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Conserved domains on  [gi|1045084609|gb|ANU39519|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Anoplolepis gracilipes]

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 ...
 1-176 1.98e-83

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: 254.79  E-value: 1.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00153   36 RAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00153  116 VESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLL 195

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00153  196 SLPVLAGAITMLLTDR 211
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-176 1.98e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 254.79  E-value: 1.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00153   36 RAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00153  116 VESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLL 195

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00153  196 SLPVLAGAITMLLTDR 211
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-176 2.29e-81

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: 248.94  E-value: 2.29e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:cd01663    29 RLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSAL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:cd01663   109 VEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLL 188

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:cd01663   189 SLPVLAGAITMLLTDR 204
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-176 3.81e-44

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 152.59  E-value: 3.81e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMmGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:COG0843    41 RLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFL-AGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLF 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:COG0843   120 VGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILL 199

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:COG0843   200 AFPVLAAALLLLLLDR 215
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-176 3.17e-27

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: 105.73  E-value: 3.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGgFGNFLVPLMLGSPDMAYPRMNNMSFWllpPSLSLLLLSNF 80
Cdd:pfam00115  25 RLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFW---LVVLGAVLLLA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLasnmfhngPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIdKMPLLVWSIFITAILLLL 160
Cdd:pfam00115 101 SFGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILL 171

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:pfam00115 172 AFPVLAAALLLLLLDR 187
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 15-176 2.83e-26

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: 104.17  E-value: 2.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  15 QIYSSMVTSHAFIMIFFMVMPFMMGgFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNFINDGTGTGWTVYPP 94
Cdd:TIGR02882  90 QHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAP 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  95 LASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLLSLPVLAGAITMLLT 174
Cdd:TIGR02882 169 LAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTT 248


                  ..
gi 1045084609 175 DR 176
Cdd:TIGR02882 249 DR 250
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-176 1.98e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 254.79  E-value: 1.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00153   36 RAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00153  116 VESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLL 195

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00153  196 SLPVLAGAITMLLTDR 211
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-176 2.29e-81

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: 248.94  E-value: 2.29e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:cd01663    29 RLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSAL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:cd01663   109 VEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLL 188

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:cd01663   189 SLPVLAGAITMLLTDR 204
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-176 7.65e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 230.36  E-value: 7.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00116   38 RAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASST 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00116  118 VEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLL 197

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00116  198 SLPVLAAGITMLLTDR 213
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-176 1.17e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 229.56  E-value: 1.17e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00167   38 RAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSG 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00167  118 VEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLL 197

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00167  198 SLPVLAAAITMLLTDR 213
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-176 9.41e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 224.86  E-value: 9.41e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00223   35 RAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00223  115 VESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLL 194

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00223  195 SLPVLAGAITMLLTDR 210
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-176 4.19e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 220.37  E-value: 4.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00142   36 RAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00142  116 VESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLL 195

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00142  196 SLPVLAGAITMLLTDR 211
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-176 1.51e-65

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 208.60  E-value: 1.51e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00007   35 RIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00007  115 VEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLL 194

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00007  195 SLPVLAGAITMLLTDR 210
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-176 4.44e-64

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 204.73  E-value: 4.44e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00103   38 RAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSM 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00103  118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLL 197

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00103  198 SLPVLAAGITMLLTDR 213
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-176 9.59e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 204.00  E-value: 9.59e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00183   38 RAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSG 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00183  118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLL 197

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00183  198 SLPVLAAGITMLLTDR 213
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-176 2.40e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 202.86  E-value: 2.40e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00077   38 RAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSG 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00077  118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLL 197

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00077  198 SLPVLAAGITMLLTDR 213
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-176 1.79e-62

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 200.83  E-value: 1.79e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00037   38 RTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAG 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00037  118 VESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLL 197

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00037  198 SLPVLAGAITMLLTDR 213
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-176 1.23e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 196.20  E-value: 1.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00184   40 RLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAF 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00184  120 VEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLL 199

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00184  200 SLPVLAGAITMLLTDR 215
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-176 8.64e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 193.88  E-value: 8.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00182   40 RLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAF 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00182  120 VEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLL 199

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00182  200 SLPVLAGAITMLLTDR 215
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-176 1.64e-57

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 187.58  E-value: 1.64e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00079   39 RLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCF 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLaSNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00079  119 VDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVL 197

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00079  198 SLPVLAGAITMLLTDR 213
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-176 6.72e-54

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 178.67  E-value: 6.72e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:MTH00026   39 RLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:MTH00026  119 VEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLL 198

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:MTH00026  199 SLPVLAGAITMLLTDR 214
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-176 1.79e-49

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: 165.40  E-value: 1.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPlMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:cd00919    27 RLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:cd00919   106 VGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLL 185

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:cd00919   186 ALPVLAAALVMLLLDR 201
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-176 3.81e-44

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 152.59  E-value: 3.81e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMmGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNF 80
Cdd:COG0843    41 RLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFL-AGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLF 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLL 160
Cdd:COG0843   120 VGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILL 199

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:COG0843   200 AFPVLAAALLLLLLDR 215
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 16-176 3.37e-38

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 136.35  E-value: 3.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  16 IYSSMVTSHAFIMIFFMVMPFMMGGFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNFIndGTGTGWTVYPPL 95
Cdd:MTH00048   54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  96 ASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIdKMPLLVWSIFITAILLLLSLPVLAGAITMLLTD 175
Cdd:MTH00048  132 SSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFD 210


                  .
gi 1045084609 176 R 176
Cdd:MTH00048  211 R 211
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 17-176 2.46e-37

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: 133.86  E-value: 2.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  17 YSSMVTSHAFIMIFFMVMPFMMGgFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNFINDGTGTGWTVYPPLA 96
Cdd:cd01662    49 YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLS 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  97 SNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLLSLPVLAGAITMLLTDR 176
Cdd:cd01662   128 GLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDR 207
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-176 3.17e-27

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: 105.73  E-value: 3.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609   1 RWELGVFKAQMNNDQIYSSMVTSHAFIMIFFMVMPFMMGgFGNFLVPLMLGSPDMAYPRMNNMSFWllpPSLSLLLLSNF 80
Cdd:pfam00115  25 RLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFW---LVVLGAVLLLA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  81 INDGTGTGWTVYPPLasnmfhngPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIdKMPLLVWSIFITAILLLL 160
Cdd:pfam00115 101 SFGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILL 171

                         170
                  ....*....|....*.
gi 1045084609 161 SLPVLAGAITMLLTDR 176
Cdd:pfam00115 172 AFPVLAAALLLLLLDR 187
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 15-176 2.83e-26

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: 104.17  E-value: 2.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  15 QIYSSMVTSHAFIMIFFMVMPFMMGgFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNFINDGTGTGWTVYPP 94
Cdd:TIGR02882  90 QHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAP 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  95 LASNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLLSLPVLAGAITMLLT 174
Cdd:TIGR02882 169 LAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTT 248


                  ..
gi 1045084609 175 DR 176
Cdd:TIGR02882 249 DR 250
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 17-176 2.33e-25

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 101.55  E-value: 2.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  17 YSSMVTSHAFIMIFFMVMPFMMGgFGNFLVPLMLGSPDMAYPRMNNMSFWLLPPSLSLLLLSNFINDGTGTGWTVYPPLA 96
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045084609  97 SNMFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKFLSIDKMPLLVWSIFITAILLLLSLPVLAGAITMLLTDR 176
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
 
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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