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Conserved domains on  [gi|943430143|gb|ALK67394|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Cardiophorus convexus]

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 ...
 1-116 6.83e-71

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 MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 219.74  E-value: 6.83e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00153 110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00153 190 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 225
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-116 6.83e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 219.74  E-value: 6.83e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00153 110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00153 190 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 225
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-116 1.16e-62

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: 197.71  E-value: 1.16e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:cd01663  103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:cd01663  183 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGD 218
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-116 6.19e-37

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 130.63  E-value: 6.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENG-AGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVI 79
Cdd:COG0843  113 LLLISLFVGGaADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALV 192

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 943430143  80 TALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:COG0843  193 TSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGD 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 9-112 2.71e-17

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: 75.69  E-value: 2.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143    9 NGAGTGWTVYPPLSAniahsgssVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFeRMPLFIWAVVITALLLLLSL 88
Cdd:pfam00115 103 GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173

                          90       100
                  ....*....|....*....|....
gi 943430143   89 PVLAGAITMLLTDRNLNTSFFDPA 112
Cdd:pfam00115 174 PVLAAALLLLLLDRSLGAGGGDPL 197
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-116 6.83e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 219.74  E-value: 6.83e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00153 110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00153 190 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 225
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-116 1.16e-62

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: 197.71  E-value: 1.16e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:cd01663  103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:cd01663  183 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGD 218
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-116 6.16e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 186.08  E-value: 6.16e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00142 110 LLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKIT 189

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00142 190 AILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGD 225
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-116 1.19e-57

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 185.57  E-value: 1.19e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00223 109 LLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVT 188

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00223 189 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGD 224
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-116 1.35e-57

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 185.27  E-value: 1.35e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00167 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVT 191

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00167 192 TILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGD 227
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-116 9.41e-55

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 177.98  E-value: 9.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00116 112 LLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLIT 191

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00116 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGD 227
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-116 3.82e-53

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 173.55  E-value: 3.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00007 109 LVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVIT 188

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00007 189 VVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 224
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-116 6.77e-49

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 162.68  E-value: 6.77e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00182 114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILIT 193

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00182 194 AFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGD 229
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-116 7.03e-49

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 162.31  E-value: 7.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00037 112 LLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFIT 191

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00037 192 AFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGD 227
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-116 1.91e-48

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 161.53  E-value: 1.91e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00184 114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVT 193

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00184 194 TFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGD 229
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-116 7.46e-48

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 159.70  E-value: 7.46e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00183 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLIT 191

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00183 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGD 227
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-116 1.20e-47

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 159.28  E-value: 1.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00103 112 LLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLIT 191

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00103 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGD 227
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-116 2.02e-47

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 158.57  E-value: 2.02e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00077 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLIT 191

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00077 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGD 227
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-116 3.53e-46

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 155.22  E-value: 3.53e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSaNIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00079 113 ILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVT 191

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00079 192 VFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGN 227
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-116 1.41e-44

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 151.32  E-value: 1.41e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:MTH00026 113 LLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFIT 192

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00026 193 AILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGD 228
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-116 2.89e-41

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: 141.51  E-value: 2.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:cd00919  100 LLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVT 179

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:cd00919  180 AILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGD 215
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-116 6.19e-37

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 130.63  E-value: 6.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENG-AGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVI 79
Cdd:COG0843  113 LLLISLFVGGaADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALV 192

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 943430143  80 TALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:COG0843  193 TSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGD 229
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 10-116 1.30e-30

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 113.23  E-value: 1.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143  10 GAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMtFERMPLFIWAVVITALLLLLSLP 89
Cdd:MTH00048 120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLP 198

                         90       100
                 ....*....|....*....|....*..
gi 943430143  90 VLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLGGGD 225
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-116 3.69e-27

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: 103.81  E-value: 3.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143   1 L*MSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVIT 80
Cdd:cd01662  106 LNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVT 185

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 943430143  81 ALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:cd01662  186 SILILFAFPVLTAALALLELDRYFGTHFFTNALGGN 221
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 11-116 5.71e-18

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 78.05  E-value: 5.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143  11 AGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFERMPLFIWAVVITALLLLLSLPV 90
Cdd:PRK15017 166 AQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPI 245

                         90       100
                 ....*....|....*....|....*.
gi 943430143  91 LAGAITMLLTDRNLNTSFFDPAGGGD 116
Cdd:PRK15017 246 LTVTVALLTLDRYLGTHFFTNDMGGN 271
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 9-112 2.71e-17

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: 75.69  E-value: 2.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943430143    9 NGAGTGWTVYPPLSAniahsgssVDLAIFSLHLAGISSILGAVNFISTVINMRSTGMTFeRMPLFIWAVVITALLLLLSL 88
Cdd:pfam00115 103 GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173

                          90       100
                  ....*....|....*....|....
gi 943430143   89 PVLAGAITMLLTDRNLNTSFFDPA 112
Cdd:pfam00115 174 PVLAAALLLLLLDRSLGAGGGDPL 197
 
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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