NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2896918|gb|AAC03283|]
View 

cytochrome oxidase subunit II, partial (mitochondrion) [Drosophila longiperda]

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
 1-121 1.37e-95

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 273.63  E-value: 1.37e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00154  98 KTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:MTH00154 178 RLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNN 218
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-121 1.37e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 273.63  E-value: 1.37e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00154  98 KTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:MTH00154 178 RLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNN 218
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 1-121 3.16e-84

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: 241.71  E-value: 3.16e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918    1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:cd13912   6 KAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPG 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 2896918   81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:cd13912  86 RLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLED 126
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
1-117 4.03e-77

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 223.44  E-value: 4.03e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918      1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:pfam00116   4 KAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPG 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2896918     81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSV 117
Cdd:pfam00116  84 RLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-118 1.18e-34

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 119.16  E-value: 1.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918    3 IGHQWYWSYEYSDFNNVefdsymiptnelandgfrlldVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPGRL 82
Cdd:COG1622 118 TGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRV 176

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 2896918   83 NQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVP 118
Cdd:COG1622 177 TELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-118 5.34e-30

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: 106.31  E-value: 5.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918      1 KSIGHQWYWSYEYSdfnnvefdsymiptnelaNDGFRlldVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:TIGR02866  94 KVTGYQWWWDFEYP------------------ESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPG 152

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2896918     81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVP 118
Cdd:TIGR02866 153 QTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVP 190
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-121 1.37e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 273.63  E-value: 1.37e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00154  98 KTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:MTH00154 178 RLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNN 218
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-121 1.17e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 248.68  E-value: 1.17e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00117  98 KAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:MTH00117 178 RLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKH 218
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 1-121 3.16e-84

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: 241.71  E-value: 3.16e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918    1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:cd13912   6 KAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPG 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 2896918   81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:cd13912  86 RLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLED 126
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-121 5.86e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 234.45  E-value: 5.86e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00140  98 KAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:MTH00140 178 RLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLED 218
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
1-117 4.03e-77

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 223.44  E-value: 4.03e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918      1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:pfam00116   4 KAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPG 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2896918     81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSV 117
Cdd:pfam00116  84 RLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-120 6.29e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 226.52  E-value: 6.29e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00139  98 KAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVN 120
Cdd:MTH00139 178 RLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPK 217
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-121 8.52e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 226.40  E-value: 8.52e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00168  98 KAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:MTH00168 178 RLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWET 218
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-120 1.12e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 218.42  E-value: 1.12e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00038  98 KAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVN 120
Cdd:MTH00038 178 RLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFN 217
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-117 8.85e-73

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 216.26  E-value: 8.85e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00008  98 KTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPG 177

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSV 117
Cdd:MTH00008 178 RLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAV 214
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-121 1.34e-72

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 215.74  E-value: 1.34e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00098  98 KTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:MTH00098 178 RLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKY 218
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-121 5.86e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 214.19  E-value: 5.86e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00129  98 KAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:MTH00129 178 RLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEH 218
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-121 4.53e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 212.05  E-value: 4.53e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00185  98 KAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:MTH00185 178 RLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEH 218
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-121 9.95e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 211.18  E-value: 9.95e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00076  98 KAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:MTH00076 178 RLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNN 218
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-120 7.64e-70

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 209.22  E-value: 7.64e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFN--NVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGT 78
Cdd:MTH00023 107 KAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAV 186

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 2896918    79 PGRLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVN 120
Cdd:MTH00023 187 PGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLD 228
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-117 1.12e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 203.47  E-value: 1.12e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDF--NNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGT 78
Cdd:MTH00051 100 KAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAV 179

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 2896918    79 PGRLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSV 117
Cdd:MTH00051 180 PGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGV 218
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-113 1.31e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 170.19  E-value: 1.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00080 101 KVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSG 180

                         90       100       110
                 ....*....|....*....|....*....|...
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIV 113
Cdd:MTH00080 181 ILSTLCYSFPMPGVFYGQCSEICGANHSFMPIA 213
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-120 3.88e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 170.21  E-value: 3.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDF--NNVEFDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGT 78
Cdd:MTH00027 130 KVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAV 209

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 2896918    79 PGRLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVN 120
Cdd:MTH00027 210 PGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLS 251
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 21-117 2.55e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 129.17  E-value: 2.55e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918    21 FDSYMIPTNELANDGFRLLDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPGRLNQTNLFINRPGLFYGRCS 100
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*..
gi 2896918   101 EICGANHSFMPIVSRSV 117
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAV 147
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 1-121 4.08e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 126.99  E-value: 4.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918     1 KSIGHQWYWSYEYSDfnNVEFDSYMIptnelaNDGFrllDVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:MTH00047  85 KVIGHQWYWSYEYSF--GGSYDSFMT------DDIF---GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPG 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 2896918    81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVPVNY 121
Cdd:MTH00047 154 RINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-118 1.18e-34

