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Conserved domains on  [gi|1927969492|gb|QOW17600|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Mytilus trossulus]

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 ...
 1-220 6.08e-120

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: 350.05  E-value: 6.08e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00223   14 TLYLIFGMWSGLVGTSLSLLIRAELGQPGA-LLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00223   93 RLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPG 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00223  173 MQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
 
Name Accession Description Interval E-value
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-220 6.08e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 350.05  E-value: 6.08e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00223   14 TLYLIFGMWSGLVGTSLSLLIRAELGQPGA-LLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00223   93 RLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPG 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00223  173 MQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-220 3.43e-115

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: 337.15  E-value: 3.43e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAVFLkSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLG-NDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:cd01663    87 RLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:cd01663   167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-220 2.55e-62

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 202.66  E-value: 2.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   2 LYLYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPR 81
Cdd:COG0843    21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPE-TYNQLFTMHGTIMIFFFATPFLAG-FGNYLVPLQIGARDMAFPR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  82 MNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEM 161
Cdd:COG0843    99 LNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGM 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1927969492 162 KGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:COG0843   179 TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-220 6.40e-37

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: 133.47  E-value: 6.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   2 LYLYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPR 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPL-TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  82 MNNLSYWLSPNALYLLMLSFStdkGVGAGWTIYPPLsvypyhsgPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEM 161
Cdd:pfam00115  83 LNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1927969492 162 kGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNttffdpAGGGDPVLFQHLF 220
Cdd:pfam00115 152 -TLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
 
Name Accession Description Interval E-value
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-220 6.08e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 350.05  E-value: 6.08e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00223   14 TLYLIFGMWSGLVGTSLSLLIRAELGQPGA-LLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00223   93 RLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPG 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00223  173 MQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-220 3.43e-115

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: 337.15  E-value: 3.43e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAVFLkSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLG-NDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:cd01663    87 RLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:cd01663   167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-220 7.14e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 309.11  E-value: 7.14e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS-LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00153   94 RMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00153  174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-220 2.38e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 285.06  E-value: 2.38e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00116   17 TLYLIFGAWAGMVGTALSLLIRAELGQPGT-LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00116   96 RMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00116  176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-220 4.68e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 281.57  E-value: 4.68e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00167   17 TLYFIFGAWAGMVGTALSLLIRAELSQPGSL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00167   96 RMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPG 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00167  176 ITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-220 4.86e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 271.21  E-value: 4.86e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00142   15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGS-LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00142   94 RMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGG 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00142  174 MKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-220 1.32e-86

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 264.84  E-value: 1.32e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00007   14 TLYFILGVWGGLLGTSMSLLIRIELGQPGA-FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00007   93 RLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKG 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00007  173 LRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-220 1.11e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 257.30  E-value: 1.11e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGaVFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00079   18 TLYFLFGLWSGMVGTSLSLIIRLELSKPG-LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPyHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00079   97 RLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLG-HPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSS 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00079  176 ISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-220 4.94e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 256.02  E-value: 4.94e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00077   17 TLYLVFGAWAGMVGTALSLLIRAELSQPGTL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00077   96 RMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPS 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00077  176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-220 1.73e-81

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 251.73  E-value: 1.73e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00103   17 TLYLLFGAWAGMVGTALSLLIRAELGQPGTL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00103   96 RMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00103  176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-220 8.26e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 250.23  E-value: 8.26e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00183   17 TLYLVFGAWAGMVGTALSLLIRAELSQPGAL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00183   96 RMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00183  176 ISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-220 5.10e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 248.21  E-value: 5.10e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00037   17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGS-LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00037   96 RMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPG 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00037  176 MTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-220 9.35e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 245.12  E-value: 9.35e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00182   19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGAM-LGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00182   98 RLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPG 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00182  178 VTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-220 1.20e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 244.74  E-value: 1.20e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00184   19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGSM-LGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00184   98 RLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPG 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00184  178 ITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-220 2.17e-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: 227.03  E-value: 2.17e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLvGGKDMIYP 80
Cdd:cd00919     6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQ-LYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-GARDLAFP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:cd00919    84 RLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPG 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:cd00919   164 MTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-220 1.26e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 224.51  E-value: 1.26e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   1 TLYLYSGVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYP 80
Cdd:MTH00026   18 SLYLVFGALSGAIGTAFSMLIRLELSSPGSM-LGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  81 RMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLE 160
Cdd:MTH00026   97 RLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPG 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492 161 MKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00026  177 MTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-220 1.20e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 207.99  E-value: 1.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   2 LYLYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPR 81
Cdd:MTH00048   19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLD-VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  82 MNNLSYWLSPNALYLLMLSFStdKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEM 161
Cdd:MTH00048   98 LNALSAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1927969492 162 KGeRAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:MTH00048  176 FS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-220 2.55e-62

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 202.66  E-value: 2.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   2 LYLYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPR 81
Cdd:COG0843    21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPE-TYNQLFTMHGTIMIFFFATPFLAG-FGNYLVPLQIGARDMAFPR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  82 MNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEM 161
Cdd:COG0843    99 LNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGM 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1927969492 162 KGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:COG0843   179 TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-220 2.76e-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: 2.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   2 LYLYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPR 81
Cdd:cd01662    13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPE-HYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  82 MNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEM 161
Cdd:cd01662    91 LNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGM 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1927969492 162 KGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 220
Cdd:cd01662   171 TLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-220 6.40e-37

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: 133.47  E-value: 6.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492   2 LYLYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPR 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPL-TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  82 MNNLSYWLSPNALYLLMLSFStdkGVGAGWTIYPPLsvypyhsgPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEM 161
Cdd:pfam00115  83 LNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1927969492 162 kGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNttffdpAGGGDPVLFQHLF 220
Cdd:pfam00115 152 -TLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 12-219 1.30e-25

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 103.86  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  12 LFGASLSLMIRMQ--LGHPGAVFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFgNWLIPLLVGGKDMIYPRMNNLSYWL 89
Cdd:PRK15017   70 LRGFADAIMMRSQqaLASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLM-NLVVPLQIGARDVAFPFLNNLSFWF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927969492  90 SPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGERAELY 169
Cdd:PRK15017  149 TVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVF 228

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1927969492 170 VLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHL 219
Cdd:PRK15017  229 TWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINL 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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