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Conserved domains on  [gi|164420795|ref|YP_001648463|]
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cytochrome c oxidase subunit II (mitochondrion) [Ephydatia muelleri]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475883)

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 MTH00051
cytochrome c oxidase subunit II; Provisional
 25-256 1.29e-168

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 465.02  E-value: 1.29e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  25 DTPEPWQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFP 104
Cdd:MTH00051   2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 105 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGSDTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAA 184
Cdd:MTH00051  82 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420795 185 DVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVANWSAS 256
Cdd:MTH00051 162 DVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
 
Name Accession Description Interval E-value
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 25-256 1.29e-168

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 465.02  E-value: 1.29e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  25 DTPEPWQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFP 104
Cdd:MTH00051   2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 105 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGSDTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAA 184
Cdd:MTH00051  82 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420795 185 DVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVANWSAS 256
Cdd:MTH00051 162 DVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 118-249 1.55e-95

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: 1.55e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 118 PALTIKAIGHQWYWSYEYSDYGsdTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLHSFAVPSLSV 197
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFN--DLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 164420795 198 KMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHW 249
Cdd:cd13912   79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
120-241 6.06e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 243.86  E-value: 6.06e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  120 LTIKAIGHQWYWSYEYSDYGsdTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLHSFAVPSLSVKM 199
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFG--DLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 164420795  200 DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAV 241
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
30-252 1.06e-67

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 208.91  E-value: 1.06e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  30 WQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIV------RALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAF 103
Cdd:COG1622   17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLyfairyRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 104 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGSDTiefdsymiptsdlnngdlrllevDNRIIVPIQTQVRVLVTA 183
Cdd:COG1622   97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-----------------------VNELVLPVGRPVRFLLTS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164420795 184 ADVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVAN 252
Cdd:COG1622  154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 37-251 1.15e-49

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: 161.78  E-value: 1.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795   37 AASPV*EEVIFLH*QI---MFILTIIITAVLWLIV---RALTTKHYHKYLYEGTLIEIIWTLIPAAILV-FIAFPSLKLL 109
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVlavSTLISLLVAALLAYVVwkfRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  110 YLMDEVIDPALTIKAIGHQWYWSYEYSDYGsdtiefdsymiptsdlnngdlrlLEVDNRIIVPIQTQVRVLVTAADVLHS 189
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPESG-----------------------FTTVNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420795  190 FAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVA 251
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 25-256 1.29e-168

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 465.02  E-value: 1.29e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  25 DTPEPWQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFP 104
Cdd:MTH00051   2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 105 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGSDTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAA 184
Cdd:MTH00051  82 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420795 185 DVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVANWSAS 256
Cdd:MTH00051 162 DVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 25-256 1.74e-155

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 431.87  E-value: 1.74e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  25 DTPEPWQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFP 104
Cdd:MTH00023   9 DIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 105 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGSDTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAA 184
Cdd:MTH00023  89 SLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGA 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420795 185 DVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVANWSAS 256
Cdd:MTH00023 169 DVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSND 240
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 31-254 6.66e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 379.17  E-value: 6.66e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  31 QLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFPSLKLLY 110
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 111 LMDEVIDPALTIKAIGHQWYWSYEYSDYGSdtIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLHSF 190
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDFKN--IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164420795 191 AVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVANWS 254
Cdd:MTH00154 164 TVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 27-252 9.12e-129