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 119.16  E-value: 1.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918    3 IGHQWYWSYEYSDFNNVefdsymiptnelandgfrlldVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPGRL 82
Cdd:COG1622 118 TGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRV 176

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 2896918   83 NQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVP 118
Cdd:COG1622 177 TELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-118 5.34e-30

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: 106.31  E-value: 5.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918      1 KSIGHQWYWSYEYSdfnnvefdsymiptnelaNDGFRlldVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPG 80
Cdd:TIGR02866  94 KVTGYQWWWDFEYP------------------ESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPG 152

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2896918     81 RLNQTNLFINRPGLFYGRCSEICGANHSFMPIVSRSVP 118
Cdd:TIGR02866 153 QTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVP 190
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 3-111 1.93e-25

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: 91.59  E-value: 1.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918    3 IGHQWYWSYEYSDFNnvefdsymiptnelandgfrlldVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPGRL 82
Cdd:cd13842   6 TGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYT 62

                        90       100
                ....*....|....*....|....*....
gi 2896918   83 NQTNLFINRPGLFYGRCSEICGANHSFMP 111
Cdd:cd13842  63 SELWFVADKPGTYTIICAEYCGLGHSYML 91
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 3-110 6.44e-23

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: 85.36  E-value: 6.44e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918    3 IGHQWYWSYEYSDFNNVEFdsymiptnELANDgfrlldvdnrIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPGRL 82
Cdd:cd04213   7 TGHQWWWEFRYPDEPGRGI--------VTANE----------LHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRT 68

                        90       100
                ....*....|....*....|....*...
gi 2896918   83 NQTNLFINRPGLFYGRCSEICGANHSFM 110
Cdd:cd04213  69 NRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 3-110 2.40e-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: 76.53  E-value: 2.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918    3 IGHQWYWSYEYSDFNNVEFDSYMIPTNELAndgfrlldvdnriaLPMNSQIRILVTVADVIHSWTVPALGVKVDGTPGRL 82
Cdd:cd13919   7 TAQQWAWTFRYPGGDGKLGTDDDVTSPELH--------------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRT 72

                        90       100
                ....*....|....*....|....*...
gi 2896918   83 NQTNLFINRPGLFYGRCSEICGANHSFM 110
Cdd:cd13919  73 TRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 3-110 3.18e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 70.74  E-value: 3.18e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918    3 IGHQWYWSYEYSDfnnvefdsymiptnelandGFRlldVDNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPGRL 82
Cdd:cd13915   7 TGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRY 64

                        90       100
                ....*....|....*....|....*...
gi 2896918   83 NQTNLFINRPGLFYGRCSEICGANHSFM 110
Cdd:cd13915  65 TYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 4-110 3.91e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 70.90  E-value: 3.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918    4 GHQWYWSYEYSDFNNVEFdsymiptnelandgfrlldvdNRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPGRLN 83
Cdd:cd13914   7 AYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65

                        90       100
                ....*....|....*....|....*..
gi 2896918   84 QTNLFINRPGLFYGRCSEICGANHSFM 110
Cdd:cd13914  66 TIKTEATEEGEYQLYCAEYCGAGHSQM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 3-110 4.82e-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: 66.32  E-value: 4.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918    3 IGHQWYWSYEYSdfNNVEFDSYMIptnelandgfrlldvdnriaLPMNSQIRILVTVADVIHSWTVPALGVKVDGTPGRL 82
Cdd:cd13918  38 EGFQFGWQFEYP--NGVTTGNTLR--------------------VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEY 95

                        90       100
                ....*....|....*....|....*...
gi 2896918   83 NQTNLFINRPGLFYGRCSEICGANHSFM 110
Cdd:cd13918  96 TSTWFEADEPGTYEAKCYELCGSGHSLM 123
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 43-110 1.27e-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: 51.42  E-value: 1.27e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2896918   43 NRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPGRLNQTNLFINRPGLFYGRCSEICGANHSFM 110
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 43-110 1.58e-07

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: 46.00  E-value: 1.58e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2896918   43 NRIALPMNSQIRILVTVADVIHSWTVPALGVKVDGTPGRLNQTNLFINRPGLFYGRCSEICGANHSFM 110
Cdd:cd04212  25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 4-110 4.40e-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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 33.89  E-value: 4.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2896918    4 GHQWYWsyeysdfnnvEFDSYMIPTNELANdgFRlldvdnrialpmnsqirilVTVADVIHSWTV--PALGV--KVDGTP 79
Cdd:cd13916   7 GHQWYW----------ELSRTEIPAGKPVE--FR-------------------VTSADVNHGFGIydPDMRLlaQTQAMP 55

                        90       100       110
                ....*....|....*....|....*....|.
gi 2896918   80 GRLNQTNLFINRPGLFYGRCSEICGANHSFM 110
Cdd:cd13916  56 GYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
 
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