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Conserved domains on  [gi|1018220775|gb|AMY40113|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Mymaridae sp. CNLMS907-14]

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 ...
 1-161 7.87e-65

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: 205.87  E-value: 7.87e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00153   60 AFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00153  140 SVDLAIFSLHLAGISSILGAINFITTIINMRSkgMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFD 219


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00153  220 PAG 222
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-161 7.87e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 205.87  E-value: 7.87e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00153   60 AFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00153  140 SVDLAIFSLHLAGISSILGAINFITTIINMRSkgMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFD 219


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00153  220 PAG 222
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-161 8.34e-62

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: 197.71  E-value: 8.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:cd01663    53 ALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:cd01663   133 SVDLAIFSLHLAGISSILGAINFITTIFNMRApgMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFD 212


                  ...
gi 1018220775 159 PSG 161
Cdd:cd01663   213 PAG 215
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-161 1.92e-32

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 120.23  E-value: 1.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   3 I*IFFFVMPvMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSV 82
Cdd:COG0843    67 IMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  83 DLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDPS 160
Cdd:COG0843   146 DLWLLGLALFGVGSILGGVNFIVTILKMRApgMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPA 225


                  .
gi 1018220775 161 G 161
Cdd:COG0843   226 G 226
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-159 9.50e-17

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: 76.07  E-value: 9.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   3 I*IFFFVMPvMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSgtgTGWTVYPPLssnlshngGSV 82
Cdd:pfam00115  51 LMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFGGAT---TGWTEYPPL--------VGV 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1018220775  83 DLSIFSLHIAGISSIMGSINFISTICNMKILKFDM-IYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 159
Cdd:pfam00115 119 DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLrMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 3-157 7.65e-14

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: 67.96  E-value: 7.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   3 I*IFFFVMPVMLGgFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSV 82
Cdd:TIGR02882 102 IMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGV 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018220775  83 DLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFF 157
Cdd:TIGR02882 181 NYYLIALQISGIGTLMTGINFFVTILKMRApgMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFF 257
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-161 7.87e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 205.87  E-value: 7.87e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00153   60 AFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00153  140 SVDLAIFSLHLAGISSILGAINFITTIINMRSkgMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFD 219


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00153  220 PAG 222
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-161 8.34e-62

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: 197.71  E-value: 8.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:cd01663    53 ALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:cd01663   133 SVDLAIFSLHLAGISSILGAINFITTIFNMRApgMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFD 212


                  ...
gi 1018220775 159 PSG 161
Cdd:cd01663   213 PAG 215
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-161 1.13e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 195.28  E-value: 1.13e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00167   62 AFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKILKFDM--IYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00167  142 SVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQyqTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFD 221


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00167  222 PAG 224
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-161 3.65e-57

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 185.95  E-value: 3.65e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00223   59 AFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNM--KILKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00223  139 SVDLAIFSLHLAGVSSILGAINFITTIINMrsPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFD 218


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00223  219 PAG 221
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-161 2.45e-56

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 184.14  E-value: 2.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00116   62 AFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKILKFDM--IYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00116  142 SVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQyqTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFD 221


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00116  222 PAG 224
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-161 1.12e-55

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 182.23  E-value: 1.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00142   60 AFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGG 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00142  140 SVDLAIFSLHLAGVSSILGAINFITTVINMRAggMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFD 219


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00142  220 PAG 222
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-161 1.17e-51

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 171.62  E-value: 1.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00007   59 AFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00007  139 SVDLAIFSLHLAGVSSILGAINFITTVINMRWkgLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFD 218


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00007  219 PAG 221
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-161 1.25e-50

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 169.24  E-value: 1.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00037   62 ALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGG 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00037  142 SVDLAIFSLHLAGASSILASINFITTIINMRTpgMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFD 221


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00037  222 PAG 224
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-161 2.38e-49

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 165.87  E-value: 2.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00183   62 AFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMK--ILKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00183  142 SVDLTIFSLHLAGVSSILGAINFITTIINMKppAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFD 221


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00183  222 PAG 224
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-161 1.47e-48

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 163.51  E-value: 1.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00103   62 AFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMK--ILKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00103  142 SVDLTIFSLHLAGVSSILGAINFITTIINMKppAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFD 221


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00103  222 PAG 224
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-161 6.78e-48

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 162.03  E-value: 6.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00077   62 AFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKILKFDMIY--LFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00077  142 SVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQtpLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFD 221


