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Conserved domains on  [gi|1503023904|gb|AYP48610|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Diapriidae sp. BIOUG13496-D11]

Protein Classification

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 ...
 2-99 9.46e-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.


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 140.00  E-value: 9.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:MTH00153  120 AGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPV 199

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:MTH00153  200 LAGAITMLLTDRNLNTSF 217
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-99 9.46e-41

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 140.00  E-value: 9.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:MTH00153  120 AGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPV 199

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:MTH00153  200 LAGAITMLLTDRNLNTSF 217
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-99 2.80e-40

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: 138.38  E-value: 2.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:cd01663   113 AGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPV 192

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:cd01663   193 LAGAITMLLTDRNFNTSF 210
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-99 4.60e-23

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 91.34  E-value: 4.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:COG0843   124 ADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPV 203

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:COG0843   204 LAAALLLLLLDRSLGTHF 221
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-97 7.72e-12

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: 59.51  E-value: 7.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLsnnlfhsnMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMnKISLFSWSILLTSILLLLLLPV 81
Cdd:pfam00115 105 ATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPV 175

                          90
                  ....*....|....*.
gi 1503023904  82 LAGAITMLLFDRNMNT 97
Cdd:pfam00115 176 LAAALLLLLLDRSLGA 191
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-99 9.46e-41

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 140.00  E-value: 9.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:MTH00153  120 AGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPV 199

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:MTH00153  200 LAGAITMLLTDRNLNTSF 217
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-99 2.80e-40

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: 138.38  E-value: 2.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:cd01663   113 AGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPV 192

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:cd01663   193 LAGAITMLLTDRNFNTSF 210
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 3-99 8.13e-37

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 129.41  E-value: 8.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   3 GTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPVL 82
Cdd:MTH00167  123 GTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVL 202

                          90
                  ....*....|....*..
gi 1503023904  83 AGAITMLLFDRNMNTSF 99
Cdd:MTH00167  203 AAAITMLLTDRNLNTTF 219
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-99 2.48e-36

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 128.17  E-value: 2.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:MTH00223  119 VGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPV 198

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:MTH00223  199 LAGAITMLLTDRNFNTSF 216
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-99 1.32e-33

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 120.60  E-value: 1.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:MTH00142  120 AGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPV 199

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:MTH00142  200 LAGAITMLLTDRNFNTSF 217
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 3-99 1.31e-32

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 117.89  E-value: 1.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   3 GTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPVL 82
Cdd:MTH00116  123 GTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVL 202

                          90
                  ....*....|....*..
gi 1503023904  83 AGAITMLLFDRNMNTSF 99
Cdd:MTH00116  203 AAGITMLLTDRNLNTTF 219
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 3-99 2.44e-31

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 114.61  E-value: 2.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   3 GTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPVL 82
Cdd:MTH00007  120 GTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVL 199

                          90
                  ....*....|....*..
gi 1503023904  83 AGAITMLLFDRNMNTSF 99
Cdd:MTH00007  200 AGAITMLLTDRNLNTSF 216
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 3-99 8.32e-30

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 110.30  E-value: 8.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   3 GTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPVL 82
Cdd:MTH00037  123 GTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVL 202

                          90
                  ....*....|....*..
gi 1503023904  83 AGAITMLLFDRNMNTSF 99
Cdd:MTH00037  203 AGAITMLLTDRNINTTF 219
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-99 4.99e-29

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 108.23  E-value: 4.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNnLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:MTH00079  123 PGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPV 201

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:MTH00079  202 LAGAITMLLTDRNLNTSF 219
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-99 8.35e-29

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 107.60  E-value: 8.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:MTH00184  124 AGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPV 203

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:MTH00184  204 LAGAITMLLTDRNFNTTF 221
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-99 1.71e-28

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 106.55  E-value: 1.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:MTH00183  122 AGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPV 201

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:MTH00183  202 LAAGITMLLTDRNLNTTF 219
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 3-99 3.69e-28

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 105.67  E-value: 3.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   3 GTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPVL 82
Cdd:MTH00182  125 GTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVL 204

                          90
                  ....*....|....*..
gi 1503023904  83 AGAITMLLFDRNMNTSF 99
Cdd:MTH00182  205 AGAITMLLTDRNFNTTF 221
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-99 7.94e-28

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 104.96  E-value: 7.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:MTH00103  122 AGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPV 201

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:MTH00103  202 LAAGITMLLTDRNLNTTF 219
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-99 1.79e-27

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 103.87  E-value: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:MTH00077  122 AGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPV 201

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:MTH00077  202 LAAGITMLLTDRNLNTTF 219
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-99 2.75e-27

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: 102.99  E-value: 2.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:cd00919   110 AGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPV 189

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:cd00919   190 LAAALVMLLLDRNFGTSF 207
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-99 2.18e-25

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 98.16  E-value: 2.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:MTH00026  123 AGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPV 202

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:MTH00026  203 LAGAITMLLTDRNFNTTF 220
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-99 4.60e-23

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 91.34  E-value: 4.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPV 81
Cdd:COG0843   124 ADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPV 203

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:COG0843   204 LAAALLLLLLDRSLGTHF 221
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-99 3.14e-22

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 88.97  E-value: 3.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMkMNKISLFSWSILLTSILLLLLLPV 81
Cdd:MTH00048  121 AGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLPV 199

                          90
                  ....*....|....*...
gi 1503023904  82 LAGAITMLLFDRNMNTSF 99
Cdd:MTH00048  200 LAAAITMLLFDRNFGSAF 217
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 4-99 9.33e-18

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: 76.47  E-value: 9.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   4 TGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPVLA 83
Cdd:cd01662   118 AGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLT 197

                          90
                  ....*....|....*.
gi 1503023904  84 GAITMLLFDRNMNTSF 99
Cdd:cd01662   198 AALALLELDRYFGTHF 213
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 4-99 6.11e-14

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 65.73  E-value: 6.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   4 TGWTIYPPLSNNLFHSNMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMNKISLFSWSILLTSILLLLLLPVLA 83
Cdd:PRK15017  168 TGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILT 247

                          90
                  ....*....|....*.
gi 1503023904  84 GAITMLLFDRNMNTSF 99
Cdd:PRK15017  248 VTVALLTLDRYLGTHF 263
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-97 7.72e-12

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: 59.51  E-value: 7.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503023904   2 SGTGWTIYPPLsnnlfhsnMSVDLTIFSLHIAGISSIMGSINTISSIIKIRSKPMKMnKISLFSWSILLTSILLLLLLPV 81
Cdd:pfam00115 105 ATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPV 175

                          90
                  ....*....|....*.
gi 1503023904  82 LAGAITMLLFDRNMNT 97
Cdd:pfam00115 176 LAAALLLLLLDRSLGA 191
 
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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