NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|22596989|gb|AAN03426|]
View 

cytochrome c oxidase II, partial (mitochondrion) [Battus philenor]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-139 1.10e-101

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 290.19  E-value: 1.10e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00154  89 EVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINNYS 139
Cdd:MTH00154 169 GVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-139 1.10e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 290.19  E-value: 1.10e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00154  89 EVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINNYS 139
Cdd:MTH00154 169 GVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 5-134 1.86e-90

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: 258.27  E-value: 1.86e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   5 PLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKI 84
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 22596989  85 DANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINW 134
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
7-126 3.82e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 226.52  E-value: 3.82e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989     7 ITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDA 86
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 22596989    87 NPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESI 126
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-137 2.72e-39

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 131.87  E-value: 2.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   7 ITLKSIGHQWYWSYEYSDFNNIefdsymiqynnsemknfrlldVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDA 86
Cdd:COG1622 113 LTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDA 171

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22596989  87 NPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINN 137
Cdd:COG1622 172 IPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 7-136 2.37e-35

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: 120.95  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989     7 ITLKSIGHQWYWSYEYSDFnniefdsymiqynnsemknfrLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDA 86
Cdd:TIGR02866  91 LKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDA 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 22596989    87 NPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWIN 136
Cdd:TIGR02866 150 IPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-139 1.10e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 290.19  E-value: 1.10e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00154  89 EVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINNYS 139
Cdd:MTH00154 169 GVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 5-134 1.86e-90

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: 258.27  E-value: 1.86e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   5 PLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKI 84
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 22596989  85 DANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINW 134
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-137 1.43e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 259.46  E-value: 1.43e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00117  89 EINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINN 137
Cdd:MTH00117 169 GVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-140 1.53e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 254.48  E-value: 1.53e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00140  89 ETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSL 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINNYSS 140
Cdd:MTH00140 169 GVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMSE 228
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-138 7.74e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 247.32  E-value: 7.74e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00139  89 EVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINNY 138
Cdd:MTH00139 169 GVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-137 2.01e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 236.42  E-value: 2.01e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00168  89 EIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINN 137
Cdd:MTH00168 169 GLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-140 5.40e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 235.37  E-value: 5.40e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00038  89 EVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSL 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINNYSS 140
Cdd:MTH00038 169 GVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLE 228
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-140 3.83e-79

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 233.21  E-value: 3.83e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00008  89 EVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSL 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINNYSS 140
Cdd:MTH00008 169 GVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
7-126 3.82e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 226.52  E-value: 3.82e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989     7 ITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDA 86
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 22596989    87 NPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESI 126
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-134 6.47e-77

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 227.29  E-value: 6.47e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00098  89 EINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINW 134
Cdd:MTH00098 169 GLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-137 1.65e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 223.89  E-value: 1.65e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00076  89 EINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINN 137
Cdd:MTH00076 169 GIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-134 1.38e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 219.20  E-value: 1.38e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00129  89 EINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPAL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINW 134
Cdd:MTH00129 169 GVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-134 2.22e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 218.60  E-value: 2.22e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSL 80
Cdd:MTH00185  89 EINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPAL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 22596989   81 GVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINW 134
Cdd:MTH00185 169 GVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-139 1.50e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 211.56  E-value: 1.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDF--NNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIP 78
Cdd:MTH00051  91 EVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVP 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22596989   79 SLGVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINNYS 139
Cdd:MTH00051 171 SLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-140 1.50e-70

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 211.92  E-value: 1.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    1 ELNNPLITLKSIGHQWYWSYEYSDFN--NIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIP 78
Cdd:MTH00023  98 EVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVP 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22596989   79 SLGVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINNYSS 140
Cdd:MTH00023 178 SLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 7-138 2.09e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 185.60  E-value: 2.09e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    7 ITLKSIGHQWYWSYEYSDFNNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDA 86
Cdd:MTH00080  98 LTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDA 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 22596989   87 NPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINNY 138
Cdd:MTH00080 178 MSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-135 5.03e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 180.61  E-value: 5.03e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    7 ITLKSIGHQWYWSYEYSDF--NNIEFDSYMIQYNNSEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKI 84
Cdd:MTH00027 127 ITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKM 206

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 22596989   85 DANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWI 135
Cdd:MTH00027 207 DAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 46-127 1.22e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 135.72  E-value: 1.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   46 RLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIES 125
Cdd:PTZ00047  67 RQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEA 146


