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Conserved domains on  [gi|20805516|gb|AAM28762|]
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cytochrome oxidase II, partial (mitochondrion) [Drosophila ercepeae]

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

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-128 1.25e-106

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 302.13  E-value: 1.25e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMP 208
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-128 1.25e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 302.13  E-value: 1.25e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMP 208
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 13-128 1.23e-89

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: 255.57  E-value: 1.23e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516  13 PSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKV 92
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 20805516  93 DGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMP 116
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
16-128 1.63e-79

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 229.60  E-value: 1.63e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    16 TLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGT 95
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 20805516    96 PGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMP 114
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-128 8.37e-40

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 132.64  E-value: 8.37e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516   1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIefdsymiptnelatdgfrlldVDNRIVLPMNSQIRILVTAADVI 80
Cdd:COG1622  99 LRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADVI 157

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 20805516  81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:COG1622 158 HSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMR 205
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 3-128 4.60e-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: 119.79  E-value: 4.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516     3 LLYLLDEINEPSVTLKSIGHQWYWSYEYSDFnniefdsymiptnelatdGFRlldVDNRIVLPMNSQIRILVTAADVIHS 82
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHS 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 20805516    83 WTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLML 183
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-128 1.25e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 302.13  E-value: 1.25e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMP 208
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-128 4.19e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 267.94  E-value: 4.19e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMP 208
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-128 1.02e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 261.80  E-value: 1.02e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMP 208
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 13-128 1.23e-89

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: 255.57  E-value: 1.23e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516  13 PSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKV 92
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 20805516  93 DGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMP 116
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-128 7.18e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 257.34  E-value: 7.18e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMP 208
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-128 1.65e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 251.05  E-value: 1.65e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMP 208
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-128 1.31e-84

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 246.31  E-value: 1.31e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMP 208
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-128 2.74e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 240.76  E-value: 2.74e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMP 208
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-128 1.48e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 238.85  E-value: 1.48e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMP 208
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-128 2.28e-80

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 235.77  E-value: 2.28e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMP 208
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-128 2.85e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 235.55  E-value: 2.85e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMP 208
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-128 6.05e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 234.67  E-value: 6.05e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVI 80
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 20805516   81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMP 208
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
16-128 1.63e-79

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 229.60  E-value: 1.63e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    16 TLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGT 95
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 20805516    96 PGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMP 114
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-128 1.20e-78

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 231.95  E-value: 1.20e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFN--NIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAAD 78
Cdd:MTH00023  90 LKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGAD 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 20805516   79 VIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00023 170 VLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMP 219
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-128 6.85e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 226.97  E-value: 6.85e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDF--NNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAAD 78
Cdd:MTH00051  83 LKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAAD 162

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 20805516   79 VIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00051 163 VLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMP 212
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-128 2.30e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 183.69  E-value: 2.30e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDE-INEPSVTLKSIGHQWYWSYEYSDF--NNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAA 77
Cdd:MTH00027 112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 20805516   78 DVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMP 242
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-128 3.78e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 179.44  E-value: 3.78e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEIN-EPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADV 79
Cdd:MTH00080  83 LSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDV 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 20805516   80 IHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00080 163 IHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMP 211
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-128 8.37e-40

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 132.64  E-value: 8.37e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516   1 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIefdsymiptnelatdgfrlldVDNRIVLPMNSQIRILVTAADVI 80
Cdd:COG1622  99 LRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADVI 157

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 20805516  81 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:COG1622 158 HSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMR 205
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 1-128 8.83e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 131.62  E-value: 8.83e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516    1 LRLLYLLDEIN-EPSVTLKSIGHQWYWSYEYSDfnNIEFDSYMiptnelaTDGFRLldVDNRIVLPMNSQIRILVTAADV 79
Cdd:MTH00047  67 LNLNFITSDLDcFSSETIKVIGHQWYWSYEYSF--GGSYDSFM-------TDDIFG--VDKPLRLVYGVPYHLLVTSSDV 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 20805516   80 IHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:MTH00047 136 IHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMP 184
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 38-128 8.70e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 128.01  E-value: 8.70e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516   38 FDSYMIPTNELATDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCS 117
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|.
gi 20805516  118 EICGANHSFMP 128
Cdd:PTZ00047 131 EMCGTLHGFMP 141
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 3-128 4.60e-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: 119.79  E-value: 4.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516     3 LLYLLDEINEPSVTLKSIGHQWYWSYEYSDFnniefdsymiptnelatdGFRlldVDNRIVLPMNSQIRILVTAADVIHS 82
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHS 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 20805516    83 WTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLML 183
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 15-128 8.48e-29