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 363.85  E-value: 9.12e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  27 PEPWQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFPSL 106
Cdd:MTH00117   2 ANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 107 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgsDTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADV 186
Cdd:MTH00117  82 RILYLMDEINNPHLTIKAIGHQWYWSYEYTDY--KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164420795 187 LHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVAN 252
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 31-252 7.88e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 351.55  E-value: 7.88e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  31 QLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFPSLKLLY 110
Cdd:MTH00140   6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 111 LMDEVIDPALTIKAIGHQWYWSYEYSDygSDTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLHSF 190
Cdd:MTH00140  86 LLDETNNPLLTVKAIGHQWYWSYEYSD--FSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420795 191 AVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVAN 252
Cdd:MTH00140 164 TVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 31-252 1.70e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 342.73  E-value: 1.70e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  31 QLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFPSLKLLY 110
Cdd:MTH00168   6 QLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 111 LMDEVIDPALTIKAIGHQWYWSYEYSDYGSdtIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLHSF 190
Cdd:MTH00168  86 LMDEIDKPDLTIKAVGHQWYWSYEYTDYND--LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420795 191 AVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVAN 252
Cdd:MTH00168 164 TLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 29-254 6.38e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 341.68  E-value: 6.38e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  29 PWQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFPSLKL 108
Cdd:MTH00038   4 WLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 109 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYGSdtIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLH 188
Cdd:MTH00038  84 LYLMDEVNNPFLTIKAIGHQWYWSYEYTDYND--LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164420795 189 SFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVANWS 254
Cdd:MTH00038 162 SWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 29-249 2.51e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 330.14  E-value: 2.51e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  29 PWQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFPSLKL 108
Cdd:MTH00129   4 PSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 109 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgsDTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLH 188
Cdd:MTH00129  84 LYLMDEINDPHLTIKAMGHQWYWSYEYTDY--EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164420795 189 SFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHW 249
Cdd:MTH00129 162 SWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 22-251 5.56e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 330.45  E-value: 5.56e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  22 IL*DTPEPWQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLY---EGTLIEIIWTLIPAAIL 98
Cdd:MTH00027  25 MIKDANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYWnklDGSLIEVIWTLIPAFIL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  99 VFIAFPSLKLLYLMDE-VIDPALTIKAIGHQWYWSYEYSDYGSDTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQV 177
Cdd:MTH00027 105 ILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNV 184

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164420795 178 RVLVTAADVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVA 251
Cdd:MTH00027 185 RVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIG 258
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 31-250 4.71e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 323.98  E-value: 4.71e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  31 QLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFPSLKLLY 110
Cdd:MTH00139   6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 111 LMDEVIDPALTIKAIGHQWYWSYEYSDYgsDTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLHSF 190
Cdd:MTH00139  86 LMDEVSDPYLTFKAVGHQWYWSYEYSDF--KNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 191 AVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWV 250
Cdd:MTH00139 164 TVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 27-256 5.95e-111

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 318.59  E-value: 5.95e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  27 PEPWQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFPSL 106
Cdd:MTH00098   2 AYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 107 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgsDTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADV 186
Cdd:MTH00098  82 RILYMMDEINNPSLTVKTMGHQWYWSYEYTDY--EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 187 LHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLdKYIHwvaNWSAS 256
Cdd:MTH00098 160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPL-KYFE---KWSAS 225
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 28-249 2.36e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 312.20  E-value: 2.36e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  28 EPWQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFPSLK 107
Cdd:MTH00185   3 HPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 108 LLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgsDTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVL 187
Cdd:MTH00185  83 ILYLMDEINDPHLTIKAMGHQWYWSYEYTDY--EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420795 188 HSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHW 249
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 31-254 3.76e-108

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 311.79  E-value: 3.76e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  31 QLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFPSLKLLY 110
Cdd:MTH00008   6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 111 LMDEVIDPALTIKAIGHQWYWSYEYSDYGSdtIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLHSF 190
Cdd:MTH00008  86 LMDEVSNPSITLKTIGHQWYWSYEYSDFSN--LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164420795 191 AVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVANWS 254
Cdd:MTH00008 164 TVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 29-249 9.16e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 308.25  E-value: 9.16e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  29 PWQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFPSLKL 108
Cdd:MTH00076   4 PSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 109 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgsDTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLH 188
Cdd:MTH00076  84 LYLMDEINDPHLTVKAIGHQWYWSYEYTDY--EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164420795 189 SFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHW 249
Cdd:MTH00076 162 SWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNW 222
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 118-249 1.55e-95

