NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1824874832|gb|QIQ54401|]
View 

cytochrome c oxidase subunit 1, partial (mitochondrion) [Spizella pusilla]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-174 3.85e-121

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 MTH00116:

Pssm-ID: 469701  Cd Length: 515  Bit Score: 351.32  E-value: 3.85e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00116   46 TLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00116  126 WTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAG 205

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00116  206 ITMLLTDRNLNTTF 219
 
Name Accession Description Interval E-value
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-174 3.85e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 351.32  E-value: 3.85e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00116   46 TLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00116  126 WTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAG 205

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00116  206 ITMLLTDRNLNTTF 219
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-174 3.04e-94

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: 281.68  E-value: 3.04e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   2 LLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGW 81
Cdd:cd01663    38 QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGW 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  82 TVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGI 161
Cdd:cd01663   118 TVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAI 197

                         170
                  ....*....|...
gi 1824874832 162 TMLLTDRNLNTTF 174
Cdd:cd01663   198 TMLLTDRNFNTSF 210
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
7-174 1.87e-48

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 164.14  E-value: 1.87e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   7 QVYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPP 86
Cdd:COG0843    55 ETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPP 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  87 LAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLT 166
Cdd:COG0843   134 LSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLL 213


                  ....*...
gi 1824874832 167 DRNLNTTF 174
Cdd:COG0843   214 DRSLGTHF 221
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-172 3.26e-30

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: 113.82  E-value: 3.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   2 LLGDDQVYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASStveAGVGTGW 81
Cdd:pfam00115  34 NFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  82 TVYPPLAGnlahagasVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQyQTPLFVWSVLITAVLLLLSLPVLAAGI 161
Cdd:pfam00115 110 TEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAAL 180

                         170
                  ....*....|.
gi 1824874832 162 TMLLTDRNLNT 172
Cdd:pfam00115 181 LLLLLDRSLGA 191
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 5-174 5.99e-29

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: 111.87  E-value: 5.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   5 DDQVYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVY 84
Cdd:TIGR02882  88 DAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  85 PPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITML 164
Cdd:TIGR02882 167 APLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALM 246

                         170
                  ....*....|
gi 1824874832 165 LTDRNLNTTF 174
Cdd:TIGR02882 247 TTDRIFDTAF 256
 
Name Accession Description Interval E-value
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-174 3.85e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 351.32  E-value: 3.85e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00116   46 TLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00116  126 WTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAG 205

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00116  206 ITMLLTDRNLNTTF 219
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-174 6.21e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 299.48  E-value: 6.21e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00153   44 SLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00153  124 WTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGA 203

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00153  204 ITMLLTDRNLNTSF 217
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-174 9.26e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 288.88  E-value: 9.26e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00167   46 SLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00167  126 WTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAA 205

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00167  206 ITMLLTDRNLNTTF 219
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-174 3.04e-94

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: 281.68  E-value: 3.04e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   2 LLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGW 81
Cdd:cd01663    38 QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGW 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  82 TVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGI 161
Cdd:cd01663   118 TVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAI 197

                         170
                  ....*....|...
gi 1824874832 162 TMLLTDRNLNTTF 174
Cdd:cd01663   198 TMLLTDRNFNTSF 210
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-174 3.31e-93

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 279.84  E-value: 3.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00103   46 TLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00103  126 WTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAG 205

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00103  206 ITMLLTDRNLNTTF 219
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-174 4.43e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 277.19  E-value: 4.43e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00183   46 ALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00183  126 WTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAG 205

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00183  206 ITMLLTDRNLNTTF 219
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-174 9.74e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 276.05  E-value: 9.74e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00077   46 TLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00077  126 WTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAG 205

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00077  206 ITMLLTDRNLNTTF 219
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-174 4.28e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 266.84  E-value: 4.28e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00223   43 ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00223  123 WTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGA 202

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00223  203 ITMLLTDRNFNTSF 216
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-174 1.41e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 265.43  E-value: 1.41e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00142   44 SLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00142  124 WTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGA 203

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00142  204 ITMLLTDRNFNTSF 217
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-174 9.62e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 242.81  E-value: 9.62e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00037   46 SLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00037  126 WTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGA 205

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00037  206 ITMLLTDRNINTTF 219
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-174 3.96e-77

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 238.65  E-value: 3.96e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00007   43 AFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00007  123 WTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGA 202

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00007  203 ITMLLTDRNLNTSF 216
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-174 3.90e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 231.25  E-value: 3.90e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00182   48 AMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00182  128 WTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGA 207

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00182  208 ITMLLTDRNFNTTF 221
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-174 6.51e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 227.79  E-value: 6.51e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00184   48 SMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00184  128 WTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGA 207

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00184  208 ITMLLTDRNFNTTF 221
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-174 9.73e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 214.16  E-value: 9.73e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   2 LLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGW 81
Cdd:MTH00079   48 LLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSW 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  82 TVYPPLAgNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGI 161
Cdd:MTH00079  128 TVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAI 206

                         170
                  ....*....|...
gi 1824874832 162 TMLLTDRNLNTTF 174
Cdd:MTH00079  207 TMLLTDRNLNTSF 219
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-174 1.48e-66

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 211.80  E-value: 1.48e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:MTH00026   47 SMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:MTH00026  127 WTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGA 206

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:MTH00026  207 ITMLLTDRNFNTTF 220
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-174 6.31e-56

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: 182.35  E-value: 6.31e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   1 ALLGDDQVYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTG 80
Cdd:cd00919    35 SLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  81 WTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAG 160
Cdd:cd00919   114 WTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAA 193

                         170
                  ....*....|....
gi 1824874832 161 ITMLLTDRNLNTTF 174
Cdd:cd00919   194 LVMLLLDRNFGTSF 207
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
7-174 1.87e-48

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 164.14  E-value: 1.87e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   7 QVYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPP 86
Cdd:COG0843    55 ETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPP 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  87 LAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLT 166
Cdd:COG0843   134 LSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLL 213


                  ....*...
gi 1824874832 167 DRNLNTTF 174
Cdd:COG0843   214 DRSLGTHF 221
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 8-174 1.79e-41

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 145.21  E-value: 1.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   8 VYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASstVEAGVGTGWTVYPPL 87
Cdd:MTH00048   54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  88 AGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSqYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTD 167
Cdd:MTH00048  132 SSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFD 210


                  ....*..
gi 1824874832 168 RNLNTTF 174
Cdd:MTH00048  211 RNFGSAF 217
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 7-174 6.02e-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: 143.49  E-value: 6.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   7 QVYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPP 86
Cdd:cd01662    47 EHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPP 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  87 LAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLT 166
Cdd:cd01662   126 LSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLEL 205


                  ....*...
gi 1824874832 167 DRNLNTTF 174
Cdd:cd01662   206 DRYFGTHF 213
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 9-174 5.64e-31

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 117.34  E-value: 5.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   9 YNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLA 88
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  89 GNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDR 168
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257


                  ....*.
gi 1824874832 169 NLNTTF 174
Cdd:PRK15017  258 YLGTHF 263
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-172 3.26e-30

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: 113.82  E-value: 3.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   2 LLGDDQVYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASStveAGVGTGW 81
Cdd:pfam00115  34 NFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  82 TVYPPLAGnlahagasVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQyQTPLFVWSVLITAVLLLLSLPVLAAGI 161
Cdd:pfam00115 110 TEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAAL 180

                         170
                  ....*....|.
gi 1824874832 162 TMLLTDRNLNT 172
Cdd:pfam00115 181 LLLLLDRSLGA 191
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 5-174 5.99e-29

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: 111.87  E-value: 5.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832   5 DDQVYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVY 84
Cdd:TIGR02882  88 DAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824874832  85 PPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITML 164
Cdd:TIGR02882 167 APLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALM 246

                         170
                  ....*....|
gi 1824874832 165 LTDRNLNTTF 174
Cdd:TIGR02882 247 TTDRIFDTAF 256
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH