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Conserved domains on  [gi|1483571529|gb|AYD73044|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Telenomus podisi]

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 ...
 1-187 3.88e-102

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: 303.33  E-value: 3.88e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00153   42 PGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMN--NWTLFTWSILITTILLLLSLPVLA 155
Cdd:MTH00153  122 TGWTVYPPLSSNIahsGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTldRMPLFVWSVLITAILLLLSLPVLA 201

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00153  202 GAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-187 3.88e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 303.33  E-value: 3.88e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00153   42 PGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMN--NWTLFTWSILITTILLLLSLPVLA 155
Cdd:MTH00153  122 TGWTVYPPLSSNIahsGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTldRMPLFVWSVLITAILLLLSLPVLA 201

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00153  202 GAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-187 2.61e-96

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: 287.46  E-value: 2.61e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:cd01663    35 PGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMN--NWTLFTWSILITTILLLLSLPVLA 155
Cdd:cd01663   115 TGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTleKMPLFVWSVLITAFLLLLSLPVLA 194

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:cd01663   195 GAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
11-187 2.03e-52

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 175.32  E-value: 2.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  11 YNSIVTSHAFVMIFFMVMPiMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTGTGWTVYPPLS 90
Cdd:COG0843    57 YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  91 TQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMNNWT--LFTWSILITTILLLLSLPVLAGAITMILSDR 165
Cdd:COG0843   136 GLEaspGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRmpLFTWAALVTSILILLAFPVLAAALLLLLLDR 215

                         170       180
                  ....*....|....*....|..
gi 1483571529 166 NLNTTFFNPAGGGDPVLYQHLF 187
Cdd:COG0843   216 SLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-187 3.20e-33

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: 122.30  E-value: 3.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMlGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSniFGAGTg 80
Cdd:pfam00115  31 PGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLAS--FGGAT- 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLstqlnPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMN-NWTLFTWSILITTILLLLSLPVLAGAIT 159
Cdd:pfam00115 107 TGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTlRMPLFVWAILATAILILLAFPVLAAALL 181

                         170       180
                  ....*....|....*....|....*...
gi 1483571529 160 MILSDRNLNttffnpAGGGDPVLYQHLF 187
Cdd:pfam00115 182 LLLLDRSLG------AGGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-187 1.35e-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: 105.71  E-value: 1.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGgFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:TIGR02882  82 PDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLST---QLNPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMN--NWTLFTWSILITTILLLLSLPVLA 155
Cdd:TIGR02882 161 AGWTNYAPLAGpefSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKlmQMPMFTWTTLITTLIIIFAFPVLT 240

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-187 3.88e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 303.33  E-value: 3.88e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00153   42 PGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMN--NWTLFTWSILITTILLLLSLPVLA 155
Cdd:MTH00153  122 TGWTVYPPLSSNIahsGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTldRMPLFVWSVLITAILLLLSLPVLA 201

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00153  202 GAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-187 2.61e-96

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: 287.46  E-value: 2.61e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:cd01663    35 PGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMN--NWTLFTWSILITTILLLLSLPVLA 155
Cdd:cd01663   115 TGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTleKMPLFVWSVLITAFLLLLSLPVLA 194

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:cd01663   195 GAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-187 4.82e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 277.33  E-value: 4.82e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00167   44 PGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNN--SMNNWTLFTWSILITTILLLLSLPVLA 155
Cdd:MTH00167  124 TGWTVYPPLAGNLahaGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPgiTQYQTPLFVWSILVTTILLLLSLPVLA 203

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00167  204 AAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-187 7.78e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 274.28  E-value: 7.78e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00116   44 PGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMN--NWTLFTWSILITTILLLLSLPVLA 155
Cdd:MTH00116  124 TGWTVYPPLAGNLahaGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSqyQTPLFVWSVLITAVLLLLSLPVLA 203

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00116  204 AGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-187 1.22e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 261.07  E-value: 1.22e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00223   41 PGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMN--NWTLFTWSILITTILLLLSLPVLA 155
Cdd:MTH00223  121 TGWTVYPPLSSNLahaGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQleRLPLFVWSVKVTAFLLLLSLPVLA 200