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: 1.55e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 118 PALTIKAIGHQWYWSYEYSDYGsdTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLHSFAVPSLSV 197
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFN--DLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 164420795 198 KMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHW 249
Cdd:cd13912   79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
120-241 6.06e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 243.86  E-value: 6.06e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  120 LTIKAIGHQWYWSYEYSDYGsdTIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLHSFAVPSLSVKM 199
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFG--DLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 164420795  200 DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAV 241
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 52-249 5.09e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 227.59  E-value: 5.09e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  52 IMFILTIIITAVLWLIVRALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAFPSLKLLYLMDEV-IDPALTIKAIGHQWY 130
Cdd:MTH00080  29 LLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVTGHQWY 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 131 WSYEYSDYGSdtIEFDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLHSFAVPSLSVKMDAVPGRLNQTS 210
Cdd:MTH00080 109 WSYEFSDIPG--LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLC 186

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 164420795 211 FFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHW 249
Cdd:MTH00080 187 YSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW 225
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
30-252 1.06e-67

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 208.91  E-value: 1.06e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  30 WQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIV------RALTTKHYHKYLYEGTLIEIIWTLIPAAILVFIAF 103
Cdd:COG1622   17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLyfairyRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 104 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGSDTiefdsymiptsdlnngdlrllevDNRIIVPIQTQVRVLVTA 183
Cdd:COG1622   97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-----------------------VNELVLPVGRPVRFLLTS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164420795 184 ADVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVAN 252
Cdd:COG1622  154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 37-251 1.15e-49

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: 161.78  E-value: 1.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795   37 AASPV*EEVIFLH*QI---MFILTIIITAVLWLIV---RALTTKHYHKYLYEGTLIEIIWTLIPAAILV-FIAFPSLKLL 109
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVlavSTLISLLVAALLAYVVwkfRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  110 YLMDEVIDPALTIKAIGHQWYWSYEYSDYGsdtiefdsymiptsdlnngdlrlLEVDNRIIVPIQTQVRVLVTAADVLHS 189
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPESG-----------------------FTTVNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420795  190 FAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWVA 251
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 82-241 3.54e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 160.51  E-value: 3.54e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  82 EGTLIEIIWTLIPAAILVFIAFpsLKLLYLM-DEVIDPALTIKAIGHQWYWSYEYSDYGsdtiEFDSYMiptSDLNNGdl 160
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVLCF--LNLNFITsDLDCFSSETIKVIGHQWYWSYEYSFGG----SYDSFM---TDDIFG-- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 161 rlleVDNRIIVPIQTQVRVLVTAADVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEA 240
Cdd:MTH00047 114 ----VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEV 189


                 .
gi 164420795 241 V 241
Cdd:MTH00047 190 V 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 145-246 9.79e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 148.04  E-value: 9.79e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 145 FDSYMIPTSDLNNGDLRLLEVDNRIIVPIQTQVRVLVTAADVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCS 224
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|..
gi 164420795 225 EICGANHSFMPIVIEAVSLDKY 246
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), ...
 119-234 1.17e-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: 110.02  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 119 ALTIKAIGHQWYWSYEYSDYGSDTIEfdsymipTSdlnngdlrllevdNRIIVPIQTQVRVLVTAADVLHSFAVPSLSVK 198
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPGRGIV-------TA-------------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGK 60

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 164420795 199 MDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 234
Cdd:cd04213   61 MDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 120-239 8.20e-29

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 104.69  E-value: 8.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 120 LTIKAIGHQWYWSYEYSDygsdtiefdsymiptsdlnngdlrlLEVDNRIIVPIQTQVRVLVTAADVLHSFAVPSLSVKM 199
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKV 55

