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Conserved domains on  [gi|321688802|gb|ADW94980|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Macrobiotus cf. hufelandi 1 MC-2011]

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 ...
 1-208 4.40e-123

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: 357.64  E-value: 4.40e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   1 LWAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  81 LLPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPL 160
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 321688802 161 FVWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 229
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-208 4.40e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 357.64  E-value: 4.40e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   1 LWAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  81 LLPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPL 160
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 321688802 161 FVWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 229
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-208 9.53e-119

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: 345.62  E-value: 9.53e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   1 LWAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 80
Cdd:cd01663   15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  81 LLPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPL 160
Cdd:cd01663   95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 321688802 161 FVWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:cd01663  175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILY 222
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-208 1.42e-65

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 210.37  E-value: 1.42e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   3 AACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPIlIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 82
Cdd:COG0843   29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  83 PPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLFV 162
Cdd:COG0843  108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 321688802 163 WSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:COG0843  188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLW 233
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-208 2.22e-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: 145.02  E-value: 2.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802    1 LWAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPIlIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 80
Cdd:pfam00115  11 LVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   81 LLPPSFTLIMtstMSEQGAGTGWTVYPPLshffahsgPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLeNMPL 160
Cdd:pfam00115  90 LVVLGAVLLL---ASFGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 321688802  161 FVWSVLITAILLLLALPVLAGGITMLLMDRNFNtsffdpAGGGDPILY 208
Cdd:pfam00115 158 FVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLD 199
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-208 4.40e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 357.64  E-value: 4.40e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   1 LWAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  81 LLPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPL 160
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 321688802 161 FVWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 229
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-208 9.53e-119

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: 345.62  E-value: 9.53e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   1 LWAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 80
Cdd:cd01663   15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  81 LLPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPL 160
Cdd:cd01663   95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 321688802 161 FVWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:cd01663  175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILY 222
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-208 3.05e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 330.10  E-value: 3.05e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   2 WAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 81
Cdd:MTH00167  25 WAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  82 LPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLF 161
Cdd:MTH00167 105 LPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLF 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 321688802 162 VWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00167 185 VWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILY 231
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-208 5.43e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 324.24  E-value: 5.43e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   1 LWAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00223  21 MWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  81 LLPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPL 160
Cdd:MTH00223 101 LLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPL 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 321688802 161 FVWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00223 181 FVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILY 228
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-208 3.50e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 322.43  E-value: 3.50e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   2 WAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 81
Cdd:MTH00116  25 WAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  82 LPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLF 161
Cdd:MTH00116 105 LPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLF 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 321688802 162 VWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00116 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILY 231
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-208 1.00e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 318.59  E-value: 1.00e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   1 LWAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00142  22 AWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  81 LLPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPL 160
Cdd:MTH00142 102 LLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPL 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 321688802 161 FVWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00142 182 FVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILY 229
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-208 7.95e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 298.39  E-value: 7.95e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   2 WAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 81
Cdd:MTH00077  25 WAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  82 LPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLF 161
Cdd:MTH00077 105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLF 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 321688802 162 VWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00077 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLY 231
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-208 5.19e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 296.45  E-value: 5.19e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   2 WAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 81
Cdd:MTH00183  25 WAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  82 LPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLF 161
Cdd:MTH00183 105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLF 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 321688802 162 VWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00183 185 VWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILY 231
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-208 7.57e-99

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 296.02  E-value: 7.57e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   2 WAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 81
Cdd:MTH00103  25 WAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  82 LPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLF 161
Cdd:MTH00103 105 LPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLF 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 321688802 162 VWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00103 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILY 231
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-208 9.13e-96

