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Conserved domains on  [gi|1424550902|gb|AXB90224|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Diapriidae sp. BIOUG22741-F01]

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 9.61e-69

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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 215.81  E-value: 9.61e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   1 MELSM--TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMT 78
Cdd:cd01663    30 LELSQpgSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  79 GNGNGTGWTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMS 158
Cdd:cd01663   110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189

                         170
                  ....*....|..
gi 1424550902 159 LPVLAGAITMLL 170
Cdd:cd01663   190 LPVLAGAITMLL 201
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-170 9.61e-69

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: 215.81  E-value: 9.61e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   1 MELSM--TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMT 78
Cdd:cd01663    30 LELSQpgSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  79 GNGNGTGWTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMS 158
Cdd:cd01663   110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189

                         170
                  ....*....|..
gi 1424550902 159 LPVLAGAITMLL 170
Cdd:cd01663   190 LPVLAGAITMLL 201
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-170 4.30e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 214.73  E-value: 4.30e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   1 MELSM--TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMT 78
Cdd:MTH00153   37 AELGQpgSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  79 GNGNGTGWTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMS 158
Cdd:MTH00153  117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                         170
                  ....*....|..
gi 1424550902 159 LPVLAGAITMLL 170
Cdd:MTH00153  197 LPVLAGAITMLL 208
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
14-170 6.24e-36

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 130.25  E-value: 6.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  14 YNFIITSHALVMIFFFVMPMlMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTGWTIYPPLS 93
Cdd:COG0843    57 YNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424550902  94 NMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGAITMLL 170
Cdd:COG0843   136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLL 212
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 14-170 9.41e-20

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: 84.93  E-value: 9.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  14 YNFIITSHALVMIFFFVMPMLMGgFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNgngTGWTIYPPLS 93
Cdd:pfam00115  41 YNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFGGAT---TGWTEYPPLV 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424550902  94 NMmfhsdtsvDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMnKVTLFSWAILLTSILLMMSLPVLAGAITMLL 170
Cdd:pfam00115 117 GV--------DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLL 184
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 14-169 1.96e-18

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: 81.44  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  14 YNFIITSHALVMIFFFVMPMLMGgFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTGWTIYPPLS 93
Cdd:TIGR02882  92 YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLA 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424550902  94 NMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGAITML 169
Cdd:TIGR02882 171 GPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALM 246
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-170 9.61e-69

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: 215.81  E-value: 9.61e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   1 MELSM--TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMT 78
Cdd:cd01663    30 LELSQpgSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  79 GNGNGTGWTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMS 158
Cdd:cd01663   110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189

                         170
                  ....*....|..
gi 1424550902 159 LPVLAGAITMLL 170
Cdd:cd01663   190 LPVLAGAITMLL 201
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-170 4.30e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 214.73  E-value: 4.30e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   1 MELSM--TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMT 78
Cdd:MTH00153   37 AELGQpgSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  79 GNGNGTGWTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMS 158
Cdd:MTH00153  117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                         170
                  ....*....|..
gi 1424550902 159 LPVLAGAITMLL 170
Cdd:MTH00153  197 LPVLAGAITMLL 208
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-170 8.71e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 201.36  E-value: 8.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   1 MELSM--TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMT 78
Cdd:MTH00223   36 AELGQpgALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  79 GNGNGTGWTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMS 158
Cdd:MTH00223  116 ESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLS 195

                         170
                  ....*....|..
gi 1424550902 159 LPVLAGAITMLL 170
Cdd:MTH00223  196 LPVLAGAITMLL 207
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-170 4.32e-62

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 199.52  E-value: 4.32e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   1 MELSM--TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMT 78
Cdd:MTH00167   39 AELSQpgSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  79 GNGNGTGWTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMS 158
Cdd:MTH00167  119 EAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLS 198

                         170
                  ....*....|..
gi 1424550902 159 LPVLAGAITMLL 170
Cdd:MTH00167  199 LPVLAAAITMLL 210
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-170 5.16e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 188.76  E-value: 5.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   1 MELSM--TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMT 78
Cdd:MTH00116   39 AELGQpgTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  79 GNGNGTGWTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMS 158
Cdd:MTH00116  119 EAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLS 198

                         170
                  ....*....|..
gi 1424550902 159 LPVLAGAITMLL 170
Cdd:MTH00116  199 LPVLAAGITMLL 210
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 7-170 3.60e-56

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 183.77  E-value: 3.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   7 FMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTGW 86
Cdd:MTH00142   45 LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGW 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  87 TIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGAI 166
Cdd:MTH00142  125 TVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAI 204


                  ....
gi 1424550902 167 TMLL 170
Cdd:MTH00142  205 TMLL 208
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 6-170 1.57e-53

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 177.02  E-value: 1.57e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   6 TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTG 85
Cdd:MTH00007   43 AFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  86 WTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGA 165
Cdd:MTH00007  123 WTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGA 202


                  ....*
gi 1424550902 166 ITMLL 170
Cdd:MTH00007  203 ITMLL 207
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 6-170 9.13e-53

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 175.02  E-value: 9.13e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   6 TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTG 85
Cdd:MTH00037   46 SLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  86 WTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGA 165
Cdd:MTH00037  126 WTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGA 205


                  ....*
gi 1424550902 166 ITMLL 170
Cdd:MTH00037  206 ITMLL 210
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 6-170 1.82e-51

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 171.93  E-value: 1.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   6 TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTG 85
Cdd:MTH00182   48 AMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  86 WTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGA 165
Cdd:MTH00182  128 WTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGA 207


                  ....*
gi 1424550902 166 ITMLL 170
Cdd:MTH00182  208 ITMLL 212
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 6-170 1.93e-51

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 171.66  E-value: 1.93e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   6 TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTG 85
Cdd:MTH00077   46 TLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  86 WTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGA 165
Cdd:MTH00077  126 WTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAG 205


                  ....*
gi 1424550902 166 ITMLL 170
Cdd:MTH00077  206 ITMLL 210
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 6-170 3.24e-51

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 170.87  E-value: 3.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   6 TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTG 85
Cdd:MTH00183   46 ALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  86 WTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGA 165
Cdd:MTH00183  126 WTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAG 205


                  ....*
gi 1424550902 166 ITMLL 170
Cdd:MTH00183  206 ITMLL 210
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 6-170 1.47e-50

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 169.24  E-value: 1.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   6 TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTG 85
Cdd:MTH00184   48 SMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  86 WTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGA 165
Cdd:MTH00184  128 WTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGA 207


                  ....*
gi 1424550902 166 ITMLL 170
Cdd:MTH00184  208 ITMLL 212
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 6-170 1.76e-50

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 168.91  E-value: 1.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   6 TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTG 85
Cdd:MTH00103   46 TLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  86 WTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGA 165
Cdd:MTH00103  126 WTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAG 205


                  ....*
gi 1424550902 166 ITMLL 170
Cdd:MTH00103  206 ITMLL 210
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 5-170 9.75e-49

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 164.47  E-value: 9.75e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   5 MTFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGT 84
Cdd:MTH00079   46 GLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGT 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  85 GWTIYPPLSNMMfHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAG 164
Cdd:MTH00079  126 SWTVYPPLSTLG-HPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAG 204


                  ....*.
gi 1424550902 165 AITMLL 170
Cdd:MTH00079  205 AITMLL 210
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 6-170 6.52e-48

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 162.49  E-value: 6.52e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902   6 TFMKNESIYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTG 85
Cdd:MTH00026   47 SMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  86 WTIYPPLSNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGA 165
Cdd:MTH00026  127 WTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGA 206


                  ....*
gi 1424550902 166 ITMLL 170
Cdd:MTH00026  207 ITMLL 211
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 13-170 8.04e-41

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: 142.67  E-value: 8.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  13 IYNFIITSHALVMIFFFVMPMLMGGFGNWLMPiMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTGWTIYPPL 92
Cdd:cd00919    42 LYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPL 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424550902  93 SNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGAITMLL 170
Cdd:cd00919   121 STLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLL 198
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 13-170 4.29e-40

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 141.35  E-value: 4.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  13 IYNFIITSHALVMIFFFVMPMLMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTgnGNGTGWTIYPPL 92
Cdd:MTH00048   54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPL 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1424550902  93 SNMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMnKVTLFSWAILLTSILLMMSLPVLAGAITMLL 170
Cdd:MTH00048  132 SSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLL 208
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
14-170 6.24e-36

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 130.25  E-value: 6.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  14 YNFIITSHALVMIFFFVMPMlMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTGWTIYPPLS 93
Cdd:COG0843    57 YNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424550902  94 NMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGAITMLL 170
Cdd:COG0843   136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLL 212
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 14-170 2.20e-27

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: 106.51  E-value: 2.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  14 YNFIITSHALVMIFFFVMPMlMGGFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTGWTIYPPLS 93
Cdd:cd01662    49 YNQIFTMHGTIMIFLFAMPL-VFGLMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLS 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424550902  94 NMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGAITMLL 170
Cdd:cd01662   128 GLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLE 204
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 14-169 1.15e-22

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 93.46  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  14 YNFIITSHALVMIFFFVMPMLMGgFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTGWTIYPPLS 93
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424550902  94 NMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGAITML 169
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALL 253
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 14-170 9.41e-20

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: 84.93  E-value: 9.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  14 YNFIITSHALVMIFFFVMPMLMGgFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNgngTGWTIYPPLS 93
Cdd:pfam00115  41 YNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFGGAT---TGWTEYPPLV 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424550902  94 NMmfhsdtsvDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMnKVTLFSWAILLTSILLMMSLPVLAGAITMLL 170
Cdd:pfam00115 117 GV--------DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLL 184
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 14-169 1.96e-18

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: 81.44  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424550902  14 YNFIITSHALVMIFFFVMPMLMGgFGNWLMPIMMNAMDMSFPRMNNMSFWLLPPSMIMLIMSMMTGNGNGTGWTIYPPLS 93
Cdd:TIGR02882  92 YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLA 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424550902  94 NMMFHSDTSVDFMIFSLHMAGMSSIMGAINMISSIINIKSKMMYMNKVTLFSWAILLTSILLMMSLPVLAGAITML 169
Cdd:TIGR02882 171 GPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALM 246
 
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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