NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2088232041|ref|YP_010133398|]
View 

cytochrome c oxidase subunit II (mitochondrion) [Exaiptasia diaphana]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475873)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 10-243 3.05e-162

cytochrome c oxidase subunit II; Validated


:

Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 448.43  E-value: 3.05e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  10 IINQFSY-DLPEPWQLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPAL 88
Cdd:MTH00023    1 MFNNFFYrDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  89 ILILIALPSLKLLYLMDEVMDPALTIKAIGHQWYWSYEYSDYQTETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTH 168
Cdd:MTH00023   81 ILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTH 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2088232041 169 VRVLVTGADVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWVL 243
Cdd:MTH00023  161 VRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
 
Name Accession Description Interval E-value
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 10-243 3.05e-162

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 448.43  E-value: 3.05e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  10 IINQFSY-DLPEPWQLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPAL 88
Cdd:MTH00023    1 MFNNFFYrDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  89 ILILIALPSLKLLYLMDEVMDPALTIKAIGHQWYWSYEYSDYQTETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTH 168
Cdd:MTH00023   81 ILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTH 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2088232041 169 VRVLVTGADVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWVL 243
Cdd:MTH00023  161 VRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 110-241 9.92e-96

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: 275.99  E-value: 9.92e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 110 PALTIKAIGHQWYWSYEYSDYqtETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLHSFAVPALAV 189
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF--NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2088232041 190 KMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISW 241
Cdd:cd13912    79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
112-232 6.46e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 238.08  E-value: 6.46e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 112 LTIKAIGHQWYWSYEYSDYqtETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLHSFAVPALAVKM 191
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDF--GDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2088232041 192 DAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEA 232
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
22-242 1.28e-60

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 190.42  E-value: 1.28e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  22 WQLGFQDAAHPVMEEIIFFHDQVMFIliiiiTTVLWLIVKAL-----------SGRAYHRYLVDGTLLEIIWTIVPALIL 90
Cdd:COG1622    17 GQLSLPDPAGPIAEEIDDLFWVSLII-----MLVIFVLVFGLllyfairyrrrKGDADPAQFHHNTKLEIVWTVIPIIIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  91 ILIALPSLKLLYLMDEVMDPALTIKAIGHQWYWSYEYSDYQTETlefdsymvptsdlkngdfrllevDNRLVVPINTHVR 170
Cdd:COG1622    92 IVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-----------------------VNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2088232041 171 VLVTGADVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWV 242
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 75-242 9.92e-46

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: 151.38  E-value: 9.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  75 GTLLEIIWTIVPALILI-LIALPSLKLLYLMDEVMDPALTIKAIGHQWYWSYEYSDYQTETlefdsymvptsdlkngdfr 153
Cdd:TIGR02866  53 NRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFTT------------------- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 154 llevDNRLVVPINTHVRVLVTGADVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAA 233
Cdd:TIGR02866 114 ----VNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVV 189


                  ....*....
gi 2088232041 234 SLDKYISWV 242
Cdd:TIGR02866 190 PKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 10-243 3.05e-162

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 448.43  E-value: 3.05e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  10 IINQFSY-DLPEPWQLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPAL 88
Cdd:MTH00023    1 MFNNFFYrDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  89 ILILIALPSLKLLYLMDEVMDPALTIKAIGHQWYWSYEYSDYQTETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTH 168
Cdd:MTH00023   81 ILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTH 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2088232041 169 VRVLVTGADVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWVL 243
Cdd:MTH00023  161 VRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 17-242 3.62e-149

