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Conserved domains on  [gi|343459435|ref|YP_004769877|]
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cytochrome c oxidase subunit II (mitochondrion) [Pieris rapae]

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
 1-226 6.89e-150

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 415.77  E-value: 6.89e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNElENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINNYS 226
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 6.89e-150

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 415.77  E-value: 6.89e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNElENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINNYS 226
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-221 1.81e-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: 259.42  E-value: 1.81e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  93 PLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKV 171
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDlEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 343459435 172 DANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINW 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 1.50e-79

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 233.84  E-value: 1.50e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   95 ITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKVDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 343459435  174 NPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESI 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-224 4.56e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 159.99  E-value: 4.56e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   6 NFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMmnLFF--------NKFINRFLLEGQMIELIWTILPAITLIFIA 77
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLL--LYFairyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  78 LPSLRLLYLLDELNNPLITLKSIGHQWYWSYEYSDfKNIEfdsyminemdnpnnfrlldVDNRIILPMNNQIRILVTATD 157
Cdd:COG1622   96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA-------------------TVNELVLPVGRPVRFLLTSAD 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343459435 158 VIHSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINN 224
Cdd:COG1622  156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-223 1.47e-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: 129.81  E-value: 1.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   13 ASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFnKFINR-------FLLEGQMIELIWTILPA-ITLIFIALPSLRLL 84
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   85 YLLDELNNPLITLKSIGHQWYWSYEYSDFkniefdsyminemdnpnnfrLLDVDNRIILPMNNQIRILVTATDVIHSWTI 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 343459435  165 PSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWIN 223
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 6.89e-150

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 415.77  E-value: 6.89e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNElENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINNYS 226
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 6.32e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 339.99  E-value: 6.32e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENElELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINNYS 226
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMS 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-225 7.29e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 334.76  E-value: 7.29e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDlSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINNY 225
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-224 3.49e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 333.03  E-value: 3.49e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMDNPN-NFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNgHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINN 224
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-226 1.93e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 326.27  E-value: 1.93e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDlSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINNYS 226
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 3.58e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 320.39  E-value: 3.58e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDlSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINN 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-226 4.55e-111

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 317.95  E-value: 4.55e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDlSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINNYS 226
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-221 5.58e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 297.40  E-value: 5.58e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDlTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINW 221
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-221 3.82e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 292.56  E-value: 3.82e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDlTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINW 221
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 9-226 2.08e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 288.57  E-value: 2.08e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   9 LQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPSLRLLYLLD 88
Cdd:MTH00023  18 FQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  89 ELNNPLITLKSIGHQWYWSYEYSDFK--NIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTIP 165
Cdd:MTH00023  98 EVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDlNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVP 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343459435 166 SLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINNYS 226
Cdd:MTH00023 178 SLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-221 4.12e-98

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 285.07  E-value: 4.12e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDlKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINW 221
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 1.25e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 281.28  E-value: 1.25e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDlTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINN 224
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 8-226 1.70e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 278.59  E-value: 1.70e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   8 NLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPSLRLLYLL 87
Cdd:MTH00051  10 GFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLM 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  88 DELNNPLITLKSIGHQWYWSYEYSDF--KNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTI 164
Cdd:MTH00051  90 DEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDlNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAV 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343459435 165 PSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINNYS 226
Cdd:MTH00051 170 PSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-221 1.81e-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: 259.42  E-value: 1.81e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  93 PLITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKV 171
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDlEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 343459435 172 DANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINW 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 1.50e-79

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 233.84  E-value: 1.50e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   95 ITLKSIGHQWYWSYEYSDFKNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKVDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 343459435  174 NPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESI 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 9-222 3.76e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 217.59  E-value: 3.76e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   9 LQNGASPLMEQMIFFHDHTLVILLMITILVMYLMM-----NLFFNKFINRflLEGQMIELIWTILPAITLIFIALPSLRL 83
Cdd:MTH00027  37 FQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrillgNNYYSYYWNK--LDGSLIEVIWTLIPAFILILIAFPSLRL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  84 LYLLDELN-NPLITLKSIGHQWYWSYEYSDF--KNIEFDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00027 115 LYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADlEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343459435 160 HSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWI 222
Cdd:MTH00027 195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-225 2.92e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 201.78  E-value: 2.92e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   6 NFNLQNGA-SPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFNKFINRFLLEGQMIELIWTILPAITLIFIALPSLRLL 84
Cdd:MTH00080   7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  85 YLLDELN-NPLITLKSIGHQWYWSYEYSDFKNIEFDSYMiNEMDNPN--NFRLLDVDNRIILPMNNQIRILVTATDVIHS 161
Cdd:MTH00080  87 YYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYM-KSLDQLRlgEPRLLEVDNRCVLPCDTNIRFCITSSDVIHS 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343459435 162 WTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINNY 225
Cdd:MTH00080 166 WALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-224 4.56e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 159.99  E-value: 4.56e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   6 NFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMmnLFF--------NKFINRFLLEGQMIELIWTILPAITLIFIA 77
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLL--LYFairyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  78 LPSLRLLYLLDELNNPLITLKSIGHQWYWSYEYSDfKNIEfdsyminemdnpnnfrlldVDNRIILPMNNQIRILVTATD 157
Cdd:COG1622   96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA-------------------TVNELVLPVGRPVRFLLTSAD 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343459435 158 VIHSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWINN 224
Cdd:COG1622  156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 34-213 6.95e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 148.18  E-value: 6.95e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  34 ITILVMYLMM-NLFFNKFINRFLLEGQMIELIWTILPAItLIFIALPSLRLLYLLDELNNPLITLKSIGHQWYWSYEYSD 112
Cdd:MTH00047  21 IPCWVYIMLCwQVVSGNGSVNFGSENQVLELLWTVVPTL-LVLVLCFLNLNFITSDLDCFSSETIKVIGHQWYWSYEYSF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435 113 fkNIEFDSYMINEMDNpnnfrlldVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKVDANPGRLNQTNFFINRPGIFF 192
Cdd:MTH00047 100 --GGSYDSFMTDDIFG--------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFV 169

                        170       180
                 ....*....|....*....|.
gi 343459435 193 GQCSEICGANHSFMPIVIESI 213
Cdd:MTH00047 170 GYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-214 5.87e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 144.96  E-value: 5.87e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435 118 FDSYMINEMD-NPNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCS 196
Cdd:PTZ00047  51 FQSNLVTDEDlKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*...
gi 343459435 197 EICGANHSFMPIVIESIS 214
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVS 148
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-223 1.47e-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: 129.81  E-value: 1.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   13 ASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFFnKFINR-------FLLEGQMIELIWTILPA-ITLIFIALPSLRLL 84
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435   85 YLLDELNNPLITLKSIGHQWYWSYEYSDFkniefdsyminemdnpnnfrLLDVDNRIILPMNNQIRILVTATDVIHSWTI 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 343459435  165 PSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWIN 223
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-211 2.78e-26

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: 97.37  E-value: 2.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  95 ITLKSIGHQWYWSYEYSDfkniefdsyminemdnpnnfrlLDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKVDAN 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAV 58

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 343459435 175 PGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIE 211
Cdd:cd13842   59 PGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-206 1.90e-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: 95.38  E-value: 1.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  95 ITLKSIGHQWYWSYEYSDFKNIEFDSymINEmdnpnnfrlldvdnrIILPMNNQIRILVTATDVIHSWTIPSLGVKVDAN 174
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPGRGIVT--ANE---------------LHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMI 64

                         90       100       110
                 ....*....|....*....|....*....|..
gi 343459435 175 PGRLNQTNFFINRPGIFFGQCSEICGANHSFM 206
Cdd:cd04213   65 PGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 2.81e-20

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: 81.61  E-value: 2.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435    1 MATWSNFNLQNGASPLMEQMIFFHDHTLVILLMITILVMYLMMNLFF------NKFINRFLLEGQMIELIWTILPAITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 343459435   75 FIA 77
Cdd:pfam02790  81 LIA 83
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 5.59e-20

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 81.53  E-value: 5.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  95 ITLKSIGHQWYWSYEY--SDFKNIEFDSYMINEMdnpnnfrlldvdnriILPMNNQIRILVTATDVIHSWTIPSLGVKVD 172
Cdd:cd13919    2 LVVEVTAQQWAWTFRYpgGDGKLGTDDDVTSPEL---------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                         90       100       110
                 ....*....|....*....|....*....|....
gi 343459435 173 ANPGRLNQTNFFINRPGIFFGQCSEICGANHSFM 206
Cdd:cd13919   67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 8.37e-20

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 80.75  E-value: 8.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  95 ITLKSIGHQWYWSYEYsdfkniefdsyminemdnPNNFRlldVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKVDAN 174
Cdd:cd13915    2 LEIQVTGRQWMWEFTY------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60

                         90       100       110
                 ....*....|....*....|....*....|..
gi 343459435 175 PGRLNQTNFFINRPGIFFGQCSEICGANHSFM 206
Cdd:cd13915   61 PGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-222 1.34e-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: 77.83  E-value: 1.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435 101 GHQWYWSYEYSDfKNIefdsyminemdnpnnfrllDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKVDANPGRLNQ 180
Cdd:cd13914    7 AYQWGWEFSYPE-ANV-------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNT 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 343459435 181 TNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINWI 222
Cdd:cd13914   67 IKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-221 5.54e-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: 77.11  E-value: 5.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  95 ITLKSIGHQWYWSYEYSdfkniefdsymiNEMDNPNNFRLldvdnriilPMNNQIRILVTATDVIHSWTIPSLGVKVDAN 174
Cdd:cd13918   33 LEVEVEGFQFGWQFEYP------------NGVTTGNTLRV---------PADTPIALRVTSTDVFHTFGIPELRVKADAI 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 343459435 175 PGRLNQTNFFINRPGIFFGQCSEICGANHSFMPIVIESISMNNFINW 221
Cdd:cd13918   92 PGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 139-206 1.28e-08

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 51.03  E-value: 1.28e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343459435 139 NRIILPMNNQIRILVTATDVIHSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFM 206
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 139-206 3.21e-06

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: 44.46  E-value: 3.21e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343459435 139 NRIILPMNNQIRILVTATDVIHSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFM 206
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 5.69e-05

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 40.83  E-value: 5.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343459435  95 ITLKSIGHQWYWsyeysdfkniefdsyminEMDnpnnfrlldvdnRIILPMNNQIRILVTATDVIHSWTIPS----LGVK 170
Cdd:cd13916    1 QVVAVTGHQWYW------------------ELS------------RTEIPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 343459435 171 VDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFM 206
Cdd:cd13916   51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 155-206 1.99e-03

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


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 36.44  E-value: 1.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 343459435 155 ATDVIHSWTIPSLGVKVDANPGRLNQTNFFINRPGIFFGQCSEICGANHSFM 206
Cdd:cd04223   36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
 
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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