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 287.95  E-value: 9.13e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   2 WAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 81
Cdd:MTH00007  22 WGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  82 LPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLF 161
Cdd:MTH00007 102 LPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLF 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 321688802 162 VWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00007 182 VWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY 228
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-208 2.81e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 284.41  E-value: 2.81e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   2 WAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 81
Cdd:MTH00037  25 WAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  82 LPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLF 161
Cdd:MTH00037 105 IPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLF 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 321688802 162 VWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00037 185 VWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILF 231
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-208 2.60e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 279.40  E-value: 2.60e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   2 WAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 81
Cdd:MTH00184  27 FAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  82 LPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLF 161
Cdd:MTH00184 107 LPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLF 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 321688802 162 VWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00184 187 VWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILY 233
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 3-208 2.96e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 276.70  E-value: 2.96e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   3 AACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 82
Cdd:MTH00182  28 AGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  83 PPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLFV 162
Cdd:MTH00182 108 PPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFV 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 321688802 163 WSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00182 188 WSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILF 233
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-208 1.62e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 261.54  E-value: 1.62e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   1 LWAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00079  25 LWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  81 LLPPSFTLIMTSTMSEQGAGTGWTVYPPLSHfFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPL 160
Cdd:MTH00079 105 LLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 321688802 161 FVWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00079 184 FVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLY 231
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 3-208 2.99e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 253.78  E-value: 2.99e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   3 AACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 82
Cdd:MTH00026  27 SGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  83 PPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLFV 162
Cdd:MTH00026 107 PPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFV 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 321688802 163 WSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00026 187 WSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILY 232
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-208 2.16e-74

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: 231.65  E-value: 2.16e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   1 LWAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPlMIGAPDMAFPRMNNMSFW 80
Cdd:cd00919   13 FVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFW 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  81 LLPPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPL 160
Cdd:cd00919   92 LFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPL 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 321688802 161 FVWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:cd00919  172 FVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLY 219
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-208 1.42e-65

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 210.37  E-value: 1.42e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   3 AACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPIlIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 82
Cdd:COG0843   29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  83 PPSFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLFV 162
Cdd:COG0843  108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 321688802 163 WSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:COG0843  188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLW 233
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-208 5.18e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 190.27  E-value: 5.18e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   1 LWAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00048  25 VWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  81 LLPPSFTLIMTSTMSeqGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENmPL 160
Cdd:MTH00048 105 LLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRT-SI 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 321688802 161 FVWSVLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:MTH00048 182 ILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLF 229
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 5-208 1.17e-52

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: 175.85  E-value: 1.17e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   5 CVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPILIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 84
Cdd:cd01662   23 LRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  85 SFTLIMTSTMSEQGAGTGWTVYPPLSHFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLFVWS 164
Cdd:cd01662  102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWT 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 321688802 165 VLITAILLLLALPVLAGGITMLLMDRNFNTSFFDPAGGGDPILY 208
Cdd:cd01662  182 TLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLW 225
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-208 2.22e-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: 145.02  E-value: 2.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802    1 LWAACVGTSLSFIIRSELSQPGILFGDEQMYNVTVTSHAFIMIFFFVMPIlIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 80
Cdd:pfam00115  11 LVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802   81 LLPPSFTLIMtstMSEQGAGTGWTVYPPLshffahsgPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLeNMPL 160
Cdd:pfam00115  90 LVVLGAVLLL---ASFGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 321688802  161 FVWSVLITAILLLLALPVLAGGITMLLMDRNFNtsffdpAGGGDPILY 208
Cdd:pfam00115 158 FVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLD 199
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 31-208 7.48e-32

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 121.58  E-value: 7.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802  31 YNVTVTSHAFIMIFFFVMPILIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFTLIMTSTMSEQGAGTGWTVYPPLS 110
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321688802 111 HFFAHSGPSVDLTIFSLHIAGISSILGAINFITTIINMRTPSLSLENMPLFVWSVLITAILLLLALPVLAGGITMLLMDR 190
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170
                 ....*....|....*...
gi 321688802 191 NFNTSFFDPAGGGDPILY 208
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMY 275
 
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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