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Conserved domains on  [gi|992008467|gb|AMH40096|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Aglaothorax ovata armiger]

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
 1-160 4.38e-110

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 312.53  E-value: 4.38e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFLTPhEFDSYMIPYNEMNMNGFRLLDVDNRTILP 80
Cdd:MTH00154  67 ILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:MTH00154 146 MNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-160 4.38e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 312.53  E-value: 4.38e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFLTPhEFDSYMIPYNEMNMNGFRLLDVDNRTILP 80
Cdd:MTH00154  67 ILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:MTH00154 146 MNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 27-157 1.50e-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: 259.42  E-value: 1.50e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  27 PIITIKTVGHQWYWSYEYTDFLTpHEFDSYMIPYNEMNMNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVK 106
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 992008467 107 VDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKW 157
Cdd:cd13912   80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
29-149 1.14e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 229.22  E-value: 1.14e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   29 ITIKTVGHQWYWSYEYTDFLTPhEFDSYMIPYNEMNMNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 108
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDL-EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 992008467  109 ATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESV 149
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-163 1.73e-41

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 138.42  E-value: 1.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDfltphefdsymipYNEmnmngfrllDVDNRTILP 80
Cdd:COG1622   85 VIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-------------QGI---------ATVNELVLP 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:COG1622  143 VGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222


                 ...
gi 992008467 161 ALQ 163
Cdd:COG1622  223 QKA 225
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 26-159 3.57e-34

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 119.02  E-value: 3.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   26 DPIITIKTVGHQWYWSYEYTDFltphefdsymipynemnmnGFRlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 105
Cdd:TIGR02866  88 KDALKVKVTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGG 145

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 992008467  106 KVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWIS 159
Cdd:TIGR02866 146 KIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-160 4.38e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 312.53  E-value: 4.38e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFLTPhEFDSYMIPYNEMNMNGFRLLDVDNRTILP 80
Cdd:MTH00154  67 ILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:MTH00154 146 MNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-160 1.48e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 265.62  E-value: 1.48e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFlTPHEFDSYMIPYNEMNMNGFRLLDVDNRTILP 80
Cdd:MTH00117  67 ILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDY-KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:MTH00117 146 MESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 27-157 1.50e-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: 259.42  E-value: 1.50e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  27 PIITIKTVGHQWYWSYEYTDFLTpHEFDSYMIPYNEMNMNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVK 106
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 992008467 107 VDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKW 157
Cdd:cd13912   80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-160 4.52e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 259.49  E-value: 4.52e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFLTpHEFDSYMIPYNEMNMNGFRLLDVDNRTILP 80
Cdd:MTH00140  67 IVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:MTH00140 146 YSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-161 1.36e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 258.11  E-value: 1.36e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFLTpHEFDSYMIPYNEMNMNGFRLLDVDNRTILP 80
Cdd:MTH00139  67 VLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-LSFDSYMIPTEDLSSGEFRLLEVDNRLVLP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:MTH00139 146 YKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225


                 .
gi 992008467 161 A 161
Cdd:MTH00139 226 K 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-160 3.00e-86

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 252.47  E-value: 3.00e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFLTPhEFDSYMIPYNEMNMNGFRLLDVDNRTILP 80
Cdd:MTH00008  67 ILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNL-EFDSYMLPTSDLSPGQFRLLEVDNRAVLP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:MTH00008 146 MQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-160 6.08e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 251.44  E-value: 6.08e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFLTpHEFDSYMIPYNEMNMNGFRLLDVDNRTILP 80
Cdd:MTH00168  67 IIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-LEFDSYMVPTQDLSPGQFRLLEVDNRLVLP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:MTH00168 146 MDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-163 4.55e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 246.92  E-value: 4.55e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFlTPHEFDSYMIPYNEMNMNGFRLLDVDNRTILP 80
Cdd:MTH00038  67 IVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY-NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:MTH00038 146 YQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225


                 ...
gi 992008467 161 ALQ 163
Cdd:MTH00038 226 FLE 228
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-160 3.67e-83

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 245.04  E-value: 3.67e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFLTPH-EFDSYMIPYNEMNMNGFRLLDVDNRTIL 79
Cdd:MTH00023  76 IIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETlEFDSYMVPTSDLNSGDFRLLEVDNRLVV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  80 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWIS 159
Cdd:MTH00023 156 PINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235


