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Conserved domains on  [gi|66774424|gb|AAY56004|]
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cytochrome c oxidase subunit II (mitochondrion) [Metopeurum fuscoviride]

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
 1-223 1.24e-124

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 351.82  E-value: 1.24e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    1 MNWLKLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSL 80
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   81 HLLYLMDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIH 158
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66774424  159 SWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKNF 223
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-223 1.24e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 351.82  E-value: 1.24e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    1 MNWLKLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSL 80
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   81 HLLYLMDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIH 158
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66774424  159 SWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKNF 223
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-219 8.08e-76

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: 224.76  E-value: 8.08e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  92 PIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKI 169
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIpeDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 66774424 170 DAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYW 219
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-211 9.18e-68

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 203.80  E-value: 9.18e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    94 MTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKIDA 171
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIptEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 66774424   172 IPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESI 211
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
57-222 9.81e-42

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 141.12  E-value: 9.81e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  57 NQMIELIWTITPPIILIFIAMPSLHLLYLMDEIKYPIMTIKIFGHQWFWSYEYSDfsniefesyminnlnkENfrlIEVD 136
Cdd:COG1622  76 NTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD----------------QG---IATV 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424 137 NKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKF 216
Cdd:COG1622 137 NELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEF 216


                ....*.
gi 66774424 217 IYWIKN 222
Cdd:COG1622 217 DAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 53-220 3.21e-36

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: 126.34  E-value: 3.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    53 KISQNQMIELIWTITPPIILI-FIAMPSLHLLYLMDEIKYPIMTIKIFGHQWFWSYEYSDFsniefesyminnlnkenfr 131
Cdd:TIGR02866  49 QIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES------------------- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   132 LIEVDNKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESI 211
Cdd:TIGR02866 110 GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVV 189


                  ....*....
gi 66774424   212 NLSKFIYWI 220
Cdd:TIGR02866 190 PKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-223 1.24e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 351.82  E-value: 1.24e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    1 MNWLKLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSL 80
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   81 HLLYLMDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIH 158
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66774424  159 SWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKNF 223
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 6-223 5.01e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 299.52  E-value: 5.01e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    6 LSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSLHLLYL 85
Cdd:MTH00117   7 LGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   86 MDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWTIP 163
Cdd:MTH00117  87 MDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIptQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  164 SLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKNF 223
Cdd:MTH00117 167 SLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 3-223 2.70e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 297.78  E-value: 2.70e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    3 WLKLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSLHL 82
Cdd:MTH00139   4 WGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   83 LYLMDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSW 160
Cdd:MTH00139  84 LYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIptEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66774424  161 TIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKNF 223
Cdd:MTH00139 164 TVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 3-222 3.20e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 297.62  E-value: 3.20e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    3 WLKLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSLHL 82
Cdd:MTH00140   4 WGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   83 LYLMDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSW 160
Cdd:MTH00140  84 LYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVpeNELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66774424  161 TIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKN 222
Cdd:MTH00140 164 TVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-222 1.56e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 288.42  E-value: 1.56e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    1 MNWLKLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSL 80
Cdd:MTH00168   2 ATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   81 HLLYLMDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMIN--NLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIH 158
Cdd:MTH00168  82 RLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPtqDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66774424  159 SWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKN 222
Cdd:MTH00168 162 SWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-223 2.45e-97

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 282.90  E-value: 2.45e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    2 NWLKLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSLH 81
Cdd:MTH00008   3 HWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   82 LLYLMDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHS 159
Cdd:MTH00008  83 LLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLptSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHS 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66774424  160 WTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKNF 223
Cdd:MTH00008 163 WTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSF 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 2-223 1.06e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 281.20  E-value: 1.06e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    2 NWLKLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSLH 81
Cdd:MTH00038   3 TWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   82 LLYLMDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHS 159
Cdd:MTH00038  83 LLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVptSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHS 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66774424  160 WTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKNF 223
Cdd:MTH00038 163 WAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNF 226
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 4-219 4.28e-92

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 269.67  E-value: 4.28e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    4 LKLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSLHLL 83
Cdd:MTH00098   5 FQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   84 YLMDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWT 161
Cdd:MTH00098  85 YMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIptSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWA 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 66774424  162 IPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYW 219
Cdd:MTH00098 165 VPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-222 1.64e-90

