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Conserved domains on  [gi|168252795|gb|ACA23083|]
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cytochrome c oxidase subunit I, partial [Mytilus edulis]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-202 6.53e-110

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.


The actual alignment was detected with superfamily member MTH00223:

Pssm-ID: 469701  Cd Length: 512  Bit Score: 323.85  E-value: 6.53e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAvFLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00223  32 LLIRAELGQPGA-LLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00223 111 SSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAF 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00223 191 LLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
 
Name Accession Description Interval E-value
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-202 6.53e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 323.85  E-value: 6.53e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAvFLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00223  32 LLIRAELGQPGA-LLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00223 111 SSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAF 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00223 191 LLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-202 1.83e-105

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: 311.72  E-value: 1.83e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVFLkSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:cd01663   26 LLIRLELSQPGSQLG-NDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:cd01663  105 LSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAF 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:cd01663  185 LLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-202 2.51e-60

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 196.50  E-value: 2.51e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVFLKSDwFFNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:COG0843   38 LLMRLQLAGPGLGLLSPE-TYNQLFTMHGTIMIFFFATPFLAG-FGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:COG0843  116 ISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSI 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:COG0843  196 LILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-202 2.59e-35

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: 128.46  E-value: 2.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795    1 LMIRMQLGHPGAVFLKSDwFFNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:pfam00115  22 LLIRLQLAFPGLNFLSPL-TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   81 LSFStdkGVGAGWTVYPPLssypyhsgPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMkGERAELYVLSISITAA 160
Cdd:pfam00115 100 ASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-TLRMPLFVWAILATAI 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 168252795  161 LLIISIPVLGGGITMILFDRNFNttffdpAGGGDPVLFQHLF 202
Cdd:pfam00115 168 LILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
 
Name Accession Description Interval E-value
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-202 6.53e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 323.85  E-value: 6.53e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAvFLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00223  32 LLIRAELGQPGA-LLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00223 111 SSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAF 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00223 191 LLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-202 1.83e-105

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: 311.72  E-value: 1.83e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVFLkSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:cd01663   26 LLIRLELSQPGSQLG-NDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:cd01663  105 LSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAF 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:cd01663  185 LLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-202 3.98e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 288.31  E-value: 3.98e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAvFLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00153  33 LLIRAELGQPGS-LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00153 112 SSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAI 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00153 192 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-202 1.69e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 263.88  E-value: 1.69e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAvFLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00116  35 LLIRAELGQPGT-LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00116 114 ASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAV 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00116 194 LLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-202 6.09e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 262.31  E-value: 6.09e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVfLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00167  35 LLIRAELSQPGSL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00167 114 ASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTI 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00167 194 LLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-202 1.89e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 256.19  E-value: 1.89e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAvFLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00142  33 LLIRAELGQPGS-LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00142 112 SSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAI 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00142 192 LLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-202 6.80e-79

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 244.43  E-value: 6.80e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAvFLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00007  32 LLIRIELGQPGA-FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00007 111 SSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVV 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00007 191 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-202 3.39e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 237.53  E-value: 3.39e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVfLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00077  35 LLIRAELSQPGTL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00077 114 ASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAV 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00077 194 LLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-202 3.95e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 236.89  E-value: 3.95e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGaVFLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00079  36 LIIRLELSKPG-LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLIL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPyHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00079 115 DSCFVDMGPGTSWTVYPPLSTLG-HPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVF 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00079 194 LLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-202 1.14e-74

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 233.62  E-value: 1.14e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVfLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00103  35 LLIRAELGQPGTL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00103 114 ASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAV 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00103 194 LLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-202 1.74e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 233.17  E-value: 1.74e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVfLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00182  37 MLIRLELSAPGAM-LGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00182 116 GSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAF 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00182 196 LLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-202 3.16e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 232.51  E-value: 3.16e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVfLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00183  35 LLIRAELSQPGAL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00183 114 ASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAV 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00183 194 LLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-202 1.64e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 230.48  E-value: 1.64e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVfLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00184  37 MLIRLELSAPGSM-LGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00184 116 GSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTF 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00184 196 LLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-202 1.68e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 230.49  E-value: 1.68e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   2 MIRMQLGHPGAvFLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLML 81
Cdd:MTH00037  36 IIRTELAQPGS-LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  82 SFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAAL 161
Cdd:MTH00037 115 SAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFL 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 168252795 162 LIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00037 195 LLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-202 3.24e-68

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: 215.47  E-value: 3.24e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVFLKSDwFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLvGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:cd00919   24 LLIRLELATPGSLFLDPQ-LYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-GARDLAFPRLNNLSFWLFPPGLLLLL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:cd00919  102 SSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAI 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:cd00919  182 LLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-202 8.32e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 213.72  E-value: 8.32e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVfLKSDWFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00026  36 MLIRLELSSPGSM-LGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00026 115 GSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAI 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00026 195 LLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-202 2.51e-60

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 196.50  E-value: 2.51e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVFLKSDwFFNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:COG0843   38 LLMRLQLAGPGLGLLSPE-TYNQLFTMHGTIMIFFFATPFLAG-FGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:COG0843  116 ISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSI 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:COG0843  196 LILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-202 1.46e-57

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 188.73  E-value: 1.46e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVFLKSDwFFNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:MTH00048  36 LLIRLNFLDPYYNVISLD-VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFStdKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTnKNMPALEMKGERAELYVLSISITAA 160
Cdd:MTH00048 115 LSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICT-IYSAFMTNVFSRTSIILWSYLFTSI 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:MTH00048 192 LLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-202 1.46e-48

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: 165.06  E-value: 1.46e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   1 LMIRMQLGHPGAVFLKSDwFFNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:cd01662   30 LLMRTQLALPGNDFLSPE-HYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLN 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  81 LSFSTDKGVGAGWTVYPPLSSYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAA 160
Cdd:cd01662  108 ASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSI 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 168252795 161 LLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 202
Cdd:cd01662  188 LILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-202 2.59e-35

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: 128.46  E-value: 2.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795    1 LMIRMQLGHPGAVFLKSDwFFNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLM 80
Cdd:pfam00115  22 LLIRLQLAFPGLNFLSPL-TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795   81 LSFStdkGVGAGWTVYPPLssypyhsgPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMkGERAELYVLSISITAA 160
Cdd:pfam00115 100 ASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-TLRMPLFVWAILATAI 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 168252795  161 LLIISIPVLGGGITMILFDRNFNttffdpAGGGDPVLFQHLF 202
Cdd:pfam00115 168 LILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 21-201 2.23e-25

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 102.71  E-value: 2.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795  21 FNVVVTTHALMMIFFAVMPILIGAFgNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTVYPPLS 100
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIGLM-NLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168252795 101 SYPYHSGPSMDVLIVGLHLAGVSSLVGAINFASTNKNMPALEMKGERAELYVLSISITAALLIISIPVLGGGITMILFDR 180
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180
                 ....*....|....*....|.
gi 168252795 181 NFNTTFFDPAGGGDPVLFQHL 201
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINL 278
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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