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00077  222 PAG 224
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-161 5.48e-47

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 159.60  E-value: 5.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00182   64 AFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGG 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00182  144 AVDMAIFSLHLAGVSSILGAINFITTIFNMRApgVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFD 223


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00182  224 PAG 226
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-161 1.35e-46

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 158.45  E-value: 1.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00184   64 AFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGG 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00184  144 SVDMAIFSLHLAGISSILGAMNFITTIFNMRApgITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFD 223


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00184  224 PAG 226
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-161 3.43e-45

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 154.45  E-value: 3.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSnLSHNGG 80
Cdd:MTH00079   63 AILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGS 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNM--KILKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00079  142 SVDLAIFSLHCAGISSILGGINFMVTTKNLrsSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFD 221


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00079  222 PST 224
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-161 3.24e-41

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 144.39  E-value: 3.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:MTH00026   63 AFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMKILKFDM--IYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:MTH00026  143 SVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMsrIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFD 222


                  ...
gi 1018220775 159 PSG 161
Cdd:MTH00026  223 PAG 225
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-161 3.70e-36

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: 129.57  E-value: 3.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   1 AFI*IFFFVMPVMLGGFGNFLIPMmLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGG 80
Cdd:cd00919    51 GVIMIFFFVMPAIFGGFGNLLPPL-IGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGV 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  81 SVDLSIFSLHIAGISSIMGSINFISTICNMK--ILKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFD 158
Cdd:cd00919   130 GVDLAILGLHLAGVSSILGAINFITTILNMRapGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFD 209


                  ...
gi 1018220775 159 PSG 161
Cdd:cd00919   210 PAG 212
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 3-161 2.80e-34

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 125.18  E-value: 2.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   3 I*IFFFVMPVMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSgtGTGWTVYPPLSSNLSHNGGSV 82
Cdd:MTH00048   65 IMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGA--GVGWTFYPPLSSSLFSSSWGV 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  83 DLSIFSLHIAGISSIMGSINFISTICNMKILKFDM-IYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDPSG 161
Cdd:MTH00048  143 DFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSrTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLG 222
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-161 1.92e-32

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 120.23  E-value: 1.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   3 I*IFFFVMPvMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSV 82
Cdd:COG0843    67 IMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  83 DLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDPS 160
Cdd:COG0843   146 DLWLLGLALFGVGSILGGVNFIVTILKMRApgMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPA 225


                  .
gi 1018220775 161 G 161
Cdd:COG0843   226 G 226
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 3-161 2.43e-24

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: 97.65  E-value: 2.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   3 I*IFFFVMPVMLGgFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSV 82
Cdd:cd01662    59 IMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775  83 DLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDPS 160
Cdd:cd01662   138 DYWILGLQFSGIGTLLGAINFIVTILKMRApgMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNA 217


                  .
gi 1018220775 161 G 161
Cdd:cd01662   218 L 218
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 3-157 5.51e-17

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 76.90  E-value: 5.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   3 I*IFFFVMPVMLGgFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSV 82
Cdd:PRK15017  109 IMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGV 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018220775  83 DLSIFSLHIAGISSIMGSINFISTICNMKILKFDMIYL--FVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFF 157
Cdd:PRK15017  188 DYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMpvFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFF 264
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-159 9.50e-17

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: 76.07  E-value: 9.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   3 I*IFFFVMPvMLGGFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSgtgTGWTVYPPLssnlshngGSV 82
Cdd:pfam00115  51 LMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFGGAT---TGWTEYPPL--------VGV 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1018220775  83 DLSIFSLHIAGISSIMGSINFISTICNMKILKFDM-IYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFFDP 159
Cdd:pfam00115 119 DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLrMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 3-157 7.65e-14

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: 67.96  E-value: 7.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018220775   3 I*IFFFVMPVMLGgFGNFLIPMMLMVPDMAFPLMNNMSFWLLPPSLMLLMFGMFIGSGTGTGWTVYPPLSSNLSHNGGSV 82
Cdd:TIGR02882 102 IMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGV 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018220775  83 DLSIFSLHIAGISSIMGSINFISTICNMKI--LKFDMIYLFVWSILLTTILLLLSLPVLAGAITMLLFDLNLNCSFF 157
Cdd:TIGR02882 181 NYYLIALQISGIGTLMTGINFFVTILKMRApgMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFF 257
 
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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