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Conserved domains on  [gi|1576834672|gb|QBF06051|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Platygastridae sp. BIOUG14909-H06]

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 ...
 1-170 2.91e-94

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: 282.53  E-value: 2.91e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00153   19 IFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNM 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00153   99 SFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIahsGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDR 178

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00153  179 MPLFVWSVLITAI 191
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-170 2.91e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 282.53  E-value: 2.91e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00153   19 IFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNM 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00153   99 SFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIahsGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDR 178

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00153  179 MPLFVWSVLITAI 191
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-170 1.01e-89

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: 270.51  E-value: 1.01e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:cd01663    12 IFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:cd01663    92 SFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEK 171

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:cd01663   172 MPLFVWSVLITAF 184
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-170 2.55e-45

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 156.06  E-value: 2.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPiMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:COG0843    24 VTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNAL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:COG0843   103 SFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEaspGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMR 182

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:COG0843   183 MPLFTWAALVTSI 195
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-170 6.79e-31

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: 115.75  E-value: 6.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMlGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:pfam00115   8 VTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMAFPRLNAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSniFGLGTgTGWTVYPPLasqlnPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMyNLSL 160
Cdd:pfam00115  87 SFWLVVLGAVLLLAS--FGGAT-TGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPL 157

                         170
                  ....*....|
gi 1576834672 161 FTWSVFITTI 170
Cdd:pfam00115 158 FVWAILATAI 167
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 10-170 1.22e-27

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: 108.02  E-value: 1.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  10 GSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGgFGNWLIPLMINAPDMAFPRLNNMSFWLLPPSI 89
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  90 ILLIYSNIFGLGTGTGWTVYPPLAS---QLNPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYNLSLFTWSVF 166
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGpefSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226


                  ....
gi 1576834672 167 ITTI 170
Cdd:TIGR02882 227 ITTL 230
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-170 2.91e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 282.53  E-value: 2.91e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00153   19 IFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNM 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00153   99 SFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIahsGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDR 178

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00153  179 MPLFVWSVLITAI 191
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-170 1.01e-89

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: 270.51  E-value: 1.01e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:cd01663    12 IFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:cd01663    92 SFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEK 171

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:cd01663   172 MPLFVWSVLITAF 184
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-170 2.07e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 265.39  E-value: 2.07e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00167   21 IFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00167  101 SFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLahaGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQ 180

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00167  181 TPLFVWSILVTTI 193
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-170 5.23e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 253.86  E-value: 5.23e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00116   21 IFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00116  101 SFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLahaGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQ 180

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00116  181 TPLFVWSVLITAV 193
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-170 2.14e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 241.94  E-value: 2.14e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00142   19 LFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNM 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00142   99 SFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLahsGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFER 178

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00142  179 VPLFVWSVKITAI 191
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-168 6.06e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 240.65  E-value: 6.06e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00223   18 IFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00223   98 SFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLahaGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLER 177

                         170
                  ....*....|.
gi 1576834672 158 LSLFTWSVFIT 168
Cdd:MTH00223  178 LPLFVWSVKVT 188
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-170 2.11e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 229.06  E-value: 2.11e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00077   21 VFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00077  101 SFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLahaGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQ 180

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00077  181 TPLFVWSVLITAV 193
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-170 4.12e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 228.65  E-value: 4.12e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00183   21 VFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNM 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00183  101 SFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLahaGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQ 180

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00183  181 TPLFVWAVLITAV 193
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-170 2.37e-72

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 226.30  E-value: 2.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00103   21 LFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00103  101 SFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLahaGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQ 180

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00103  181 TPLFVWSVLITAV 193
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-170 6.66e-71

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 222.85  E-value: 6.66e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00007   18 ILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00007   98 SFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLahaGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLER 177

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00007  178 IPLFVWAVVITVV 190
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-170 2.42e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 221.24  E-value: 2.42e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00037   21 IFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNM 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00037  101 SFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIahaGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDR 180

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00037  181 LPLFVWSVFITAF 193
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-168 1.17e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 209.15  E-value: 1.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00079   22 LFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLAS--QLNPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYNL 158
Cdd:MTH00079  102 SFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTlgHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHM 181

