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Conserved domains on  [gi|72385086|gb|AAZ67808|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Uromenus catalaunicus]

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
 1-137 2.71e-103

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 294.43  E-value: 2.71e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    1 SMDPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPAL 80
Cdd:MTH00154  90 VNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 72385086   81 GVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNN 137
Cdd:MTH00154 169 GVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-137 2.71e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 294.43  E-value: 2.71e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    1 SMDPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPAL 80
Cdd:MTH00154  90 VNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 72385086   81 GVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNN 137
Cdd:MTH00154 169 GVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 4-134 1.80e-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: 1.80e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   4 PLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVK 83
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 72385086  84 VDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKW 134
Cdd:cd13912  80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
6-126 9.56e-79

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 228.45  E-value: 9.56e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086     6 ITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 85
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 72385086    86 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESI 126
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-143 1.92e-38

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 129.95  E-value: 1.92e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   3 DPLITVKTIGHQWYWSYEYTDfstpyefdsymlpYNEmplngfrllDVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:COG1622 110 EDPLTVEVTGYQWKWLFRYPD-------------QGI---------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGG 167

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72385086  83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNNALNSSS 143
Cdd:COG1622 168 KQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 3-136 2.02e-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: 121.33  E-value: 2.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086     3 DPLITVKTIGHQWYWSYEYtdfstpyefdsymlpynemPLNGFRlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:TIGR02866  88 KDALKVKVTGYQWWWDFEY-------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGG 145

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 72385086    83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVN 136
Cdd:TIGR02866 146 KIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-137 2.71e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 294.43  E-value: 2.71e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    1 SMDPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPAL 80
Cdd:MTH00154  90 VNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 72385086   81 GVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNN 137
Cdd:MTH00154 169 GVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 4-134 1.80e-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: 1.80e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   4 PLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVK 83
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 72385086  84 VDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKW 134
Cdd:cd13912  80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 3-137 2.18e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 251.76  E-value: 2.18e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    3 DPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:MTH00117  92 NPHLTIKAIGHQWYWSYEYTDYKD-LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGV 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 72385086   83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNN 137
Cdd:MTH00117 171 KTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 3-137 1.90e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 244.46  E-value: 1.90e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    3 DPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:MTH00140  92 NPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGV 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 72385086   83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNN 137
Cdd:MTH00140 171 KVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 2-138 3.32e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 241.16  E-value: 3.32e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    2 MDPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALG 81
Cdd:MTH00139  91 SDPYLTFKAVGHQWYWSYEYSDFKN-LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLG 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 72385086   82 VKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNNA 138
Cdd:MTH00139 170 VKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 3-137 9.28e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 234.87  E-value: 9.28e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    3 DPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:MTH00168  92 KPDLTIKAVGHQWYWSYEYTDYND-LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGL 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 72385086   83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNN 137
Cdd:MTH00168 171 KMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-137 1.74e-79

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 234.37  E-value: 1.74e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    2 MDPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALG 81
Cdd:MTH00008  91 SNPSITLKTIGHQWYWSYEYSDFSN-LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLG 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 72385086   82 VKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNN 137
Cdd:MTH00008 170 VKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
6-126 9.56e-79

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 228.45  E-value: 9.56e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086     6 ITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 85
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 72385086    86 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESI 126
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 3-141 2.27e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 231.51  E-value: 2.27e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    3 DPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:MTH00038  92 NPFLTIKAIGHQWYWSYEYTDYND-LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGV 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 72385086   83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNNALNS 141
Cdd:MTH00038 171 KMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-141 2.09e-75

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 224.24  E-value: 2.09e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    2 MDPLITVKTIGHQWYWSYEYTDFSTP-YEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPAL 80
Cdd:MTH00023 100 VSPALTIKAIGHQWYWSYEYSDYEGEtLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSL 179

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72385086   81 GVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNNALNS 141
Cdd:MTH00023 180 GLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSND 240
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-135 3.49e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 221.19  E-value: 3.49e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    2 MDPLITVKTIGHQWYWSYEYTDFSTP-YEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPAL 80
Cdd:MTH00051  93 IDPALTIKAIGHQWYWSYEYSDYGTDtIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSL 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 72385086   81 GVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWV 135
Cdd:MTH00051 173 SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 3-140 4.77e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 220.42  E-value: 4.77e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    3 DPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:MTH00076  92 DPHLTVKAIGHQWYWSYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGI 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 72385086   83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNNALN 140
Cdd:MTH00076 171 KTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 3-134 7.38e-74

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 219.97  E-value: 7.38e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    3 DPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:MTH00098  92 NPSLTVKTMGHQWYWSYEYTDYED-LSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGL 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 72385086   83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKW 134
Cdd:MTH00098 171 KTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 3-134 9.23e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 217.27  E-value: 9.23e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    3 DPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:MTH00129  92 DPHLTIKAMGHQWYWSYEYTDYED-LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGV 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 72385086   83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKW 134
Cdd:MTH00129 171 KMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 3-142 1.42e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 214.36  E-value: 1.42e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    3 DPLITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:MTH00185  92 DPHLTIKAMGHQWYWSYEYTDYEQ-LEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGV 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNNALNSS 142
Cdd:MTH00185 171 KMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEEA 230
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-135 5.00e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 186.00  E-value: 5.00e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    6 ITVKTIGHQWYWSYEYTDFSTP-YEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKV 84
Cdd:MTH00027 127 ITIKVTGHQWYWSYSYEDYGEKnIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKM 206

