|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
2.16e-135 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 389.23 E-value: 2.16e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00153 21 GAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00153 101 WLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00153 181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH 231
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-211 |
2.83e-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: 359.87 E-value: 2.83e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:cd01663 14 GLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:cd01663 94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:cd01663 174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH 224
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
4-211 |
5.45e-68 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 216.92 E-value: 5.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 4 AAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPvMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 83
Cdd:COG0843 29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 84 PPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMPLFV 163
Cdd:COG0843 108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1181531687 164 WAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:COG0843 188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQH 235
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
6-211 |
1.66e-42 |
|
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: 148.10 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 6 MVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPvMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 85
Cdd:pfam00115 15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 86 SLILLLASSGveaGAGTGWTVYPPLAGnlahagasVDLTIFSLHLAGVSSILGAINFITTIINMKPPGAShYQMPLFVWA 165
Cdd:pfam00115 94 GAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT-LRMPLFVWA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1181531687 166 VFVTAILLLLSLPVLAAAITMLLTDRNLNttffdpAGGGDPILYQH 211
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQH 201
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
8-209 |
2.31e-36 |
|
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: 134.21 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 8 GTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 87
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 88 ILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMPLFVWAVF 167
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1181531687 168 VTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILY 209
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLW 268
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
2.16e-135 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 389.23 E-value: 2.16e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00153 21 GAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00153 101 WLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00153 181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH 231
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.10e-128 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 372.12 E-value: 1.10e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00116 23 GAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00116 103 WLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00116 183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 233
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
5.20e-128 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 370.55 E-value: 5.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00167 23 GAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00167 103 WLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00167 183 LFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 233
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-211 |
2.83e-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: 359.87 E-value: 2.83e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:cd01663 14 GLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:cd01663 94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:cd01663 174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH 224
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.84e-120 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 351.15 E-value: 1.84e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00183 23 GAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00183 103 WLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00183 183 LFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 233
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
3.66e-118 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 345.17 E-value: 3.66e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00142 21 GAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00142 101 WLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00142 181 LFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH 231
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
4.01e-118 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 345.39 E-value: 4.01e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00077 23 GAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00077 103 WLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00077 183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQH 233
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-211 |
3.37e-117 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 343.02 E-value: 3.37e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00103 23 GAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00103 103 WLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00103 183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 233
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.70e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 335.79 E-value: 1.70e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00223 20 GMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00223 100 WLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00223 180 LFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH 230
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
2.75e-106 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 315.23 E-value: 2.75e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00037 23 GAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00037 103 WLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00037 183 LFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQH 233
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-211 |
3.67e-102 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 304.52 E-value: 3.67e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00007 20 GVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00007 100 WLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00007 180 LFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH 230
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
4.54e-97 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 291.73 E-value: 4.54e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00182 25 GAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00182 105 WLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLP 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00182 185 LFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQH 235
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
1.33e-96 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 290.57 E-value: 1.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00184 25 GAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00184 105 WLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMP 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00184 185 LFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQH 235
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
3.43e-90 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 273.48 E-value: 3.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00079 24 GLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00079 104 WLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00079 183 LFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQH 233
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
6.41e-87 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 266.11 E-value: 6.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00026 24 GALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:MTH00026 104 WLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00026 184 LFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQH 234
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-211 |
3.06e-77 |
|
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.
Pssm-ID: 238461 Cd Length: 463 Bit Score: 238.97 E-value: 3.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPlMIGAPDMAFPRMNNMSF 80
Cdd:cd00919 12 AFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMP 160
Cdd:cd00919 91 WLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:cd00919 171 LFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQH 221
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
4-211 |
5.45e-68 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 216.92 E-value: 5.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 4 AAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPvMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 83
Cdd:COG0843 29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 84 PPSLILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMPLFV 163
Cdd:COG0843 108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1181531687 164 WAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:COG0843 188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQH 235
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-211 |
5.05e-59 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 192.97 E-value: 5.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 1 GAWAAMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 80
Cdd:MTH00048 24 GVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 81 WLLPPSLILLLASsgVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHyQMP 160
Cdd:MTH00048 104 WLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1181531687 161 LFVWAVFVTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:MTH00048 181 IILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQH 231
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
8-211 |
6.82e-58 |
|
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: 189.71 E-value: 6.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 8 GTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 87
Cdd:cd01662 25 GGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 88 ILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMPLFVWAVF 167
Cdd:cd01662 104 LLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1181531687 168 VTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 211
Cdd:cd01662 184 VTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQH 227
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
6-211 |
1.66e-42 |
|
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: 148.10 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 6 MVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPvMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 85
Cdd:pfam00115 15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 86 SLILLLASSGveaGAGTGWTVYPPLAGnlahagasVDLTIFSLHLAGVSSILGAINFITTIINMKPPGAShYQMPLFVWA 165
Cdd:pfam00115 94 GAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT-LRMPLFVWA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1181531687 166 VFVTAILLLLSLPVLAAAITMLLTDRNLNttffdpAGGGDPILYQH 211
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQH 201
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
32-209 |
1.08e-36 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 135.06 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 32 YNVIVTAHAFVMIFFMVMPVMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLILLLASSGVEAGAGTGWTVYPPLA 111
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 112 GNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMPLFVWAVFVTAILLLLSLPVLAAAITMLLTDR 191
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170
....*....|....*...
gi 1181531687 192 NLNTTFFDPAGGGDPILY 209
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMY 275
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
8-209 |
2.31e-36 |
|
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: 134.21 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 8 GTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 87
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181531687 88 ILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPGASHYQMPLFVWAVF 167
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1181531687 168 VTAILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILY 209
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLW 268
|
|
|