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Conserved domains on  [gi|256985338|ref|YP_003162773|]
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cytochrome c oxidase subunit II (mitochondrion) [Dermatophagoides farinae]

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
 1-236 4.82e-108

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 310.99  E-value: 4.82e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  81 MKVLYFMEDVKSPSLTFKVIAHQWYWSYVCPLFKNFSyklsdcfFFSYEYDSlfEEDSKISPRLLGCSSDLILPVNMVSR 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIE-------FDSYMIPT--NELENNGFRLLDVDNRLVLPMNTQIR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256985338 161 LLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDNVSKLYL 236
Cdd:MTH00154 152 ILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-236 4.82e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 310.99  E-value: 4.82e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  81 MKVLYFMEDVKSPSLTFKVIAHQWYWSYVCPLFKNFSyklsdcfFFSYEYDSlfEEDSKISPRLLGCSSDLILPVNMVSR 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIE-------FDSYMIPT--NELENNGFRLLDVDNRLVLPMNTQIR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256985338 161 LLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDNVSKLYL 236
Cdd:MTH00154 152 ILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-230 2.06e-55

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: 173.91  E-value: 2.06e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  93 PSLTFKVIAHQWYWSYVCPLFKNFSyklsdcfFFSYEYDSlfEEDSKISPRLLGCSSDLILPVNMVSRLLISSSDVIHSF 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLE-------FDSYMIPE--DDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSW 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 256985338 173 AVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDN 230
Cdd:cd13912   72 AVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLS 129
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-229 4.00e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 161.15  E-value: 4.00e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   6 SLNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLldFKYYK--------NLSEGTFIETIWSIVPAFLLIILV 77
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFA--IRYRRrkgdadpaQFHHNTKLEIVWTVIPIIIVIVLA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  78 LPSMKVLYFMEDVKSPSLTFKVIAHQWYWSyvcplfknfsyklsdcffFSYEydslfEEDSKISPRLlgcssdlILPVNM 157
Cdd:COG1622   96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWL------------------FRYP-----DQGIATVNEL-------VLPVGR 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256985338 158 VSRLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYD 229
Cdd:COG1622  146 PVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-221 6.85e-47

