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Conserved domains on  [gi|72385072|gb|AAZ67801|]
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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
 12-150 2.14e-104

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 297.90  E-value: 2.14e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVP 91
Cdd:MTH00154  88 DEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVP 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 72385072   92 ALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNS 150
Cdd:MTH00154 167 SLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 12-150 2.14e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 297.90  E-value: 2.14e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVP 91
Cdd:MTH00154  88 DEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVP 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 72385072   92 ALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNS 150
Cdd:MTH00154 167 SLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 17-147 2.58e-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: 258.65  E-value: 2.58e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072  17 PLITVKTIGHQWYWSYEYTDFSaPYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVK 96
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFN-DLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 72385072  97 VDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKW 147
Cdd:cd13912  80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
19-139 1.18e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 228.83  E-value: 1.18e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072    19 ITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 98
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 72385072    99 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESI 139
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
16-156 7.37e-38

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 128.79  E-value: 7.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072  16 DPLITVKTIGHQWYWSYEYTDFSApyefdsymlpysdmpingfrllDVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 95
Cdd:COG1622 110 EDPLTVEVTGYQWKWLFRYPDQGI----------------------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGG 167

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72385072  96 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNSTLNSSS 156
Cdd:COG1622 168 KQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 16-149 2.39e-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: 121.72  E-value: 2.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072    16 DPLITVKTIGHQWYWSYEYtdfsapyefdsymlpysdmPINGFRlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 95
Cdd:TIGR02866  88 KDALKVKVTGYQWWWDFEY-------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGG 145

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 72385072    96 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVN 149
Cdd:TIGR02866 146 KIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 12-150 2.14e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 297.90  E-value: 2.14e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVP 91
Cdd:MTH00154  88 DEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVP 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 72385072   92 ALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNS 150
Cdd:MTH00154 167 SLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 17-147 2.58e-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: 258.65  E-value: 2.58e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072  17 PLITVKTIGHQWYWSYEYTDFSaPYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVK 96
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFN-DLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 72385072  97 VDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKW 147
Cdd:cd13912  80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 12-152 1.46e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 255.22  E-value: 1.46e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSaPYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVP 91
Cdd:MTH00117  88 DEINNPHLTIKAIGHQWYWSYEYTDYK-DLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVP 166

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72385072   92 ALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNSTL 152
Cdd:MTH00117 167 SLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 12-151 2.34e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 247.16  E-value: 2.34e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVP 91
Cdd:MTH00140  88 DETNNPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVP 166

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   92 ALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNST 151
Cdd:MTH00140 167 SLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 12-148 8.66e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 245.78  E-value: 8.66e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVP 91
Cdd:MTH00139  88 DEVSDPYLTFKAVGHQWYWSYEYSDFKN-LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVP 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 72385072   92 ALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWV 148
Cdd:MTH00139 167 SLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 12-150 3.99e-82

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 241.68  E-value: 3.99e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVP 91
Cdd:MTH00008  88 DEVSNPSITLKTIGHQWYWSYEYSDFSN-LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVP 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 72385072   92 ALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNS 150
Cdd:MTH00008 167 SLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 12-150 1.10e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 240.27  E-value: 1.10e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVP 91
Cdd:MTH00168  88 DEIDKPDLTIKAVGHQWYWSYEYTDYND-LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLP 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 72385072   92 ALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNS 150
Cdd:MTH00168 167 SLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 12-154 1.17e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 238.06  E-value: 1.17e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVP 91
Cdd:MTH00038  88 DEVNNPFLTIKAIGHQWYWSYEYTDYND-LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVP 166

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 72385072   92 ALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNSTLNS 154
Cdd:MTH00038 167 SLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
19-139 1.18e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 228.83  E-value: 1.18e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072    19 ITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 98
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 72385072    99 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESI 139
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 12-154 1.90e-78

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 232.72  E-value: 1.90e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSAP-YEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTV 90
Cdd:MTH00023  97 DEVVSPALTIKAIGHQWYWSYEYSDYEGEtLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAV 176

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72385072   91 PALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNSTLNS 154
Cdd:MTH00023 177 PSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSND 240
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 12-150 3.47e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 226.59  E-value: 3.47e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSAP-YEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTV 90
Cdd:MTH00051  90 DEVIDPALTIKAIGHQWYWSYEYSDYGTDtIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAV 169

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   91 PALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNS 150
Cdd:MTH00051 170 PSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVAT 229
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 12-152 7.83e-76

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 225.75  E-value: 7.83e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDfsapYE---FDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSW 88
Cdd:MTH00098  88 DEINNPSLTVKTMGHQWYWSYEYTD----YEdlsFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSW 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72385072   89 TVPALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNSTL 152
Cdd:MTH00098 164 AVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 12-153 2.06e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 221.96  E-value: 2.06e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVP 91
Cdd:MTH00076  88 DEINDPHLTVKAIGHQWYWSYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVP 166

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 72385072   92 ALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNSTLN 153
Cdd:MTH00076 167 SLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 12-155 3.12e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 221.51  E-value: 3.12e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVP 91
Cdd:MTH00129  88 DEINDPHLTIKAMGHQWYWSYEYTDYED-LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVP 166

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72385072   92 ALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNSTLNSS 155
Cdd:MTH00129 167 ALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEDA 230
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 12-155 7.87e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 215.52  E-value: 7.87e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   12 DESMDPLITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVP 91
Cdd:MTH00185  88 DEINDPHLTIKAMGHQWYWSYEYTDYEQ-LEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVP 166

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72385072   92 ALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNSTLNSS 155
Cdd:MTH00185 167 ALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEEA 230
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 19-148 1.51e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 187.93  E-value: 1.51e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   19 ITVKTIGHQWYWSYEYTDFSAP-YEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKV 97
Cdd:MTH00027 127 ITIKVTGHQWYWSYSYEDYGEKnIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKM 206

