|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
9.69e-123 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 356.49 E-value: 9.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00153 28 GTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00153 108 TLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00153 188 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-206 |
7.42e-118 |
|
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: 343.31 E-value: 7.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:cd01663 21 GTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:cd01663 101 LLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:cd01663 181 ITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-206 |
2.93e-65 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 209.60 E-value: 2.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFmIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:COG0843 33 GGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:COG0843 112 LLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAAL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:COG0843 192 VTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-206 |
1.74e-39 |
|
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: 139.63 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFmIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:pfam00115 17 GGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTfinNGAGTGWTVYPPLssnifhsgPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMeKIPLLVWSIL 160
Cdd:pfam00115 96 VLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAIL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTtffdpsGGGDPILYQHLF 206
Cdd:pfam00115 164 ATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-206 |
1.11e-33 |
|
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: 126.51 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGgFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
9.69e-123 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 356.49 E-value: 9.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00153 28 GTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00153 108 TLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00153 188 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-206 |
7.42e-118 |
|
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: 343.31 E-value: 7.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:cd01663 21 GTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:cd01663 101 LLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:cd01663 181 ITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
7.66e-107 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 316.23 E-value: 7.66e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00167 30 GTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00167 110 LLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSIL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00167 190 VTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
9.90e-106 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 313.57 E-value: 9.90e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00116 30 GTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00116 110 LLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00116 190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
1.22e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 310.37 E-value: 1.22e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00223 27 GTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00223 107 YLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVK 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00223 187 VTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
7.33e-103 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 305.88 E-value: 7.33e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00142 28 GTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00142 108 LLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVK 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00142 188 ITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-206 |
4.05e-95 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 286.03 E-value: 4.05e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00007 27 GTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00007 107 ILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00007 187 ITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
1.99e-92 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 279.52 E-value: 1.99e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00077 30 GTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00077 110 LLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00077 190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
4.42e-92 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 278.73 E-value: 4.42e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00183 30 GTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00183 110 LLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00183 190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-206 |
1.39e-91 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 277.15 E-value: 1.39e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00103 30 GTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00103 110 LLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00103 190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
1.97e-91 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 276.71 E-value: 1.97e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00037 30 GTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00037 110 LLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVF 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00037 190 ITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
2.35e-88 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 269.00 E-value: 2.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00184 32 GTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00184 112 TLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSIL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00184 192 VTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
3.97e-88 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 268.61 E-value: 3.97e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00182 32 GTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00182 112 ILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSIL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00182 192 ITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
1.39e-85 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 261.54 E-value: 1.39e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00079 31 GTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSnIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00079 111 FLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVF 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00079 190 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
1.28e-80 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 249.55 E-value: 1.28e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00026 31 GTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:MTH00026 111 FLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVF 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00026 191 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-206 |
5.74e-74 |
|
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: 230.50 E-value: 5.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPlMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:cd00919 19 GGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:cd00919 98 LLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:cd00919 178 VTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-206 |
2.93e-65 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 209.60 E-value: 2.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFmIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:COG0843 33 GGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:COG0843 112 LLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAAL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:COG0843 192 VTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
2.62e-62 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 201.44 E-value: 2.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:MTH00048 31 GLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFInnGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSmEKIPLLVWSIL 160
Cdd:MTH00048 111 VFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:MTH00048 188 FTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-206 |
4.65e-53 |
|
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: 177.00 E-value: 4.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSC-NSLLHNDQiYNSIVTGHAFIMIFFMVMPFMIGgFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPS 79
Cdd:cd01662 25 GGVDALLMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 80 IFLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSI 159
Cdd:cd01662 103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 313176806 160 LITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
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 ... |
1-206 |
1.74e-39 |
|
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: 139.63 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFmIGGFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:pfam00115 17 GGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTfinNGAGTGWTVYPPLssnifhsgPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMeKIPLLVWSIL 160
Cdd:pfam00115 96 VLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAIL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTtffdpsGGGDPILYQHLF 206
Cdd:pfam00115 164 ATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-206 |
1.11e-33 |
|
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: 126.51 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 1 GASMSMIIRLELGSCNSLLHNDQIYNSIVTGHAFIMIFFMVMPFMIGgFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSI 80
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 81 FLLLMSTFINNGAGTGWTVYPPLSSNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSIL 160
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313176806 161 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPSGGGDPILYQHLF 206
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
25-205 |
5.24e-32 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 121.58 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 25 YNSIVTGHAFIMIFFMVMPFMIGgFGNFLVPLMLGAPDMAYPRMNNMSFWLLPPSIFLLLMSTFINNGAGTGWTVYPPLS 104
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313176806 105 SNIFHSGPSVDLTIFSLHIAGASSIMGAINFIATIINMHQSQLSMEKIPLLVWSILITAILLLLSLPVLAGAITMLLTDR 184
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180
....*....|....*....|.
gi 313176806 185 NFNTTFFDPSGGGDPILYQHL 205
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINL 278
|
|
|