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 151.79  E-value: 6.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   95 LTFKVIAHQWYWSYVCPLFKNFsyklsdcfffsyEYDSLFEEDSKISP---RLLGCSSDLILPVNMVSRLLISSSDVIHS 171
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDL------------EFDSYMIPTEDLEEgqlRLLEVDNRVVLPVETHIRVIVTAADVIHS 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 256985338  172 FAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLK 221
Cdd:pfam00116  69 WAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-229 3.09e-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: 124.42  E-value: 3.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   14 SPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYY------KNLSEGTFIETIWSIVPAFLLIILVLPS-MKVLYF 86
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKgdeekpSQIHGNRRLEYVWTVIPLIIVVGLFAATaKGLLYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   87 MEDVKSPSLTFKVIAHQWYWSYVCPlfknfsyklsdcfffsyeyDSLFEEDSkisprllgcssDLILPVNMVSRLLISSS 166
Cdd:TIGR02866  83 ERPIPKDALKVKVTGYQWWWDFEYP-------------------ESGFTTVN-----------ELVLPAGTPVELQVTSK 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256985338  167 DVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYD 229
Cdd:TIGR02866 133 DVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFD 195
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-236 4.82e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 310.99  E-value: 4.82e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  81 MKVLYFMEDVKSPSLTFKVIAHQWYWSYVCPLFKNFSyklsdcfFFSYEYDSlfEEDSKISPRLLGCSSDLILPVNMVSR 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIE-------FDSYMIPT--NELENNGFRLLDVDNRLVLPMNTQIR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256985338 161 LLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDNVSKLYL 236
Cdd:MTH00154 152 ILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-228 5.84e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 242.54  E-value: 5.84e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  81 MKVLYFMEDVKSPSLTFKVIAHQWYWSYVCPLFKNFSYKlsdcfffSYEYDslfEEDSKIS-PRLLGCSSDLILPVNMVS 159
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFD-------SYMVP---ENELELGdFRLLEVDNRLVLPYSVDT 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256985338 160 RLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVY 228
Cdd:MTH00140 151 RVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDF 219
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-230 2.19e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 235.75  E-value: 2.19e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  81 MKVLYFMEDVKSPSLTFKVIAHQWYWSYvcplfknfsyKLSDcfFFSYEYDSLFEEDSKIS---PRLLGCSSDLILPVNM 157
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSY----------EYTD--YNDLEFDSYMVPTSDLStglPRLLEVDNRLVLPYQT 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256985338 158 VSRLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDN 230
Cdd:MTH00038 149 PIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFEN 221
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-220 1.65e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 233.46  E-value: 1.65e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  81 MKVLYFMEDVKSPSLTFKVIAHQWYWSYVCPLFKNFSYKlsdcfffSYEYDSlfEEDSKISPRLLGCSSDLILPVNMVSR 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFD-------SYMIPT--EDLSSGEFRLLEVDNRLVLPYKSNIR 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338 161 LLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISL 220
Cdd:MTH00139 152 ALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVV 211
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-219 6.31e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 232.11  E-value: 6.31e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMsgviLLISYVIFYLLLDFK----YYKNLSEGTFIETIWSIVPAFLLIIL 76
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVA----LLISSLVLYLLTLMLttklTHTNTVDAQEVELIWTILPAIVLILL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  77 VLPSMKVLYFMEDVKSPSLTFKVIAHQWYWSYVCPLFKNFSyklsdcfFFSYeydSLFEED-SKISPRLLGCSSDLILPV 155
Cdd:MTH00117  77 ALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLS-------FDSY---MIPTQDlPNGHFRLLEVDHRMVIPM 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256985338 156 NMVSRLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPIS 219
Cdd:MTH00117 147 ESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIV 210
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-222 4.80e-76

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 230.13  E-value: 4.80e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  81 MKVLYFMEDVKSPSLTFKVIAHQWYWSYvcplfknfsyKLSDcfFFSYEYDSLFEEDSKISP---RLLGCSSDLILPVNM 157
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSY----------EYSD--FSNLEFDSYMLPTSDLSPgqfRLLEVDNRAVLPMQT 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256985338 158 VSRLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKV 222
Cdd:MTH00008 149 EIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEA 213
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-230 5.05e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 229.87  E-value: 5.05e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  81 MKVLYFMEDVKSPSLTFKVIAHQWYWsyvcplfknfSYKLSDcfFFSYEYDSLFEEDSKISP---RLLGCSSDLILPVNM 157
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYW----------SYEYTD--YNDLEFDSYMVPTQDLSPgqfRLLEVDNRLVLPMDS 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256985338 158 VSRLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDN 230
Cdd:MTH00168 149 KIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFEN 221
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-230 2.41e-72

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 221.16  E-value: 2.41e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   7 LNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPSMKVLYF 86
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  87 MEDVKSPSLTFKVIAHQWYWSYvcplfknfsyKLSDCFFFSYEYDSLFEEDSKISP---RLLGCSSDLILPVNMVSRLLI 163
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSY----------EYSDYEGETLEFDSYMVPTSDLNSgdfRLLEVDNRLVVPINTHVRILV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256985338 164 SSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDN 230
Cdd:MTH00023 166 TGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIN 232
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-232 1.64e-71

