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Conserved domains on  [gi|2447729415|gb|WDQ54084|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Chalcididae sp.]

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 ...
2-101 1.85e-40

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: 139.23  E-value: 1.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   2 STDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKIYKM--EIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDR 79
Cdd:MTH00153  132 SNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMtlDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDR 211
                          90       100
                  ....*....|....*....|..
gi 2447729415  80 NFNTS*FDPMGGGDPILYQHLF 101
Cdd:MTH00153  212 NLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
2-101 1.85e-40

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 139.23  E-value: 1.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   2 STDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKIYKM--EIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDR 79
Cdd:MTH00153  132 SNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMtlDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDR 211
                          90       100
                  ....*....|....*....|..
gi 2447729415  80 NFNTS*FDPMGGGDPILYQHLF 101
Cdd:MTH00153  212 NLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
2-101 3.89e-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: 138.00  E-value: 3.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   2 STDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKI--YKMEIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDR 79
Cdd:cd01663   125 SILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRApgMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDR 204
                          90       100
                  ....*....|....*....|..
gi 2447729415  80 NFNTS*FDPMGGGDPILYQHLF 101
Cdd:cd01663   205 NFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-101 8.35e-22

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 87.88  E-value: 8.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   2 STDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKI--YKMEIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDR 79
Cdd:COG0843   136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRApgMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDR 215
                          90       100
                  ....*....|....*....|..
gi 2447729415  80 NFNTS*FDPMGGGDPILYQHLF 101
Cdd:COG0843   216 SLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
11-101 3.12e-11

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: 57.97  E-value: 3.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415  11 VDLSIFSLHMAGISSIMGSINFISTILNMKIYKMEI-ISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRNFNTs*fdpm 89
Cdd:pfam00115 118 VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLrMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------ 191
                          90
                  ....*....|..
gi 2447729415  90 GGGDPILYQHLF 101
Cdd:pfam00115 192 GGGDPLLDQHLF 203
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
2-101 1.85e-40

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 139.23  E-value: 1.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   2 STDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKIYKM--EIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDR 79
Cdd:MTH00153  132 SNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMtlDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDR 211
                          90       100
                  ....*....|....*....|..
gi 2447729415  80 NFNTS*FDPMGGGDPILYQHLF 101
Cdd:MTH00153  212 NLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
2-101 3.89e-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: 138.00  E-value: 3.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   2 STDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKI--YKMEIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDR 79
Cdd:cd01663   125 SILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRApgMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDR 204
                          90       100
                  ....*....|....*....|..
gi 2447729415  80 NFNTS*FDPMGGGDPILYQHLF 101
Cdd:cd01663   205 NFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
5-101 1.08e-37

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 131.72  E-value: 1.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   5 GHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKI--YKMEIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRNFN 82
Cdd:MTH00167  137 AHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPpgITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLN 216
                          90
                  ....*....|....*....
gi 2447729415  83 TS*FDPMGGGDPILYQHLF 101
Cdd:MTH00167  217 TTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
2-101 8.43e-37

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 129.33  E-value: 8.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   2 STDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNM--KIYKMEIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDR 79
Cdd:MTH00223  131 SNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMrsPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDR 210
                          90       100
                  ....*....|....*....|..
gi 2447729415  80 NFNTS*FDPMGGGDPILYQHLF 101
Cdd:MTH00223  211 NFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
5-101 2.95e-34

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 122.52  E-value: 2.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   5 GHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKI--YKMEIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRNFN 82
Cdd:MTH00142  135 AHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAggMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFN 214
                          90
                  ....*....|....*....
gi 2447729415  83 TS*FDPMGGGDPILYQHLF 101
Cdd:MTH00142  215 TSFFDPAGGGDPILYQHLF 233
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
6-101 8.56e-33

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 118.66  E-value: 8.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   6 HLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKIYKMEI--ISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRNFNT 83
Cdd:MTH00116  138 HAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQyqTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217
                          90
                  ....*....|....*...
gi 2447729415  84 S*FDPMGGGDPILYQHLF 101
Cdd:MTH00116  218 TFFDPAGGGDPILYQHLF 235
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
6-101 3.04e-31

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 114.23  E-value: 3.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   6 HLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKI--YKMEIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRNFNT 83
Cdd:MTH00007  135 HAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWkgLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNT 214
                          90
                  ....*....|....*...
gi 2447729415  84 S*FDPMGGGDPILYQHLF 101
Cdd:MTH00007  215 SFFDPAGGGDPILYQHLF 232
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
2-101 1.22e-30

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 112.61  E-value: 1.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   2 STDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKI--YKMEIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDR 79
Cdd:MTH00184  136 SIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRApgITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDR 215
                          90       100
                  ....*....|....*....|..
gi 2447729415  80 NFNTS*FDPMGGGDPILYQHLF 101
Cdd:MTH00184  216 NFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
1-101 2.18e-30

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 112.08  E-value: 2.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   1 LSTDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKIYKM--EIISLFSWSMLLTAILLLLSLPVLAGAITMLLFD 78
Cdd:MTH00079  133 LSTLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSIslEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTD 212
                          90       100
                  ....*....|....*....|...
gi 2447729415  79 RNFNTS*FDPMGGGDPILYQHLF 101
Cdd:MTH00079  213 RNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
6-101 3.11e-29

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 108.87  E-value: 3.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   6 HLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKIYKMEI--ISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRNFNT 83
Cdd:MTH00077  138 HAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQyqTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217
                          90
                  ....*....|....*...
gi 2447729415  84 S*FDPMGGGDPILYQHLF 101
Cdd:MTH00077  218 TFFDPAGGGDPVLYQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
6-101 3.45e-29

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 108.86  E-value: 3.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   6 HLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKIYKMEI--ISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRNFNT 83
Cdd:MTH00183  138 HAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQyqTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217
                          90
                  ....*....|....*...
gi 2447729415  84 S*FDPMGGGDPILYQHLF 101
Cdd:MTH00183  218 TFFDPAGGGDPILYQHLF 235
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
6-101 4.02e-28

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 105.73  E-value: 4.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   6 HLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKIYKMEI--ISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRNFNT 83
Cdd:MTH00103  138 HAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQyqTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217
                          90
                  ....*....|....*...
gi 2447729415  84 S*FDPMGGGDPILYQHLF 101
Cdd:MTH00103  218 TFFDPAGGGDPILYQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
6-101 5.55e-28

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 105.29  E-value: 5.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   6 HLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKI--YKMEIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRNFNT 83
Cdd:MTH00182  140 HSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRApgVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNT 219
                          90
                  ....*....|....*...
gi 2447729415  84 S*FDPMGGGDPILYQHLF 101
Cdd:MTH00182  220 TFFDPAGGGDPILFQHLF 237
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
6-101 8.03e-28

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 104.91  E-value: 8.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   6 HLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKI--YKMEIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRNFNT 83
Cdd:MTH00037  138 HAGGSVDLAIFSLHLAGASSILASINFITTIINMRTpgMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINT 217
                          90
                  ....*....|....*...
gi 2447729415  84 S*FDPMGGGDPILYQHLF 101
Cdd:MTH00037  218 TFFDPAGGGDPILFQHLF 235
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
2-101 2.09e-26

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 101.24  E-value: 2.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   2 STDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKIYKMEI--ISLFSWSMLLTAILLLLSLPVLAGAITMLLFDR 79
Cdd:MTH00026  135 SIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMsrIPLFVWSVFITAILLLLSLPVLAGAITMLLTDR 214
                          90       100
                  ....*....|....*....|..
gi 2447729415  80 NFNTS*FDPMGGGDPILYQHLF 101
Cdd:MTH00026  215 NFNTTFFDPAGGGDPILYQHLF 236
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
2-101 1.36e-25

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: 98.37  E-value: 1.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   2 STDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMK--IYKMEIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDR 79
Cdd:cd00919   122 TLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRapGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDR 201
                          90       100
                  ....*....|....*....|..
gi 2447729415  80 NFNTS*FDPMGGGDPILYQHLF 101
Cdd:cd00919   202 NFGTSFFDPAGGGDPVLYQHLF 223
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
2-101 1.59e-24

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 95.51  E-value: 1.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   2 STDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKIYKMEI-ISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRN 80
Cdd:MTH00048  133 SSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSrTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRN 212
                          90       100
                  ....*....|....*....|.
gi 2447729415  81 FNTS*FDPMGGGDPILYQHLF 101
Cdd:MTH00048  213 FGSAFFDPLGGGDPVLFQHMF 233
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-101 8.35e-22

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 87.88  E-value: 8.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   2 STDGHLGPSVDLSIFSLHMAGISSIMGSINFISTILNMKI--YKMEIISLFSWSMLLTAILLLLSLPVLAGAITMLLFDR 79
Cdd:COG0843   136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRApgMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDR 215
                          90       100
                  ....*....|....*....|..
gi 2447729415  80 NFNTS*FDPMGGGDPILYQHLF 101
Cdd:COG0843   216 SLGTHFFDPAGGGDPLLWQHLF 237
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
8-101 1.16e-15

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: 70.69  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415   8 GPSVDLSIFSLHMAGISSIMGSINFISTILNMKIYKMEI--ISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRNFNTS* 85
Cdd:cd01662   134 GVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLmrMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHF 213
                          90
                  ....*....|....*.
gi 2447729415  86 FDPMGGGDPILYQHLF 101
Cdd:cd01662   214 FTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
11-101 3.12e-11

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: 57.97  E-value: 3.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447729415  11 VDLSIFSLHMAGISSIMGSINFISTILNMKIYKMEI-ISLFSWSMLLTAILLLLSLPVLAGAITMLLFDRNFNTs*fdpm 89
Cdd:pfam00115 118 VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLrMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------ 191
                          90
                  ....*....|..
gi 2447729415  90 GGGDPILYQHLF 101
Cdd:pfam00115 192 GGGDPLLDQHLF 203
 
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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