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: 100.45  E-value: 8.48e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516  15 VTLKSIGHQWYWSYEYSDFNniefdsymiptnelatdgfrlldVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 94
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....
gi 20805516  95 TPGRLNQTNFFINRPGLFYGQCSEICGANHSFMP 128
Cdd:cd13842  58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYML 91
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 14-127 6.00e-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: 93.45  E-value: 6.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516  14 SVTLKSIGHQWYWSYEYSDfnniefdsymiptnelaTDGFRLLDVdNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVD 93
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPD-----------------EPGRGIVTA-NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                        90       100       110
                ....*....|....*....|....*....|....
gi 20805516  94 GTPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 127
Cdd:cd04213  63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 15-127 1.21e-22

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: 85.00  E-value: 1.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516  15 VTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELatdgfrlldvdnriVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 94
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 20805516  95 TPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 127
Cdd:cd13919  68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 20-127 3.07e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 78.82  E-value: 3.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516  20 IGHQWYWSYEYSDfnniefdsymiptnelatdGFRlldVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 99
Cdd:cd13915   7 TGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRY 64

                        90       100
                ....*....|....*....|....*...
gi 20805516 100 NQTNFFINRPGLFYGQCSEICGANHSFM 127
Cdd:cd13915  65 TYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 3-127 6.50e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 79.04  E-value: 6.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516   3 LLYLLD---EINEPSVTLKSIGHQWYWSYEYSdfnniefdsymiptNELATDgfrlldvdNRIVLPMNSQIRILVTAADV 79
Cdd:cd13918  18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYP--------------NGVTTG--------NTLRVPADTPIALRVTSTDV 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 20805516  80 IHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 127
Cdd:cd13918  76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 15-127 1.29e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 74.75  E-value: 1.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516  15 VTLKSIGHQWYWSYEYSDFNNIEFdsymiptnelatdgfrlldvdNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 94
Cdd:cd13914   1 VEIEVEAYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                        90       100       110
                ....*....|....*....|....*....|...
gi 20805516  95 TPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 127
Cdd:cd13914  60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 60-127 7.14e-12

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: 57.19  E-value: 7.14e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20805516  60 NRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 127
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 60-127 8.43e-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: 46.77  E-value: 8.43e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20805516  60 NRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 127
Cdd:cd04212  25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 21-127 7.68e-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: 38.90  E-value: 7.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516  21 GHQWYWsyeysdfnniefdsymiptnELATDgfrlldvdnriVLPMNSQIRILVTAADVIHSWTI--PALGV--KVDGTP 96
Cdd:cd13916   7 GHQWYW--------------------ELSRT-----------EIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMP 55

                        90       100       110
                ....*....|....*....|....*....|.
gi 20805516  97 GRLNQTNFFINRPGLFYGQCSEICGANHSFM 127
Cdd:cd13916  56 GYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 40-128 6.11e-03

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 34.13  E-value: 6.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20805516  40 SYMIPTNELATDGFrlldVDNRIVLPMNSQIR-ILVTAADVIHSWTIPALGVKVDG---------------TPGRLNQTN 103
Cdd:cd00920   7 DWGWSFTYNGVLLF----GPPVLVVPVGDTVRvQFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVT 82

                        90       100
                ....*....|....*....|....*
gi 20805516 104 FFINRPGLFYGQCSEICGaNHSFMP 128
Cdd:cd00920  83 FTTDQAGVYWFYCTIPGH-NHAGMV 106
 
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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