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 72385086   85 DATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWV 135
Cdd:MTH00027 207 DAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-140 4.94e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 179.82  E-value: 4.94e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    6 ITVKTIGHQWYWSYEYTDFSTpYEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 85
Cdd:MTH00080  98 LTVKVTGHQWYWSYEFSDIPG-LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMD 176

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 72385086   86 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNNALN 140
Cdd:MTH00080 177 AMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 7-130 1.23e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 134.31  E-value: 1.23e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086    7 TVKTIGHQWYWSYEYTDFStpyEFDSYMLPYNEMplngfrlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDA 86
Cdd:MTH00047  83 TIKVIGHQWYWSYEYSFGG---SYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDA 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 72385086   87 TPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININS 130
Cdd:MTH00047 151 IPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 28-131 3.03e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 132.64  E-value: 3.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   28 YEFDSYMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLYYGQ 107
Cdd:PTZ00047  49 YSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128

                         90       100
                 ....*....|....*....|....
gi 72385086  108 CSEICGANHSFMPIVIESININSF 131
Cdd:PTZ00047 129 CSEMCGTLHGFMPIVVEAVSPEAY 152
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-143 1.92e-38

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 129.95  E-value: 1.92e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   3 DPLITVKTIGHQWYWSYEYTDfstpyefdsymlpYNEmplngfrllDVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:COG1622 110 EDPLTVEVTGYQWKWLFRYPD-------------QGI---------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGG 167

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72385086  83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNNALNSSS 143
Cdd:COG1622 168 KQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 3-136 2.02e-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: 121.33  E-value: 2.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086     3 DPLITVKTIGHQWYWSYEYtdfstpyefdsymlpynemPLNGFRlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:TIGR02866  88 KDALKVKVTGYQWWWDFEY-------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGG 145

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 72385086    83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVN 136
Cdd:TIGR02866 146 KIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 6-124 4.56e-30

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: 104.30  E-value: 4.56e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   6 ITVKTIGHQWYWSYEYTDFSTPyefdsymlpynemplngfrlldvdNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 85
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPNVRTP------------------------NEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 72385086  86 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIE 124
Cdd:cd13842  57 AVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 6-119 5.20e-24

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: 89.22  E-value: 5.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   6 ITVKTIGHQWYWSYEYTDfSTPYEFDSYmlpyNEMplngfrlldvdnrtILPMNTQIRMLITAADVLHSWTVPALGVKVD 85
Cdd:cd04213   2 LTIEVTGHQWWWEFRYPD-EPGRGIVTA----NEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                        90       100       110
                ....*....|....*....|....*....|....
gi 72385086  86 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFM 119
Cdd:cd04213  63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 6-119 3.97e-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: 84.61  E-value: 3.97e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   6 ITVKTIGHQWYWSYEYTDFSTPYEFDSyMLPYNEMplngfrlldvdnrtILPMNTQIRMLITAADVLHSWTVPALGVKVD 85
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGGDGKLGTDD-DVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                        90       100       110
                ....*....|....*....|....*....|....
gi 72385086  86 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFM 119
Cdd:cd13919  67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 6-119 1.36e-21

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: 83.06  E-value: 1.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   6 ITVKTIGHQWYWSYEYtdfstpyefdsymlpynempLNGFRlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 85
Cdd:cd13915   2 LEIQVTGRQWMWEFTY--------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                        90       100       110
                ....*....|....*....|....*....|....
gi 72385086  86 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFM 119
Cdd:cd13915  59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 3-135 1.15e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 76.73  E-value: 1.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   3 DPLiTVKTIGHQWYWSYEYtdfSTPYEFDSYMlpynemplngfrlldvdnrtILPMNTQIRMLITAADVLHSWTVPALGV 82
Cdd:cd13918  31 DAL-EVEVEGFQFGWQFEY---PNGVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPELRV 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 72385086  83 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWV 135
Cdd:cd13918  87 KADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 6-135 3.42e-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: 74.37  E-value: 3.42e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   6 ITVKTIGHQWYWSYEYTDFStpyefdsymlpynemplngfrlLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 85
Cdd:cd13914   1 VEIEVEAYQWGWEFSYPEAN----------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 72385086  86 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWV 135
Cdd:cd13914  59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 56-119 1.54e-10

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 54.50  E-value: 1.54e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72385086  56 LPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFM 119
Cdd:cd13913  29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 52-119 2.57e-06

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: 43.31  E-value: 2.57e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 72385086  52 NRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFM 119
Cdd:cd04212  25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 6-119 6.10e-06

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: 42.37  E-value: 6.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   6 ITVKTIGHQWYWsyeytdfstpyefdsymlpynEMplngfrlldvdNRTILPMNTQIRMLITAADVLHSWTV--PALGV- 82
Cdd:cd13916   1 QVVAVTGHQWYW---------------------EL-----------SRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLl 48

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 72385086  83 -KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFM 119
Cdd:cd13916  49 aQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 33-124 3.33e-05

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: 40.68  E-value: 3.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086  33 YMLPYNEMPLNGFRLLDVDNRTILPMNTQIRMLIT-AADVLHSWTVPALGVKVDA---------------TPGRLNQTSF 96
Cdd:cd00920   4 TASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTF 83

                        90       100
                ....*....|....*....|....*...
gi 72385086  97 FMNRPGLYYGQCSEICGaNHSFMPIVIE 124
Cdd:cd00920  84 TTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 52-142 2.33e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 36.70  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385086   52 NRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPI-VIESININS 130
Cdd:PRK10525 151 NEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFkAIATPDRAE 230

                         90
                 ....*....|..
gi 72385086  131 FIKWVNNALNSS 142
Cdd:PRK10525 231 FDQWVAKAKQSP 242
 
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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