|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
5.14e-132 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 380.37 E-value: 5.14e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00153 25 GMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00153 105 PSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVW 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00153 185 SVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-209 |
8.48e-124 |
|
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: 358.72 E-value: 8.48e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:cd01663 18 GLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:cd01663 98 PSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVW 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:cd01663 178 SVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-209 |
4.57e-71 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 225.01 E-value: 4.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 2 LVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 81
Cdd:COG0843 31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 82 SLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWS 161
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 987217249 162 VMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
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 ... |
1-209 |
1.93e-43 |
|
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: 150.42 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:pfam00115 14 FLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIvdtGVGTGWTVYPPLAGpiahsgaaVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMdQLPLFVW 160
Cdd:pfam00115 93 LGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVW 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLF 209
Cdd:pfam00115 161 AILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
4-209 |
9.80e-37 |
|
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: 134.98 E-value: 9.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 4 GTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 83
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 84 ILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVM 163
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 987217249 164 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
5.14e-132 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 380.37 E-value: 5.14e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00153 25 GMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00153 105 PSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVW 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00153 185 SVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-209 |
8.48e-124 |
|
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: 358.72 E-value: 8.48e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:cd01663 18 GLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:cd01663 98 PSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVW 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:cd01663 178 SVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
7.10e-120 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 349.36 E-value: 7.10e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00167 27 GMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00167 107 PSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVW 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00167 187 SILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
4.84e-118 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 345.15 E-value: 4.84e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00116 27 GMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00116 107 PSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVW 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00116 187 SVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
2.89e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 335.41 E-value: 2.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00223 24 GLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00223 104 PSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVW 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00223 184 SVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
9.22e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 328.99 E-value: 9.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00142 25 GMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00142 105 PALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVW 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00142 185 SVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
4.72e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 309.45 E-value: 4.72e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00037 27 GMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00037 107 PSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVW 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00037 187 SVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
8.29e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 308.79 E-value: 8.29e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00077 27 GMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00077 107 PSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVW 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00077 187 SVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
1.98e-103 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 307.62 E-value: 1.98e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00183 27 GMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00183 107 PSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVW 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00183 187 AVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-209 |
2.30e-103 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 307.58 E-value: 2.30e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00103 27 GMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00103 107 PSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVW 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00103 187 SVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
9.10e-100 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 298.66 E-value: 9.10e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00182 29 GMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00182 109 PALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVW 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00182 189 SILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-209 |
1.51e-97 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 292.58 E-value: 1.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00007 24 GLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00007 104 PALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVW 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00007 184 AVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
2.65e-97 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 292.12 E-value: 2.65e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00184 29 GMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00184 109 PALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVW 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00184 189 SILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
3.25e-92 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 278.87 E-value: 3.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00079 28 GMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGpIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00079 108 TSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVW 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00079 187 TVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
2.67e-88 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 269.58 E-value: 2.67e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00026 28 GAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:MTH00026 108 PALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVW 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00026 188 SVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-209 |
2.75e-79 |
|
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: 243.98 E-value: 2.75e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPlMIGAPDMAFPRMNNMSFWLLP 80
Cdd:cd00919 16 LLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVW 160
Cdd:cd00919 95 PGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVW 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:cd00919 175 SVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-209 |
4.57e-71 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 225.01 E-value: 4.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 2 LVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 81
Cdd:COG0843 31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 82 SLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWS 161
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 987217249 162 VMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
5.81e-60 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 195.28 E-value: 5.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:MTH00048 28 GFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIVdtGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMdQLPLFVW 160
Cdd:MTH00048 108 PSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILW 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:MTH00048 185 SYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-209 |
3.85e-57 |
|
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: 187.79 E-value: 3.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 2 LVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 81
Cdd:cd01662 23 LRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 82 SLILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWS 161
Cdd:cd01662 102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 987217249 162 VMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:cd01662 182 TLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-209 |
1.93e-43 |
|
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: 150.42 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 1 GLVGTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 80
Cdd:pfam00115 14 FLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 81 PSLILLISSSIvdtGVGTGWTVYPPLAGpiahsgaaVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMdQLPLFVW 160
Cdd:pfam00115 93 LGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVW 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 987217249 161 SVMITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLF 209
Cdd:pfam00115 161 AILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
4-209 |
9.80e-37 |
|
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: 134.98 E-value: 9.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 4 GTALSMIIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 83
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 84 ILLISSSIVDTGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVM 163
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 987217249 164 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 209
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
28-208 |
2.43e-34 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 128.51 E-value: 2.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 28 YNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLILLISSSIVDTGVGTGWTVYPPLA 107
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987217249 108 GPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDR 187
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180
....*....|....*....|.
gi 987217249 188 NLNTSFFDPAGGGDPILYQHL 208
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINL 278
|
|
|