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Conserved domains on  [gi|367056760|gb|AEX10307|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Carcinus maenas]

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 ...
 1-212 1.78e-141

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: 404.64  E-value: 1.78e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-212 1.78e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 404.64  E-value: 1.78e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-212 1.76e-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: 1.76e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:cd01663   15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:cd01663   95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:cd01663  175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-212 6.22e-67

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 214.22  E-value: 6.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   3 AGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGGPDMAFPRMNNMSFWLL 82
Cdd:COG0843   29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  83 PPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLFV 162
Cdd:COG0843  108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 367056760 163 WAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:COG0843  188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-212 1.30e-39

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: 140.40  E-value: 1.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760    3 AGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGGPDMAFPRMNNMSFWLL 82
Cdd:pfam00115  13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   83 PPSLTLLLMSGMvesGVGTGWTVYPPLAGaiahagasVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMdQMPLFV 162
Cdd:pfam00115  92 VLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 367056760  163 WAVFITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPVLYQHLF 212
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-212 1.90e-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: 1.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   11 SLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGGPDMAFPRMNNMSFWLLPPSLTLLL 90
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   91 MSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLFVWAVFITAI 170
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 367056760  171 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-212 1.78e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 404.64  E-value: 1.78e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-212 1.76e-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: 1.76e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:cd01663   15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:cd01663   95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:cd01663  175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-212 2.50e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 358.61  E-value: 2.50e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00167  24 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00167 104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00167 184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-212 9.37e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 346.71  E-value: 9.37e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00142  22 AWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00142 102 LLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00142 182 FVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-212 1.84e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 346.31  E-value: 1.84e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00116  24 AWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00116 104 LLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00116 184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-212 9.95e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 339.26  E-value: 9.95e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   2 WAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFWL 81
Cdd:MTH00223  22 WSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  82 LPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLF 161
Cdd:MTH00223 102 LPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLF 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 367056760 162 VWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00223 182 VWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-212 2.99e-107

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 317.59  E-value: 2.99e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00103  24 AWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00103 104 LLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00103 184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-212 5.20e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 316.88  E-value: 5.20e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00077  24 AWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00077 104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00077 184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-212 2.05e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 315.32  E-value: 2.05e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00183  24 AWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00183 104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00183 184 FVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-212 5.18e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 314.46  E-value: 5.18e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00037  24 AWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00037 104 LIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00037 184 FVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-212 5.89e-104

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 309.14  E-value: 5.89e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00007  21 VWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00007 101 LLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPL 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00007 181 FVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-212 4.33e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 288.89  E-value: 4.33e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   2 WAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFWL 81
Cdd:MTH00079  26 WSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  82 LPPSLTLLLMSGMVESGVGTGWTVYPPLAgAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLF 161
Cdd:MTH00079 106 LPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLF 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 367056760 162 VWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00079 185 VWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-212 5.07e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 286.34  E-value: 5.07e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00184  26 AFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00184 106 LLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPL 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00184 186 FVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-212 1.30e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 285.56  E-value: 1.30e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00182  26 AGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00182 106 LLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPL 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00182 186 FVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-212 6.46e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 263.41  E-value: 6.46e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   1 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 80
Cdd:MTH00026  25 ALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  81 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 160
Cdd:MTH00026 105 LLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPL 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 367056760 161 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00026 185 FVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-212 2.26e-76

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: 236.66  E-value: 2.26e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   2 WAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPlMLGGPDMAFPRMNNMSFWL 81
Cdd:cd00919   14 VALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  82 LPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLF 161
Cdd:cd00919   93 FPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLF 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 367056760 162 VWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:cd00919  173 VWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-212 6.22e-67

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 214.22  E-value: 6.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   3 AGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGGPDMAFPRMNNMSFWLL 82
Cdd:COG0843   29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  83 PPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLFV 162
Cdd:COG0843  108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 367056760 163 WAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:COG0843  188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-212 1.29e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 194.51  E-value: 1.29e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   2 WAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFWL 81
Cdd:MTH00048  26 WSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  82 LPPSLTLLLMSgmVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMdQMPLF 161
Cdd:MTH00048 106 LVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSII 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 367056760 162 VWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:MTH00048 183 LWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 7-212 5.58e-55

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: 182.40  E-value: 5.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   7 GTSLSLIIRAELGQP-GTLIGNDQiYNVVVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGGPDMAFPRMNNMSFWLLPPS 85
Cdd:cd01662   25 GGVDALLMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  86 LTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLFVWAV 165
Cdd:cd01662  103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 367056760 166 FITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:cd01662  183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-212 1.30e-39

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: 140.40  E-value: 1.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760    3 AGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGGPDMAFPRMNNMSFWLL 82
Cdd:pfam00115  13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   83 PPSLTLLLMSGMvesGVGTGWTVYPPLAGaiahagasVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMdQMPLFV 162
Cdd:pfam00115  92 VLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 367056760  163 WAVFITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPVLYQHLF 212
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 31-211 1.38e-34

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 129.29  E-value: 1.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760  31 YNVVVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGGPDMAFPRMNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLA 110
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760 111 GAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLFVWAVFITAILLLLSLPVLAGAITMLLTDR 190
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180
                 ....*....|....*....|.
gi 367056760 191 NLNTSFFDPAGGGDPVLYQHL 211
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINL 278
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-212 1.90e-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: 1.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   11 SLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGGPDMAFPRMNNMSFWLLPPSLTLLL 90
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367056760   91 MSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLFVWAVFITAI 170
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 367056760  171 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLF 212
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
 
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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