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 415.33  E-value: 3.62e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  17 DLPEPWQLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALP 96
Cdd:MTH00051    2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  97 SLKLLYLMDEVMDPALTIKAIGHQWYWSYEYSDYQTETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGA 176
Cdd:MTH00051   82 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2088232041 177 DVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWV 242
Cdd:MTH00051  162 DVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 23-242 1.38e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 368.00  E-value: 1.38e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  23 QLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALPSLKLLY 102
Cdd:MTH00154    6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 103 LMDEVMDPALTIKAIGHQWYWSYEYSDYqtETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLHSF 182
Cdd:MTH00154   86 LLDEVNNPSITLKTIGHQWYWSYEYSDF--KNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSW 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 183 AVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWV 242
Cdd:MTH00154  164 TVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 18-246 2.62e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 362.31  E-value: 2.62e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  18 LPEPWQLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALPS 97
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  98 LKLLYLMDEVMDPALTIKAIGHQWYWSYEYSDYqtETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGAD 177
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDY--KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAED 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2088232041 178 VLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWVLQES 246
Cdd:MTH00117  159 VLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 23-242 5.24e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 343.84  E-value: 5.24e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  23 QLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALPSLKLLY 102
Cdd:MTH00140    6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 103 LMDEVMDPALTIKAIGHQWYWSYEYSDYQTetLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLHSF 182
Cdd:MTH00140   86 LLDETNNPLLTVKAIGHQWYWSYEYSDFSV--IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSW 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 183 AVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWV 242
Cdd:MTH00140  164 TVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWL 223
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 21-244 9.45e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 333.21  E-value: 9.45e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  21 PWQLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALPSLKL 100
Cdd:MTH00038    4 WLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 101 LYLMDEVMDPALTIKAIGHQWYWSYEYSDYQTetLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLH 180
Cdd:MTH00038   84 LYLMDEVNNPFLTIKAIGHQWYWSYEYTDYND--LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLH 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2088232041 181 SFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWVLQ 244
Cdd:MTH00038  162 SWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 23-244 8.63e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 330.40  E-value: 8.63e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  23 QLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALPSLKLLY 102
Cdd:MTH00168    6 QLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 103 LMDEVMDPALTIKAIGHQWYWSYEYSDYqtETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLHSF 182
Cdd:MTH00168   86 LMDEIDKPDLTIKAVGHQWYWSYEYTDY--NDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSW 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2088232041 183 AVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWVLQ 244
Cdd:MTH00168  164 TLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 21-241 1.42e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 330.14  E-value: 1.42e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  21 PWQLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALPSLKL 100
Cdd:MTH00129    4 PSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 101 LYLMDEVMDPALTIKAIGHQWYWSYEYSDYqtETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLH 180
Cdd:MTH00129   84 LYLMDEINDPHLTIKAMGHQWYWSYEYTDY--EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLH 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2088232041 181 SFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISW 241
Cdd:MTH00129  162 SWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 23-243 3.11e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 326.67  E-value: 3.11e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  23 QLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALPSLKLLY 102
Cdd:MTH00139    6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 103 LMDEVMDPALTIKAIGHQWYWSYEYSDyqTETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLHSF 182
Cdd:MTH00139   86 LMDEVSDPYLTFKAVGHQWYWSYEYSD--FKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSW 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2088232041 183 AVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWVL 243
Cdd:MTH00139  164 TVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWIL 224
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 18-241 9.01e-111

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 317.82  E-value: 9.01e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  18 LPEPWQLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALPS 97
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  98 LKLLYLMDEVMDPALTIKAIGHQWYWSYEYSDYqtETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGAD 177
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY--EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSED 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2088232041 178 VLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISW 241
Cdd:MTH00098  159 VLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 17-247 9.23e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 316.58  E-value: 9.23e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  17 DLPEPWQLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYL---VDGTLLEIIWTIVPALILILI 93
Cdd:MTH00027   28 DANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  94 ALPSLKLLYLMDE-VMDPALTIKAIGHQWYWSYEYSDYQTETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVL 172
Cdd:MTH00027  108 AFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVL 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2088232041 173 VTGADVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWVLQESL 247
Cdd:MTH00027  188 ITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGREDV 262
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 18-241 9.38e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 310.28  E-value: 9.38e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  18 LPEPWQLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALPS 97
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  98 LKLLYLMDEVMDPALTIKAIGHQWYWSYEYSDYqtETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGAD 177
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY--EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAED 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2088232041 178 VLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISW 241
Cdd:MTH00185  159 VLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 21-241 3.01e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 309.02  E-value: 3.01e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  21 PWQLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALPSLKL 100
Cdd:MTH00076    4 PSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 101 LYLMDEVMDPALTIKAIGHQWYWSYEYSDYqtETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLH 180
Cdd:MTH00076   84 LYLMDEINDPHLTVKAIGHQWYWSYEYTDY--EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLH 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2088232041 181 SFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISW 241
Cdd:MTH00076  162 SWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 23-243 2.60e-106

