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Conserved domains on  [gi|1829740872|gb|QIX11872|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Gryllidae sp. GRILLIDAE32]

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 ...
 2-221 4.56e-149

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: 424.28  E-value: 4.56e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00153    6 FSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLML 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00153   86 GAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITT 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00153  166 IINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 225
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-221 4.56e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 424.28  E-value: 4.56e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00153    6 FSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLML 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00153   86 GAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITT 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00153  166 IINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 225
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 4-221 5.91e-131

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: 377.59  E-value: 5.91e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   4 TNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGA 83
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  84 PDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITTMI 163
Cdd:cd01663    81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1829740872 164 NMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:cd01663   161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGD 218
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-221 3.12e-72

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 228.47  E-value: 3.12e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLML 81
Cdd:COG0843    11 TTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:COG0843    90 GARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVT 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:COG0843   170 ILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGD 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 8-217 2.00e-43

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: 150.80  E-value: 2.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   8 DIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMA 87
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  88 FPRMNNMSFWLLPPSLTLLLTSSMvenGAGTGWTVYPPLstgiahagASVDLAIFSLHLAGISSILGAVNFITTMINMRA 167
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1829740872 168 PGMSLdQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 217
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDPL 197
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 3-220 3.14e-34

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: 128.43  E-value: 3.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   3 STNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLG 82
Cdd:TIGR02882  47 TVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  83 APDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITTM 162
Cdd:TIGR02882 126 ARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTI 205

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1829740872 163 INMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 220
Cdd:TIGR02882 206 LKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGG 263
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-221 4.56e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 424.28  E-value: 4.56e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00153    6 FSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLML 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00153   86 GAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITT 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00153  166 IINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 225
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 4-221 5.91e-131

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: 377.59  E-value: 5.91e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   4 TNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGA 83
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  84 PDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITTMI 163
Cdd:cd01663    81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1829740872 164 NMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:cd01663   161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGD 218
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-221 8.35e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 372.86  E-value: 8.35e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00167    8 FSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00167   88 GAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITT 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00167  168 IINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGD 227
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-221 1.53e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 364.80  E-value: 1.53e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00116    8 FSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00116   88 GAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITT 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00116  168 CINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGD 227
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-221 9.71e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 362.50  E-value: 9.71e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00142    6 FSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLML 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00142   86 GAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITT 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00142  166 VINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGD 225
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-221 1.59e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 359.29  E-value: 1.59e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00223    5 FSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLML 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00223   85 GAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITT 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00223  165 IINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGD 224
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-221 1.07e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 334.49  E-value: 1.07e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00037    8 FSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00037   88 GAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITT 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00037  168 IINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGD 227
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-221 3.02e-113

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 333.39  E-value: 3.02e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00103    8 FSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00103   88 GAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITT 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00103  168 IINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGD 227
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-221 1.06e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 331.89  E-value: 1.06e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00183    8 FSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00183   88 GAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITT 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00183  168 IINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGD 227
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-221 3.32e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 330.75  E-value: 3.32e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00077    8 FSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00077   88 GAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITT 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00077  168 SINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGD 227
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-221 8.56e-110

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 324.55  E-value: 8.56e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00007    5 YSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLML 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00007   85 GAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITT 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00007  165 VINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 224
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-221 1.97e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 305.98  E-value: 1.97e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00182   10 FSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00182   90 GAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITT 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00182  170 IFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGD 229
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-221 3.12e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 305.21  E-value: 3.12e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00184   10 FSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00184   90 GAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITT 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00184  170 IFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGD 229
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 3-221 3.01e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 297.36  E-value: 3.01e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   3 STNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLG 82
Cdd:MTH00079   10 SSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  83 APDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTgIAHAGASVDLAIFSLHLAGISSILGAVNFITTM 162
Cdd:MTH00079   90 APDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTT 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1829740872 163 INMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00079  169 KNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGN 227
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-221 7.98e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 276.51  E-value: 7.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00026    9 FSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00026   89 GAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITT 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00026  169 VMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGD 228
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 6-221 2.43e-80

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: 247.44  E-value: 2.43e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   6 HKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMLGAPD 85
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  86 MAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITTMINM 165
Cdd:cd00919    80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1829740872 166 RAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:cd00919   160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGD 215
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-221 3.12e-72

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 228.47  E-value: 3.12e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLML 81
Cdd:COG0843    11 TTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:COG0843    90 GARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVT 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:COG0843   170 ILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGD 229
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-221 8.17e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 203.37  E-value: 8.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   2 FSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLML 81
Cdd:MTH00048    9 FTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  82 GAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVenGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITT 161
Cdd:MTH00048   89 GLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICT 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872 162 MINMRAPGMSLdQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:MTH00048  167 IYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGD 225
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 3-221 2.47e-56

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: 186.25  E-value: 2.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   3 STNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLG 82
Cdd:cd01662     4 TVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  83 APDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITTM 162
Cdd:cd01662    83 ARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTI 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1829740872 163 INMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:cd01662   163 LKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGN 221
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 8-217 2.00e-43

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: 150.80  E-value: 2.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   8 DIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMA 87
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  88 FPRMNNMSFWLLPPSLTLLLTSSMvenGAGTGWTVYPPLstgiahagASVDLAIFSLHLAGISSILGAVNFITTMINMRA 167
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1829740872 168 PGMSLdQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 217
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDPL 197
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 3-221 4.52e-36

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 133.91  E-value: 4.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   3 STNHKDIGTLYFIFGAWAGMVGTSLSILIRTE-----LGQPGYLigDDQTYNVIVTAHAFVMIFFMVMPIMIGgFGNWLV 77
Cdd:PRK15017   51 SVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqalasAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVV 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  78 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVN 157
Cdd:PRK15017  128 PLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGIN 207

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1829740872 158 FITTMINMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 221
Cdd:PRK15017  208 FFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGN 271
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 3-220 3.14e-34

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: 128.43  E-value: 3.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872   3 STNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGQPGYLIGDDQTYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLG 82
Cdd:TIGR02882  47 TVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740872  83 APDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGAGTGWTVYPPLSTGIAHAGASVDLAIFSLHLAGISSILGAVNFITTM 162
Cdd:TIGR02882 126 ARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTI 205

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1829740872 163 INMRAPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGG 220
Cdd:TIGR02882 206 LKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGG 263
 
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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