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 265.85  E-value: 1.64e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    6 LSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSLHLLYL 85
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   86 MDEIKYPIMTIKIFGHQWFWSYEYSDF--SNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWT 161
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVptSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66774424  162 IPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKN 222
Cdd:MTH00023 176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 5-219 3.08e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 260.03  E-value: 3.08e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    5 KLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSLHLLY 84
Cdd:MTH00129   6 QLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   85 LMDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWTI 162
Cdd:MTH00129  86 LMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIptQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAV 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 66774424  163 PSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYW 219
Cdd:MTH00129 166 PALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 5-219 1.25e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 258.28  E-value: 1.25e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    5 KLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSLHLLY 84
Cdd:MTH00185   6 QLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   85 LMDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWTI 162
Cdd:MTH00185  86 LMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTptQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTV 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 66774424  163 PSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYW 219
Cdd:MTH00185 166 PALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 5-222 1.95e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 257.79  E-value: 1.95e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    5 KLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSLHLLY 84
Cdd:MTH00076   6 QLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   85 LMDEIKYPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWTI 162
Cdd:MTH00076  86 LMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIptQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  163 PSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKN 222
Cdd:MTH00076 166 PSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 5-222 2.21e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 252.78  E-value: 2.21e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    5 KLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPSLHLLY 84
Cdd:MTH00051   8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   85 LMDEIKYPIMTIKIFGHQWFWSYEYSDF--SNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSW 160
Cdd:MTH00051  88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIptSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66774424  161 TIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKN 222
Cdd:MTH00051 168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVAT 229
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-219 8.08e-76

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: 224.76  E-value: 8.08e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  92 PIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKI 169
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIpeDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 66774424 170 DAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYW 219
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-211 9.18e-68

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 203.80  E-value: 9.18e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    94 MTIKIFGHQWFWSYEYSDFSNIEFESYMI--NNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKIDA 171
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIptEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 66774424   172 IPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESI 211
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 5-220 1.22e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 208.73  E-value: 1.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    5 KLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFI-MKNKFINIKISQ--NQMIELIWTITPPIILIFIAMPSLH 81
Cdd:MTH00027  34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRIlLGNNYYSYYWNKldGSLIEVIWTLIPAFILILIAFPSLR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   82 LLYLMDEIKYPI-MTIKIFGHQWFWSYEYSDF--SNIEFESYMINNLNKE--NFRLIEVDNKTIMPFKFNIRLLISSEDV 156
Cdd:MTH00027 114 LLYIMDECGFSAnITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEfgDLRLLEVDNRLILPVDTNVRVLITAADV 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66774424  157 IHSWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWI 220
Cdd:MTH00027 194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 8-223 9.46e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 200.24  E-value: 9.46e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    8 FQNSNSPLMEQLIF--------FHDHTIFIIIMIMSTITYMMFFIMKNKFINIKISQNQMIELIWTITPPIILIFIAMPS 79
Cdd:MTH00080   3 FQGYNLNFSNSLFSsymdwfhnFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   80 LHLLYLMDEIKYPI-MTIKIFGHQWFWSYEYSDFSNIEFESYM--INNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDV 156
Cdd:MTH00080  83 LSLLYYYGLMNLDSnLTVKVTGHQWYWSYEFSDIPGLEFDSYMksLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDV 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66774424  157 IHSWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWIKNF 223
Cdd:MTH00080 163 IHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 39-211 1.49e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 144.71  E-value: 1.49e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   39 YMMFFIMKNKFINIKI-SQNQMIELIWTITPPIILIFIAMPSLHLLYlMDEIKYPIMTIKIFGHQWFWSYEYSDfsNIEF 117
Cdd:MTH00047  27 IMLCWQVVSGNGSVNFgSENQVLELLWTVVPTLLVLVLCFLNLNFIT-SDLDCFSSETIKVIGHQWYWSYEYSF--GGSY 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  118 ESYMINNLNKenfrlieVDNKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEIC 197
Cdd:MTH00047 104 DSFMTDDIFG-------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELC 176

                        170
                 ....*....|....
gi 66774424  198 GINHSFMPIQIESI 211
Cdd:MTH00047 177 GVGHSYMPIVIEVV 190
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
57-222 9.81e-42

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 141.12  E-value: 9.81e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  57 NQMIELIWTITPPIILIFIAMPSLHLLYLMDEIKYPIMTIKIFGHQWFWSYEYSDfsniefesyminnlnkENfrlIEVD 136
Cdd:COG1622  76 NTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD----------------QG---IATV 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424 137 NKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKF 216
Cdd:COG1622 137 NELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEF 216


                ....*.
gi 66774424 217 IYWIKN 222
Cdd:COG1622 217 DAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 53-220 3.21e-36

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: 126.34  E-value: 3.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424    53 KISQNQMIELIWTITPPIILI-FIAMPSLHLLYLMDEIKYPIMTIKIFGHQWFWSYEYSDFsniefesyminnlnkenfr 131
Cdd:TIGR02866  49 QIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES------------------- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424   132 LIEVDNKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESI 211
Cdd:TIGR02866 110 GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVV 189


                  ....*....
gi 66774424   212 NLSKFIYWI 220
Cdd:TIGR02866 190 PKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-216 8.91e-35

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 121.47  E-value: 8.91e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  117 FESYMINN--LNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCS 194
Cdd:PTZ00047  51 FQSNLVTDedLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|..
gi 66774424  195 EICGINHSFMPIQIESINLSKF 216
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), ...
 94-204 1.51e-25

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: 95.76  E-value: 1.51e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  94 MTIKIFGHQWFWSYEYSDfsniefesyminnlnkENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKIDAIP 173
Cdd:cd04213   2 LTIEVTGHQWWWEFRYPD----------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIP 65

                        90       100       110
                ....*....|....*....|....*....|.
gi 66774424 174 GRMNQINLFMNRPGMFFGQCSEICGINHSFM 204
Cdd:cd04213  66 GRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 94-209 6.30e-23

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 88.51  E-value: 6.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  94 MTIKIFGHQWFWSYEYsdfsniefesyminnLNKENFRLIEVdnKTIMPfkfnIRLLISSEDVIHSWTIPSLAIKIDAIP 173
Cdd:cd13842   1 LTVYVTGVQWSWTFIY---------------PNVRTPNEIVV--PAGTP----VRFRVTSPDVIHGFYIPNLGVKVDAVP 59

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 66774424 174 GRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIE 209
Cdd:cd13842  60 GYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-204 1.02e-21

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 85.77  E-value: 1.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  94 MTIKIFGHQWFWSYEYsdfsniefesymINNLNKENFRLIEVDNKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKIDAIP 173
Cdd:cd13919   2 LVVEVTAQQWAWTFRY------------PGGDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVP 69

                        90       100       110
                ....*....|....*....|....*....|.
gi 66774424 174 GRMNQINLFMNRPGMFFGQCSEICGINHSFM 204
Cdd:cd13919  70 GRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-204 9.53e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 75.36  E-value: 9.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  94 MTIKIFGHQWFWSYEYSDfsniefesyminnlNKENfrlievDNKTIMPFKFNIRLLISSEDVIHSWTIPSLAIKIDAIP 173
Cdd:cd13915   2 LEIQVTGRQWMWEFTYPN--------------GKRE------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVP 61

                        90       100       110
                ....*....|....*....|....*....|.
gi 66774424 174 GRMNQINLFMNRPGMFFGQCSEICGINHSFM 204
Cdd:cd13915  62 GRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 66-219 3.01e-16

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: 72.49  E-value: 3.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  66 ITPPIILIFIAMPSLHLLYLMD---EIKYPIMTIKIFGHQWFWSYEYSdfsniefesymiNNLNKENFRLIEVDNKtimp 142
Cdd:cd13918   2 LSAIIVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYP------------NGVTTGNTLRVPADTP---- 65

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66774424 143 fkfnIRLLISSEDVIHSWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYW 219
Cdd:cd13918  66 ----IALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-220 7.95e-16

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: 70.51  E-value: 7.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424  95 TIKIFGHQWFWSYEYSDFSNIEFESyminnlnkenfrlievdnkTIMPFKFNIRLLISSEDVIHSWTIPSLAIKIDAIPG 174
Cdd:cd13914   2 EIEVEAYQWGWEFSYPEANVTTSEQ-------------------LVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPG 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 66774424 175 RMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIESINLSKFIYWI 220
Cdd:cd13914  63 QYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 2-82 1.49e-12

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: 61.19  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774424     2 NWLKLSFQNSNSPLMEQLIFFHDHTIFIIIMIMSTITYMMFFIM------KNKFINIKISQNQMIELIWTITPPIILIFI 75
Cdd:pfam02790   3 TPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILILI 82


                  ....*..
gi 66774424    76 AMPSLHL 82
Cdd:pfam02790  83 ALPSFKL 89
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 151-204 2.95e-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: 47.18  E-value: 2.95e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 66774424 151 ISSEDVIHSWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFM 204
Cdd:cd13913  39 VTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 148-204 2.09e-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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 41.59  E-value: 2.09e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 66774424 148 RLLISSEDVIHSWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFM 204
Cdd:cd13917  25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 146-204 3.69e-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: 38.68  E-value: 3.69e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66774424 146 NIRLLISSEDVIHSWTIPSLAIKIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFM 204
Cdd:cd04212  34 PVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 151-209 1.95e-03

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: 36.21  E-value: 1.95e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66774424 151 ISSEDVIHSWTI--PSLAI--KIDAIPGRMNQINLFMNRPGMFFGQCSEICGINHSFMPIQIE 209
Cdd:cd13916  29 VTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFT 91
 
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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