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Conserved domains on  [gi|18026502|gb|AAL55510|]
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cytochrome oxidase 1, partial (mitochondrion) [Cardita calyculata]

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 ...
 1-220 3.97e-98

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: 293.62  E-value: 3.97e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   1 IGTLYFTFAFGAGVMGITLSLLMRLHLSkASGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:cd01663   6 IGTLYLIFGLWSGLVGTSLSLLIRLELS-QPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502  81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLSAVG---GSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:cd01663  85 FPRLNNLSFWLLPPSLLLLLLSALVEGgAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRA 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502 157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:cd01663 165 PGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 228
 
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 ...
 1-220 3.97e-98

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: 293.62  E-value: 3.97e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   1 IGTLYFTFAFGAGVMGITLSLLMRLHLSkASGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:cd01663   6 IGTLYLIFGLWSGLVGTSLSLLIRLELS-QPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502  81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLSAVG---GSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:cd01663  85 FPRLNNLSFWLLPPSLLLLLLSALVEGgAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRA 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502 157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:cd01663 165 PGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 228
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-220 1.77e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 285.22  E-value: 1.77e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKaSGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00153  13 IGTLYFIFGAWSGMVGTSLSLLIRAELGQ-PGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLSAV---GGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00153  92 FPRMNNMSFWLLPPSLTLLLSSSMVESgAGTGWTVYPPLSSNiahSGASVDLAIFSLHLAGISSILGAINFITTIINMRS 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00153 172 KGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 235
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-220 6.41e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 219.61  E-value: 6.41e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKASGALISTGTvYNAVITAHALVMIFFFLMPFmIGGFGNWLIPLMVACPDMA 80
Cdd:COG0843  18 IGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET-YNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502  81 FPRFNNLSFWLLPGAFLLLLIGISVN-PADAGWTIYPPLSAVGGS---GVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:COG0843  96 FPRLNALSFWLYLFGGLLLLISLFVGgAADVGWTFYPPLSGLEASpgvGVDLWLLGLALFGVGSILGGVNFIVTILKMRA 175

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502 157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:COG0843 176 PGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWF 239
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-220 1.67e-41

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: 145.79  E-value: 1.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502     1 IGTLYFTFAFGAGVMGITLSLLMRLHLSkASGALISTGTVYNAVITAHALVMIFFFLMPFmIGGFGNWLIPLMVACPDMA 80
Cdd:pfam00115   2 IGLLYLVTALVWFLVGGLLGLLIRLQLA-FPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    81 FPRFNNLSFWLLPGAFLLLLIGIsvNPADAGWTIYPPLsavggSGVDFVILSLHVAGASSVLGAMNFLTTIICFKHPNMS 160
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASF--GGATTGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   161 FaKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNtsffdpAGGGSPVLFQHLFWF 220
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWW 205
 
