|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-215 |
8.02e-131 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 377.67 E-value: 8.02e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 1 MLYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPR 80
Cdd:MTH00153 15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 81 MNNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLF 160
Cdd:MTH00153 95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 229425702 161 IMDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 229
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-215 |
9.41e-121 |
|
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: 351.01 E-value: 9.41e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 1 MLYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPR 80
Cdd:cd01663 8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 81 MNNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLF 160
Cdd:cd01663 88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 229425702 161 IMDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:cd01663 168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILY 222
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-215 |
3.35e-64 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 207.29 E-value: 3.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 1 MLYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPvMIGGFGNWLIPLMLGAPDMSFPR 80
Cdd:COG0843 20 IMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 81 MNNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLF 160
Cdd:COG0843 99 LNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 229425702 161 IMDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:COG0843 179 TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLW 233
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-215 |
8.55e-36 |
|
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: 130.39 E-value: 8.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 1 MLYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPvMIGGFGNWLIPLMLGAPDMSFPR 80
Cdd:pfam00115 4 LLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 81 MNNMSFWLLIPSLFLLILSGfinVGVGTGWTVYPPLslilghggMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLF 160
Cdd:pfam00115 83 LNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 229425702 161 IMdKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILY 215
Cdd:pfam00115 152 TL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLD 199
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
18-215 |
3.30e-30 |
|
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: 116.88 E-value: 3.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 18 SLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGgFGNWLIPLMLGAPDMSFPRMNNMSFWLLIPSLFLLI 97
Cdd:TIGR02882 72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 98 LSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFIMDKMSLFIWSVFITAI 177
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
|
170 180 190
....*....|....*....|....*....|....*...
gi 229425702 178 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLW 268
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-215 |
8.02e-131 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 377.67 E-value: 8.02e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 1 MLYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPR 80
Cdd:MTH00153 15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 81 MNNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLF 160
Cdd:MTH00153 95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 229425702 161 IMDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 229
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-215 |
9.41e-121 |
|
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: 351.01 E-value: 9.41e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 1 MLYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPR 80
Cdd:cd01663 8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 81 MNNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLF 160
Cdd:cd01663 88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 229425702 161 IMDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:cd01663 168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILY 222
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
2-215 |
3.77e-113 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 332.80 E-value: 3.77e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00167 18 LYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00167 98 NNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGIT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00167 178 QYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILY 231
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
2-215 |
1.47e-109 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 323.47 E-value: 1.47e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00223 15 LYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00223 95 NNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00223 175 LERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILY 228
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
2-215 |
2.25e-108 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 320.50 E-value: 2.25e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00116 18 LYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00116 98 NNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00116 178 QYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILY 231
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
2-215 |
6.02e-106 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 314.35 E-value: 6.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00142 16 LYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00142 96 NNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMK 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00142 176 FERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILY 229
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
2-215 |
5.80e-97 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 291.42 E-value: 5.80e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00007 15 LYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00007 95 NNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00007 175 LERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 228
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
2-215 |
1.57e-96 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 290.19 E-value: 1.57e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00037 18 LYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00037 98 NNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00037 178 FDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILF 231
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
2-215 |
3.59e-94 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 284.08 E-value: 3.59e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00103 18 LYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00103 98 NNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00103 178 QYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILY 231
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
2-215 |
8.98e-94 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 283.35 E-value: 8.98e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00183 18 LYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00183 98 NNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00183 178 QYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILY 231
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
2-215 |
1.02e-93 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 282.98 E-value: 1.02e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00077 18 LYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00077 98 NNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00077 178 QYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLY 231
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
2-215 |
4.71e-91 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 276.70 E-value: 4.71e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00182 20 LYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00182 100 NNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00182 180 FNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILF 233
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
2-215 |
3.62e-90 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 274.01 E-value: 3.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00184 20 LYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00184 100 NNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGIT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00184 180 MDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILY 233
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
2-215 |
1.43e-88 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 269.63 E-value: 1.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00079 19 LYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLiLGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00079 99 NNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00079 178 LEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLY 231
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
2-215 |
5.64e-80 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 248.39 E-value: 5.64e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPRM 81
Cdd:MTH00026 19 LYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:MTH00026 99 NNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00026 179 MSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILY 232
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-215 |
3.44e-72 |
|
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: 226.26 E-value: 3.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 1 MLYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPlMLGAPDMSFPR 80
Cdd:cd00919 6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 81 MNNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLF 160
Cdd:cd00919 85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 229425702 161 IMDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:cd00919 165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLY 219
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-215 |
2.70e-64 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 206.84 E-value: 2.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 1 MLYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGAPDMSFPR 80
Cdd:MTH00048 18 VIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 81 MNNMSFWLLIPSLFLLILSGFInvGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILN-MRVNL 159
Cdd:MTH00048 98 LNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSaFMTNV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 229425702 160 FImdKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:MTH00048 176 FS--RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLF 229
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-215 |
3.35e-64 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 207.29 E-value: 3.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 1 MLYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPvMIGGFGNWLIPLMLGAPDMSFPR 80
Cdd:COG0843 20 IMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 81 MNNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLF 160
Cdd:COG0843 99 LNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 229425702 161 IMDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:COG0843 179 TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLW 233
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-215 |
4.17e-49 |
|
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: 166.99 E-value: 4.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 2 LYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGgFGNWLIPLMLGAPDMSFPRM 81
Cdd:cd01662 13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 82 NNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFI 161
Cdd:cd01662 92 NALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 229425702 162 MDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:cd01662 172 LMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLW 225
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-215 |
8.55e-36 |
|
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: 130.39 E-value: 8.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 1 MLYFLFGLWAGMLGFSMSLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPvMIGGFGNWLIPLMLGAPDMSFPR 80
Cdd:pfam00115 4 LLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 81 MNNMSFWLLIPSLFLLILSGfinVGVGTGWTVYPPLslilghggMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLF 160
Cdd:pfam00115 83 LNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 229425702 161 IMdKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILY 215
Cdd:pfam00115 152 TL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLD 199
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
18-215 |
3.30e-30 |
|
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: 116.88 E-value: 3.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 18 SLIIRLELGMPESLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGgFGNWLIPLMLGAPDMSFPRMNNMSFWLLIPSLFLLI 97
Cdd:TIGR02882 72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 98 LSGFINVGVGTGWTVYPPLSLILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFIMDKMSLFIWSVFITAI 177
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
|
170 180 190
....*....|....*....|....*....|....*...
gi 229425702 178 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 215
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLW 268
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
38-215 |
1.12e-29 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 115.42 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 38 YNSIVTSHAFIMIFFMVMPVMIGgFGNWLIPLMLGAPDMSFPRMNNMSFWLLIPSLFLLILSGFINVGVGTGWTVYPPLS 117
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229425702 118 LILGHGGMSVDMGIFSLHLAGASSIMGAINFITTILNMRVNLFIMDKMSLFIWSVFITAILLLLSLPVLAGAITMLLTDR 197
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170
....*....|....*...
gi 229425702 198 NLNTSFFDPAGGGDPILY 215
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMY 275
|
|
|