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00223  201 GAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-187 4.90e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 259.27  E-value: 4.90e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00142   42 PGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMN--NWTLFTWSILITTILLLLSLPVLA 155
Cdd:MTH00142  122 TGWTVYPPLSSNLahsGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKfeRVPLFVWSVKITAILLLLSLPVLA 201

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00142  202 GAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-187 8.31e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 246.01  E-value: 8.31e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00077   44 PGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMNNWT--LFTWSILITTILLLLSLPVLA 155
Cdd:MTH00077  124 TGWTVYPPLAGNLahaGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQtpLFVWSVLITAVLLLLSLPVLA 203

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00077  204 AGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-187 3.57e-79

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 244.41  E-value: 3.57e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00103   44 PGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMNNWT--LFTWSILITTILLLLSLPVLA 155
Cdd:MTH00103  124 TGWTVYPPLAGNLahaGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQtpLFVWSVLITAVLLLLSLPVLA 203

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00103  204 AGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-187 4.16e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 244.45  E-value: 4.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00183   44 PGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMNNWT--LFTWSILITTILLLLSLPVLA 155
Cdd:MTH00183  124 TGWTVYPPLAGNLahaGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQtpLFVWAVLITAVLLLLSLPVLA 203

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00183  204 AGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-187 1.52e-77

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 240.19  E-value: 1.52e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00007   41 PGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSM--NNWTLFTWSILITTILLLLSLPVLA 155
Cdd:MTH00007  121 TGWTVYPPLASNLahaGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLrlERIPLFVWAVVITVVLLLLSLPVLA 200

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00007  201 GAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-187 1.98e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 232.41  E-value: 1.98e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00037   44 PGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNN--SMNNWTLFTWSILITTILLLLSLPVLA 155
Cdd:MTH00037  124 TGWTIYPPLSSNIahaGGSVDLAIFSLHLAGASSILASINFITTIINMRTPgmTFDRLPLFVWSVFITAFLLLLSLPVLA 203

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00037  204 GAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-187 7.65e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 230.34  E-value: 7.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00079   45 PGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLST--QLNPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSM--NNWTLFTWSILITTILLLLSLPVLAG 156
Cdd:MTH00079  125 TSWTVYPPLSTlgHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSIslEHMSLFVWTVFVTVFLLVLSLPVLAG 204

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1483571529 157 AITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00079  205 AITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-187 2.21e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 227.02  E-value: 2.21e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00184   46 PGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLS---TQLNPSIDLTIFSLHIAGISSILSSINFLCTIINMKNN--SMNNWTLFTWSILITTILLLLSLPVLA 155
Cdd:MTH00184  126 TGWTVYPPLSsiqAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPgiTMDRMPLFVWSILVTTFLLLLSLPVLA 205

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00184  206 GAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-187 8.45e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 220.46  E-value: 8.45e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00182   46 PGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLS---TQLNPSIDLTIFSLHIAGISSILSSINFLCTIINMK--NNSMNNWTLFTWSILITTILLLLSLPVLA 155
Cdd:MTH00182  126 TGWTVYPPLSsiqAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRapGVTFNRLPLFVWSILITAFLLLLSLPVLA 205

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00182  206 GAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-187 4.07e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 206.02  E-value: 4.07e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:MTH00026   45 PGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLST---QLNPSIDLTIFSLHIAGISSILSSINFLCTIINMKNN--SMNNWTLFTWSILITTILLLLSLPVLA 155
Cdd:MTH00026  125 TGWTVYPPLASiqaHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPgmTMSRIPLFVWSVFITAILLLLSLPVLA 204

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00026  205 GAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-187 3.77e-61

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: 196.60  E-value: 3.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPlMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:cd00919    33 PGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLSTQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMK--NNSMNNWTLFTWSILITTILLLLSLPVLA 155
Cdd:cd00919   112 TGWTFYPPLSTLSyssGVGVDLAILGLHLAGVSSILGAINFITTILNMRapGMTLDKMPLFVWSVLVTAILLLLALPVLA 191

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:cd00919   192 AALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 10-187 1.47e-53

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 177.95  E-value: 1.47e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  10 IYNSIVTSHAFVMIFFMVMPIMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAgtGTGWTVYPPL 89
Cdd:MTH00048   54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGA--GVGWTFYPPL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  90 STQLNPS---IDLTIFSLHIAGISSILSSINFLCTIINMKNNSMNNWT-LFTWSILITTILLLLSLPVLAGAITMILSDR 165
Cdd:MTH00048  132 SSSLFSSswgVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRTsIILWSYLFTSILLLLSLPVLAAAITMLLFDR 211

                         170       180
                  ....*....|....*....|..
gi 1483571529 166 NLNTTFFNPAGGGDPVLYQHLF 187
Cdd:MTH00048  212 NFGSAFFDPLGGGDPVLFQHMF 233
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
11-187 2.03e-52

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 175.32  E-value: 2.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  11 YNSIVTSHAFVMIFFMVMPiMLGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTGTGWTVYPPLS 90
Cdd:COG0843    57 YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  91 TQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMNNWT--LFTWSILITTILLLLSLPVLAGAITMILSDR 165
Cdd:COG0843   136 GLEaspGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRmpLFTWAALVTSILILLAFPVLAAALLLLLLDR 215

                         170       180
                  ....*....|....*....|..
gi 1483571529 166 NLNTTFFNPAGGGDPVLYQHLF 187
Cdd:COG0843   216 SLGTHFFDPAGGGDPLLWQHLF 237
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 11-187 1.17e-41

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: 146.19  E-value: 1.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  11 YNSIVTSHAFVMIFFMVMPIMLGgFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTGTGWTVYPPLS 90
Cdd:cd01662    49 YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLS 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  91 TQLN---PSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSM--NNWTLFTWSILITTILLLLSLPVLAGAITMILSDR 165
Cdd:cd01662   128 GLEYspgVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMtlMRMPIFTWTTLVTSILILFAFPVLTAALALLELDR 207

                         170       180
                  ....*....|....*....|..
gi 1483571529 166 NLNTTFFNPAGGGDPVLYQHLF 187
Cdd:cd01662   208 YFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-187 3.20e-33

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: 122.30  E-value: 3.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMlGGFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSniFGAGTg 80
Cdd:pfam00115  31 PGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLAS--FGGAT- 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLstqlnPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMN-NWTLFTWSILITTILLLLSLPVLAGAIT 159
Cdd:pfam00115 107 TGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTlRMPLFVWAILATAILILLAFPVLAAALL 181

                         170       180
                  ....*....|....*....|....*...
gi 1483571529 160 MILSDRNLNttffnpAGGGDPVLYQHLF 187
Cdd:pfam00115 182 LLLLDRSLG------AGGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-187 1.35e-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: 105.71  E-value: 1.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529   1 PGMLIGNDQIYNSIVTSHAFVMIFFMVMPIMLGgFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTG 80
Cdd:TIGR02882  82 PDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  81 TGWTVYPPLST---QLNPSIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMN--NWTLFTWSILITTILLLLSLPVLA 155
Cdd:TIGR02882 161 AGWTNYAPLAGpefSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKlmQMPMFTWTTLITTLIIIFAFPVLT 240

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1483571529 156 GAITMILSDRNLNTTFFNPAGGGDPVLYQHLF 187
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 11-186 3.25e-26

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 104.63  E-value: 3.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  11 YNSIVTSHAFVMIFFMVMPIMLGgFGNWLVPLMLNAPDMAFPRLNNMSFWLLIPSLTLLIYSNIFGAGTGTGWTVYPPLS 90
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483571529  91 -TQLNP--SIDLTIFSLHIAGISSILSSINFLCTIINMKNNSMNNWTL--FTWSILITTILLLLSLPVLAGAITMILSDR 165
Cdd:PRK15017  178 gIEYSPgvGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMpvFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180
                  ....*....|....*....|.
gi 1483571529 166 NLNTTFFNPAGGGDPVLYQHL 186
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINL 278
 
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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