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Conserved domains on  [gi|2206973347|ref|YP_010292391|]
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cytochrome c oxidase subunit II (mitochondrion) [Nudaurelia wahlbergi]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 1.53e-149

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 415.00  E-value: 1.53e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWINNYY 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 1.53e-149

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 415.00  E-value: 1.53e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWINNYY 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 9.00e-89

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: 257.50  E-value: 9.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  93 PLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVIHSWTIPSLGVKV 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2206973347 173 DANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.33e-76

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 226.52  E-value: 1.33e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  95 ITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2206973347 175 NPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
61-225 1.57e-47

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 156.14  E-value: 1.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  61 IELIWTILPTITLIFIALPSLRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIefdsymlpmnnlmlnnfrlldVNN 140
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347 141 RIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFI 220
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                  ....*
gi 2206973347 221 NWINN 225
Cdd:COG1622   218 AWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 61-224 4.17e-37

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: 128.65  E-value: 4.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  61 IELIWTILP-TITLIFIALPSLRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFnniefdsymlpmnnlmlnnfrLLDVN 139
Cdd:TIGR02866  56 LEYVWTVIPlIIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347 140 NRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNF 219
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194


                  ....*
gi 2206973347 220 INWIN 224
Cdd:TIGR02866 195 DAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 1.53e-149

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 415.00  E-value: 1.53e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWINNYY 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 2.00e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 341.31  E-value: 2.00e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWINNY 226
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-225 7.10e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 339.99  E-value: 7.10e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWINN 225
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-225 9.36e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 337.27  E-value: 9.36e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWINN 225
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-226 4.73e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 327.81  E-value: 4.73e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWINNY 226
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNF 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-226 6.92e-114

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 324.89  E-value: 6.92e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWINNY 226
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSF 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 7.53e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 322.32  E-value: 7.53e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWINN 225
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-222 4.09e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 305.48  E-value: 4.09e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINW 222
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-222 9.04e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 299.49  E-value: 9.04e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINW 222
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-225 4.10e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 295.15  E-value: 4.10e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWINN 225
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-222 1.74e-100

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 290.85  E-value: 1.74e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  81 LRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVI 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2206973347 161 HSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINW 222
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 9-225 1.60e-98

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 286.65  E-value: 1.60e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   9 LQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPSLRLLYLMD 88
Cdd:MTH00023   18 FQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  89 ELNNPLITLKSIGHQWYWSYEYSDFN--NIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVIHSWTIP 166
Cdd:MTH00023   98 EVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVP 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2206973347 167 SLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWINN 225
Cdd:MTH00023  178 SLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 8-223 3.50e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 280.13  E-value: 3.50e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   8 NLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPSLRLLYLM 87
Cdd:MTH00051   10 GFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLM 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  88 DELNNPLITLKSIGHQWYWSYEYSDF--NNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVIHSWTI 165
Cdd:MTH00051   90 DEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAV 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2206973347 166 PSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWI 223
Cdd:MTH00051  170 PSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 9.00e-89

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: 257.50  E-value: 9.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  93 PLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVIHSWTIPSLGVKV 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2206973347 173 DANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.33e-76

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 226.52  E-value: 1.33e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  95 ITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2206973347 175 NPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 9-223 4.39e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 227.99  E-value: 4.39e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   9 LQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFF-NNFINRFL--LEEQMIELIWTILPTITLIFIALPSLRLLY 85
Cdd:MTH00027   37 FQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLgNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRLLY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  86 LMDELN-NPLITLKSIGHQWYWSYEYSDF--NNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVIHS 162
Cdd:MTH00027  117 IMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHS 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2206973347 163 WTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWI 223
Cdd:MTH00027  197 WTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-226 7.07e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 213.33  E-value: 7.07e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   6 NFNLQNSA-SPLMEQIIFFHDHTLIILIIITILVSYLMLNLFFNNFINRFLLEEQMIELIWTILPTITLIFIALPSLRLL 84
Cdd:MTH00080    7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  85 YLMDELN-NPLITLKSIGHQWYWSYEYSDFNNIEFDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVIHSW 163
Cdd:MTH00080   87 YYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSW 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2206973347 164 TIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWINNY 226
Cdd:MTH00080  167 ALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 40-214 1.54e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 155.11  E-value: 1.54e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  40 YLML--NLFFNNFINRFLLEEQMIELIWTILPTitLIFIALPSLRLLYLMDELN-NPLITLKSIGHQWYWSYEYSdfNNI 116
Cdd:MTH00047   26 YIMLcwQVVSGNGSVNFGSENQVLELLWTVVPT--LLVLVLCFLNLNFITSDLDcFSSETIKVIGHQWYWSYEYS--FGG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347 117 EFDSYMLPMNNLmlnnfrlldVNNRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQC 196
Cdd:MTH00047  102 SYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYC 172

