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Conserved domains on  [gi|124808998|ref|XP_001348462|]
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cytochrome c oxidase subunit 2, putative [Plasmodium falciparum 3D7]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 10015171)

cytochrome c oxidase subunit II, together with subunit I, forms the functional core of the enzyme that catalyzes the reduction of O2 and simultaneously pumps protons across the membrane; similar to Toxoplasma gondii cytochrome c oxidase subunit IIB (COXIIB)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
1-172 1.10e-119

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 240243  Cd Length: 162  Bit Score: 334.48  E-value: 1.10e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998   1 MDKIKSWLGFNKkivftenkflLRNVNDQESLQAENVRAEDYPIPEKYLEDPDKIPKYYVFQSNMVTDEDLQPGMLRQLE 80
Cdd:PTZ00047   1 MNLLRSLLGPAN----------ISNANEEGEVKLQDVSAEDYPIPQKYLEDPDLIPKYYSFQSNLVTDEDLKPGMLRQLE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  81 VDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFMPIVVEAVSPE 160
Cdd:PTZ00047  71 VDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVSPE 150
                        170
                 ....*....|..
gi 124808998 161 AYAAHAKKYYKE 172
Cdd:PTZ00047 151 AYAAHAKKYYKD 162
 
Name Accession Description Interval E-value
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
1-172 1.10e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243  Cd Length: 162  Bit Score: 334.48  E-value: 1.10e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998   1 MDKIKSWLGFNKkivftenkflLRNVNDQESLQAENVRAEDYPIPEKYLEDPDKIPKYYVFQSNMVTDEDLQPGMLRQLE 80
Cdd:PTZ00047   1 MNLLRSLLGPAN----------ISNANEEGEVKLQDVSAEDYPIPQKYLEDPDLIPKYYSFQSNLVTDEDLKPGMLRQLE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  81 VDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFMPIVVEAVSPE 160
Cdd:PTZ00047  71 VDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVSPE 150
                        170
                 ....*....|..
gi 124808998 161 AYAAHAKKYYKE 172
Cdd:PTZ00047 151 AYAAHAKKYYKD 162
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
59-162 3.70e-62

C-terminal domain of Cytochrome c Oxidase subunit II; 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 187.78  E-value: 3.70e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  59 YVFQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQ 138
Cdd:cd13912   24 LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQ 103
                         90       100
                 ....*....|....*....|....
gi 124808998 139 CSEMCGTLHGFMPIVVEAVSPEAY 162
Cdd:cd13912  104 CSEICGANHSFMPIVVEAVSLEDF 127
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
61-157 3.10e-55

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 169.90  E-value: 3.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998   61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:pfam00116  24 FDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCS 103
                          90
                  ....*....|....*..
gi 124808998  141 EMCGTLHGFMPIVVEAV 157
Cdd:pfam00116 104 EICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
79-168 7.63e-31

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 224537 [Multi-domain]  Cd Length: 247  Bit Score: 111.69  E-value: 7.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  79 LEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFMPIVVEAVS 158
Cdd:COG1622  133 IATVNELVLPVGRPVRFKLTSADVIHSFWIPQLGGKIDAIPGMTTELWLTANKPGTYRGICAEYCGPGHSFMRFKVIVVS 212
                         90
                 ....*....|
gi 124808998 159 PEAYAAHAKK 168
Cdd:COG1622  213 QEDFDAWVAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
85-164 5.47e-29

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 105.54  E-value: 5.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998   85 LTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFMPIVVEAVSPEAYAA 164
Cdd:TIGR02866 117 LVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDA 196
 
Name Accession Description Interval E-value
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
1-172 1.10e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243  Cd Length: 162  Bit Score: 334.48  E-value: 1.10e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998   1 MDKIKSWLGFNKkivftenkflLRNVNDQESLQAENVRAEDYPIPEKYLEDPDKIPKYYVFQSNMVTDEDLQPGMLRQLE 80
Cdd:PTZ00047   1 MNLLRSLLGPAN----------ISNANEEGEVKLQDVSAEDYPIPQKYLEDPDLIPKYYSFQSNLVTDEDLKPGMLRQLE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  81 VDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFMPIVVEAVSPE 160
Cdd:PTZ00047  71 VDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVSPE 150
                        170
                 ....*....|..
gi 124808998 161 AYAAHAKKYYKE 172
Cdd:PTZ00047 151 AYAAHAKKYYKD 162
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
59-162 3.70e-62

C-terminal domain of Cytochrome c Oxidase subunit II; 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 187.78  E-value: 3.70e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  59 YVFQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQ 138
Cdd:cd13912   24 LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQ 103
                         90       100
                 ....*....|....*....|....
gi 124808998 139 CSEMCGTLHGFMPIVVEAVSPEAY 162
Cdd:cd13912  104 CSEICGANHSFMPIVVEAVSLEDF 127
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
61-157 3.10e-55

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 169.90  E-value: 3.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998   61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:pfam00116  24 FDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCS 103
                          90
                  ....*....|....*..
gi 124808998  141 EMCGTLHGFMPIVVEAV 157
Cdd:pfam00116 104 EICGINHSFMPIVIEAV 120
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
61-162 2.07e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 161.26  E-value: 2.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:MTH00140 118 FDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCS 197
                         90       100
                 ....*....|....*....|..
gi 124808998 141 EMCGTLHGFMPIVVEAVSPEAY 162
Cdd:MTH00140 198 EICGANHSFMPIVVEAVPLEDF 219
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
61-162 4.64e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 160.53  E-value: 4.64e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:MTH00168 118 FDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCS 197
                         90       100
                 ....*....|....*....|..
gi 124808998 141 EMCGTLHGFMPIVVEAVSPEAY 162
Cdd:MTH00168 198 EICGANHSFMPIVVEFVPWETF 219
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
61-157 2.38e-48

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 156.23  E-value: 2.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:MTH00117 118 FDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCS 197
                         90
                 ....*....|....*..
gi 124808998 141 EMCGTLHGFMPIVVEAV 157
Cdd:MTH00117 198 EICGANHSFMPIVVESV 214
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
61-162 5.64e-48

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 154.99  E-value: 5.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:MTH00154 118 FDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCS 197
                         90       100
                 ....*....|....*....|..
gi 124808998 141 EMCGTLHGFMPIVVEAVSPEAY 162
Cdd:MTH00154 198 EICGANHSFMPIVIESVSVNNF 219
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
61-162 1.14e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 154.49  E-value: 1.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:MTH00139 118 FDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCS 197
                         90       100
                 ....*....|....*....|..
gi 124808998 141 EMCGTLHGFMPIVVEAVSPEAY 162
Cdd:MTH00139 198 EICGANHSFMPIVVEAISPKFF 219
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
61-162 4.73e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 152.93  E-value: 4.73e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:MTH00038 118 FDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCS 197
                         90       100
                 ....*....|....*....|..
gi 124808998 141 EMCGTLHGFMPIVVEAVSPEAY 162
Cdd:MTH00038 198 EICGANHSFMPIVIESVPFNTF 219
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
61-158 7.63e-45

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 147.17  E-value: 7.63e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:MTH00098 118 FDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCS 197
                         90
                 ....*....|....*...
gi 124808998 141 EMCGTLHGFMPIVVEAVS 158
Cdd:MTH00098 198 EICGSNHSFMPIVLELVP 215
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
61-162 5.03e-44

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 145.66  E-value: 5.03e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:MTH00023 129 FDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCS 208
                         90       100
                 ....*....|....*....|..
gi 124808998 141 EMCGTLHGFMPIVVEAVSPEAY 162
Cdd:MTH00023 209 EICGANHSFMPIVIEAVSLDKY 230
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
61-162 5.07e-44

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 145.38  E-value: 5.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:MTH00008 118 FDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCS 197
                         90       100
                 ....*....|....*....|..
gi 124808998 141 EMCGTLHGFMPIVVEAVSPEAY 162
Cdd:MTH00008 198 EICGANHSFMPIVLEAVDTKSF 219
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
61-162 1.18e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 141.84  E-value: 1.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:MTH00051 122 FDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCS 201
                         90       100
                 ....*....|....*....|..
gi 124808998 141 EMCGTLHGFMPIVVEAVSPEAY 162
Cdd:MTH00051 202 EICGANHSFMPIVIEGVSLDKY 223
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
60-157 1.51e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 138.76  E-value: 1.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  60 VFQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQC 139
Cdd:MTH00076 117 SFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQC 196
                         90
                 ....*....|....*...
gi 124808998 140 SEMCGTLHGFMPIVVEAV 157
Cdd:MTH00076 197 SEICGANHSFMPIVVEAT 214
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
61-162 5.19e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 137.54  E-value: 5.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKiTTFIL-REGVYYGQC 139
Cdd:MTH00129 118 FDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQ-TAFIAsRPGVFYGQC 196
                         90       100
                 ....*....|....*....|...
gi 124808998 140 SEMCGTLHGFMPIVVEAVSPEAY 162
Cdd:MTH00129 197 SEICGANHSFMPIVVEAVPLEHF 219
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
61-157 1.08e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 134.24  E-value: 1.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:MTH00185 118 FDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCS 197
                         90
                 ....*....|....*..
gi 124808998 141 EMCGTLHGFMPIVVEAV 157
Cdd:MTH00185 198 EICGANHSFMPIVVEAV 214
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
61-158 1.67e-35

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 123.20  E-value: 1.67e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  61 FQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCS 140
Cdd:MTH00080 121 FDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCS 200
                         90
                 ....*....|....*...
gi 124808998 141 EMCGTLHGFMPIVVEAVS 158
Cdd:MTH00080 201 EICGANHSFMPIAVEVTL 218
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
57-162 1.69e-35

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 124.37  E-value: 1.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  57 KYYVFQSNMVTDEDLQPGMLRQLEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYY 136
Cdd:MTH00027 148 KNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFY 227
                         90       100
                 ....*....|....*....|....*.
gi 124808998 137 GQCSEMCGTLHGFMPIVVEAVSPEAY 162
Cdd:MTH00027 228 GQCSEICGANHSFMPIVVESVSLSKY 253
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
79-168 7.63e-31

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 224537 [Multi-domain]  Cd Length: 247  Bit Score: 111.69  E-value: 7.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  79 LEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFMPIVVEAVS 158
Cdd:COG1622  133 IATVNELVLPVGRPVRFKLTSADVIHSFWIPQLGGKIDAIPGMTTELWLTANKPGTYRGICAEYCGPGHSFMRFKVIVVS 212
                         90
                 ....*....|
gi 124808998 159 PEAYAAHAKK 168
Cdd:COG1622  213 QEDFDAWVAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
85-164 5.47e-29

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 105.54  E-value: 5.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998   85 LTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFMPIVVEAVSPEAYAA 164
Cdd:TIGR02866 117 LVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDA 196
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
81-159 1.46e-28

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 104.27  E-value: 1.46e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124808998  81 VDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFMPIVVEAVSP 159
Cdd:MTH00047 114 VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDV 192
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
79-155 8.41e-21

Cupredoxin domain of Heme-copper oxidase subunit II; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 81.57  E-value: 8.41e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124808998  79 LEVDKRLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFMPIVVE 155
Cdd:cd13842   19 VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
84-162 1.49e-20

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 81.30  E-value: 1.49e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124808998  84 RLTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFMPIVVEAVSPEAY 162
Cdd:cd13914   26 QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEY 104
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
85-157 1.05e-18

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 76.50  E-value: 1.05e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124808998  85 LTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFMPIVVEAV 157
Cdd:cd04213   31 LHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
67-155 1.22e-16

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 71.13  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  67 TDEDLQPGMLRqLEVDKRltlptrthISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTL 146
Cdd:cd13919   26 TDDDVTSPELH-LPVGRP--------VLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLG 96
                         90
                 ....*....|.
gi 124808998 147 HGFM--PIVVE 155
Cdd:cd13919   97 HYRMraTVKVV 107
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
85-164 1.52e-15

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 69.41  E-value: 1.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808998  85 LTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRlHKITTFILRE-GVYYGQCSEMCGTLHGFMPIVVEAVSPEAYA 163
Cdd:cd13918   58 LRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGE-YTSTWFEADEpGTYEAKCYELCGSGHSLMTGDVIVMDEEEFE 136

                 .
gi 124808998 164 A 164
Cdd:cd13918  137 A 137
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
85-156 3.60e-11

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 56.48  E-value: 3.60e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124808998  85 LTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFMPIVVEA 156
Cdd:cd13915   27 LHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
85-155 1.37e-10

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 55.27  E-value: 1.37e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124808998  85 LTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFM--PIVVE 155
Cdd:cd13913   27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
83-150 9.53e-05

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 39.29  E-value: 9.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124808998  83 KRLTLPTRTHISFLVTATDVIHSWSI--PSLGIKAD--AIPGRLHKITTFILREGVYYGQCSEMCGTLHGFM 150
Cdd:cd13916   15 SRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLLAQtqAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
85-157 4.67e-04

The cupredoxin domain of Ubiquinol oxidase subunit II; 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. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 37.53  E-value: 4.67e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124808998  85 LTLPTRTHISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGtlHGF--MPIVVEAV 157
Cdd:cd04212   27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSG--EGFsdMKFKVLAV 99
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
92-147 1.83e-03

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 36.06  E-value: 1.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124808998  92 HISFLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLH 147
Cdd:cd04223   29 HLTNLEQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALH 84
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
95-155 6.54e-03

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 34.27  E-value: 6.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124808998  95 FLVTATDVIHSWSIPSLGIKADAIPGRLHKITTFILREGVYYGQCSEMCGTLHGFM--PIVVE 155
Cdd:cd13917   26 LHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMhgRIIVE 88
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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