|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-208 |
9.48e-138 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 395.01 E-value: 9.48e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00153 26 MVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00153 106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00153 186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-208 |
6.96e-123 |
|
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: 356.41 E-value: 6.96e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:cd01663 19 LVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:cd01663 99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:cd01663 179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-208 |
4.38e-69 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 219.61 E-value: 4.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:COG0843 31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-208 |
2.63e-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: 144.64 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:pfam00115 15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSlveNGAGTGWTVYPPLSAniahagasVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLdQTPLFVWA 160
Cdd:pfam00115 94 GAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPIFNQHLF 208
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
7-208 |
3.30e-33 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I 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: 131928 Cd Length: 643 Bit Score: 124.97 E-value: 3.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 7 SMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLSLLL 86
Cdd:TIGR02882 72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 87 ASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWAVGITAL 166
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2327433781 167 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-208 |
9.48e-138 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 395.01 E-value: 9.48e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00153 26 MVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00153 106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00153 186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-208 |
6.96e-123 |
|
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: 356.41 E-value: 6.96e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:cd01663 19 LVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:cd01663 99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:cd01663 179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-208 |
3.85e-118 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 345.12 E-value: 3.85e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00167 28 MVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00167 108 SLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00167 188 ILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-208 |
7.68e-117 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 341.69 E-value: 7.68e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00116 28 MVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00116 108 SFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00116 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-208 |
1.98e-115 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 338.24 E-value: 1.98e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00142 26 MVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00142 106 ALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00142 186 VKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-208 |
1.65e-113 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 333.10 E-value: 1.65e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00223 25 LVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00223 105 SLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWS 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00223 185 VKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-208 |
1.23e-105 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 313.40 E-value: 1.23e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00183 28 MVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00183 108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWA 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00183 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-208 |
2.86e-105 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 312.20 E-value: 2.86e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00103 28 MVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00103 108 SFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00103 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-208 |
1.35e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 310.72 E-value: 1.35e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00077 28 MVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00077 108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00077 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-208 |
5.79e-103 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 306.37 E-value: 5.79e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00037 28 MVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00037 108 SFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00037 188 VFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-208 |
2.60e-102 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 304.52 E-value: 2.60e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00007 25 LLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00007 105 ALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00007 185 VVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-208 |
6.35e-96 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 288.64 E-value: 6.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00182 30 MIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00182 110 ALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00182 190 ILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-208 |
1.95e-95 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 287.49 E-value: 1.95e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00184 30 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00184 110 ALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00184 190 ILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-208 |
1.30e-92 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 279.64 E-value: 1.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00079 29 MVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSaNIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:MTH00079 109 SLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00079 188 VFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
2-208 |
4.66e-86 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 263.80 E-value: 4.66e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 2 VGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPS 81
Cdd:MTH00026 30 IGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 82 LSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWAV 161
Cdd:MTH00026 110 LFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSV 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2327433781 162 GITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00026 190 FITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-208 |
3.62e-77 |
|
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: 238.58 E-value: 3.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:cd00919 17 LLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:cd00919 96 GLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:cd00919 176 VLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-208 |
4.38e-69 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 219.61 E-value: 4.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:COG0843 31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWA 160
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-208 |
1.67e-58 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 191.43 E-value: 1.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 2 VGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPS 81
Cdd:MTH00048 30 VGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 82 LSLLLASSLVenGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLdQTPLFVWAV 161
Cdd:MTH00048 110 IVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSY 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2327433781 162 GITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:MTH00048 187 LFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
3-208 |
2.91e-55 |
|
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: 182.78 E-value: 2.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 3 GTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSL 82
Cdd:cd01662 25 GGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 83 SLLLASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWAVG 162
Cdd:cd01662 104 LLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2327433781 163 ITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:cd01662 184 VTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-208 |
2.63e-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: 144.64 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 1 MVGTSLSMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:pfam00115 15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 81 SLSLLLASSlveNGAGTGWTVYPPLSAniahagasVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLdQTPLFVWA 160
Cdd:pfam00115 94 GAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2327433781 161 VGITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPIFNQHLF 208
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
12-200 |
1.99e-33 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 125.82 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 12 AELGQPGYLigDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLV 91
Cdd:PRK15017 86 ASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 92 ENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWAVGITALLLLLS 171
Cdd:PRK15017 163 GEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIAS 242
|
170 180
....*....|....*....|....*....
gi 2327433781 172 LPVLAGAITMLLTDRNLNTSFFDPAGGGD 200
Cdd:PRK15017 243 FPILTVTVALLTLDRYLGTHFFTNDMGGN 271
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
7-208 |
3.30e-33 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I 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: 131928 Cd Length: 643 Bit Score: 124.97 E-value: 3.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 7 SMLIRAELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLSLLL 86
Cdd:TIGR02882 72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327433781 87 ASSLVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLDQTPLFVWAVGITAL 166
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2327433781 167 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIFNQHLF 208
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
|
|
|