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Conserved domains on  [gi|295300486|gb|ADF91627|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Tetrix tenuicornis]

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 ...
 1-217 5.45e-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 MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 393.46  E-value: 5.45e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00153  17 YFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00153  97 NMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTL 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00153 177 DRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-217 5.45e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 393.46  E-value: 5.45e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00153  17 YFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00153  97 NMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTL 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00153 177 DRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-217 1.48e-127

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: 368.73  E-value: 1.48e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:cd01663   10 YLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:cd01663   90 NLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTL 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:cd01663  170 EKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-217 5.08e-71

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 225.01  E-value: 5.08e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:COG0843   22 YLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:COG0843  101 ALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTL 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:COG0843  181 MRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-217 2.69e-43

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: 150.42  E-value: 2.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486    1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:pfam00115   6 YLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   81 NMSFWLLPPSLILLISSSIvdsGVGTGWTVYPPLAGpiahsgvaVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:pfam00115  85 ALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486  161 dQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLF 217
Cdd:pfam00115 154 -RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 12-217 7.51e-37

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 135.75  E-value: 7.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   12 GTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 91
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   92 ILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNMDQLPLFVWSVM 171
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 295300486  172 ITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-217 5.45e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 393.46  E-value: 5.45e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00153  17 YFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00153  97 NMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTL 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00153 177 DRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-217 1.48e-127

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: 368.73  E-value: 1.48e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:cd01663   10 YLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:cd01663   90 NLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTL 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:cd01663  170 EKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-217 5.48e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 360.53  E-value: 5.48e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00167  19 YFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00167  99 NMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQ 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00167 179 YQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-217 1.05e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 357.09  E-value: 1.05e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00116  19 YLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00116  99 NMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQ 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00116 179 YQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-217 4.27e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 345.42  E-value: 4.27e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00223  16 YLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00223  96 NMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00223 176 ERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-217 6.45e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 342.47  E-value: 6.45e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00142  17 YFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00142  97 NMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKF 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00142 177 ERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-217 2.36e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 325.63  E-value: 2.36e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00037  19 YLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00037  99 NMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTF 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00037 179 DRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-217 2.05e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 318.04  E-value: 2.05e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00077  19 YLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00077  99 NMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQ 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00077 179 YQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-217 1.58e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 316.09  E-value: 1.58e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00183  19 YLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00183  99 NMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQ 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00183 179 YQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-217 2.38e-106

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 315.28  E-value: 2.38e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00103  19 YLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00103  99 NMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQ 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00103 179 YQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-217 1.06e-101

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 303.36  E-value: 1.06e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00007  16 YFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00007  96 NMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00007 176 ERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-217 1.24e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 303.67  E-value: 1.24e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00182  21 YLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00182 101 NISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTF 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00182 181 NRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-217 1.61e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 295.58  E-value: 1.61e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00184  21 YLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00184 101 NISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITM 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00184 181 DRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-217 1.95e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 287.35  E-value: 1.95e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00079  20 YFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGpIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00079 100 NLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISL 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00079 179 EHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-217 3.35e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 272.27  E-value: 3.35e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00026  20 YLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00026 100 NISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTM 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00026 180 SRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-217 4.26e-80

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: 246.67  E-value: 4.26e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPlMIGAPDMAFPRMN 80
Cdd:cd00919    8 YLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:cd00919   87 NLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTL 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:cd00919  167 DKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-217 5.08e-71

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 225.01  E-value: 5.08e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:COG0843   22 YLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:COG0843  101 ALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTL 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:COG0843  181 MRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-217 3.13e-62

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 201.83  E-value: 3.13e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00048  20 YTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  81 NMSFWLLPPSLILLISSSIVdsGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00048 100 ALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486 161 dQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00048 178 -RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 10-217 1.66e-56

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: 186.63  E-value: 1.66e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  10 LVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 89
Cdd:cd01662   23 LRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  90 SLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNMDQLPLFVWS 169
Cdd:cd01662  102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWT 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 295300486 170 VMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:cd01662  182 TLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-217 2.69e-43

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: 150.42  E-value: 2.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486    1 YFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:pfam00115   6 YLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   81 NMSFWLLPPSLILLISSSIvdsGVGTGWTVYPPLAGpiahsgvaVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNM 160
Cdd:pfam00115  85 ALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 295300486  161 dQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLF 217
Cdd:pfam00115 154 -RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 12-217 7.51e-37

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 135.75  E-value: 7.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   12 GTALSMIIRMELSVPGHLINDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 91
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486   92 ILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNMDQLPLFVWSVM 171
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 295300486  172 ITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF 217
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 36-216 1.18e-33

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 126.97  E-value: 1.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486  36 YNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLA 115
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295300486 116 GPIAHSGVAVDLAIFSLHLAGASSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDR 195
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180
                 ....*....|....*....|.
gi 295300486 196 NINTSFFDPAGGGDPILYQHL 216
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINL 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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