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Conserved domains on  [gi|1995713605|gb|QSG71453|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Symbion americanus]

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 ...
 1-162 3.25e-86

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: 261.34  E-value: 3.25e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00153   43 GSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00153  123 GWTVYPPLSsnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAG 202


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00153  203 AITM 206
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-162 3.25e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 261.34  E-value: 3.25e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00153   43 GSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00153  123 GWTVYPPLSsnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAG 202


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00153  203 AITM 206
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-162 1.28e-82

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: 251.25  E-value: 1.28e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:cd01663    36 GSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGT 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLSFQ--HSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:cd01663   116 GWTVYPPLSSIlaHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAG 195


                  ....
gi 1995713605 159 AITM 162
Cdd:cd01663   196 AITM 199
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
10-162 2.41e-46

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 157.98  E-value: 2.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  10 YNVIITGHGFIMIFFFVMPIlIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGTGWTIYPPLS 89
Cdd:COG0843    57 YNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1995713605  90 FQ--HSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAGAITM 162
Cdd:COG0843   136 GLeaSPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLL 210
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-162 2.20e-29

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: 111.13  E-value: 2.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPIlIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLvstGAGT 80
Cdd:pfam00115  32 GLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATT 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLsfqhsgSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMfKVPLFVWSVLITAVLLLLSLPVFAGAI 160
Cdd:pfam00115 108 GWTEYPPL------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAAL 180


                  ..
gi 1995713605 161 TM 162
Cdd:pfam00115 181 LL 182
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 6-162 5.42e-25

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: 99.93  E-value: 5.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   6 DDQIYNVIITGHGFIMIFFFVMPILIGgFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGTGWTIY 85
Cdd:TIGR02882  88 DAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  86 PPLS---FQHsGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAGAITM 162
Cdd:TIGR02882 167 APLAgpeFSP-GVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALAL 245
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-162 3.25e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 261.34  E-value: 3.25e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00153   43 GSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00153  123 GWTVYPPLSsnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAG 202


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00153  203 AITM 206
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-162 1.28e-82

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: 251.25  E-value: 1.28e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:cd01663    36 GSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGT 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLSFQ--HSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:cd01663   116 GWTVYPPLSSIlaHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAG 195


                  ....
gi 1995713605 159 AITM 162
Cdd:cd01663   196 AITM 199
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-162 6.18e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 234.96  E-value: 6.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00167   45 GSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGT 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00167  125 GWTVYPPLAgnLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAA 204


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00167  205 AITM 208
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-162 7.47e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 234.60  E-value: 7.47e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00116   45 GTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGT 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00116  125 GWTVYPPLAgnLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAA 204


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00116  205 GITM 208
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-162 8.12e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 229.48  E-value: 8.12e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00223   42 GALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00223  122 GWTVYPPLSsnLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAG 201


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00223  202 AITM 205
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-162 1.68e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 226.14  E-value: 1.68e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00142   43 GSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00142  123 GWTVYPPLSsnLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAG 202


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00142  203 AITM 206
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-162 6.38e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 211.72  E-value: 6.38e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00077   45 GTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGT 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00077  125 GWTVYPPLAgnLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAA 204


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00077  205 GITM 208
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-162 2.14e-66

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 210.55  E-value: 2.14e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00183   45 GALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGT 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00183  125 GWTVYPPLAgnLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAA 204


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00183  205 GITM 208
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-162 2.81e-66

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 210.12  E-value: 2.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00103   45 GTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGT 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00103  125 GWTVYPPLAgnLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAA 204


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00103  205 GITM 208
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-162 9.44e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 203.52  E-value: 9.44e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00037   45 GSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGT 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00037  125 GWTIYPPLSsnIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAG 204


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00037  205 AITM 208
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-162 2.40e-63

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 202.44  E-value: 2.40e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00007   42 GAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00007  122 GWTVYPPLAsnLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAG 201


