|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
14-222 |
4.93e-128 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 371.12 E-value: 4.93e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:MTH00153 30 SLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:MTH00153 110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00153 190 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
14-222 |
1.36e-122 |
|
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: 1.36e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:cd01663 23 SLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:cd01663 103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:cd01663 183 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 231
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
15-222 |
5.08e-69 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 220.38 E-value: 5.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 15 FSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPiMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTLL 94
Cdd:COG0843 36 LALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 95 LSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMITA 174
Cdd:COG0843 115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254575733 175 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:COG0843 195 ILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
15-222 |
5.33e-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: 5.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 15 FSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPiMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTLL 94
Cdd:pfam00115 20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 95 LSSSMvdcGVGTGWTVYPPLSGqmahsgpaIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMdQIPLFVWSVMITA 174
Cdd:pfam00115 99 LASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254575733 175 ILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGH 222
Cdd:pfam00115 167 ILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGH 208
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
14-222 |
4.93e-128 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 371.12 E-value: 4.93e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:MTH00153 30 SLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:MTH00153 110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00153 190 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
14-222 |
1.36e-122 |
|
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: 1.36e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:cd01663 23 SLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:cd01663 103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:cd01663 183 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 231
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
8-222 |
5.98e-115 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 337.80 E-value: 5.98e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 8 WAAFWDS-FSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWL 86
Cdd:MTH00167 25 WAGMVGTaLSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 87 LPPSLTLLLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLF 166
Cdd:MTH00167 105 LPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLF 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254575733 167 VWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00167 185 VWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
16-222 |
2.60e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 336.29 E-value: 2.60e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 16 SMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTLLL 95
Cdd:MTH00116 34 SLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 96 SSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMITAI 175
Cdd:MTH00116 114 ASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAV 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 254575733 176 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00116 194 LLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
14-222 |
9.03e-110 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 324.62 E-value: 9.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:MTH00223 29 SLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:MTH00223 109 LLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVT 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00223 189 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 237
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
14-222 |
9.71e-109 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 321.67 E-value: 9.71e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:MTH00142 30 GLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:MTH00142 110 LLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKIT 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00142 190 AILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 238
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
14-222 |
2.91e-100 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 300.32 E-value: 2.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:MTH00077 32 ALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:MTH00077 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLIT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00077 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
14-222 |
5.95e-99 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 296.81 E-value: 5.95e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:MTH00007 29 SMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:MTH00007 109 LVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVIT 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00007 189 VVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 237
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
14-222 |
1.75e-98 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 295.64 E-value: 1.75e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:MTH00103 32 ALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:MTH00103 112 LLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLIT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00103 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
14-222 |
1.15e-97 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 293.75 E-value: 1.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:MTH00183 32 ALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:MTH00183 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLIT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00183 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
14-222 |
3.30e-97 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 292.50 E-value: 3.30e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:MTH00037 32 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:MTH00037 112 LLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFIT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00037 192 AFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
14-222 |
3.43e-95 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 287.49 E-value: 3.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:MTH00182 34 AFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALIL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:MTH00182 114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILIT 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00182 194 AFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
14-222 |
2.14e-94 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 285.04 E-value: 2.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:MTH00079 33 SLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSgQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:MTH00079 113 ILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00079 192 VFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGH 240
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
14-222 |
3.97e-94 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 284.80 E-value: 3.97e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:MTH00184 34 AFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:MTH00184 114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVT 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00184 194 TFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGH 242
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
9-222 |
1.93e-87 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 268.03 E-value: 1.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 9 AAFWDSFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLP 88
Cdd:MTH00026 28 GAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 89 PSLTLLLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVW 168
Cdd:MTH00026 108 PALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVW 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254575733 169 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00026 188 SVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGH 241
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
14-222 |
1.01e-76 |
|
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: 238.20 E-value: 1.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 14 SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLlPLMIGAPDMAFPRMNNMSFWLLPPSLTL 93
Cdd:cd00919 21 LLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLL-PPLIGARDLAFPRLNNLSFWLFPPGLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 94 LLSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMIT 173
Cdd:cd00919 100 LLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254575733 174 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:cd00919 180 AILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGH 228
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
15-222 |
5.08e-69 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 220.38 E-value: 5.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 15 FSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPiMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTLL 94
Cdd:COG0843 36 LALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 95 LSSSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMITA 174
Cdd:COG0843 115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254575733 175 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:COG0843 195 ILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
8-222 |
2.21e-62 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 202.60 E-value: 2.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 8 WAAFWD-SFSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWL 86
Cdd:MTH00048 26 WSGFVGlSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 87 LPPSLTLLLSSSMVDCGVGtgWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMdQIPLF 166
Cdd:MTH00048 106 LVPSIVFLLLSMCLGAGVG--WTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSII 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254575733 167 VWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:MTH00048 183 LWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGH 238
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
17-222 |
2.62e-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: 183.55 E-value: 2.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 17 MLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPIMIGgFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLS 96
Cdd:cd01662 30 LLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 97 SSMVDCGVGTGWTVYPPLSGQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMITAIL 176
Cdd:cd01662 109 SLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSIL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254575733 177 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:cd01662 189 ILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGH 234
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
15-222 |
5.33e-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: 5.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 15 FSMLIRMELSTPGHLINNEQLYNVIVTSHAFIMIFFMVMPiMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTLL 94
Cdd:pfam00115 20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 95 LSSSMvdcGVGTGWTVYPPLSGqmahsgpaIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMdQIPLFVWSVMITA 174
Cdd:pfam00115 99 LASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254575733 175 ILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGH 222
Cdd:pfam00115 167 ILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGH 208
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
36-222 |
8.93e-33 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 124.66 E-value: 8.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 36 YNVIVTSHAFIMIFFMVMPIMIGgFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVDCGVGTGWTVYPPLS 115
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575733 116 GQMAHSGPAIDLAIFSLHLAGASSILGAINFITTTMNMKSSSLTMDQIPLFVWSVMITAILLLLSLPVLAGAITMLLTDR 195
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180
....*....|....*....|....*..
gi 254575733 196 NLNTSFFDPAGGGDPILYQHLFWFFGH 222
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGH 284
|
|
|