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 72385072   98 DATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWV 148
Cdd:MTH00027 207 DAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 19-153 1.66e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 181.75  E-value: 1.66e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   19 ITVKTIGHQWYWSYEYTDFSApYEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 98
Cdd:MTH00080  98 LTVKVTGHQWYWSYEFSDIPG-LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMD 176

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 72385072   99 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNSTLN 153
Cdd:MTH00080 177 AMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 20-143 3.31e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 136.62  E-value: 3.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   20 TVKTIGHQWYWSYEYTDFSapyEFDSYMLPYSDMpingfrlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDA 99
Cdd:MTH00047  83 TIKVIGHQWYWSYEYSFGG---SYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDA 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 72385072  100 TPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININS 143
Cdd:MTH00047 151 IPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 41-144 5.86e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 134.95  E-value: 5.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072   41 YEFDSYMLPYSDMPINGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLYYGQ 120
Cdd:PTZ00047  49 YSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128

                         90       100
                 ....*....|....*....|....
gi 72385072  121 CSEICGANHSFMPIVIESININSF 144
Cdd:PTZ00047 129 CSEMCGTLHGFMPIVVEAVSPEAY 152
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
16-156 7.37e-38

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 128.79  E-value: 7.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072  16 DPLITVKTIGHQWYWSYEYTDFSApyefdsymlpysdmpingfrllDVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 95
Cdd:COG1622 110 EDPLTVEVTGYQWKWLFRYPDQGI----------------------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGG 167

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72385072  96 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVNSTLNSSS 156
Cdd:COG1622 168 KQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 16-149 2.39e-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: 121.72  E-value: 2.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072    16 DPLITVKTIGHQWYWSYEYtdfsapyefdsymlpysdmPINGFRlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 95
Cdd:TIGR02866  88 KDALKVKVTGYQWWWDFEY-------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGG 145

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 72385072    96 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWVN 149
Cdd:TIGR02866 146 KIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 19-137 8.15e-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: 8.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072  19 ITVKTIGHQWYWSYEYTDfsapyefdsymlpysdmpingfrlLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 98
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 72385072  99 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIE 137
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), ...
 19-132 9.98e-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: 88.83  E-value: 9.98e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072  19 ITVKTIGHQWYWsyeytdfsapyEFDsymlpYSDMPINGFRLLdvdNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 98
Cdd:cd04213   2 LTIEVTGHQWWW-----------EFR-----YPDEPGRGIVTA---NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                        90       100       110
                ....*....|....*....|....*....|....
gi 72385072  99 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFM 132
Cdd:cd04213  63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 19-132 1.70e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 83.46  E-value: 1.70e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072  19 ITVKTIGHQWYWSYEYtdfsapyefdsymlpysdmPINGFRLLDVDNRTI----LPMNTQIRMLITAADVLHSWTVPALG 94
Cdd:cd13919   2 LVVEVTAQQWAWTFRY-------------------PGGDGKLGTDDDVTSpelhLPVGRPVLFNLRSKDVIHSFWVPEFR 62

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 72385072  95 VKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFM 132
Cdd:cd13919  63 VKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 19-132 3.09e-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: 82.29  E-value: 3.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072  19 ITVKTIGHQWYWSYEYTdfsapyefdsymlpysdmpiNGFRlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 98
Cdd:cd13915   2 LEIQVTGRQWMWEFTYP--------------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                        90       100       110
                ....*....|....*....|....*....|....
gi 72385072  99 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFM 132
Cdd:cd13915  59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 16-148 3.52e-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: 75.95  E-value: 3.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072  16 DPLiTVKTIGHQWYWSYEYtdfSAPYEFDSYMlpysdmpingfrlldvdnrtILPMNTQIRMLITAADVLHSWTVPALGV 95
Cdd:cd13918  31 DAL-EVEVEGFQFGWQFEY---PNGVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPELRV 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 72385072  96 KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWV 148
Cdd:cd13918  87 KADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 19-148 4.11e-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: 4.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072  19 ITVKTIGHQWYWSYEYTDFSapyefdsymlpysdmpingfrlLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 98
Cdd:cd13914   1 VEIEVEAYQWGWEFSYPEAN----------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 72385072  99 ATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFMPIVIESININSFIKWV 148
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 ...
 69-132 1.44e-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: 54.88  E-value: 1.44e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72385072  69 LPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFM 132
Cdd:cd13913  29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 65-132 2.80e-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: 2.80e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 72385072  65 NRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFM 132
Cdd:cd04212  25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 19-132 8.33e-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: 41.98  E-value: 8.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072  19 ITVKTIGHQWYWSYEYTDFSA--PYEFDsymlpysdmpingfrlldvdnrtilpmntqirmlITAADVLHSWTV--PALG 94
Cdd:cd13916   1 QVVAVTGHQWYWELSRTEIPAgkPVEFR----------------------------------VTSADVNHGFGIydPDMR 46

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 72385072  95 V--KVDATPGRLNQTSFFMNRPGLYYGQCSEICGANHSFM 132
Cdd:cd13916  47 LlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 48-137 1.35e-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: 41.83  E-value: 1.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72385072  48 LPYSDMPINGFrLLDVDNRTILPMNTQIRMLIT-AADVLHSWTVPALGVKVDA---------------TPGRLNQTSFFM 111
Cdd:cd00920   7 DWGWSFTYNGV-LLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTT 85

                        90       100
                ....*....|....*....|....*.
gi 72385072 112 NRPGLYYGQCSEICGaNHSFMPIVIE 137
Cdd:cd00920  86 DQAGVYWFYCTIPGH-NHAGMVGTIN 110
 
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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