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00007  202 AITM 205
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-162 3.85e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 201.98  E-value: 3.85e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00184   47 GSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00184  127 GWTVYPPLSsiQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAG 206


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00184  207 AITM 210
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-162 9.51e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 201.20  E-value: 9.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00182   47 GAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00182  127 GWTVYPPLSsiQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAG 206


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00182  207 AITM 210
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-162 3.08e-57

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 186.76  E-value: 3.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00026   46 GSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGT 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLSF--QHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:MTH00026  126 GWTVYPPLASiqAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAG 205


                  ....
gi 1995713605 159 AITM 162
Cdd:MTH00026  206 AITM 209
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-162 3.44e-56

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 183.73  E-value: 3.44e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:MTH00079   46 GLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGT 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLSFQ-HSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAGA 159
Cdd:MTH00079  126 SWTVYPPLSTLgHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGA 205


                  ...
gi 1995713605 160 ITM 162
Cdd:MTH00079  206 ITM 208
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-162 5.53e-50

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: 166.17  E-value: 5.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPILIGGFGNFLVPlMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGT 80
Cdd:cd00919    34 GSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLS--FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAG 158
Cdd:cd00919   113 GWTFYPPLStlSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAA 192


                  ....
gi 1995713605 159 AITM 162
Cdd:cd00919   193 ALVM 196
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
10-162 2.41e-46

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 157.98  E-value: 2.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  10 YNVIITGHGFIMIFFFVMPIlIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGTGWTIYPPLS 89
Cdd:COG0843    57 YNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1995713605  90 FQ--HSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAGAITM 162
Cdd:COG0843   136 GLeaSPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLL 210
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 9-162 1.13e-41

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 145.21  E-value: 1.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   9 IYNVIITGHGFIMIFFFVMPILIGGFGNFLVPLMLLSPDMCFPRMNNLSFWllPPALSLLLLSTLVSTGAGTGWTIYPPL 88
Cdd:MTH00048   54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAW--LLVPSIVFLLLSMCLGAGVGWTFYPPL 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1995713605  89 SFQH--SGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMpMFKVPLFVWSVLITAVLLLLSLPVFAGAITM 162
Cdd:MTH00048  132 SSSLfsSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLPVLAAAITM 206
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 10-162 2.96e-39

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: 138.48  E-value: 2.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  10 YNVIITGHGFIMIFFFVMPILIGgFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGTGWTIYPPLS 89
Cdd:cd01662    49 YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLS 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1995713605  90 --FQHSGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAGAITM 162
Cdd:cd01662   128 glEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALAL 202
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 10-162 1.68e-30

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 115.80  E-value: 1.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  10 YNVIITGHGFIMIFFFVMPILIGgFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGTGWTIYPPLS 89
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1995713605  90 -FQHS-GSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAGAITM 162
Cdd:PRK15017  178 gIEYSpGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVAL 252
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-162 2.20e-29

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: 111.13  E-value: 2.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   1 GSLLGDDQIYNVIITGHGFIMIFFFVMPIlIGGFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLvstGAGT 80
Cdd:pfam00115  32 GLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATT 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  81 GWTIYPPLsfqhsgSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMfKVPLFVWSVLITAVLLLLSLPVFAGAI 160
Cdd:pfam00115 108 GWTEYPPL------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAAL 180


                  ..
gi 1995713605 161 TM 162
Cdd:pfam00115 181 LL 182
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 6-162 5.42e-25

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: 99.93  E-value: 5.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605   6 DDQIYNVIITGHGFIMIFFFVMPILIGgFGNFLVPLMLLSPDMCFPRMNNLSFWLLPPALSLLLLSTLVSTGAGTGWTIY 85
Cdd:TIGR02882  88 DAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995713605  86 PPLS---FQHsGSSVDLTIFSMHLAGVSSLLGAVNFISTILNMRVIGMPMFKVPLFVWSVLITAVLLLLSLPVFAGAITM 162
Cdd:TIGR02882 167 APLAgpeFSP-GVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALAL 245
 
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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