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 ...
 1-220 3.97e-98

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: 293.62  E-value: 3.97e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   1 IGTLYFTFAFGAGVMGITLSLLMRLHLSkASGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:cd01663   6 IGTLYLIFGLWSGLVGTSLSLLIRLELS-QPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502  81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLSAVG---GSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:cd01663  85 FPRLNNLSFWLLPPSLLLLLLSALVEGgAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRA 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502 157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:cd01663 165 PGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 228
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-220 1.77e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 285.22  E-value: 1.77e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKaSGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00153  13 IGTLYFIFGAWSGMVGTSLSLLIRAELGQ-PGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLSAV---GGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00153  92 FPRMNNMSFWLLPPSLTLLLSSSMVESgAGTGWTVYPPLSSNiahSGASVDLAIFSLHLAGISSILGAINFITTIINMRS 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00153 172 KGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-220 1.13e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 272.62  E-value: 1.13e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKAsGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00223  12 IGTLYLIFGMWSGLVGTSLSLLIRAELGQP-GALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISV-NPADAGWTIYPPLS---AVGGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00223  91 FPRLNNMSFWLLPPSLYLLLSSSAVeSGVGTGWTVYPPLSsnlAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRS 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00223 171 PGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 234
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-220 3.78e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 266.16  E-value: 3.78e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKaSGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00167  15 IGTLYFIFGAWAGMVGTALSLLIRAELSQ-PGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLS---AVGGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00167  94 FPRMNNMSFWLLPPSLLLLLASSGVEAgAGTGWTVYPPLAgnlAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKP 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00167 174 PGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-220 2.53e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 264.26  E-value: 2.53e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKAsGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00116  15 IGTLYLIFGAWAGMVGTALSLLIRAELGQP-GTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLS---AVGGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00116  94 FPRMNNMSFWLLPPSFLLLLASSTVEAgAGTGWTVYPPLAgnlAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKP 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00116 174 PAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-220 2.22e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 246.17  E-value: 2.22e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKaSGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00142  13 IGTLYFLFGAWAGMVGTGLSLLIRAELGQ-PGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLS---AVGGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00142  92 FPRMNNMSFWLLPPALLLLLSSAAVESgAGTGWTVYPPLSsnlAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRA 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00142 172 GGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 235
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-220 4.19e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 245.36  E-value: 4.19e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKaSGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00079  16 IGTLYFLFGLWSGMVGTSLSLIIRLELSK-PGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLSAVG--GSGVDFVILSLHVAGASSVLGAMNFLTTIICFKHP 157
Cdd:MTH00079  95 FPRLNNLSFWLLPTSLFLILDSCFVDMgPGTSWTVYPPLSTLGhpGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSS 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18026502  158 NMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00079 175 SISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWF 237
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-220 2.26e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 235.97  E-value: 2.26e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKAsGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00183  15 IGTLYLVFGAWAGMVGTALSLLIRAELSQP-GALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLS---AVGGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00183  94 FPRMNNMSFWLLPPSFLLLLASSGVEAgAGTGWTVYPPLAgnlAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKP 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00183 174 PAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-220 6.09e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 234.83  E-value: 6.09e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKAsGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00077  15 IGTLYLVFGAWAGMVGTALSLLIRAELSQP-GTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLS---AVGGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00077  94 FPRMNNMSFWLLPPSFLLLLASSGVEAgAGTGWTVYPPLAgnlAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKP 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00077 174 PSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWF 237
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-220 6.64e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 235.10  E-value: 6.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSkASGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00182  17 IGTLYLVFGAGAGMIGTAFSMLIRLELS-APGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLSAV---GGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00182  96 FPRLNNISFWLLPPALILLLGSAFVEQgAGTGWTVYPPLSSIqahSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00182 176 PGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWF 239
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-220 1.14e-74

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 234.39  E-value: 1.14e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKaSGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00103  15 IGTLYLLFGAWAGMVGTALSLLIRAELGQ-PGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLS---AVGGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00103  94 FPRMNNMSFWLLPPSFLLLLASSMVEAgAGTGWTVYPPLAgnlAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKP 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00103 174 PAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-220 6.09e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 232.41  E-value: 6.09e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKAsGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00037  15 IGTLYLIFGAWAGMVGTAMSVIIRTELAQP-GSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISV-NPADAGWTIYPPLS---AVGGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00037  94 FPRMNNMSFWLIPPSFLLLLASAGVeSGAGTGWTIYPPLSsniAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRT 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00037 174 PGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWF 237
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-220 7.43e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 229.71  E-value: 7.43e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSkASGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00184  17 IGTLYLLFGAFAGMIGTAFSMLIRLELS-APGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLSAV---GGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00184  96 FPRLNNISFWLLPPALTLLLGSAFVEQgAGTGWTVYPPLSSIqahSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00184 176 PGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 239
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-220 2.88e-72

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 227.86  E-value: 2.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKAsGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00007  12 IGTLYFILGVWGGLLGTSMSLLIRIELGQP-GAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLS---AVGGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00007  91 FPRLNNMSFWLLPPALILLVSSAAVEKgVGTGWTVYPPLAsnlAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRW 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00007 171 KGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 234
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-220 6.41e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 219.61  E-value: 6.41e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKASGALISTGTvYNAVITAHALVMIFFFLMPFmIGGFGNWLIPLMVACPDMA 80
Cdd:COG0843  18 IGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET-YNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502  81 FPRFNNLSFWLLPGAFLLLLIGISVN-PADAGWTIYPPLSAVGGS---GVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:COG0843  96 FPRLNALSFWLYLFGGLLLLISLFVGgAADVGWTFYPPLSGLEASpgvGVDLWLLGLALFGVGSILGGVNFIVTILKMRA 175

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502 157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:COG0843 176 PGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWF 239
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-220 6.05e-66

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 212.18  E-value: 6.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSkASGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00026  16 IGSLYLVFGALSGAIGTAFSMLIRLELS-SPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLSAV---GGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:MTH00026  95 FPRLNNISFWLLPPALFLLLGSSLVEQgAGTGWTVYPPLASIqahSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRT 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502  157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00026 175 PGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 238
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-220 1.23e-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.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 209.31  E-value: 1.23e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   1 IGTLYFTFAFGAGVMGITLSLLMRLHLSkASGALISTGTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVAcPDMA 80
Cdd:cd00919   4 IGLLYLIFAFVALLLGGLLALLIRLELA-TPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGA-RDLA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502  81 FPRFNNLSFWLLPGAFLLLLIGISV-NPADAGWTIYPPLSA---VGGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:cd00919  82 FPRLNNLSFWLFPPGLLLLLSSVLVgGGAGTGWTFYPPLSTlsySSGVGVDLAILGLHLAGVSSILGAINFITTILNMRA 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502 157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:cd00919 162 PGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWF 225
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-220 1.34e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 207.99  E-value: 1.34e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKASGALISTgTVYNAVITAHALVMIFFFLMPFMIGGFGNWLIPLMVACPDMA 80
Cdd:MTH00048  16 IGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISL-DVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLN 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   81 FPRFNNLSFWLLPGAFLLLLIGISVNpADAGWTIYPPLSAV---GGSGVDFVILSLHVAGASSVLGAMNFLTTIICFKHP 157
Cdd:MTH00048  95 LPRLNALSAWLLVPSIVFLLLSMCLG-AGVGWTFYPPLSSSlfsSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMT 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18026502  158 NMSFaKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:MTH00048 174 NVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWF 235
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-220 1.71e-59

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: 194.34  E-value: 1.71e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   1 IGTLYFTFAFGAGVMGITLSLLMRLHLSKASGALISTGTvYNAVITAHALVMIFFFLMPFMIGgFGNWLIPLMVACPDMA 80
Cdd:cd01662  10 IGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVA 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502  81 FPRFNNLSFWLLPGAFLLLLIGISVN-PADAGWTIYPPLSAVGGS---GVDFVILSLHVAGASSVLGAMNFLTTIICFKH 156
Cdd:cd01662  88 FPRLNALSFWLFLFGGLLLNASLLIGgFPDAGWFAYPPLSGLEYSpgvGVDYWILGLQFSGIGTLLGAINFIVTILKMRA 167

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18026502 157 PNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFWF 220
Cdd:cd01662 168 PGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWI 231
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-220 1.67e-41

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: 145.79  E-value: 1.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502     1 IGTLYFTFAFGAGVMGITLSLLMRLHLSkASGALISTGTVYNAVITAHALVMIFFFLMPFmIGGFGNWLIPLMVACPDMA 80
Cdd:pfam00115   2 IGLLYLVTALVWFLVGGLLGLLIRLQLA-FPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    81 FPRFNNLSFWLLPGAFLLLLIGIsvNPADAGWTIYPPLsavggSGVDFVILSLHVAGASSVLGAMNFLTTIICFKHPNMS 160
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASF--GGATTGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   161 FaKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNtsffdpAGGGSPVLFQHLFWF 220
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWW 205
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-219 1.33e-34

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 129.67  E-value: 1.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502    1 IGTLYFTFAFGAGVMGITLSLLMRLH--LSKASGALISTGTVYNAVITAHALVMIFFFLMPFMIGgFGNWLIPLMVACPD 78
Cdd:PRK15017  57 LGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARD 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   79 MAFPRFNNLSFWLLPGAFLLLLIGISVNP-ADAGWTIYPPLSAVG---GSGVDFVILSLHVAGASSVLGAMNFLTTIICF 154
Cdd:PRK15017 136 VAFPFLNNLSFWFTVVGVILVNVSLGVGEfAQTGWLAYPPLSGIEyspGVGVDYWIWSLQLSGIGTTLTGINFFVTILKM 215

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18026502  155 KHPNMSFAKYPMFIWAMAVTSVLLAFSIPVLAAAVTMLLTDRHFNTSFFDPAGGGSPVLFQHLFW 219
Cdd:PRK15017 216 RAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 5-193 1.86e-03

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 38.81  E-value: 1.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502   5 YFTFAFGAGVMGITLSLLMRLHLSKAsGALISTGTVYNAVITAHALVMIFFFLMpFMIGGFGNWLIPLMVACPDMAfPRF 84
Cdd:cd01660   9 HFVVAFLALLLGGLFGLLQVLVRTGV-FPLPSSGILYYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN-RRL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18026502  85 NNLSFWLLPGAFLLLLIGISVNPADAGWTIYPPLSAvggSGVDFVILSLHVAGaSSVLGAMNFLTTIICFK-HPNmsfAK 163
Cdd:cd01660  86 AWAGFWLMVIGTVMAAVPILLGQASVLYTFYPPLQA---HPLFYIGAALVVVG-SWISGFAMFVTLWRWKKaNPG---KK 158

                       170       180       190
                ....*....|....*....|....*....|
gi 18026502 164 YPMFIWAMAVTSVLLAFSIPVLAAAVTMLL 193
Cdd:cd01660 159 VPLATFMVVTTMILWLVASLGVALEVLFQL 188
 
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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