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Conserved domains on  [gi|2083536762|gb|QZC92365|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Torquaratoridae sp. USNM IZ 1185900]

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 ...
1-200 1.56e-123

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: 444803  Cd Length: 511  Bit Score: 358.41  E-value: 1.56e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00153   25 GMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00153  105 PSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVW 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00153  185 SVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 224
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-200 1.56e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 358.41  E-value: 1.56e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00153   25 GMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00153  105 PSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVW 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00153  185 SVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 224
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-200 6.56e-116

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: 338.30  E-value: 6.56e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:cd01663    18 GLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:cd01663    98 PSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVW 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:cd01663   178 SVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGG 217
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-200 7.41e-67

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


Pssm-ID: 223913 [Multi-domain]  Cd Length: 566  Bit Score: 214.47  E-value: 7.41e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPG--PFLGDDHiYNVIVTAHALIMIFFMVMPiMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWL 78
Cdd:COG0843    31 LLVGGALALLMRLELATPSgsQFLDPQL-YNQILTLHGVIMIFFFAMP-AIGGFANYLVPLMIGARDVAFPRLNAISFWL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  79 LPPALLLLLASSGVEGGAG-TGWTIYPPLASNIAHSGGsVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPL 157
Cdd:COG0843   109 LVVGAILLVTSFFVPGGAAdTGWTAYPPLSAISYSGPG-VDLFILGLHLLGIGSLLGAINFIVTILNMRAPGMTMMKMPL 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2083536762 158 FVWSVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:COG0843   188 FTWSILITAILILLAFPVLAAALTMLLLDRNFGTSFFTPAGGG 230
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I;
1-197 1.15e-40

Cytochrome C and Quinol oxidase polypeptide I;


Pssm-ID: 425471  Cd Length: 432  Bit Score: 142.71  E-value: 1.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPiMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:pfam00115  14 FLVGGLLGLLIRLQLAFPGLNFLSPLTYNRLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSgveGGAGTGWTIYPPLAsniahsggSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFdRLPLFVW 160
Cdd:pfam00115  93 LGAVLLLASF---GGATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVW 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPA 197
Cdd:pfam00115 161 AILATAILILLAFPVLAAALLLLLLDRSLGAGGGDPL 197
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
4-200 3.13e-34

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: 127.66  E-value: 3.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   4 GTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGgFGNWLLPLMLGAPDMAFPRLNNMSFWLLPPAL 83
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  84 LLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVWSVF 163
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2083536762 164 ITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGG 263
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-200 1.56e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 358.41  E-value: 1.56e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00153   25 GMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00153  105 PSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVW 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00153  185 SVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 224
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-200 6.56e-116

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: 338.30  E-value: 6.56e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:cd01663    18 GLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:cd01663    98 PSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVW 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:cd01663   178 SVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGG 217
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
1-200 1.08e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 325.86  E-value: 1.08e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00167   27 GMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00167  107 PSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVW 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00167  187 SILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGG 226
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
1-200 2.15e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 324.75  E-value: 2.15e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00142   25 GMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00142  105 PALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVW 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00142  185 SVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGG 224
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
1-200 9.72e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 320.77  E-value: 9.72e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00223   24 GLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00223  104 PSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVW 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00223  184 SVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGG 223
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
1-200 1.69e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 320.12  E-value: 1.69e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00116   27 GMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00116  107 PSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVW 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00116  187 SVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGG 226
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
1-200 1.13e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 302.90  E-value: 1.13e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00037   27 GMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00037  107 PSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVW 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00037  187 SVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGG 226
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
1-200 1.09e-96

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 289.88  E-value: 1.09e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00007   24 GLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00007  104 PALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVW 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00007  184 AVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 223
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
1-200 2.98e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 286.43  E-value: 2.98e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00183   27 GMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00183  107 PSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVW 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00183  187 AVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGG 226
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
1-200 9.17e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 284.91  E-value: 9.17e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00077   27 GMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00077  107 PSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVW 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00077  187 SVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGG 226
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
1-200 4.70e-94

