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Conserved domains on  [gi|1770808513|gb|QFU95127|]
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cytochrome oxidase subunit 1, partial [Visia cayennensis]

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 ...
 1-221 8.49e-137

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: 392.23  E-value: 8.49e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIItWLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:cd01663    86 PRLNNLSFWLLPPSLLLL-LLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:cd01663   165 PGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 225
 
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 ...
 1-221 8.49e-137

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: 392.23  E-value: 8.49e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIItWLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:cd01663    86 PRLNNLSFWLLPPSLLLL-LLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:cd01663   165 PGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 225
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-221 1.20e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 382.68  E-value: 1.20e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIITwLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00153   93 PRMNNMSFWLLPPSLTLLL-SSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRS 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00153  172 KGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 232
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-221 5.47e-79

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 245.81  E-value: 5.47e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   2 LYLFFGAFSGILGSFMSILIRMELLQPGNHLLLGNHqlYNVLITAHGFLMIFFMVMPvLIGGFGNWLVPIMIGSPDMAFP 81
Cdd:COG0843    21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  82 RLNNVSFWLLPPSlFIITWLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRSP 161
Cdd:COG0843    98 RLNALSFWLYLFG-GLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAP 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513 162 GQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:COG0843   177 GMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHL 236
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-221 4.99e-49

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: 165.44  E-value: 4.99e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   2 LYLFFGAFSGILGSFMSILIRMELLQPGNHLLlgNHQLYNVLITAHGFLMIFFMVMPVlIGGFGNWLVPIMIGSPDMAFP 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  82 RLNNVSFWLLPPSLfiITWLSSIieIGVGTGWTVYPPLssiqnhsgGSVDLAIFSLHLAGASSILGAINFISTILNMRSP 161
Cdd:pfam00115  82 RLNALSFWLVVLGA--VLLLASF--GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAP 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513 162 GQDLyRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTtffdssGGGDPILYQHL 221
Cdd:pfam00115 150 GMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHL 202
 
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 ...
 1-221 8.49e-137

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: 392.23  E-value: 8.49e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIItWLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:cd01663    86 PRLNNLSFWLLPPSLLLL-LLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:cd01663   165 PGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 225
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-221 1.20e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 382.68  E-value: 1.20e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIITwLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00153   93 PRMNNMSFWLLPPSLTLLL-SSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRS 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00153  172 KGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 232
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-221 3.46e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 353.60  E-value: 3.46e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00167   17 TLYFIFGAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIITwLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00167   95 PRMNNMSFWLLPPSLLLLL-ASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00167  174 PGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-221 2.03e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 346.31  E-value: 2.03e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00116   17 TLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIITwLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00116   95 PRMNNMSFWLLPPSFLLLL-ASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00116  174 PAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-221 7.98e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 344.65  E-value: 7.98e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGnhLLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00223   14 TLYLIFGMWSGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIITWlSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00223   92 PRLNNMSFWLLPPSLYLLLS-SSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRS 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00223  171 PGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 231
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-221 2.34e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 328.22  E-value: 2.34e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00142   15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIITwLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00142   93 PRMNNMSFWLLPPALLLLL-SSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRA 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00142  172 GGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 232
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-221 2.93e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 315.61  E-value: 2.93e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00182   19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIITWlSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00182   97 PRLNNISFWLLPPALILLLG-SAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00182  176 PGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHL 236
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-221 3.53e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 312.92  E-value: 3.53e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00184   19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLfIITWLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00184   97 PRLNNISFWLLPPAL-TLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00184  176 PGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHL 236
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-221 1.24e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 308.68  E-value: 1.24e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00037   17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSlFIITWLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00037   95 PRMNNMSFWLIPPS-FLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRT 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00037  174 PGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHL 234
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-221 1.96e-103

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 308.35  E-value: 1.96e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00103   17 TLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSlFIITWLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00103   95 PRMNNMSFWLLPPS-FLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00103  174 PAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-221 3.77e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 304.94  E-value: 3.77e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00077   17 TLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIITwLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00077   95 PRMNNMSFWLLPPSFLLLL-ASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00077  174 PSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHL 234
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-221 9.11e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 304.15  E-value: 9.11e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00183   17 TLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSlFIITWLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00183   95 PRMNNMSFWLLPPS-FLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00183  174 PAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-221 6.81e-100