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 306.78  E-value: 2.60e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  23 QLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALPSLKLLY 102
Cdd:MTH00008    6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 103 LMDEVMDPALTIKAIGHQWYWSYEYSDYQTetLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLHSF 182
Cdd:MTH00008   86 LMDEVSNPSITLKTIGHQWYWSYEYSDFSN--LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSW 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2088232041 183 AVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWVL 243
Cdd:MTH00008  164 TVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 110-241 9.92e-96

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: 275.99  E-value: 9.92e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 110 PALTIKAIGHQWYWSYEYSDYqtETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLHSFAVPALAV 189
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF--NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2088232041 190 KMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISW 241
Cdd:cd13912    79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
112-232 6.46e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 238.08  E-value: 6.46e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 112 LTIKAIGHQWYWSYEYSDYqtETLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLHSFAVPALAVKM 191
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDF--GDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2088232041 192 DAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEA 232
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 40-241 6.46e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 224.50  E-value: 6.46e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  40 FHDQVMFILIIIITTVLWLIVKALSGRAYHRYLVDGTLLEIIWTIVPALILILIALPSLKLLYLMdEVM--DPALTIKAI 117
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYY-GLMnlDSNLTVKVT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 118 GHQWYWSYEYSDYQTetLEFDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLHSFAVPALAVKMDAVPGR 197
Cdd:MTH00080  104 GHQWYWSYEFSDIPG--LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGI 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2088232041 198 LNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISW 241
Cdd:MTH00080  182 LSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW 225
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
22-242 1.28e-60

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 190.42  E-value: 1.28e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  22 WQLGFQDAAHPVMEEIIFFHDQVMFIliiiiTTVLWLIVKAL-----------SGRAYHRYLVDGTLLEIIWTIVPALIL 90
Cdd:COG1622    17 GQLSLPDPAGPIAEEIDDLFWVSLII-----MLVIFVLVFGLllyfairyrrrKGDADPAQFHHNTKLEIVWTVIPIIIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  91 ILIALPSLKLLYLMDEVMDPALTIKAIGHQWYWSYEYSDYQTETlefdsymvptsdlkngdfrllevDNRLVVPINTHVR 170
Cdd:COG1622    92 IVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-----------------------VNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2088232041 171 VLVTGADVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWV 242
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 77-231 6.79e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 154.34  E-value: 6.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  77 LLEIIWTIVPALI-LILIALPSLKLLYLMDEVMDPalTIKAIGHQWYWSYEYSDyqteTLEFDSYMvptSDLKNGdfrll 155
Cdd:MTH00047   48 VLELLWTVVPTLLvLVLCFLNLNFITSDLDCFSSE--TIKVIGHQWYWSYEYSF----GGSYDSFM---TDDIFG----- 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2088232041 156 eVDNRLVVPINTHVRVLVTGADVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIE 231
Cdd:MTH00047  114 -VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 75-242 9.92e-46

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: 151.38  E-value: 9.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  75 GTLLEIIWTIVPALILI-LIALPSLKLLYLMDEVMDPALTIKAIGHQWYWSYEYSDYQTETlefdsymvptsdlkngdfr 153
Cdd:TIGR02866  53 NRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFTT------------------- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 154 llevDNRLVVPINTHVRVLVTGADVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAA 233
Cdd:TIGR02866 114 ----VNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVV 189


                  ....*....
gi 2088232041 234 SLDKYISWV 242
Cdd:TIGR02866 190 PKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 137-238 7.04e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 148.04  E-value: 7.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 137 FDSYMVPTSDLKNGDFRLLEVDNRLVVPINTHVRVLVTGADVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCS 216
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 2088232041 217 EICGANHSFMPIVIEAASLDKY 238
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 111-226 7.91e-30

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: 107.32  E-value: 7.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 111 ALTIKAIGHQWYWSYEYSDYQTETLEfdsymvpTSdlkngdfrllevdNRLVVPINTHVRVLVTGADVLHSFAVPALAVK 190
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGIV-------TA-------------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGK 60