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 164420795 200 DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIE 239
Cdd:cd13842   56 DAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 27-108 2.02e-27

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: 100.87  E-value: 2.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795   27 PEPWQLGFQDAASPV*EEVIFLH*QIMFILTIIITAVLWLIVRALTTKHY------HKYLYEGTLIEIIWTLIPAAILVF 100
Cdd:pfam02790   2 PTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILIL 81


                  ....*...
gi 164420795  101 IAFPSLKL 108
Cdd:pfam02790  82 IALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 119-234 1.39e-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: 96.94  E-value: 1.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 119 ALTIKAIGHQWYWSYEYSDYGSDTIEFDsymiptsDLNNGDLRLlevdnriivPIQTQVRVLVTAADVLHSFAVPSLSVK 198
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPGGDGKLGTDD-------DVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVK 64

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 164420795 199 MDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 234
Cdd:cd13919   65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 119-234 2.75e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 95.77  E-value: 2.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 119 ALTIKAIGHQWYWSYEYSdygsdtiefdsymiptsdlnNGDlrllEVDNRIIVPIQTQVRVLVTAADVLHSFAVPSLSVK 198
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYP--------------------NGK----REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIK 56

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 164420795 199 MDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 234
Cdd:cd13915   57 QDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-250 1.46e-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: 1.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795  96 AILV--FIAFPSLKLLYLMD---EVIDPALTIKAIGHQWYWSYEYSDYGSDTiefdsymiptsdlnngdlrllevdNRII 170
Cdd:cd13918    4 AIIVisLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTG------------------------NTLR 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 171 VPIQTQVRVLVTAADVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWV 250
Cdd:cd13918   60 VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 121-250 2.15e-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: 85.92  E-value: 2.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 121 TIKAIGHQWYWSYEYSDYGSDTiefdsymiptsdlnngdlrllevDNRIIVPIQTQVRVLVTAADVLHSFAVPSLSVKMD 200
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEANVTT-----------------------SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 164420795 201 AVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIHWV 250
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 ...
 167-234 2.05e-12

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: 61.82  E-value: 2.05e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164420795 167 NRIIVPIQTQVRVLVTAADVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 234
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 120-241 6.98e-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: 49.08  E-value: 6.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 120 LTIKAIGHQWYWSYEYSDYGSDTIefdsymiptsdlnngdlrllevdNRIIVPIQTQVRVLVTAADVLHSFAVPSLSVKM 199
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQGIATV-----------------------NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQI 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 164420795 200 DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAV 241
Cdd:cd04212   58 YAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 121-234 1.31e-05

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 42.75  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 121 TIKAIGHQWYWSyeysdygsdtiefdsymIPTSDLNNGDlrllevdnriivPIQTQVrvlvTAADVLHSFAVPS----LS 196
Cdd:cd13916    2 VVAVTGHQWYWE-----------------LSRTEIPAGK------------PVEFRV----TSADVNHGFGIYDpdmrLL 48

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 164420795 197 VKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 234
Cdd:cd13916   49 AQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 177-234 1.37e-04

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 39.91  E-value: 1.37e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420795 177 VRVLVT----AADVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 234
Cdd:cd04223   26 VTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 156-239 2.21e-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: 39.91  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420795 156 NNGDLRLLEVDNRIIVPIQTQVRV-LVTAADVLHSFAVPSLSVKMDA---------------VPGRLNQTSFFIKRPGVF 219
Cdd:cd00920   12 FTYNGVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVY 91

                         90       100
                 ....*....|....*....|
gi 164420795 220 YGQCSEICGaNHSFMPIVIE 239
Cdd:cd00920   92 WFYCTIPGH-NHAGMVGTIN 110
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 176-234 7.72e-03

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 37.26  E-value: 7.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164420795 176 QVRVLVT----AADVLHSFAVPSLSVKMDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 234
Cdd:PRK02888 564 EVTVIVTnldkVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEM 626
 
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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