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Conserved domains on  [gi|939320640|gb|ALJ77125|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Tettigonia cf. longealata tmo2a]

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 ...
 2-182 2.26e-30

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: 116.51  E-value: 2.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   2 STIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGN-CYPFMLG 69
Cdd:MTH00153   7 STNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAhafimiffmvmPIMIGGFGNwLVPLMLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640  70 AP-MYIP-------------------SNMYTSG------YYPLLYPFMKYLKSVLVLERFTLlyHqvlLCGGLSDLQSSH 123
Cdd:MTH00153  87 APdMAFPrmnnmsfwllppsltlllsSSMVESGagtgwtVYPPLSSNIAHSGASVDLAIFSL--H---LAGISSILGAIN 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 939320640 124 YICrSFIHPRSSKLYYNNhqytsswyitgsNTFICWAVAITALLLLLSLPVQAGAITML 182
Cdd:MTH00153 162 FIT-TIINMRSKGMTLDR------------MPLFVWSVLITAILLLLSLPVLAGAITML 207
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-182 2.26e-30

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 116.51  E-value: 2.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   2 STIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGN-CYPFMLG 69
Cdd:MTH00153   7 STNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAhafimiffmvmPIMIGGFGNwLVPLMLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640  70 AP-MYIP-------------------SNMYTSG------YYPLLYPFMKYLKSVLVLERFTLlyHqvlLCGGLSDLQSSH 123
Cdd:MTH00153  87 APdMAFPrmnnmsfwllppsltlllsSSMVESGagtgwtVYPPLSSNIAHSGASVDLAIFSL--H---LAGISSILGAIN 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 939320640 124 YICrSFIHPRSSKLYYNNhqytsswyitgsNTFICWAVAITALLLLLSLPVQAGAITML 182
Cdd:MTH00153 162 FIT-TIINMRSKGMTLDR------------MPLFVWSVLITAILLLLSLPVLAGAITML 207
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 3-71 5.56e-22

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: 92.93  E-value: 5.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   3 TIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSSciH-------------IGGFGNCY-PFML 68
Cdd:cd01663    1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTA--HalimiffmvmpalIGGFGNWLvPLMI 78


                 ...
gi 939320640  69 GAP 71
Cdd:cd01663   79 GAP 81
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-71 5.33e-05

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 43.19  E-value: 5.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   1 WSTIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSscIH------------IGGFGNcY--PF 66
Cdd:COG0843   11 TTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFT--MHgtimifffatpfLAGFGN-YlvPL 87


                 ....*
gi 939320640  67 MLGAP 71
Cdd:COG0843   88 QIGAR 92
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 7-72 7.05e-04

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: 39.86  E-value: 7.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939320640    7 DIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSscIH------------IGGFGN-CYPFMLGAPM 72
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRT--LHgnlmifwfatpfLFGFGNyLVPLMIGARD 77
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-182 2.26e-30

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 116.51  E-value: 2.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   2 STIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGN-CYPFMLG 69
Cdd:MTH00153   7 STNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAhafimiffmvmPIMIGGFGNwLVPLMLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640  70 AP-MYIP-------------------SNMYTSG------YYPLLYPFMKYLKSVLVLERFTLlyHqvlLCGGLSDLQSSH 123
Cdd:MTH00153  87 APdMAFPrmnnmsfwllppsltlllsSSMVESGagtgwtVYPPLSSNIAHSGASVDLAIFSL--H---LAGISSILGAIN 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 939320640 124 YICrSFIHPRSSKLYYNNhqytsswyitgsNTFICWAVAITALLLLLSLPVQAGAITML 182
Cdd:MTH00153 162 FIT-TIINMRSKGMTLDR------------MPLFVWSVLITAILLLLSLPVLAGAITML 207
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-182 1.63e-25

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 103.22  E-value: 1.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   2 STIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGN-CYPFMLG 69
Cdd:MTH00167   9 STNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAhafvmiffmvmPIMIGGFGNwLVPLMIG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640  70 AP-MYIP-------------------SNMYTSG------YYPLLYPFMKYLKSVLVLERFTLlyHqvlLCGGLSDLQSSH 123
Cdd:MTH00167  89 APdMAFPrmnnmsfwllppslllllaSSGVEAGagtgwtVYPPLAGNLAHAGASVDLAIFSL--H---LAGVSSILGSIN 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 939320640 124 YICRSFihprssklyyNNHQYTSSWYITgsnTFICWAVAITALLLLLSLPVQAGAITML 182
Cdd:MTH00167 164 FITTII----------NMKPPGITQYQT---PLFVWSILVTTILLLLSLPVLAAAITML 209
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-182 7.05e-25

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 101.32  E-value: 7.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   2 STIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGN-CYPFMLG 69
Cdd:MTH00116   9 STNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAhafvmiffmvmPIMIGGFGNwLVPLMIG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640  70 AP-MYIP--SNM------------YTSGY-----------YPLLYPFMKYLKSVLVLERFTLlyHqvlLCGGLSDLQSSH 123
Cdd:MTH00116  89 APdMAFPrmNNMsfwllppsflllLASSTveagagtgwtvYPPLAGNLAHAGASVDLAIFSL--H---LAGVSSILGAIN 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939320640 124 YI--CRSFIHPRSSklyynnhQYTSSWYItgsntficWAVAITALLLLLSLPVQAGAITML 182
Cdd:MTH00116 164 FIttCINMKPPAMS-------QYQTPLFV--------WSVLITAVLLLLSLPVLAAGITML 209
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-182 2.93e-24

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 99.41  E-value: 2.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   2 STIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGN-CYPFMLG 69
Cdd:MTH00142   7 STNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAhafvmiffmvmPVMIGGFGNwLVPLMLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640  70 AP-MYIP--SNMytsgYYPLLYPFMKYLKSVLVLER--------FTLLYHQVLLCGGLSDLQsshyICRSFIHPRSSKLY 138
Cdd:MTH00142  87 APdMAFPrmNNM----SFWLLPPALLLLLSSAAVESgagtgwtvYPPLSSNLAHSGGSVDLA----IFSLHLAGVSSILG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 939320640 139 YNNHQYTSSWYITGSNTF-----ICWAVAITALLLLLSLPVQAGAITML 182
Cdd:MTH00142 159 AINFITTVINMRAGGMKFervplFVWSVKITAILLLLSLPVLAGAITML 207
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-99 3.98e-22

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 93.41  E-value: 3.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   1 WSTIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGN-CYPFML 68
Cdd:MTH00103   8 FSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAhafvmiffmvmPIMIGGFGNwLVPLMI 87

                         90       100       110
                 ....*....|....*....|....*....|.
gi 939320640  69 GAPMYIPSNMYTSGYYPLLYPFMKYLKSVLV 99
Cdd:MTH00103  88 GAPDMAFPRMNNMSFWLLPPSFLLLLASSMV 118
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-99 4.48e-22

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 93.47  E-value: 4.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   1 WSTIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGN-CYPFML 68
Cdd:MTH00077   8 FSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAhafvmiffmvmPIMIGGFGNwLVPLMI 87

                         90       100       110
                 ....*....|....*....|....*....|.
gi 939320640  69 GAPMYIPSNMYTSGYYPLLYPFMKYLKSVLV 99
Cdd:MTH00077  88 GAPDMAFPRMNNMSFWLLPPSFLLLLASSGV 118
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 3-71 5.56e-22

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: 92.93  E-value: 5.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   3 TIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSSciH-------------IGGFGNCY-PFML 68
Cdd:cd01663    1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTA--HalimiffmvmpalIGGFGNWLvPLMI 78


                 ...
gi 939320640  69 GAP 71
Cdd:cd01663   79 GAP 81
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-71 9.79e-22

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 92.29  E-value: 9.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   1 WSTIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGN-CYPFML 68
Cdd:MTH00183   8 FSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAhafvmiffmvmPIMIGGFGNwLIPLMI 87


