|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
4.10e-132 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 380.75 E-value: 4.10e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00153 19 IFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00153 99 SFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00153 179 MPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 230
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-212 |
1.10e-123 |
|
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 358.33 E-value: 1.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:cd01663 12 IFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:cd01663 92 SFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEK 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:cd01663 172 MPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 223
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-212 |
1.64e-69 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 221.15 E-value: 1.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:COG0843 24 VTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:COG0843 103 SFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMR 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:COG0843 183 MPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQ 234
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-212 |
4.43e-41 |
|
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: 144.25 E-value: 4.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:pfam00115 8 VTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSitnSGVGTGWTVYPPLAGpiahsgvaVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLdQ 160
Cdd:pfam00115 87 SFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-R 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQ 212
Cdd:pfam00115 155 MPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQ 200
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
10-211 |
7.46e-38 |
|
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: 138.45 E-value: 7.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 10 GTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 89
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 90 MMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQLPLFVWSVM 169
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 338190168 170 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 211
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLW 268
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
4.10e-132 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 380.75 E-value: 4.10e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00153 19 IFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00153 99 SFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00153 179 MPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 230
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-212 |
1.10e-123 |
|
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 358.33 E-value: 1.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:cd01663 12 IFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:cd01663 92 SFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEK 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:cd01663 172 MPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 223
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
3.88e-118 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 345.12 E-value: 3.88e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00167 21 IFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00167 101 SFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00167 181 TPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQ 232
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
5.84e-116 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 339.76 E-value: 5.84e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00116 21 IFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00116 101 SFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00116 181 TPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQ 232
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
9.33e-115 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 336.56 E-value: 9.33e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00223 18 IFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00223 98 SFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLER 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00223 178 LPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 229
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
1.91e-111 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 328.22 E-value: 1.91e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00142 19 LFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00142 99 SFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFER 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00142 179 VPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 230
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
3.42e-105 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 312.53 E-value: 3.42e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00037 21 IFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00037 101 SFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00037 181 LPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQ 232
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
8.15e-103 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 306.10 E-value: 8.15e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00077 21 VFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00077 101 SFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00077 181 TPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQ 232
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-212 |
1.08e-102 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 306.04 E-value: 1.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00103 21 LFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00103 101 SFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00103 181 TPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQ 232
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
3.45e-102 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 304.54 E-value: 3.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00183 21 VFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00183 101 SFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00183 181 TPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQ 232
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
1.65e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 295.58 E-value: 1.65e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00182 23 VFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00182 103 SFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNR 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00182 183 LPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQ 234
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-212 |
2.72e-98 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 294.50 E-value: 2.72e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00007 18 ILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00007 98 SFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLER 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00007 178 IPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 229
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
2.65e-95 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 287.11 E-value: 2.65e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00184 23 LFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00184 103 SFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDR 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00184 183 MPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQ 234
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
2.94e-91 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 276.56 E-value: 2.94e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00079 22 LFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGpIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00079 102 SFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEH 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00079 181 MSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQ 232
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
1.00e-86 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 265.72 E-value: 1.00e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00026 22 VFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:MTH00026 102 SFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00026 182 IPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQ 233
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-212 |
8.78e-79 |
|
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.
Pssm-ID: 238461 Cd Length: 463 Bit Score: 242.82 E-value: 8.78e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPlMIGAPDMAFPRMNNM 80
Cdd:cd00919 10 IFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:cd00919 89 SFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:cd00919 169 MPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQ 220
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-212 |
1.64e-69 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 221.15 E-value: 1.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:COG0843 24 VTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQ 160
Cdd:COG0843 103 SFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMR 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:COG0843 183 MPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQ 234
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-212 |
1.93e-59 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 194.13 E-value: 1.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:MTH00048 22 LLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSITnsGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLdQ 160
Cdd:MTH00048 102 SAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-R 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:MTH00048 179 TSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQ 230
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
8-212 |
7.40e-56 |
|
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: 184.71 E-value: 7.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 8 IMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 87
Cdd:cd01662 23 LRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 88 SLMMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQLPLFVWS 167
Cdd:cd01662 102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 338190168 168 VMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 212
Cdd:cd01662 182 TLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQ 226
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-212 |
4.43e-41 |
|
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: 144.25 E-value: 4.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 1 IFGAWAGIMGTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNM 80
Cdd:pfam00115 8 VTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 81 SFWLLPPSLMMLLSSSitnSGVGTGWTVYPPLAGpiahsgvaVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLdQ 160
Cdd:pfam00115 87 SFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-R 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338190168 161 LPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQ 212
Cdd:pfam00115 155 MPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQ 200
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
10-211 |
7.46e-38 |
|
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: 138.45 E-value: 7.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 10 GTALSMMIRMELSTPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 89
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 90 MMLLSSSITNSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQLPLFVWSVM 169
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 338190168 170 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 211
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLW 268
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
34-211 |
1.09e-33 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 126.59 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 34 YNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLMMLLSSSITNSGVGTGWTVYPPLA 113
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338190168 114 GPIAHSGVAVDLAIFSLHLAGASSILGAINFITTIINMRAPEMKLDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDR 193
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170
....*....|....*...
gi 338190168 194 NLNTSFFDPAGGGDPILY 211
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMY 275
|
|
|