|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
4.83e-137 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 393.46 E-value: 4.83e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00153 20 FGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00153 100 FWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRM 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00153 180 PLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-214 |
9.59e-132 |
|
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: 379.13 E-value: 9.59e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:cd01663 13 FGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:cd01663 93 FWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:cd01663 173 PLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
5-214 |
3.84e-75 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 235.79 E-value: 3.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 5 AGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIvIGGFGNWLIPLMMGSPDMAFPRLNNISFWLL 84
Cdd:COG0843 29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 85 PPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQIPLFP 164
Cdd:COG0843 108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827490927 165 WSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:COG0843 188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
3-214 |
2.95e-45 |
|
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: 155.42 E-value: 2.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 3 IWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIvIGGFGNWLIPLMMGSPDMAFPRLNNISFW 82
Cdd:pfam00115 11 LVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 83 LLPPSLMMMICSFMinnGTGTGWTIYPPLsnniahnnISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLnQIPL 162
Cdd:pfam00115 90 LVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 827490927 163 FPWSIIITATLLILSLPVLAGAITMLLTDRNLNTsffdpsGGGDPILYQHLF 214
Cdd:pfam00115 158 FVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
9-214 |
2.48e-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: 142.69 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 9 GSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGgFGNWLIPLMMGSPDMAFPRLNNISFWLLPPSL 88
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 89 MMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQIPLFPWSII 168
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 827490927 169 ITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
4.83e-137 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 393.46 E-value: 4.83e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00153 20 FGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00153 100 FWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRM 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00153 180 PLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-214 |
9.59e-132 |
|
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: 379.13 E-value: 9.59e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:cd01663 13 FGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:cd01663 93 FWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:cd01663 173 PLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
4.70e-121 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 352.83 E-value: 4.70e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00167 22 FGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00167 102 FWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00167 182 PLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
5.03e-117 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 342.34 E-value: 5.03e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00223 19 FGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00223 99 FWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00223 179 PLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
6.46e-116 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 339.76 E-value: 6.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00116 22 FGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00116 102 FWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00116 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
8.96e-113 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 331.69 E-value: 8.96e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00142 20 FGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00142 100 FWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00142 180 PLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
1.52e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 310.70 E-value: 1.52e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00183 22 FGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00183 102 FWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00183 182 PLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
1.63e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 310.72 E-value: 1.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00077 22 FGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00077 102 FWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00077 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-214 |
1.24e-103 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 308.35 E-value: 1.24e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00103 22 FGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00103 102 FWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00103 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
3-214 |
1.88e-103 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 307.98 E-value: 1.88e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 3 IWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNISFW 82
Cdd:MTH00007 21 VWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 83 LLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQIPL 162
Cdd:MTH00007 101 LLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 827490927 163 FPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00007 181 FVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
8.06e-99 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 295.82 E-value: 8.06e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00079 23 FGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSnNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00079 103 FWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHM 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00079 182 SLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
2.37e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 294.82 E-value: 2.37e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00037 22 FGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00037 102 FWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00037 182 PLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
1.93e-97 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 292.88 E-value: 1.93e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00182 24 FGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNIS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00182 104 FWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00182 184 PLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
3.67e-97 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 292.12 E-value: 3.67e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00184 24 FGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNIS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00184 104 FWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00184 184 PLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-214 |
6.67e-87 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 266.11 E-value: 6.67e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 1 FWIWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNIS 80
Cdd:MTH00026 23 FGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNIS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 81 FWLLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQI 160
Cdd:MTH00026 103 FWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827490927 161 PLFPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00026 183 PLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
3-214 |
3.87e-83 |
|
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: 254.38 E-value: 3.87e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 3 IWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPlMMGSPDMAFPRLNNISFW 82
Cdd:cd00919 13 FVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 83 LLPPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQIPL 162
Cdd:cd00919 92 LFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 827490927 163 FPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:cd00919 172 FVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
5-214 |
3.84e-75 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 235.79 E-value: 3.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 5 AGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIvIGGFGNWLIPLMMGSPDMAFPRLNNISFWLL 84
Cdd:COG0843 29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 85 PPSLMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQIPLFP 164
Cdd:COG0843 108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827490927 165 WSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:COG0843 188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
3-214 |
1.38e-69 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 220.70 E-value: 1.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 3 IWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGGFGNWLIPLMMGSPDMAFPRLNNISFW 82
Cdd:MTH00048 25 VWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 83 LLPPSLMMMICSFMInnGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNqIPL 162
Cdd:MTH00048 105 LLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSR-TSI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 827490927 163 FPWSIIITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:MTH00048 182 ILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
8-214 |
4.76e-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: 190.48 E-value: 4.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 8 MGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGgFGNWLIPLMMGSPDMAFPRLNNISFWLLPPS 87
Cdd:cd01662 24 RGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 88 LMMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQIPLFPWSI 167
Cdd:cd01662 103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 827490927 168 IITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:cd01662 183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
3-214 |
2.95e-45 |
|
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: 155.42 E-value: 2.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 3 IWAGMMGSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIvIGGFGNWLIPLMMGSPDMAFPRLNNISFW 82
Cdd:pfam00115 11 LVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 83 LLPPSLMMMICSFMinnGTGTGWTIYPPLsnniahnnISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLnQIPL 162
Cdd:pfam00115 90 LVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 827490927 163 FPWSIIITATLLILSLPVLAGAITMLLTDRNLNTsffdpsGGGDPILYQHLF 214
Cdd:pfam00115 158 FVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
9-214 |
2.48e-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: 142.69 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 9 GSSLSMLIRLELSQINSIINNNQLYNVIVTIHAFIMIFFMTMPIVIGgFGNWLIPLMMGSPDMAFPRLNNISFWLLPPSL 88
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 89 MMMICSFMINNGTGTGWTIYPPLSNNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQIPLFPWSII 168
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 827490927 169 ITATLLILSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 214
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
33-213 |
5.69e-35 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 130.44 E-value: 5.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 33 YNVIVTIHAFIMIFFMTMPIVIGgFGNWLIPLMMGSPDMAFPRLNNISFWLLPPSLMMMICSFMINNGTGTGWTIYPPLS 112
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827490927 113 NNIAHNNISVDLTIFSLHLAGISSILGAINFICTILNMMPNNLKLNQIPLFPWSIIITATLLILSLPVLAGAITMLLTDR 192
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180
....*....|....*....|.
gi 827490927 193 NLNTSFFDPSGGGDPILYQHL 213
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINL 278
|
|
|