                         170
                  ....*....|
gi 1576834672 159 SLFTWSVFIT 168
Cdd:MTH00079  182 SLFVWTVFVT 191
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-170 2.59e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 208.53  E-value: 2.59e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00184   23 LFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLAS---QLNPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00184  103 SFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSiqaHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDR 182

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00184  183 MPLFVWSILVTTF 195
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-170 9.52e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 206.98  E-value: 9.52e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00182   23 VFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQLNPS---IDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00182  103 SFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSggaVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNR 182

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00182  183 LPLFVWSILITAF 195
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-170 2.06e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 190.61  E-value: 2.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00026   22 VFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNI 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLAS---QLNPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:MTH00026  102 SFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASiqaHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSR 181

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00026  182 IPLFVWSVFITAI 194
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-170 4.47e-54

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: 177.72  E-value: 4.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPlMINAPDMAFPRLNNM 80
Cdd:cd00919    10 IFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:cd00919    89 SFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSyssGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDK 168

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:cd00919   169 MPLFVWSVLVTAI 181
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-170 2.55e-45

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 156.06  E-value: 2.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPiMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:COG0843    24 VTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNAL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLASQL---NPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYN 157
Cdd:COG0843   103 SFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEaspGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMR 182

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:COG0843   183 MPLFTWAALVTSI 195
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-170 1.49e-42

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 148.29  E-value: 1.49e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:MTH00048   22 LLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNAL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSNIFglGTGTGWTVYPPLASQLNPS---IDLTIFSLHLAGISSILSSINFLCTIMNMkTMKFYMYN 157
Cdd:MTH00048  102 SAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSswgVDFLMFSLHLAGVSSLFGSINFICTIYSA-FMTNVFSR 178

                         170
                  ....*....|...
gi 1576834672 158 LSLFTWSVFITTI 170
Cdd:MTH00048  179 TSIILWSYLFTSI 191
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 9-170 1.46e-35

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: 129.24  E-value: 1.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   9 LGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGgFGNWLIPLMINAPDMAFPRLNNMSFWLLPPS 88
Cdd:cd01662    24 RGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  89 IILLIYSNIFGLGTGTGWTVYPPLASQLN---PSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYNLSLFTWSV 165
Cdd:cd01662   103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYspgVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182


                  ....*
gi 1576834672 166 FITTI 170
Cdd:cd01662   183 LVTSI 187
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-170 6.79e-31

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: 115.75  E-value: 6.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672   1 IFGIWAGMLGSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMlGGFGNWLIPLMINAPDMAFPRLNNM 80
Cdd:pfam00115   8 VTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMAFPRLNAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  81 SFWLLPPSIILLIYSniFGLGTgTGWTVYPPLasqlnPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMyNLSL 160
Cdd:pfam00115  87 SFWLVVLGAVLLLAS--FGGAT-TGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPL 157

                         170
                  ....*....|
gi 1576834672 161 FTWSVFITTI 170
Cdd:pfam00115 158 FVWAILATAI 167
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 10-170 1.22e-27

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: 108.02  E-value: 1.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  10 GSSMSMMIRMELSAPGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGgFGNWLIPLMINAPDMAFPRLNNMSFWLLPPSI 89
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  90 ILLIYSNIFGLGTGTGWTVYPPLAS---QLNPSIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYNLSLFTWSVF 166
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGpefSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226


                  ....
gi 1576834672 167 ITTI 170
Cdd:TIGR02882 227 ITTL 230
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 34-170 1.36e-24

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 99.62  E-value: 1.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672  34 YNSIVTSHAFVMIFFMVMPIMLGgFGNWLIPLMINAPDMAFPRLNNMSFWLLPPSIILLIYSNIFGLGTGTGWTVYPPLA 113
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576834672 114 S-QLNP--SIDLTIFSLHLAGISSILSSINFLCTIMNMKTMKFYMYNLSLFTWSVFITTI 170
Cdd:PRK15017  178 GiEYSPgvGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANV 237
 
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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