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 218.43  E-value: 1.64e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  81 MKVLYFMEDVKSPSLTFKVIAHQWYWSYVCPLFKNFSyklsdcfFFSYEYDSLFEEDSKIspRLLGCSSDLILPVNMVSR 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLS-------FDSYMIPTSDLKPGEL--RLLEVDNRVVLPMEMPIR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256985338 161 LLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDNVS 232
Cdd:MTH00098 152 MLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWS 223
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-230 1.61e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 213.49  E-value: 1.61e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   7 LNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPSMKVLYF 86
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  87 MEDVKSPSLTFKVIAHQWYWSYvcplfknfsyKLSDCFFFSYEYDSLFEEDSKISP---RLLGCSSDLILPVNMVSRLLI 163
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSY----------EYSDYGTDTIEFDSYMIPTSDLNSgdlRLLEVDNRLIVPIQTQVRVLV 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256985338 164 SSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDN 230
Cdd:MTH00051 159 TAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYIN 225
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 7-234 3.39e-64

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 199.62  E-value: 3.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   7 LNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPSMKVLYF 86
Cdd:MTH00076   7 LGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  87 MEDVKSPSLTFKVIAHQWYWSYVCPLFKNFSYklsdcfffsyeyDSLFEEDSKISP---RLLGCSSDLILPVNMVSRLLI 163
Cdd:MTH00076  87 MDEINDPHLTVKAIGHQWYWSYEYTDYEDLSF------------DSYMIPTQDLTPgqfRLLEVDNRMVVPMESPIRMLI 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256985338 164 SSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDNVSKL 234
Cdd:MTH00076 155 TAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 7-236 1.29e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 195.70  E-value: 1.29e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   7 LNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPSMKVLYF 86
Cdd:MTH00129   7 LGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  87 MEDVKSPSLTFKVIAHQWYWSYVCPLFKNFsyklsdcfffsyEYDSLFEEDSKISP---RLLGCSSDLILPVNMVSRLLI 163
Cdd:MTH00129  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEDL------------GFDSYMIPTQDLTPgqfRLLEADHRMVVPVESPIRVLV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256985338 164 SSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDNVSKLYL 236
Cdd:MTH00129 155 SAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 7-236 3.11e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 194.72  E-value: 3.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   7 LNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPSMKVLYF 86
Cdd:MTH00185   7 LGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  87 MEDVKSPSLTFKVIAHQWYWSYvcplfknfsyKLSDcfFFSYEYDSLFEEDSKISP---RLLGCSSDLILPVNMVSRLLI 163
Cdd:MTH00185  87 MDEINDPHLTIKAMGHQWYWSY----------EYTD--YEQLEFDSYMTPTQDLTPgqfRLLETDHRMVVPMESPIRVLI 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256985338 164 SSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDNVSKLYL 236
Cdd:MTH00185 155 TAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-230 2.06e-55

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: 173.91  E-value: 2.06e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  93 PSLTFKVIAHQWYWSYVCPLFKNFSyklsdcfFFSYEYDSlfEEDSKISPRLLGCSSDLILPVNMVSRLLISSSDVIHSF 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLE-------FDSYMIPE--DDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSW 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 256985338 173 AVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDN 230
Cdd:cd13912   72 AVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLS 129
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-228 2.44e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 178.30  E-value: 2.44e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   7 LNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLD---FKYYKNLSEGTFIETIWSIVPAFLLIILVLPSMKV 83
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGnnyYSYYWNKLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  84 LYFMED-VKSPSLTFKVIAHQWYWSYVcplFKNFSYKlsdcfffSYEYDSLFEEDSKIS---PRLLGCSSDLILPVNMVS 159
Cdd:MTH00027 115 LYIMDEcGFSANITIKVTGHQWYWSYS---YEDYGEK-------NIEFDSYMIPTADLEfgdLRLLEVDNRLILPVDTNV 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256985338 160 RLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVY 228
Cdd:MTH00027 185 RVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKY 253
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 7-237 6.56e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 165.95  E-value: 6.56e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   7 LNFQDSSSPS-MGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYYKNLSEGTFIETIWSIVPAFLLIILVLPSMKVLY 85
Cdd:MTH00080   8 LNFSNSLFSSyMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  86 FMEDVKSPS-LTFKVIAHQWYWSYVCPLFKNFSYklsDCFFFSYEYDSLFEedskisPRLLGCSSDLILPVNMVSRLLIS 164
Cdd:MTH00080  88 YYGLMNLDSnLTVKVTGHQWYWSYEFSDIPGLEF---DSYMKSLDQLRLGE------PRLLEVDNRCVLPCDTNIRFCIT 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256985338 165 SSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYDNVSKLYLL 237
Cdd:MTH00080 159 SSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-229 4.00e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 161.15  E-value: 4.00e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   6 SLNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLldFKYYK--------NLSEGTFIETIWSIVPAFLLIILV 77
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFA--IRYRRrkgdadpaQFHHNTKLEIVWTVIPIIIVIVLA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  78 LPSMKVLYFMEDVKSPSLTFKVIAHQWYWSyvcplfknfsyklsdcffFSYEydslfEEDSKISPRLlgcssdlILPVNM 157
Cdd:COG1622   96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWL------------------FRYP-----DQGIATVNEL-------VLPVGR 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256985338 158 VSRLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYD 229
Cdd:COG1622  146 PVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-221 6.85e-47

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 151.79  E-value: 6.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   95 LTFKVIAHQWYWSYVCPLFKNFsyklsdcfffsyEYDSLFEEDSKISP---RLLGCSSDLILPVNMVSRLLISSSDVIHS 171
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDL------------EFDSYMIPTEDLEEgqlRLLEVDNRVVLPVETHIRVIVTAADVIHS 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 256985338  172 FAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLK 221
Cdd:pfam00116  69 WAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 56-222 1.63e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 135.47  E-value: 1.63e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  56 SEGTFIETIWSIVPAFLLIILVLPSMKVLYFMEDVKSpSLTFKVIAHQWYWSYvcplfknfsyklsdcfffsyEYDSLFE 135
Cdd:MTH00047  44 SENQVLELLWTVVPTLLVLVLCFLNLNFITSDLDCFS-SETIKVIGHQWYWSY--------------------EYSFGGS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338 136 EDSKISPRLLGCSSDLILPVNMVSRLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSF 215
Cdd:MTH00047 103 YDSFMTDDIFGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSY 182


                 ....*..
gi 256985338 216 MPISLKV 222
Cdd:MTH00047 183 MPIVIEV 189
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-229 3.09e-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: 124.42  E-value: 3.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   14 SPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKYY------KNLSEGTFIETIWSIVPAFLLIILVLPS-MKVLYF 86
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKgdeekpSQIHGNRRLEYVWTVIPLIIVVGLFAATaKGLLYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338   87 MEDVKSPSLTFKVIAHQWYWSYVCPlfknfsyklsdcfffsyeyDSLFEEDSkisprllgcssDLILPVNMVSRLLISSS 166
Cdd:TIGR02866  83 ERPIPKDALKVKVTGYQWWWDFEYP-------------------ESGFTTVN-----------ELVLPAGTPVELQVTSK 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256985338  167 DVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYD 229
Cdd:TIGR02866 133 DVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFD 195
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-216 3.63e-27

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: 100.77  E-value: 3.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  94 SLTFKVIAHQWYWsyvcplfkNFSYKLSDcfffsyeydslfeedskisPRLLGCSSDLILPVNMVSRLLISSSDVIHSFA 173
Cdd:cd04213    1 ALTIEVTGHQWWW--------EFRYPDEP-------------------GRGIVTANELHIPVGRPVRLRLTSADVIHSFW 53

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 256985338 174 VPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFM 216
Cdd:cd04213   54 VPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 128-235 4.39e-27

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 102.21  E-value: 4.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338 128 YEYDSLFEEDSKISP---RLLGCSSDLILPVNMVSRLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQ 204
Cdd:PTZ00047  49 YSFQSNLVTDEDLKPgmlRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128

                         90       100       110
                 ....*....|....*....|....*....|.
gi 256985338 205 CSEICGSNHSFMPISLKVSSLSVYDNVSKLY 235
Cdd:PTZ00047 129 CSEMCGTLHGFMPIVVEAVSPEAYAAHAKKY 159
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-222 4.12e-25

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: 95.40  E-value: 4.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  95 LTFKVIAHQWYWSyvcplfknfsyklsdcffFSYEydslfEEDSKISPRLLGCSSDLILPVNMVSRLLISSSDVIHSFAV 174
Cdd:cd13919    2 LVVEVTAQQWAWT------------------FRYP-----GGDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWV 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 256985338 175 PSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKV 222
Cdd:cd13919   59 PEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKV 106
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-221 1.44e-22

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: 88.51  E-value: 1.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  95 LTFKVIAHQWYWSYVCPLfknfsyklsdcfffsyeydslfeedskisprlLGCSSDLILPVNMVSRLLISSSDVIHSFAV 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN--------------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYI 48

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 256985338 175 PSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLK 221
Cdd:cd13842   49 PNLGVKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-222 3.16e-20

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 82.29  E-value: 3.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  94 SLTFKVIAHQWYWSyvcplfknfsyklsdcffFSYeydslfeedskisPRLLGCSSDLILPVNMVSRLLISSSDVIHSFA 173
Cdd:cd13915    1 ALEIQVTGRQWMWE------------------FTY-------------PNGKREINELHVPVGKPVRLILTSKDVIHSFY 49

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 256985338 174 VPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKV 222
Cdd:cd13915   50 VPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.14e-19

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 80.45  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338    1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVILLISYVIFYLLLDFKY------YKNLSEGTFIETIWSIVPAFLLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 256985338   75 ILVLPSMKV 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-229 1.13e-17

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 75.91  E-value: 1.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  99 VIAHQWYWsyvcplfkNFSYklsdcfffsyeydslfeEDSKISPrllgcSSDLILPVNMVSRLLISSSDVIHSFAVPSLG 178
Cdd:cd13914    5 VEAYQWGW--------EFSY-----------------PEANVTT-----SEQLVIPADRPVYFRITSRDVIHAFHVPELG 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 256985338 179 LKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKVSSLSVYD 229
Cdd:cd13914   55 LKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQ 105
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-230 9.60e-14

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 66.32  E-value: 9.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338  67 IVPAFLLIILVLPSMKVLYFMEDVKSPS----LTFKVIAHQWYWsyvcplfkNFSYklsdcfffsyeydslfeedskisP 142
Cdd:cd13918    1 GLSAIIVISLIVWTYGMLLYVEDPPDEAdedaLEVEVEGFQFGW--------QFEY-----------------------P 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256985338 143 RLLGCSSDLILPVNMVSRLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKV 222
Cdd:cd13918   50 NGVTTGNTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIV 129


                 ....*...
gi 256985338 223 SSLSVYDN 230
Cdd:cd13918  130 MDEEEFEA 137
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 149-222 3.20e-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: 50.26  E-value: 3.20e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256985338 149 SDLILPVNMVSRLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKV 222
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIV 98
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 160-216 1.11e-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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 40.05  E-value: 1.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 256985338 160 RLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFM 216
Cdd:cd13917   25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 151-222 2.02e-04

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: 39.45  E-value: 2.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256985338 151 LILPVNMVSRLLISSSDVIHSFAVPSLGLKVDALPGRINQLFVFPSRLGVFYGQCSEICGSNHSFMPISLKV 222
Cdd:cd04212   27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLA 98
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 153-223 3.64e-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: 38.52  E-value: 3.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256985338 153 LPVNMVSRLLISSSDVIHSFAV--PSLGL--KVDALPGRINQL-FVFPsRLGVFYGQCSEICGSNHSFMPISLKVS 223
Cdd:cd13916   19 IPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLrYTFD-KPGTYTILCLEYCGLAHHVMMAEFTVV 93
 
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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