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Conserved domains on  [gi|1524089985|gb|AZB87214|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Annelida sp. WCH_2683]

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 ...
 1-205 6.88e-125

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: 361.88  E-value: 6.88e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00153   28 GTSLSLLIRAELGQPGSLIGDdQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00153  108 TLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVL 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00153  188 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-205 6.88e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 361.88  E-value: 6.88e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00153   28 GTSLSLLIRAELGQPGSLIGDdQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00153  108 TLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVL 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00153  188 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-205 7.66e-125

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: 361.03  E-value: 7.66e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLG-TQAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:cd01663    21 GTSLSLLIRLELSQPGSQLGnDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:cd01663   101 LLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVL 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:cd01663   181 ITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-205 3.18e-74

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 232.71  E-value: 3.18e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGS-LLGTQAYNTIVTAHAFLMIFFLVMPaFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:COG0843    33 GGLLALLMRLQLAGPGLgLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:COG0843   112 LLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAAL 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:COG0843   192 VTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-205 3.33e-44

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: 152.34  E-value: 3.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPaFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:pfam00115  17 GGLLGLLIRLQLAFPGLNFLSpLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAaveGGAATGWTVYPPLssniahasPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMeRVPLFIWSLM 159
Cdd:pfam00115  96 VLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAIL 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTtffdpvGGGDPVLYQHLF 205
Cdd:pfam00115 164 ATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 5-205 9.78e-37

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: 134.98  E-value: 9.78e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   5 SLMIRVELGTP-GSLLGTQAYNTIVTAHAFLMIFFLVMPaFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSLFLLV 83
Cdd:TIGR02882  72 ALLMRAQLTVPdNKFLDAQHYNEIFTTHGVIMIIFMAMP-FIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  84 CSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLMITSG 163
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1524089985 164 LLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-205 6.88e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 361.88  E-value: 6.88e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00153   28 GTSLSLLIRAELGQPGSLIGDdQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00153  108 TLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVL 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00153  188 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-205 7.66e-125

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: 361.03  E-value: 7.66e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLG-TQAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:cd01663    21 GTSLSLLIRLELSQPGSQLGnDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:cd01663   101 LLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVL 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:cd01663   181 ITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-205 4.55e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 339.73  E-value: 4.55e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00167   30 GTALSLLIRAELSQPGSLLGDdQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00167  110 LLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSIL 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00167  190 VTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-205 1.38e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 338.49  E-value: 1.38e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLG-TQAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00223   27 GTSLSLLIRAELGQPGALLGdDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00223  107 YLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVK 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00223  187 VTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-205 1.54e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 322.83  E-value: 1.54e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00142   28 GTGLSLLIRAELGQPGSLLGDdQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPAL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00142  108 LLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVK 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00142  188 ITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-205 5.01e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 321.66  E-value: 5.01e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00116   30 GTALSLLIRAELGQPGTLLGDdQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00116  110 LLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVL 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00116  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-205 2.64e-105

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 312.22  E-value: 2.64e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00007   27 GTSMSLLIRIELGQPGAFLGSdQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPAL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00007  107 ILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVV 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00007  187 ITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-205 2.87e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 294.16  E-value: 2.87e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00077   30 GTALSLLIRAELSQPGTLLGDdQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00077  110 LLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVL 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00077  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-205 3.29e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 294.04  E-value: 3.29e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00037   30 GTAMSVIIRTELAQPGSLLQDdQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00037  110 LLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVF 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00037  190 ITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-205 6.54e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 293.37  E-value: 6.54e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00183   30 GTALSLLIRAELSQPGALLGDdQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00183  110 LLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVL 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00183  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-205 8.78e-97

