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Conserved domains on  [gi|1524090517|gb|AZB87480|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Tanystylum orbiculare]

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 ...
 1-217 4.55e-139

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: 398.86  E-value: 4.55e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00153   17 YFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00153   97 NMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00153  177 DRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-217 4.55e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 398.86  E-value: 4.55e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00153   17 YFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00153   97 NMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00153  177 DRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-217 4.30e-127

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: 367.58  E-value: 4.30e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:cd01663    10 YLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:cd01663    90 NLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:cd01663   170 EKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-217 1.29e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 221.54  E-value: 1.29e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMmIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:COG0843    22 YLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:COG0843   101 ALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTL 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:COG0843   181 MRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-217 4.06e-41

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: 144.64  E-value: 4.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMmIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:pfam00115   6 YLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSmveMGAGTGWTVYPPLssslahsgASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:pfam00115  85 ALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 eQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNtsffdpAGGGDPILYQHLF 217
Cdd:pfam00115 154 -RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-217 5.47e-37

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: 136.14  E-value: 5.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGgFGNWLVPIMINAPDMAFPRMN 80
Cdd:TIGR02882  57 YIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLN 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:TIGR02882 136 ALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKL 215

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:TIGR02882 216 MQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-217 4.55e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 398.86  E-value: 4.55e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00153   17 YFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00153   97 NMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00153  177 DRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-217 4.30e-127

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: 367.58  E-value: 4.30e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:cd01663    10 YLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:cd01663    90 NLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:cd01663   170 EKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-217 1.24e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 351.67  E-value: 1.24e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00167   19 YFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00167   99 NMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQ 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00167  179 YQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-217 1.75e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 343.88  E-value: 1.75e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00223   16 YLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00223   96 NMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQL 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00223  176 ERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-217 2.11e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 340.93  E-value: 2.11e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00142   17 YFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00142   97 NMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKF 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00142  177 ERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-217 5.03e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 335.14  E-value: 5.03e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00116   19 YLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00116   99 NMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQ 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00116  179 YQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-217 8.45e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 311.47  E-value: 8.45e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00183   19 YLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00183   99 NMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQ 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00183  179 YQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-217 9.92e-105

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 311.43  E-value: 9.92e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00103   19 YLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00103   99 NMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQ 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00103  179 YQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-217 6.05e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 309.18  E-value: 6.05e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00077   19 YLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00077   99 NMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQ 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00077  179 YQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-217 1.26e-101

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 303.36  E-value: 1.26e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00007   16 YFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00007   96 NMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRL 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00007  176 ERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-217 2.08e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 302.90  E-value: 2.08e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00037   19 YLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00037   99 NMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTF 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00037  179 DRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-217 8.41e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 301.74  E-value: 8.41e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00182   21 YLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00182  101 NISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTF 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00182  181 NRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-217 1.21e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 295.97  E-value: 1.21e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00184   21 YLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00184  101 NISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITM 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00184  181 DRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-217 1.41e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 282.72  E-value: 1.41e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00079   20 YFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLsSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00079  100 NLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISL 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00079  179 EHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-217 9.77e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 276.12  E-value: 9.77e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00026   20 YLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:MTH00026  100 NISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTM 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00026  180 SRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-217 3.31e-79

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: 244.36  E-value: 3.31e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPiMINAPDMAFPRMN 80
Cdd:cd00919     8 YLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:cd00919    87 NLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:cd00919   167 DKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-217 1.29e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 221.54  E-value: 1.29e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMmIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:COG0843    22 YLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:COG0843   101 ALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTL 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:COG0843   181 MRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-217 1.34e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 205.30  E-value: 1.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:MTH00048   20 YTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMveMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMkL 160
Cdd:MTH00048  100 ALSAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV-F 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:MTH00048  177 SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-217 7.58e-57

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: 187.40  E-value: 7.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGgFGNWLVPIMINAPDMAFPRMN 80
Cdd:cd01662    14 YIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:cd01662    93 ALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:cd01662   173 MRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-217 4.06e-41

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: 144.64  E-value: 4.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMmIGGFGNWLVPIMINAPDMAFPRMN 80
Cdd:pfam00115   6 YLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSmveMGAGTGWTVYPPLssslahsgASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:pfam00115  85 ALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 eQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNtsffdpAGGGDPILYQHLF 217
Cdd:pfam00115 154 -RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-217 5.47e-37

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: 136.14  E-value: 5.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517   1 YLIFGVWSAMMGTALSMLIRIELGTPSSLIGDDQIYNVIVTSHAFVMIFFMVMPMMIGgFGNWLVPIMINAPDMAFPRMN 80
Cdd:TIGR02882  57 YIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLN 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  81 NMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLSSSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKL 160
Cdd:TIGR02882 136 ALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKL 215

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524090517 161 EQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 217
Cdd:TIGR02882 216 MQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 36-216 8.82e-32

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 121.58  E-value: 8.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517  36 YNVIVTSHAFVMIFFMVMPMMIGgFGNWLVPIMINAPDMAFPRMNNMSFWLLPPSLLLLISSSMVEMGAGTGWTVYPPLS 115
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524090517 116 SSLAHSGASVDLTIFSLHLAGVSSILGAINFISTILNMRTVGMKLEQMPLFVWSVLITAVLLLLSLPVLAGAITMLLTDR 195
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180
                  ....*....|....*....|.
gi 1524090517 196 NFNTSFFDPAGGGDPILYQHL 216
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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