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2088232041 191 MDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFM 226
Cdd:cd04213    61 MDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 112-231 1.43e-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: 103.92  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 112 LTIKAIGHQWYWSYEYSDyqtetlefdsymvptsdlkngdfrlLEVDNRLVVPINTHVRVLVTGADVLHSFAVPALAVKM 191
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKV 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2088232041 192 DAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIE 231
Cdd:cd13842    56 DAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 111-226 5.27e-26

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: 97.31  E-value: 5.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 111 ALTIKAIGHQWYWSYEYSDYQTEtlefdsymvptsdlkngdfrllevDNRLVVPINTHVRVLVTGADVLHSFAVPALAVK 190
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKRE------------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIK 56

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2088232041 191 MDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFM 226
Cdd:cd13915    57 QDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 19-100 3.33e-25

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: 95.09  E-value: 3.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  19 PEPWQLGFQDAAHPVMEEIIFFHDQVMFILIIIITTVLWLIVKALSGRAY------HRYLVDGTLLEIIWTIVPALILIL 92
Cdd:pfam02790   2 PTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILIL 81


                  ....*...
gi 2088232041  93 IALPSLKL 100
Cdd:pfam02790  82 IALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 111-226 4.74e-24

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: 92.70  E-value: 4.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 111 ALTIKAIGHQWYWSYEYsdyqtetlefdsymvPTSDLKNGDFRLLEVdNRLVVPINTHVRVLVTGADVLHSFAVPALAVK 190
Cdd:cd13919     1 ALVVEVTAQQWAWTFRY---------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVK 64

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2088232041 191 MDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFM 226
Cdd:cd13919    65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 84-242 1.43e-22

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 89.82  E-value: 1.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041  84 IVPALILI-LIALPSLKLLYLMD---EVMDPALTIKAIGHQWYWSYEYSDYQTETlefdsymvptsdlkngdfrllevdN 159
Cdd:cd13918     1 GLSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTG------------------------N 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 160 RLVVPINTHVRVLVTGADVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYI 239
Cdd:cd13918    57 TLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFE 136


                  ...
gi 2088232041 240 SWV 242
Cdd:cd13918   137 AWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 113-242 3.29e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 85.15  E-value: 3.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 113 TIKAIGHQWYWSYEYSDYQTETlefdsymvptsdlkngdfrllevDNRLVVPINTHVRVLVTGADVLHSFAVPALAVKMD 192
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTT-----------------------SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2088232041 193 AVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFMPIVIEAASLDKYISWV 242
Cdd:cd13914    59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 159-226 1.19e-11

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: 59.51  E-value: 1.19e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2088232041 159 NRLVVPINTHVRVLVTGADVLHSFAVPALAVKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFM 226
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 112-226 2.59e-08

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: 50.24  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 112 LTIKAIGHQWYWSYEYSDYQTETLefdsymvptsdlkngdfrllevdNRLVVPINTHVRVLVTGADVLHSFAVPALAVKM 191
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQGIATV-----------------------NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQI 57

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2088232041 192 DAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFM 226
Cdd:cd04212    58 YAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 113-226 1.15e-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: 40.06  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 113 TIKAIGHQWYWSyeysdyqtetlefdsyMVPTsdlkngdfrllevdnrlVVPINTHVRVLVTGADVLHSFAVPA----LA 188
Cdd:cd13916     2 VVAVTGHQWYWE----------------LSRT-----------------EIPAGKPVEFRVTSADVNHGFGIYDpdmrLL 48

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2088232041 189 VKMDAVPGRLNQTGVFIKRPGIFYGQCSEICGANHSFM 226
Cdd:cd13916    49 AQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 148-231 3.34e-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: 39.14  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088232041 148 KNGDFRLLEVDNRLVVPINTHVRV-LVTGADVLHSFAVPALAVKMDA---------------VPGRLNQTGVFIKRPGIF 211
Cdd:cd00920    12 FTYNGVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVY 91

                          90       100
                  ....*....|....*....|
gi 2088232041 212 YGQCSEICGaNHSFMPIVIE 231
Cdd:cd00920    92 WFYCTIPGH-NHAGMVGTIN 110
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH