|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.30e-149 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 425.05 E-value: 1.30e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00153 27 VGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00153 107 LTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00153 187 LITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-211 |
1.74e-134 |
|
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: 386.07 E-value: 1.74e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:cd01663 20 VGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:cd01663 100 LLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:cd01663 180 LITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-211 |
9.09e-77 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 239.64 E-value: 9.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:COG0843 32 IGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:COG0843 111 GLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:COG0843 191 LVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-211 |
1.84e-47 |
|
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: 161.20 E-value: 1.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:pfam00115 16 VGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMvntGVGTGWTVYPPLSGpiahgggsVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLdQTPLFVWSV 160
Cdd:pfam00115 95 AVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFG 211
Cdd:pfam00115 163 LATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFG 207
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
6-211 |
5.14e-39 |
|
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: 141.53 E-value: 5.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 6 SLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLMLLI 85
Cdd:TIGR02882 72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 86 SSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITAL 165
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 751143478 166 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWG 276
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.30e-149 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 425.05 E-value: 1.30e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00153 27 VGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00153 107 LTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00153 187 LITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-211 |
1.74e-134 |
|
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: 386.07 E-value: 1.74e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:cd01663 20 VGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:cd01663 100 LLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:cd01663 180 LITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.91e-130 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 376.71 E-value: 1.91e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00167 29 VGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00167 109 LLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSI 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00167 189 LVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.59e-129 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 374.43 E-value: 1.59e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00116 29 VGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00116 109 FLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00116 189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.47e-124 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 361.60 E-value: 1.47e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00223 26 VGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00223 106 LYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00223 186 KVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 236
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
2.86e-124 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 360.96 E-value: 2.86e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00142 27 VGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00142 107 LLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00142 187 KITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 237
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-211 |
6.93e-115 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 336.85 E-value: 6.93e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00103 29 VGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00103 109 FLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00103 189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.99e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 335.76 E-value: 1.99e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00077 29 VGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00077 109 FLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00077 189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFG 239
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
2.58e-113 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 332.95 E-value: 2.58e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00037 29 VGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00037 109 FLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00037 189 FITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 239
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-211 |
2.82e-113 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 332.64 E-value: 2.82e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00007 26 LGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00007 106 LILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00007 186 VITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 236
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
2.86e-113 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 333.04 E-value: 2.86e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00183 29 VGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00183 109 FLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00183 189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
6.26e-105 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 311.76 E-value: 6.26e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00182 31 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00182 111 LILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSI 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00182 191 LITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 241
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.33e-103 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 308.29 E-value: 1.33e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00184 31 IGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00184 111 LTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSI 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00184 191 LVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.03e-100 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 300.44 E-value: 1.03e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00079 30 VGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGpIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00079 110 LFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00079 189 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFG 239
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.95e-95 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 288.07 E-value: 1.95e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00026 30 IGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:MTH00026 110 LFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00026 190 FITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 240
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-211 |
1.38e-86 |
|
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: 262.85 E-value: 1.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:cd00919 18 LGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:cd00919 97 LLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:cd00919 177 LVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFG 227
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-211 |
9.09e-77 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 239.64 E-value: 9.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:COG0843 32 IGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSV 160
Cdd:COG0843 111 GLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:COG0843 191 LVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.27e-66 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 213.00 E-value: 1.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00048 30 VGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMVntGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLdQTPLFVWSV 160
Cdd:MTH00048 110 IVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSY 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:MTH00048 187 LFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-211 |
1.48e-61 |
|
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: 199.34 E-value: 1.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 2 GTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 81
Cdd:cd01662 25 GGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 82 MLLISSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVV 161
Cdd:cd01662 104 LLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 751143478 162 ITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:cd01662 184 VTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFG 233
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-211 |
1.84e-47 |
|
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: 161.20 E-value: 1.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 1 VGTSMSLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 80
Cdd:pfam00115 16 VGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 81 LMLLISSSMvntGVGTGWTVYPPLSGpiahgggsVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLdQTPLFVWSV 160
Cdd:pfam00115 95 AVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 751143478 161 VITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFG 211
Cdd:pfam00115 163 LATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFG 207
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
6-211 |
5.14e-39 |
|
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: 141.53 E-value: 5.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 6 SLLIRAELGQPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLMLLI 85
Cdd:TIGR02882 72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 86 SSSMVNTGVGTGWTVYPPLSGPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITAL 165
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 751143478 166 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWG 276
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
26-211 |
8.04e-35 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 130.06 E-value: 8.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 26 YNTIITSHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLMLLISSSMVNTGVGTGWTVYPPLS 105
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751143478 106 GPIAHGGGSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITMLLTDR 185
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180
....*....|....*....|....*.
gi 751143478 186 NLNTSFFDPAGGGDPILYQHLFWFFG 211
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWG 283
|
|
|