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 290.63  E-value: 8.78e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00103   30 GTALSLLIRAELGQPGTLLGDdQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00103  110 LLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVL 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00103  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-205 7.73e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 285.95  E-value: 7.73e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00182   32 GTAFSMLIRLELSAPGAMLGDdHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPAL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00182  112 ILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSIL 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00182  192 ITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-205 2.29e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 284.41  E-value: 2.29e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00184   32 GTAFSMLIRLELSAPGSMLGDdHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPAL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00184  112 TLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSIL 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00184  192 VTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-205 9.73e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 274.64  E-value: 9.73e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLG-TQAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00079   31 GTSLSLIIRLELSKPGLLLGnGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSnIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00079  111 FLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVF 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00079  190 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-205 6.67e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 263.03  E-value: 6.67e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00026   31 GTAFSMLIRLELSSPGSMLGDdHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPAL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:MTH00026  111 FLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVF 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00026  191 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-205 7.23e-81

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: 248.21  E-value: 7.23e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMmLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:cd00919    19 GGLLALLIRLELATPGSLFLDpQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPL-IGARDLAFPRLNNLSFWLFPPGL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:cd00919    98 LLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVL 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:cd00919   178 VTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-205 3.18e-74

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 232.71  E-value: 3.18e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGS-LLGTQAYNTIVTAHAFLMIFFLVMPaFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:COG0843    33 GGLLALLMRLQLAGPGLgLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:COG0843   112 LLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAAL 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:COG0843   192 VTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-205 5.64e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 218.78  E-value: 5.64e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTP-GSLLGTQAYNTIVTAHAFLMIFFLVMPAFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:MTH00048   31 GLSLSLLIRLNFLDPyYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSaaVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTmERVPLFIWSLM 159
Cdd:MTH00048  111 VFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYL 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:MTH00048  188 FTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-205 3.33e-57

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: 187.79  E-value: 3.33e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTP-GSLLGTQAYNTIVTAHAFLMIFFLVMPaFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:cd01662    25 GGVDALLMRTQLALPgNDFLSPEHYNQIFTMHGTIMIFLFAMP-LVFGLMNYLVPLQIGARDVAFPRLNALSFWLFLFGG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLM 159
Cdd:cd01662   104 LLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTL 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:cd01662   184 VTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-205 3.33e-44

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: 152.34  E-value: 3.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   1 GTSMSLMIRVELGTPGSLLGT-QAYNTIVTAHAFLMIFFLVMPaFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSL 79
Cdd:pfam00115  17 GGLLGLLIRLQLAFPGLNFLSpLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  80 FLLVCSAaveGGAATGWTVYPPLssniahasPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMeRVPLFIWSLM 159
Cdd:pfam00115  96 VLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAIL 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1524089985 160 ITSGLLVLAIPVLAAGITMLLTDRNLNTtffdpvGGGDPVLYQHLF 205
Cdd:pfam00115 164 ATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 5-205 9.78e-37

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: 134.98  E-value: 9.78e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985   5 SLMIRVELGTP-GSLLGTQAYNTIVTAHAFLMIFFLVMPaFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSLFLLV 83
Cdd:TIGR02882  72 ALLMRAQLTVPdNKFLDAQHYNEIFTTHGVIMIIFMAMP-FIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  84 CSAAVEGGAATGWTVYPPLSSNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLMITSG 163
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1524089985 164 LLVLAIPVLAAGITMLLTDRNLNTTFFDPVGGGDPVLYQHLF 205
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 24-204 2.43e-35

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 131.21  E-value: 2.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985  24 YNTIVTAHAFLMIFFLVMPaFMGGFGNWLIPMMLNIPDLAFPRLNNLSFWLLPPSLFLLVCSAAVEGGAATGWTVYPPLS 103
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMP-FVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524089985 104 SNIAHASPAVDMAIFSLHLAGASSVIASINFMTTIYNMRNEGFTMERVPLFIWSLMITSGLLVLAIPVLAAGITMLLTDR 183
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180
                  ....*....|....*....|.
gi 1524089985 184 NLNTTFFDPVGGGDPVLYQHL 204
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINL 278
 
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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