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Conserved domains on  [gi|46243713|gb|AAS84097|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Ena montana]

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 ...
 1-175 5.66e-103

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: 304.87  E-value: 5.66e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGVLV-DDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00153  35 IRAELGQPGSLIgDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00153 115 MVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLL 194

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00153 195 LSLPVLAGAITMLLTD 210
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-175 5.66e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 304.87  E-value: 5.66e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGVLV-DDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00153  35 IRAELGQPGSLIgDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00153 115 MVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLL 194

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00153 195 LSLPVLAGAITMLLTD 210
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-175 3.60e-102

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: 302.09  E-value: 3.60e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   1 IRLELGTTG-VLVDDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:cd01663  28 IRLELSQPGsQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSA 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713  80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:cd01663 108 LVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLL 187

                       170
                ....*....|....*.
gi 46243713 160 LSLPVLAGAITMLLTD 175
Cdd:cd01663 188 LSLPVLAGAITMLLTD 203
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-175 1.48e-56

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 185.72  E-value: 1.48e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   1 IRLELGTTGV-LVDDHFYNVVVTAHAFVMIFFMVMPiMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:COG0843  40 MRLQLAGPGLgLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISL 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713  80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:COG0843 119 FVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILIL 198

                       170
                ....*....|....*.
gi 46243713 160 LSLPVLAGAITMLLTD 175
Cdd:COG0843 199 LAFPVLAAALLLLLLD 214
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-175 7.69e-34

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: 123.45  E-value: 7.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713     1 IRLELGTTGV-LVDDHFYNVVVTAHAFVMIFFMVMPiMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:pfam00115  24 IRLQLAFPGLnFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    80 lveGGAGTGWTVYPPLsslsghggASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLeRMSLFVWSILVTVFLLL 159
Cdd:pfam00115 103 ---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILIL 170

                         170
                  ....*....|....*.
gi 46243713   160 LSLPVLAGAITMLLTD 175
Cdd:pfam00115 171 LAFPVLAAALLLLLLD 186
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-175 5.64e-28

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: 109.17  E-value: 5.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    11 LVDDHFYNVVVTAHAFVMIFFMVMPIMIGgFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSSLVEGGAGTGWT 90
Cdd:TIGR02882  86 FLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWT 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    91 VYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLLLSLPVLAGAIT 170
Cdd:TIGR02882 165 NYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALA 244


                  ....*
gi 46243713   171 MLLTD 175
Cdd:TIGR02882 245 LMTTD 249
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-175 5.66e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 304.87  E-value: 5.66e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGVLV-DDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00153  35 IRAELGQPGSLIgDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00153 115 MVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLL 194

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00153 195 LSLPVLAGAITMLLTD 210
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-175 3.60e-102

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: 302.09  E-value: 3.60e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   1 IRLELGTTG-VLVDDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:cd01663  28 IRLELSQPGsQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSA 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713  80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:cd01663 108 LVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLL 187

                       170
                ....*....|....*.
gi 46243713 160 LSLPVLAGAITMLLTD 175
Cdd:cd01663 188 LSLPVLAGAITMLLTD 203
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-175 2.78e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 293.04  E-value: 2.78e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGV-LVDDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00223  34 IRAELGQPGAlLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00223 114 AVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLL 193

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00223 194 LSLPVLAGAITMLLTD 209
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-175 2.86e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 277.33  E-value: 2.86e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTG-VLVDDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00167  37 IRAELSQPGsLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASS 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00167 117 GVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLL 196

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00167 197 LSLPVLAAAITMLLTD 212
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-175 3.70e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 264.28  E-value: 3.70e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGVLV-DDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00142  35 IRAELGQPGSLLgDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00142 115 AVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLL 194

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00142 195 LSLPVLAGAITMLLTD 210
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-175 2.77e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 262.34  E-value: 2.77e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGVLV-DDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00116  37 IRAELGQPGTLLgDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASS 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00116 117 TVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLL 196

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00116 197 LSLPVLAAGITMLLTD 212
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-175 4.51e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 246.66  E-value: 4.51e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGVLV-DDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00182  39 IRLELSAPGAMLgDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00182 119 FVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLL 198

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00182 199 LSLPVLAGAITMLLTD 214
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-175 5.02e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 246.28  E-value: 5.02e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTG-VLVDDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00184  39 IRLELSAPGsMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00184 119 FVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLL 198

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00184 199 LSLPVLAGAITMLLTD 214
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-175 2.10e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 244.74  E-value: 2.10e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGVLV-DDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00037  37 IRTELAQPGSLLqDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00037 117 GVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLL 196

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00037 197 LSLPVLAGAITMLLTD 212
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-175 2.76e-78

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 241.71  E-value: 2.76e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGVLV-DDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00103  37 IRAELGQPGTLLgDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASS 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00103 117 MVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLL 196

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00103 197 LSLPVLAAGITMLLTD 212
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-175 7.03e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 237.90  E-value: 7.03e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGVLV-DDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00183  37 IRAELSQPGALLgDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASS 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00183 117 GVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLL 196

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00183 197 LSLPVLAAGITMLLTD 212
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-175 3.39e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 236.38  E-value: 3.39e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGVLV-DDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00077  37 IRAELSQPGTLLgDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASS 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00077 117 GVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLL 196

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00077 197 LSLPVLAAGITMLLTD 212
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-175 1.32e-75

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 234.80  E-value: 1.32e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGVLV-DDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00007  34 IRIELGQPGAFLgSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSA 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00007 114 AVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLL 193

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00007 194 LSLPVLAGAITMLLTD 209
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-175 7.96e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 229.95  E-value: 7.96e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTGV-LVDDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00079  38 IRLELSKPGLlLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSC 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLsGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00079 118 FVDMGPGTSWTVYPPLSTL-GHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLV 196

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00079 197 LSLPVLAGAITMLLTD 212
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-175 1.01e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 222.58  E-value: 1.01e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    1 IRLELGTTG-VLVDDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:MTH00026  38 IRLELSSPGsMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSS 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:MTH00026 118 LVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLL 197

                        170
                 ....*....|....*.
gi 46243713  160 LSLPVLAGAITMLLTD 175
Cdd:MTH00026 198 LSLPVLAGAITMLLTD 213
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-175 2.82e-61

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 196.21  E-value: 2.82e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   1 IRLELGTTGV-LVDDHFYNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLlIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:cd00919  26 IRLELATPGSlFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPL-IGARDLAFPRLNNLSFWLFPPGLLLLLSSV 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713  80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:cd00919 105 LVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLL 184

                       170
                ....*....|....*.
gi 46243713 160 LSLPVLAGAITMLLTD 175
Cdd:cd00919 185 LALPVLAAALVMLLLD 200
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-175 1.48e-56

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 185.72  E-value: 1.48e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   1 IRLELGTTGV-LVDDHFYNVVVTAHAFVMIFFMVMPiMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:COG0843  40 MRLQLAGPGLgLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISL 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713  80 LVEGGAGTGWTVYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLL 159
Cdd:COG0843 119 FVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILIL 198

                       170
                ....*....|....*.
gi 46243713 160 LSLPVLAGAITMLLTD 175
Cdd:COG0843 199 LAFPVLAAALLLLLLD 214
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 17-175 1.83e-44

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 153.29  E-value: 1.83e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   17 YNVVVTAHAFVMIFFMVMPIMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSSLveGGAGTGWTVYPPLS 96
Cdd:MTH00048  55 YNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLS 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46243713   97 SLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITlERMSLFVWSILVTVFLLLLSLPVLAGAITMLLTD 175
Cdd:MTH00048 133 SSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFD 210
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 11-175 1.90e-43

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: 150.42  E-value: 1.90e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713  11 LVDDHFYNVVVTAHAFVMIFFMVMPIMIGgFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSSLVEGGAGTGWT 90
Cdd:cd01662  43 FLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWF 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713  91 VYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLLLSLPVLAGAIT 170
Cdd:cd01662 122 AYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALA 201


                ....*
gi 46243713 171 MLLTD 175
Cdd:cd01662 202 LLELD 206
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-175 7.69e-34

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: 123.45  E-value: 7.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713     1 IRLELGTTGV-LVDDHFYNVVVTAHAFVMIFFMVMPiMIGGFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSS 79
Cdd:pfam00115  24 IRLQLAFPGLnFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    80 lveGGAGTGWTVYPPLsslsghggASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLeRMSLFVWSILVTVFLLL 159
Cdd:pfam00115 103 ---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILIL 170

                         170
                  ....*....|....*.
gi 46243713   160 LSLPVLAGAITMLLTD 175
Cdd:pfam00115 171 LAFPVLAAALLLLLLD 186
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 15-154 4.14e-30

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 115.03  E-value: 4.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   15 HFYNVVVTAHAFVMIFFMVMPIMIGgFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSSLVEGGAGTGWTVYPP 94
Cdd:PRK15017  97 HHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPP 175

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713   95 LSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVT 154
Cdd:PRK15017 176 LSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCA 235
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-175 5.64e-28

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: 109.17  E-value: 5.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    11 LVDDHFYNVVVTAHAFVMIFFMVMPIMIGgFGNWMIPLLIGAPDMSFPRMNNMSFWLLPPAFILLISSSLVEGGAGTGWT 90
Cdd:TIGR02882  86 FLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWT 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46243713    91 VYPPLSSLSGHGGASVDLAIFSLHLAGLSSILGAINFITTIFNMRAPSITLERMSLFVWSILVTVFLLLLSLPVLAGAIT 170
Cdd:TIGR02882 165 NYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALA 244


                  ....*
gi 46243713   171 MLLTD 175
Cdd:TIGR02882 245 LMTTD 249
 
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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