 ASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221394320 94 ENGAGTGCTVYPPLSANIAHAGASVDLTIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVCAVGITALLLLLS 173
Cdd:PRK15017 163 GEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIAS 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1221394320 174 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPNFNQHLFSFLGPREVY 219
Cdd:PRK15017 243 FPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVY 288
|
|
|