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 283.31  E-value: 4.70e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00103   27 GMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00103  107 PSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVW 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00103  187 SVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGG 226
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
1-200 3.21e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 281.32  E-value: 3.21e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00182   29 GMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLP 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00182  109 PALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVW 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00182  189 SILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGG 228
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
1-200 4.47e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 278.25  E-value: 4.47e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00184   29 GMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLP 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00184  109 PALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVW 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00184  189 SILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGG 228
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
1-200 3.76e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 275.41  E-value: 3.76e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00079   28 GMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLaSNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00079  108 TSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVW 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00079  187 TVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGG 226
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
1-200 2.79e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 256.09  E-value: 2.79e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00026   28 GAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:MTH00026  108 PALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVW 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00026  188 SVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGG 227
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
1-200 8.02e-73

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: 227.03  E-value: 8.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLlPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:cd00919    16 LLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLL-PPLIGARDLAFPRLNNLSFWLFP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:cd00919    95 PGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVW 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:cd00919   175 SVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGG 214
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-200 7.41e-67

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


Pssm-ID: 223913 [Multi-domain]  Cd Length: 566  Bit Score: 214.47  E-value: 7.41e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPG--PFLGDDHiYNVIVTAHALIMIFFMVMPiMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWL 78
Cdd:COG0843    31 LLVGGALALLMRLELATPSgsQFLDPQL-YNQILTLHGVIMIFFFAMP-AIGGFANYLVPLMIGARDVAFPRLNAISFWL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  79 LPPALLLLLASSGVEGGAG-TGWTIYPPLASNIAHSGGsVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPL 157
Cdd:COG0843   109 LVVGAILLVTSFFVPGGAAdTGWTAYPPLSAISYSGPG-VDLFILGLHLLGIGSLLGAINFIVTILNMRAPGMTMMKMPL 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2083536762 158 FVWSVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:COG0843   188 FTWSILITAILILLAFPVLAAALTMLLLDRNFGTSFFTPAGGG 230
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
1-200 8.48e-55

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 181.41  E-value: 8.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:MTH00048   28 GFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASsgVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFdRLPLFVW 160
Cdd:MTH00048  108 PSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILW 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:MTH00048  185 SYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGG 224
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
2-200 3.95e-54

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: 179.70  E-value: 3.95e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   2 LVGTALSIIIRIELAQP-GPFLGDDHiYNVIVTAHALIMIFFMVMPIMIGgFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:cd01662    23 LRGGVDALLMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVW 160
Cdd:cd01662   101 FGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTW 180
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:cd01662   181 TTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGG 220
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I;
1-197 1.15e-40

Cytochrome C and Quinol oxidase polypeptide I;


Pssm-ID: 425471  Cd Length: 432  Bit Score: 142.71  E-value: 1.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   1 GLVGTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPiMIGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLP 80
Cdd:pfam00115  14 FLVGGLLGLLIRLQLAFPGLNFLSPLTYNRLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  81 PALLLLLASSgveGGAGTGWTIYPPLAsniahsggSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFdRLPLFVW 160
Cdd:pfam00115  93 LGAVLLLASF---GGATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVW 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2083536762 161 SVFITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPA 197
Cdd:pfam00115 161 AILATAILILLAFPVLAAALLLLLLDRSLGAGGGDPL 197
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
4-200 3.13e-34

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: 127.66  E-value: 3.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762   4 GTALSIIIRIELAQPGPFLGDDHIYNVIVTAHALIMIFFMVMPIMIGgFGNWLLPLMLGAPDMAFPRLNNMSFWLLPPAL 83
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  84 LLLLASSGVEGGAGTGWTIYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVWSVF 163
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2083536762 164 ITVILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 200
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGG 263
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
26-200 4.78e-34

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 127.36  E-value: 4.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762  26 HIYNVIVTAHALIMIFFMVMPIMIGgFGNWLLPLMLGAPDMAFPRLNNMSFWLLPPALLLLLASSGVEGGAGTGWTIYPP 105
Cdd:PRK15017   97 HHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPP 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083536762 106 LASNIAHSGGSVDLAIFSLHLAGISSILGAINFMTTTINMRAPGVNFDRLPLFVWSVFITVILLLLSLPVLAGAITMLLT 185
Cdd:PRK15017  176 LSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTL 255
                         170
                  ....*....|....*
gi 2083536762 186 DRNLNTSFFDPAGGG 200
Cdd:PRK15017  256 DRYLGTHFFTNDMGG 270
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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