                 .
gi 992008467 160 N 160
Cdd:MTH00023 236 S 236
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-162 6.18e-80

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 236.15  E-value: 6.18e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDF--LTpheFDSYMIPYNEMNMNGFRLLDVDNRTI 78
Cdd:MTH00098  67 ILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYedLS---FDSYMIPTSDLKPGELRLLEVDNRVV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  79 LPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWI 158
Cdd:MTH00098 144 LPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWS 223


                 ....
gi 992008467 159 SNAL 162
Cdd:MTH00098 224 ASML 227
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-160 7.94e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 236.22  E-value: 7.94e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFLTPH-EFDSYMIPYNEMNMNGFRLLDVDNRTIL 79
Cdd:MTH00051  69 LIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTiEFDSYMIPTSDLNSGDLRLLEVDNRLIV 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  80 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWIS 159
Cdd:MTH00051 149 PIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVA 228


                 .
gi 992008467 160 N 160
Cdd:MTH00051 229 T 229
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-163 2.71e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 234.61  E-value: 2.71e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFlTPHEFDSYMIPYNEMNMNGFRLLDVDNRTILP 80
Cdd:MTH00129  67 VLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:MTH00129 146 VESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSL 225


                 ...
gi 992008467 161 ALQ 163
Cdd:MTH00129 226 MLE 228
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
29-149 1.14e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 229.22  E-value: 1.14e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   29 ITIKTVGHQWYWSYEYTDFLTPhEFDSYMIPYNEMNMNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 108
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDL-EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 992008467  109 ATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESV 149
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-162 6.18e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 231.21  E-value: 6.18e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFlTPHEFDSYMIPYNEMNMNGFRLLDVDNRTILP 80
Cdd:MTH00076  67 IMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDY-EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:MTH00076 146 MESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225


                 ..
gi 992008467 161 AL 162
Cdd:MTH00076 226 ML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-163 4.08e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 226.69  E-value: 4.08e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFLTpHEFDSYMIPYNEMNMNGFRLLDVDNRTILP 80
Cdd:MTH00185  67 ILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQ-LEFDSYMTPTQDLTPGQFRLLETDHRMVVP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:MTH00185 146 MESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSL 225


                 ...
gi 992008467 161 ALQ 163
Cdd:MTH00185 226 MLE 228
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-158 9.04e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 194.09  E-value: 9.04e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDES-MDPIITIKTVGHQWYWSYEYTDFLTPH-EFDSYMIPYNEMNMNGFRLLDVDNRTI 78
Cdd:MTH00027  98 LIPAFILILIAFPSLRLLYIMDECgFSANITIKVTGHQWYWSYSYEDYGEKNiEFDSYMIPTADLEFGDLRLLEVDNRLI 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  79 LPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWI 158
Cdd:MTH00027 178 LPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 29-162 2.67e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 181.36  E-value: 2.67e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  29 ITIKTVGHQWYWSYEYTDFLTPhEFDSYMIPYNEMNMNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 108
Cdd:MTH00080  98 LTVKVTGHQWYWSYEFSDIPGL-EFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMD 176

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 992008467 109 ATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISNAL 162
Cdd:MTH00080 177 AMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLL 230
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 53-154 1.63e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 136.49  E-value: 1.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  53 FDSYMIPYNEMNMNGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCS 132
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|..
gi 992008467 133 EICGANHSFMPIVIESVNTKTF 154
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVSPEAY 152
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-163 1.73e-41

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 138.42  E-value: 1.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   1 ILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDfltphefdsymipYNEmnmngfrllDVDNRTILP 80
Cdd:COG1622   85 VIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-------------QGI---------ATVNELVLP 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  81 MNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWISN 160
Cdd:COG1622  143 VGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222


                 ...
gi 992008467 161 ALQ 163
Cdd:COG1622  223 QKA 225
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 30-149 3.22e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 134.31  E-value: 3.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  30 TIKTVGHQWYWSYEYTDFLtphEFDSYMIPYNEMnmngfrlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDA 109
Cdd:MTH00047  83 TIKVIGHQWYWSYEYSFGG---SYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDA 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 992008467 110 TPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESV 149
Cdd:MTH00047 151 IPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 26-159 3.57e-34

