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Conserved domains on  [gi|893665615|gb|AKQ96041|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Mymaridae sp. CNRME4278-12]

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 ...
 1-151 7.26e-60

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: 192.78  E-value: 7.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00153  68 VMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFS 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00153 148 LHLAGISSILGAINFITTIINMRSkgMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 220
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-151 7.26e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 192.78  E-value: 7.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00153  68 VMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFS 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00153 148 LHLAGISSILGAINFITTIINMRSkgMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 220
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-151 4.17e-57

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: 184.99  E-value: 4.17e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:cd01663   61 VMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFS 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:cd01663  141 LHLAGISSILGAINFITTIFNMRApgMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 213
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-151 6.01e-30

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 112.91  E-value: 6.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   5 MLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFSLHIA 84
Cdd:COG0843   76 FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALF 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 893665615  85 GISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:COG0843  156 GVGSILGGVNFIVTILKMRApgMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDP 224
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-151 1.27e-15

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: 72.61  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615    5 MLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSgtgTGWTVYPPLssnlshngGSVDLSIFSLHIA 84
Cdd:pfam00115  60 FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFGGAT---TGWTEYPPL--------VGVDLWYIGLLLA 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 893665615   85 GISSIMGSINFISTICNMKILKFDM-IYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:pfam00115 129 GVSSLLGAINFIVTILKRRAPGMTLrMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 8-149 3.29e-12

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 62.95  E-value: 3.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615    8 GFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFSLHIAGIS 87
Cdd:TIGR02882 114 GLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIG 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 893665615   88 SIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFF 149
Cdd:TIGR02882 194 TLMTGINFFVTILKMRApgMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFF 257
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-151 7.26e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 192.78  E-value: 7.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00153  68 VMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFS 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00153 148 LHLAGISSILGAINFITTIINMRSkgMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 220
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-151 4.17e-57

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: 184.99  E-value: 4.17e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:cd01663   61 VMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFS 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:cd01663  141 LHLAGISSILGAINFITTIFNMRApgMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 213
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-151 1.55e-55

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 181.41  E-value: 1.55e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00167  70 VMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFS 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKILKFDM--IYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00167 150 LHLAGVSSILGSINFITTIINMKPPGITQyqTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDP 222
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-151 1.93e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 173.24  E-value: 1.93e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00223  67 VMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFS 146

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNM--KILKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00223 147 LHLAGVSSILGAINFITTIINMrsPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 219
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-151 8.50e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 171.45  E-value: 8.50e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00142  68 VMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFS 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00142 148 LHLAGVSSILGAINFITTVINMRAggMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDP 220
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-151 1.64e-51

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 171.04  E-value: 1.64e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00116  70 VMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFS 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKILKFDM--IYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00116 150 LHLAGVSSILGAINFITTCINMKPPAMSQyqTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-151 3.98e-48

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 161.99  E-value: 3.98e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00007  67 VMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFS 146

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00007 147 LHLAGVSSILGAINFITTVINMRWkgLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDP 219
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-151 2.53e-47

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 160.00  E-value: 2.53e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00037  70 VMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFS 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00037 150 LHLAGASSILASINFITTIINMRTpgMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDP 222
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-151 2.51e-45

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 154.70  E-value: 2.51e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00183  70 VMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFS 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMK--ILKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00183 150 LHLAGVSSILGAINFITTIINMKppAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-151 1.81e-44

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 152.34  E-value: 1.81e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00103  70 VMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFS 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMK--ILKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00103 150 LHLAGVSSILGAINFITTIINMKppAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-151 4.50e-44

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 151.25  E-value: 4.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00077  70 VMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFS 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKILKFDMIY--LFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00077 150 LHLAGVSSILGAINFITTSINMKPPSMSQYQtpLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-151 2.58e-43

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 149.59  E-value: 2.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00182  72 VMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFS 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00182 152 LHLAGVSSILGAINFITTIFNMRApgVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDP 224
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-151 3.08e-43

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 149.21  E-value: 3.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00184  72 VMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFS 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00184 152 LHLAGISSILGAMNFITTIFNMRApgITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDP 224
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-151 3.64e-42

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 145.98  E-value: 3.64e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSnLSHNGGSVDLSIFS 80
Cdd:MTH00079  71 VMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFS 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNM--KILKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00079 150 LHCAGISSILGGINFMVTTKNLrsSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDP 222
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-151 6.27e-38

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 135.14  E-value: 6.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:MTH00026  71 VMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFS 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMKILKFDM--IYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00026 151 LHLAGLSSILGAMNFITTVMNMRTPGMTMsrIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDP 223
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-151 7.87e-34

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: 123.02  E-value: 7.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   1 VMPVMLGGFGNFLIPMmLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFS 80
Cdd:cd00919   59 VMPAIFGGFGNLLPPL-IGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILG 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893665615  81 LHIAGISSIMGSINFISTICNMK--ILKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:cd00919  138 LHLAGVSSILGAINFITTILNMRapGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDP 210
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-151 1.12e-30

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 115.16  E-value: 1.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   2 MPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGtgWTVYPPLSSNLSHNGGSVDLSIFSL 81
Cdd:MTH00048  72 MPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAGVG--WTFYPPLSSSLFSSSWGVDFLMFSL 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 893665615  82 HIAGISSIMGSINFISTICNMKILKFDM-IYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:MTH00048 150 HLAGVSSLFGSINFICTIYSAFMTNVFSrTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDP 220
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-151 6.01e-30

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 112.91  E-value: 6.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   5 MLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFSLHIA 84
Cdd:COG0843   76 FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALF 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 893665615  85 GISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:COG0843  156 GVGSILGGVNFIVTILKMRApgMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDP 224
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-151 1.05e-21

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: 89.95  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   2 MPVMLGgFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFSL 81
Cdd:cd01662   66 MPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGL 144

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 893665615  82 HIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:cd01662  145 QFSGIGTLLGAINFIVTILKMRApgMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTN 216
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-151 1.27e-15

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: 72.61  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615    5 MLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSgtgTGWTVYPPLssnlshngGSVDLSIFSLHIA 84
Cdd:pfam00115  60 FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFGGAT---TGWTEYPPL--------VGVDLWYIGLLLA 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 893665615   85 GISSIMGSINFISTICNMKILKFDM-IYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 151
Cdd:pfam00115 129 GVSSLLGAINFIVTILKRRAPGMTLrMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-149 5.66e-15

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 70.73  E-value: 5.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615   2 MPVMLGgFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFSL 81
Cdd:PRK15017 116 MPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSL 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615  82 HIAGISSIMGSINFISTICNMKILKFDMIYL--FVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFF 149
Cdd:PRK15017 195 QLSGIGTTLTGINFFVTILKMRAPGMTMFKMpvFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFF 264
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 8-149 3.29e-12

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 62.95  E-value: 3.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665615    8 GFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSVDLSIFSLHIAGIS 87
Cdd:TIGR02882 114 GLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIG 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 893665615   88 SIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFF 149
Cdd:TIGR02882 194 TLMTGINFFVTILKMRApgMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFF 257
 
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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