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 299.12  E-value: 6.81e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00007   14 TLYFILGVWGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIITwLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00007   92 PRLNNMSFWLLPPALILLV-SSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRW 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00007  171 KGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 231
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-221 1.49e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 287.73  E-value: 1.49e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGnhLLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00079   18 TLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIItWLSSIIEIGVGTGWTVYPPLSSiQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00079   96 PRLNNLSFWLLPTSLFLI-LDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRS 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00079  174 SSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHL 234
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-221 1.38e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 286.14  E-value: 1.38e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00026   18 SLYLVFGALSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSLFIITWlSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:MTH00026   96 PRLNNISFWLLPPALFLLLG-SSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00026  175 PGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHL 235
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-221 3.05e-85

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: 259.77  E-value: 3.05e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   1 TLYLFFGAFSGILGSFMSILIRMELLQPGNhlLLGNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPiMIGSPDMAF 80
Cdd:cd00919     6 LLYLIFAFVALLLGGLLALLIRLELATPGS--LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  81 PRLNNVSFWLLPPSlFIITWLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRS 160
Cdd:cd00919    83 PRLNNLSFWLFPPG-LLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770808513 161 PGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:cd00919   162 PGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHL 222
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-221 5.47e-79

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 245.81  E-value: 5.47e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   2 LYLFFGAFSGILGSFMSILIRMELLQPGNHLLLGNHqlYNVLITAHGFLMIFFMVMPvLIGGFGNWLVPIMIGSPDMAFP 81
Cdd:COG0843    21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  82 RLNNVSFWLLPPSlFIITWLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRSP 161
Cdd:COG0843    98 RLNALSFWLYLFG-GLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAP 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513 162 GQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:COG0843   177 GMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHL 236
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-221 7.00e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 214.16  E-value: 7.00e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   2 LYLFFGAFSGILGSFMSILIRMELLQPGNHLLlgNHQLYNVLITAHGFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFP 81
Cdd:MTH00048   19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  82 RLNNVSFWLLPPSLFiitWLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRSP 161
Cdd:MTH00048   97 RLNALSAWLLVPSIV---FLLLSMCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMT 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513 162 GQDLyRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:MTH00048  174 NVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHM 232
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-221 4.28e-63

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: 203.97  E-value: 4.28e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   2 LYLFFGAFSGILGSFMSILIRMELLQPGNHLLLGNHqlYNVLITAHGFLMIFFMVMPVLIGgFGNWLVPIMIGSPDMAFP 81
Cdd:cd01662    13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  82 RLNNVSFWLlppSLF--IITWLSSIIEIGVGTGWTVYPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMR 159
Cdd:cd01662    90 RLNALSFWL---FLFggLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMR 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770808513 160 SPGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:cd01662   167 APGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHL 228
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-221 4.99e-49

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: 165.44  E-value: 4.99e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513   2 LYLFFGAFSGILGSFMSILIRMELLQPGNHLLlgNHQLYNVLITAHGFLMIFFMVMPVlIGGFGNWLVPIMIGSPDMAFP 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  82 RLNNVSFWLLPPSLfiITWLSSIieIGVGTGWTVYPPLssiqnhsgGSVDLAIFSLHLAGASSILGAINFISTILNMRSP 161
Cdd:pfam00115  82 RLNALSFWLVVLGA--VLLLASF--GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAP 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513 162 GQDLyRLPLFVWSILVTAFILLLAVPVLAGAITMLLTDRNFNTtffdssGGGDPILYQHL 221
Cdd:pfam00115 150 GMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHL 202
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 40-221 2.00e-38

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 140.46  E-value: 2.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513  40 YNVLITAHGFLMIFFMVMPVLIGgFGNWLVPIMIGSPDMAFPRLNNVSFWLLPPSLFIITwlssiIEIGVG----TGWTV 115
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVN-----VSLGVGefaqTGWLA 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770808513 116 YPPLSSIQNHSGGSVDLAIFSLHLAGASSILGAINFISTILNMRSPGQDLYRLPLFVWSILVTAFILLLAVPVLAGAITM 195
Cdd:PRK15017  173 YPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVAL 252

                         170       180
                  ....*....|....*....|....*.
gi 1770808513 196 LLTDRNFNTTFFDSSGGGDPILYQHL 221
Cdd:PRK15017  253 LTLDRYLGTHFFTNDMGGNMMMYINL 278
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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