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 119.02  E-value: 3.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467   26 DPIITIKTVGHQWYWSYEYTDFltphefdsymipynemnmnGFRlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGV 105
Cdd:TIGR02866  88 KDALKVKVTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGG 145

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 992008467  106 KVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWIS 159
Cdd:TIGR02866 146 KIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 29-147 1.16e-28

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: 101.60  E-value: 1.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  29 ITIKTVGHQWYWSYEYTDFLTPHEFdsymipynemnmngfrlldvdnrtILPMNTQIRMLITAADVLHSWTVPALGVKVD 108
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNVRTPNEI------------------------VVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 992008467 109 ATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIE 147
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), ...
 29-142 5.52e-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: 89.60  E-value: 5.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  29 ITIKTVGHQWYWSYEYTDfLTPHEFDSYmipyNEMnmngfrlldvdnrtILPMNTQIRMLITAADVLHSWTVPALGVKVD 108
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPD-EPGRGIVTA----NEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 992008467 109 ATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFM 142
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 29-142 7.00e-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: 81.52  E-value: 7.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  29 ITIKTVGHQWYWSYEYTdfltphefdsymipynemnmNGFRlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 108
Cdd:cd13915    2 LEIQVTGRQWMWEFTYP--------------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100       110
                 ....*....|....*....|....*....|....
gi 992008467 109 ATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFM 142
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 29-142 9.85e-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: 81.53  E-value: 9.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  29 ITIKTVGHQWYWSYEYTDFLTPHEFDSyMIPYNEMNmngfrlldvdnrtiLPMNTQIRMLITAADVLHSWTVPALGVKVD 108
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDGKLGTDD-DVTSPELH--------------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                         90       100       110
                 ....*....|....*....|....*....|....
gi 992008467 109 ATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFM 142
Cdd:cd13919   67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 29-158 5.05e-20

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 79.76  E-value: 5.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  29 ITIKTVGHQWYWSYEYtdfltphefdsymipyNEMNMNGFrlldvdNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 108
Cdd:cd13914    1 VEIEVEAYQWGWEFSY----------------PEANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 992008467 109 ATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKWI 158
Cdd:cd13914   59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 22-157 1.43e-17

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 74.41  E-value: 1.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  22 DESMDPIITIKTVGHQWYWSYEYTDFLTphefdsymipynemNMNGFRLldvdnrtilPMNTQIRMLITAADVLHSWTVP 101
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYPNGVT--------------TGNTLRV---------PADTPIALRVTSTDVFHTFGIP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 992008467 102 ALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPIVIESVNTKTFIKW 157
Cdd:cd13918   83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 79-142 2.64e-08

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: 49.11  E-value: 2.64e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992008467  79 LPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFM 142
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 75-142 2.08e-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: 44.08  E-value: 2.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992008467  75 NRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFM 142
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 29-142 1.07e-04

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: 39.29  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  29 ITIKTVGHQWYWsyeytdfltphefdsymipynEMNmngfrlldvdnRTILPMNTQIRMLITAADVLHSWTV--PALGV- 105
Cdd:cd13916    1 QVVAVTGHQWYW---------------------ELS-----------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLl 48

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 992008467 106 -KVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFM 142
Cdd:cd13916   49 aQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 55-147 5.76e-04

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: 37.60  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  55 SYMIPYNEMNMNGFrlldVDNRTILPMNTQIRMLIT-AADVLHSWTVPALGVKVDA---------------TPGRLNQTS 118
Cdd:cd00920    7 DWGWSFTYNGVLLF----GPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVT 82

                         90       100
                 ....*....|....*....|....*....
gi 992008467 119 FFVNRPGIFYGQCSEICGaNHSFMPIVIE 147
Cdd:cd00920   83 FTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 75-163 9.28e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 35.55  E-value: 9.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008467  75 NRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFYGQCSEICGANHSFMPI-VIESVNTKT 153
Cdd:PRK10525 151 NEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFkAIATPDRAE 230

                         90
                 ....*....|
gi 992008467 154 FIKWISNALQ 163
Cdd:PRK10525 231 FDQWVAKAKQ 240
 
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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