                 ..
gi 22596989  126 IS 127
Cdd:PTZ00047 147 VS 148
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 8-126 2.03e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 131.23  E-value: 2.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989    8 TLKSIGHQWYWSYEYSDfnNIEFDSYMIQYNNSemknfrlldVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDAN 87
Cdd:MTH00047  83 TIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAI 151

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 22596989   88 PGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESI 126
Cdd:MTH00047 152 PGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-137 2.72e-39

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 131.87  E-value: 2.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   7 ITLKSIGHQWYWSYEYSDFNNIefdsymiqynnsemknfrlldVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDA 86
Cdd:COG1622 113 LTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDA 171

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22596989  87 NPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWINN 137
Cdd:COG1622 172 IPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 7-136 2.37e-35

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: 120.95  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989     7 ITLKSIGHQWYWSYEYSDFnniefdsymiqynnsemknfrLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDA 86
Cdd:TIGR02866  91 LKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDA 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 22596989    87 NPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWIN 136
Cdd:TIGR02866 150 IPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 7-124 6.83e-27

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: 96.21  E-value: 6.83e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   7 ITLKSIGHQWYWSYEYSDFNniefdsymiqynnsemknfrlldVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDA 86
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 22596989  87 NPGRLNQGNLYINRPGIFYGQCSEICGSNHSFMPIVIE 124
Cdd:cd13842  58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 7-119 2.57e-26

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: 94.99  E-value: 2.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   7 ITLKSIGHQWYWSYEYSDfnniefdsymiqynnSEMKNFRLLdvdNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDA 86
Cdd:cd04213   2 LTIEVTGHQWWWEFRYPD---------------EPGRGIVTA---NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                        90       100       110
                ....*....|....*....|....*....|...
gi 22596989  87 NPGRLNQGNLYINRPGIFYGQCSEICGSNHSFM 119
Cdd:cd04213  64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 13-135 3.93e-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: 79.37  E-value: 3.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989  13 GHQWYWSYEYSDFNNIEFdsymiqynnsemknfrlldvdNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDANPGRLN 92
Cdd:cd13914   7 AYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 22596989  93 QGNLYINRPGIFYGQCSEICGSNHSFMPIVIESISIKNFINWI 135
Cdd:cd13914  66 TIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 7-119 3.59e-19

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: 76.91  E-value: 3.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   7 ITLKSIGHQWYWSYEYSDFNniefdsymiqynnsEMKNFRLLDVDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDA 86
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGGD--------------GKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 22596989  87 NPGRLNQGNLYINRPGIFYGQCSEICGSNHSFM 119
Cdd:cd13919  68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 7-119 7.03e-18

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: 73.05  E-value: 7.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   7 ITLKSIGHQWYWSYEYSDfnniefdsymiqyNNSEmknfrlldvDNRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDA 86
Cdd:cd13915   2 LEIQVTGRQWMWEFTYPN-------------GKRE---------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                        90       100       110
                ....*....|....*....|....*....|...
gi 22596989  87 NPGRLNQGNLYINRPGIFYGQCSEICGSNHSFM 119
Cdd:cd13915  60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 7-119 1.00e-17

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: 74.03  E-value: 1.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22596989   7 ITLKSIGHQWYWSYEYSdfNNIEFDSYMiqynnsemknfrlldvdnriVLPMNNQIRIMITATDVIHSWTIPSLGVKIDA 86
Cdd:cd13918  33 LEVEVEGFQFGWQFEYP--NGVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPELRVKADA 90

                        90       100       110
                ....*....|....*....|....*....|...
gi 22596989  87 NPGRLNQGNLYINRPGIFYGQCSEICGSNHSFM 119
Cdd:cd13918  91 IPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 52-119 5.38e-09

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: 50.26  E-value: 5.38e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22596989  52 NRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFM 119
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 52-119 3.23e-08

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: 48.31  E-value: 3.23e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22596989  52 NRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFM 119
Cdd:cd04212  25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 52-119 4.42e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 35.93  E-value: 4.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22596989   52 NRIVLPMNNQIRIMITATDVIHSWTIPSLGVKIDANPGRLNQGNLYINRPGIFYGQCSEICGSNHSFM 119
Cdd:PRK10525 151 NEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGM 218
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH