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Conserved domains on  [gi|1557930526|gb|QAA09420|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Insecta sp. INDOBIOSYS-CCDB24684-G10]

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 ...
1-158 3.00e-61

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 cd01663:

Pssm-ID: 412277  Cd Length: 488  Bit Score: 196.16  E-value: 3.00e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:cd01663    58 FFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKL--YKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:cd01663   138 IFSLHLAGISSILGAINFITTIFNMRApgMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGG 217
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-158 3.00e-61

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: 196.16  E-value: 3.00e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:cd01663    58 FFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKL--YKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:cd01663   138 IFSLHLAGISSILGAINFITTIFNMRApgMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGG 217
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-158 3.64e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 196.24  E-value: 3.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00153   65 FFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKLY--KIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00153  145 IFSLHLAGISSILGAINFITTIINMRSKgmTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 224
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-158 5.21e-32

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


Pssm-ID: 223913  Cd Length: 566  Bit Score: 119.32  E-value: 5.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPvMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGW-TVYPPLSSNlSHAGPSVDL 79
Cdd:COG0843    72 FFFAMP-AIGGFANYLVPLMIGARDVAFPRLNAISFWLLVVGAILLVTSFFVPGGAADTGwTAYPPLSAI-SYSGPGVDL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  80 SIFSLHIAGISSIMGSINFISTIMNMK--LYKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGG 157
Cdd:COG0843   150 FILGLHLLGIGSLLGAINFIVTILNMRapGMTMMKMPLFTWSILITAILILLAFPVLAAALTMLLLDRNFGTSFFTPAGG 229

                  .
gi 1557930526 158 G 158
Cdd:COG0843   230 G 230
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I;
1-157 1.09e-17

Cytochrome C and Quinol oxidase polypeptide I;


Pssm-ID: 395065  Cd Length: 434  Bit Score: 78.38  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGgFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFigTGTGTGWTVYPPLSsnlshagpSVDLS 80
Cdd:pfam00115  50 FGFATPFIFG-FGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFF--GGATTGWTEYPPLT--------GVDLW 118
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMK--LYKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGG 157
Cdd:pfam00115 119 YLGLLLAGVGSLLGAINFIVTILKRRapGMYLSRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSFGTHFFDPGDP 197
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-158 3.00e-61

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: 196.16  E-value: 3.00e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:cd01663    58 FFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKL--YKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:cd01663   138 IFSLHLAGISSILGAINFITTIFNMRApgMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGG 217
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-158 3.64e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 196.24  E-value: 3.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00153   65 FFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKLY--KIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00153  145 IFSLHLAGISSILGAINFITTIINMRSKgmTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 224
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
1-158 1.09e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 192.58  E-value: 1.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00167   67 FFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKL--YKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00167  147 IFSLHLAGVSSILGSINFITTIINMKPpgITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGG 226
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
1-158 5.04e-56

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 182.98  E-value: 5.04e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00116   67 FFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKLYKIE--NISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00116  147 IFSLHLAGVSSILGAINFITTCINMKPPAMSqyQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGG 226
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
1-158 8.13e-56

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 182.48  E-value: 8.13e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00223   64 FFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKL--YKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00223  144 IFSLHLAGVSSILGAINFITTIINMRSpgMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGG 223
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
1-158 1.34e-54

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 179.15  E-value: 1.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00142   65 FFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKL--YKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00142  145 IFSLHLAGVSSILGAINFITTVINMRAggMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGG 224
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
1-158 5.54e-52

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 172.39  E-value: 5.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00007   64 FFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKL--YKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00007  144 IFSLHLAGVSSILGAINFITTVINMRWkgLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 223
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
1-158 2.52e-50

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 168.18  E-value: 2.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00183   67 FFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLT 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKLYKIE--NISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00183  147 IFSLHLAGVSSILGAINFITTIINMKPPAISqyQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGG 226
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
1-158 1.06e-48

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 163.96  E-value: 1.06e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00077   67 FFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLT 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKLYKIE--NISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00077  147 IFSLHLAGVSSILGAINFITTSINMKPPSMSqyQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGG 226
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
1-158 6.20e-48

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 161.59  E-value: 6.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00103   67 FFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLT 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKLYKIE--NISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00103  147 IFSLHLAGVSSILGAINFITTIINMKPPAMSqyQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGG 226
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
1-158 5.96e-47

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 159.22  E-value: 5.96e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00037   67 FFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKL--YKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00037  147 IFSLHLAGASSILASINFITTIINMRTpgMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGG 226
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
1-158 4.67e-45

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 154.21  E-value: 4.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00184   69 FFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMA 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKLYKI--ENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00184  149 IFSLHLAGISSILGAMNFITTIFNMRAPGItmDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGG 228
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
1-158 7.43e-44

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 151.13  E-value: 7.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00182   69 FFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMA 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKL--YKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00182  149 IFSLHLAGVSSILGAINFITTIFNMRApgVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGG 228
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
1-158 5.71e-43

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 148.29  E-value: 5.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSnLSHAGPSVDLS 80
Cdd:MTH00079   68 FFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKLYKI--ENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00079  147 IFSLHCAGISSILGGINFMVTTKNLRSSSIslEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGG 226
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
1-158 6.81e-40

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 140.53  E-value: 6.81e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00026   68 FFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMA 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKL--YKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00026  148 IFSLHLAGLSSILGAMNFITTVMNMRTpgMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGG 227
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
1-158 7.63e-37

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: 131.50  E-value: 7.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMmLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:cd00919    56 FFFVMPAIFGGFGNLLPPL-IGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMK--LYKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:cd00919   135 ILGLHLAGVSSILGAINFITTILNMRapGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGG 214
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
1-158 1.38e-34

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 125.95  E-value: 1.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWtvYPPLSSNLSHAGPSVDLS 80
Cdd:MTH00048   68 FFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAGVGWTF--YPPLSSSLFSSSWGVDFL 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKLYKI-ENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:MTH00048  146 MFSLHLAGVSSLFGSINFICTIYSAFMTNVfSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGG 224
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-158 5.21e-32

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


Pssm-ID: 223913  Cd Length: 566  Bit Score: 119.32  E-value: 5.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPvMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGW-TVYPPLSSNlSHAGPSVDL 79
Cdd:COG0843    72 FFFAMP-AIGGFANYLVPLMIGARDVAFPRLNAISFWLLVVGAILLVTSFFVPGGAADTGwTAYPPLSAI-SYSGPGVDL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  80 SIFSLHIAGISSIMGSINFISTIMNMK--LYKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGG 157
Cdd:COG0843   150 FILGLHLLGIGSLLGAINFIVTILNMRapGMTMMKMPLFTWSILITAILILLAFPVLAAALTMLLLDRNFGTSFFTPAGG 229

                  .
gi 1557930526 158 G 158
Cdd:COG0843   230 G 230
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
1-158 5.13e-26

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: 102.27  E-value: 5.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPvMMGGFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:cd01662    62 FLFAMP-LVFGLMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYW 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKL--YKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:cd01662   141 ILGLQFSGIGTLLGAINFIVTILKMRApgMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGG 220
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I;
1-157 1.09e-17

Cytochrome C and Quinol oxidase polypeptide I;


Pssm-ID: 395065  Cd Length: 434  Bit Score: 78.38  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGgFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFigTGTGTGWTVYPPLSsnlshagpSVDLS 80
Cdd:pfam00115  50 FGFATPFIFG-FGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFF--GGATTGWTEYPPLT--------GVDLW 118
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMK--LYKIENISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGG 157
Cdd:pfam00115 119 YLGLLLAGVGSLLGAINFIVTILKRRapGMYLSRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSFGTHFFDPGDP 197
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
1-158 9.37e-16

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 73.05  E-value: 9.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526   1 FFFVMPVMMGgFGNFLIPMMLGVPDMAFPRMNNMSFWLLPPSLMLLLSSMFIGTGTGTGWTVYPPLSSNLSHAGPSVDLS 80
Cdd:PRK15017  112 FFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYW 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557930526  81 IFSLHIAGISSIMGSINFISTIMNMKLYKIE--NISLFSWAMLLTAILLLLSLPVLAGAITMLLFDRNLNTTFFDPSGGG 158
Cdd:PRK15017  191 IWSLQLSGIGTTLTGINFFVTILKMRAPGMTmfKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGG 270
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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