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Conserved domains on  [gi|1169413183|gb|ARC52362|]
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cytochrome c oxidase subunit 1, partial (mitochondrion) [Zeugodacus cucurbitae]

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 2.07e-142

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: 407.33  E-value: 2.07e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00153   22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00153  102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00153  182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-217 2.07e-142

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 407.33  E-value: 2.07e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00153   22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00153  102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00153  182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-217 2.67e-125

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: 362.96  E-value: 2.67e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:cd01663    15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:cd01663    95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:cd01663   175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 231
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-217 1.23e-70

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 224.24  E-value: 1.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   3 AGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 82
Cdd:COG0843    29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  83 PPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFV 162
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1169413183 163 WAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-217 3.72e-42

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: 147.33  E-value: 3.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   3 AGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 82
Cdd:pfam00115  13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  83 PPSLTLLLVSSMvenGAGTGWTVYPPLssiiahggASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFdRMPLFV 162
Cdd:pfam00115  92 VLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1169413183 163 WAVVLTALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGH 217
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGH 208
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-217 2.17e-34

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: 128.82  E-value: 2.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  11 SILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLL 90
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  91 VSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWAVVLTAL 170
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1169413183 171 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGH 277
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-217 2.07e-142

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 407.33  E-value: 2.07e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00153   22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00153  102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00153  182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-217 2.67e-125

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: 362.96  E-value: 2.67e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:cd01663    15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:cd01663    95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:cd01663   175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 231
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-217 5.52e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 355.14  E-value: 5.52e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00167   24 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00167  104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00167  184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-217 2.22e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 348.51  E-value: 2.22e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   2 WAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 81
Cdd:MTH00223   22 WSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  82 LPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLF 161
Cdd:MTH00223  102 LPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLF 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169413183 162 VWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00223  182 VWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 237
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-217 2.55e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 348.64  E-value: 2.55e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00142   22 AWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00142  102 LLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPL 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00142  182 FVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 238
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-217 6.52e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 345.15  E-value: 6.52e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00116   24 AWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00116  104 LLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00116  184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-217 2.29e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 318.31  E-value: 2.29e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00037   24 AWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00037  104 LIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00037  184 FVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-217 2.41e-107

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 317.98  E-value: 2.41e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00103   24 AWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00103  104 LLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00103  184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-217 7.33e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 316.86  E-value: 7.33e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00183   24 AWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00183  104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00183  184 FVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-217 1.35e-106

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 316.07  E-value: 1.35e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00007   21 VWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00007  101 LLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPL 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00007  181 FVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 237
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-217 2.68e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 315.34  E-value: 2.68e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00077   24 AWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00077  104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00077  184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-217 2.83e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 300.20  E-value: 2.83e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00184   26 AFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00184  106 LLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPL 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00184  186 FVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGH 242
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-217 7.01e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 299.43  E-value: 7.01e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00182   26 AGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00182  106 LLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPL 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00182  186 FVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-217 6.10e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 291.20  E-value: 6.10e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   2 WAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 81
Cdd:MTH00079   26 WSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  82 LPPSLTLLLVSSMVENGAGTGWTVYPPLSSIiAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLF 161
Cdd:MTH00079  106 LPTSLFLILDSCFVDMGPGTSWTVYPPLSTL-GHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLF 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169413183 162 VWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00079  185 VWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGH 240
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-217 1.64e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 275.35  E-value: 1.64e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   1 AWAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 80
Cdd:MTH00026   25 ALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  81 LLPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPL 160
Cdd:MTH00026  105 LLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPL 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169413183 161 FVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00026  185 FVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGH 241
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-217 1.11e-79

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: 245.52  E-value: 1.11e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   2 WAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPRMNNMSFWL 81
Cdd:cd00919    14 VALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  82 LPPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLF 161
Cdd:cd00919    93 FPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLF 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169413183 162 VWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:cd00919   173 VWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGH 228
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-217 1.23e-70

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 224.24  E-value: 1.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   3 AGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 82
Cdd:COG0843    29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  83 PPSLTLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFV 162
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1169413183 163 WAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-217 1.81e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 204.91  E-value: 1.81e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   2 WAGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 81
Cdd:MTH00048   26 WSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  82 LPPSLTLLLVSSMVenGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFdRMPLF 161
Cdd:MTH00048  106 LVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSII 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169413183 162 VWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:MTH00048  183 LWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGH 238
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 7-217 8.55e-59

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 192.41  E-value: 8.55e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   7 GTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSL 86
Cdd:cd01662    25 GGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  87 TLLLVSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWAVV 166
Cdd:cd01662   104 LLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169413183 167 LTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:cd01662   184 VTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGH 234
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-217 3.72e-42

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: 147.33  E-value: 3.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183   3 AGMVGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 82
Cdd:pfam00115  13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  83 PPSLTLLLVSSMvenGAGTGWTVYPPLssiiahggASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFdRMPLFV 162
Cdd:pfam00115  92 VLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1169413183 163 WAVVLTALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGH 217
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGH 208
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 31-217 4.14e-36

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 133.91  E-value: 4.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  31 YNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLS 110
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183 111 SIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDR 190
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180
                  ....*....|....*....|....*..
gi 1169413183 191 NLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINLIWAWGH 284
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-217 2.17e-34

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: 128.82  E-value: 2.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  11 SILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLL 90
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169413183  91 VSSMVENGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWAVVLTAL 170
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1169413183 171 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 217
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGH 277
 
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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