                 ...
gi 939320640  69 GAP 71
Cdd:MTH00183  88 GAP 90
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-71 2.49e-20

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 88.50  E-value: 2.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   1 WSTIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGN-CYPFML 68
Cdd:MTH00223   5 FSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAhafvmifflvmPMMIGGFGNwLVPLML 84


                 ...
gi 939320640  69 GAP 71
Cdd:MTH00223  85 GAP 87
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-182 2.90e-20

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 88.35  E-value: 2.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   1 WSTIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGN-CYPFML 68
Cdd:MTH00037   8 FSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAhalvmiffmvmPIMIGGFGNwLIPLMI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640  69 GAPMYIPSNMYTSGYYPLLYPFMKYLKSVLV-------LERFTLLYHQVLLCGGLSDLQsshyICRSFIHPRSSKLYYNN 141
Cdd:MTH00037  88 GAPDMAFPRMNNMSFWLIPPSFLLLLASAGVesgagtgWTIYPPLSSNIAHAGGSVDLA----IFSLHLAGASSILASIN 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 939320640 142 HQYTSSWYITGSNTF-----ICWAVAITALLLLLSLPVQAGAITML 182
Cdd:MTH00037 164 FITTIINMRTPGMTFdrlplFVWSVFITAFLLLLSLPVLAGAITML 209
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-71 2.67e-15

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 73.71  E-value: 2.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   1 WSTIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGNCY-PFML 68
Cdd:MTH00184  10 FSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAhafvmifflvmPVMIGGFGNWFvPLYI 89


                 ...
gi 939320640  69 GAP 71
Cdd:MTH00184  90 GAP 92
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-71 1.37e-13

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 68.94  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   2 STIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGN-CYPFMLG 69
Cdd:MTH00079  10 SSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAhailmiffmvmPSMIGGFGNwMLPLMLG 89


                 ..
gi 939320640  70 AP 71
Cdd:MTH00079  90 AP 91
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-182 9.97e-13

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 66.19  E-value: 9.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   1 WSTIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGNCY-PFML 68
Cdd:MTH00026   9 FSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAhafvmifflvmPTMIGGFGNWFvPLMI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640  69 GAPMYIPSNMYTSGYYPLLYPFMKYLKSVLVLER-------FTLLYHQVLLCGGLSDLQ--SSHYICRSFIHPRSSKLYY 139
Cdd:MTH00026  89 GAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGagtgwtvYPPLASIQAHSGGSVDMAifSLHLAGLSSILGAMNFITT 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 939320640 140 NNHQYTSSWYITGSNTFIcWAVAITALLLLLSLPVQAGAITML 182
Cdd:MTH00026 169 VMNMRTPGMTMSRIPLFV-WSVFITAILLLLSLPVLAGAITML 210
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 5-71 8.53e-11

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: 60.62  E-value: 8.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   5 HKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSscIH-------------IGGFGNCYPFMLGAP 71
Cdd:cd00919    1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVT--AHgvimifffvmpaiFGGFGNLLPPLIGAR 78
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 5-71 3.18e-07

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 50.06  E-value: 3.18e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939320640   5 HKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSS-----------CIHIGGFGNCY-PFMLGAP 71
Cdd:MTH00048  13 HKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNhgiimiffflmPVLIGGFGNYLlPLLLGLS 91
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-71 5.33e-05

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 43.19  E-value: 5.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939320640   1 WSTIHKDIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSscIH------------IGGFGNcY--PF 66
Cdd:COG0843   11 TTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFT--MHgtimifffatpfLAGFGN-YlvPL 87


                 ....*
gi 939320640  67 MLGAP 71
Cdd:COG0843   88 QIGAR 92
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 7-72 7.05e-04

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: 39.86  E-value: 7.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939320640    7 DIGTLYFIFGASAGMVGTSLSLLIRAEFGQPGYLIGEDQIYNVLYSscIH------------IGGFGN-CYPFMLGAPM 72
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRT--LHgnlmifwfatpfLFGFGNyLVPLMIGARD 77
 
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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