                         170
                  ....*....|....*...
gi 2206973347 197 SEICGTNHSFMPIVIESI 214
Cdd:MTH00047  173 SELCGVGHSYMPIVIEVV 190
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
61-225 1.57e-47

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 156.14  E-value: 1.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  61 IELIWTILPTITLIFIALPSLRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFNNIefdsymlpmnnlmlnnfrlldVNN 140
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347 141 RIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFI 220
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                  ....*
gi 2206973347 221 NWINN 225
Cdd:COG1622   218 AWLAE 222
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-227 2.66e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 128.01  E-value: 2.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347 118 FDSYMLPMNNLMLNNFRLLDVNNRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100       110
                  ....*....|....*....|....*....|
gi 2206973347 198 EICGTNHSFMPIVIESIPMKNFINWINNYY 227
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAYAAHAKKYY 160
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 61-224 4.17e-37

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: 128.65  E-value: 4.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  61 IELIWTILP-TITLIFIALPSLRLLYLMDELNNPLITLKSIGHQWYWSYEYSDFnniefdsymlpmnnlmlnnfrLLDVN 139
Cdd:TIGR02866  56 LEYVWTVIPlIIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347 140 NRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNF 219
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194


                  ....*
gi 2206973347 220 INWIN 224
Cdd:TIGR02866 195 DAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 9.72e-24

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: 90.82  E-value: 9.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  95 ITLKSIGHQWYWSYEYSDFNniefdsymlpmnnlmlnnfrlldVNNRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2206973347 175 NPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 1.15e-23

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: 90.76  E-value: 1.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  95 ITLKSIGHQWYWSYEYSDFNNIEFDSymlpmnnlmlnnfrlldvNNRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDA 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2206973347 175 NPGRLNQTNFLINQLGIFFGQCSEICGTNHSFM 207
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 8.54e-19

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: 78.05  E-value: 8.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  95 ITLKSIGHQWYWSYEYsdfnniefdsymlpmnnlmLNNFRlldVNNRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDA 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2206973347 175 NPGRLNQTNFLINQLGIFFGQCSEICGTNHSFM 207
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-222 1.31e-18

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 78.65  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  83 LLYLMD---ELNNPLITLKSIGHQWYWSYEYSdfNNIEFDSYMlpmnnlmlnnfrlldvnnriILPMNNQIRIMVTASDV 159
Cdd:cd13918    18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYP--NGVTTGNTL--------------------RVPADTPIALRVTSTDV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2206973347 160 IHSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINW 222
Cdd:cd13918    76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-223 2.92e-18

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 77.06  E-value: 2.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347 101 GHQWYWSYEYSDFNNiefdsymlpmnnlmlnnfrllDVNNRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDANPGRLN 180
Cdd:cd13914     7 AYQWGWEFSYPEANV---------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2206973347 181 QTNFLINQLGIFFGQCSEICGTNHSFMPIVIESIPMKNFINWI 223
Cdd:cd13914    66 TIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 4.03e-18

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 76.53  E-value: 4.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347  95 ITLKSIGHQWYWSYEYSDfNNIEFdsymlpmnnlmlnNFRLLDVNNRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDA 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPG-GDGKL-------------GTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2206973347 175 NPGRLNQTNFLINQLGIFFGQCSEICGTNHSFM 207
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 2.21e-17

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: 73.91  E-value: 2.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2206973347   1 MATWSNFNLQNSASPLMEQIIFFHDHTLIILIIITILVSYLMLNLFF------NNFINRFLLEEQMIELIWTILPTITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 2206973347  75 FIALPSLRL 83
Cdd:pfam02790  81 LIALPSFKL 89
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 8.19e-07

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: 46.02  E-value: 8.19e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2206973347 140 NRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFM 207
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-207 1.14e-04

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 39.84  E-value: 1.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2206973347 140 NRIILPMNNQIRIMVTASDVIHSWTIPSLGVKVDANPGRLNQTNFLINQLGIFFGQCSEICGTNHSFM 207
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
 
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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