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Conserved domains on  [gi|1172045830|gb|ARD25124|]
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cytochrome oxidase subunit II, partial [Heliconius timareta linaresi]

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 1.31e-142

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 397.28  E-value: 1.31e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNElENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172045830 160 HSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINNYS 226
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 1.31e-142

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 397.28  E-value: 1.31e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNElENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172045830 160 HSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINNYS 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 6.49e-92

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: 265.59  E-value: 6.49e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  93 PLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKI 171
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDlEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1172045830 172 DANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINW 221
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 1.80e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 231.14  E-value: 1.80e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  95 ITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKIDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1172045830 174 NPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESI 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
61-224 3.57e-46

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 152.68  E-value: 3.57e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  61 IELIWTILPAITLIFIALPSLRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIefdsymiqsnenlnnfrlldVDNR 140
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA--------------------TVNE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830 141 IILPMNNQIRILVTATDVIHSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFIN 220
Cdd:COG1622   139 LVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDA 218


                  ....
gi 1172045830 221 WINN 224
Cdd:COG1622   219 WLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-223 5.23e-38

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: 130.96  E-value: 5.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  13 ASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFF------NNYINRFLLEGQMIELIWTILPA-ITLIFIALPSLRLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkgDEEKPSQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  86 LLDELNNPLITLKSIGHQWYWSYEYSDFnniefdsymiqsnenlnnfrLLDVDNRIILPMNNQIRILVTATDVIHSWTIP 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPES--------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVP 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1172045830 166 SLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWIN 223
Cdd:TIGR02866 142 ELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 1.31e-142

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 397.28  E-value: 1.31e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNElENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172045830 160 HSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINNYS 226
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 5.86e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 327.67  E-value: 5.86e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENElELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172045830 160 HSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINNYS 226
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMS 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-225 1.01e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 327.06  E-value: 1.01e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDlSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172045830 160 HSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINNY 225
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-224 6.81e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 319.55  E-value: 6.81e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAY-----LMMNLFFNNyinrfLLEGQMIELIWTILPAITLIF 75
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYlltlmLTTKLTHTN-----TVDAQEVELIWTILPAIVLIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  76 IALPSLRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNENLN-NFRLLDVDNRIILPMNNQIRILVT 154
Cdd:MTH00117   76 LALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNgHFRLLEVDHRMVIPMESPIRILIT 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830 155 ATDVIHSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINN 224
Cdd:MTH00117  156 AEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-226 4.65e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 310.09  E-value: 4.65e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDlSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172045830 160 HSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINNYS 226
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 3.45e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 307.68  E-value: 3.45e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSnENLNN--FRLLDVDNRIILPMNNQIRILVTATDV 158
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPT-QDLSPgqFRLLEVDNRLVLPMDSKIRVLVTSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172045830 159 IHSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINN 224
Cdd:MTH00168  160 LHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-226 4.02e-107

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 307.94  E-value: 4.02e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNENL-NNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSpGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172045830 160 HSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINNYS 226
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-221 1.79e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 285.84  E-value: 1.79e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNENL-NNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTpGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172045830 160 HSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINW 221
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-221 2.47e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 282.93  E-value: 2.47e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDlTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172045830 160 HSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINW 221
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 2.83e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 277.82  E-value: 2.83e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDlTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172045830 160 HSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINN 224
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-226 1.39e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 276.28  E-value: 1.39e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   7 LNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPSLRLLYL 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  87 LDELNNPLITLKSIGHQWYWSYEYSDF--NNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWT 163
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDlNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172045830 164 IPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINNYS 226
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-221 1.76e-94

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 275.83  E-value: 1.76e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  81 LRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDlKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172045830 160 HSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINW 221
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-224 8.51e-93

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 272.01  E-value: 8.51e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   7 LNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPSLRLLYL 86
Cdd:MTH00023   16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  87 LDELNNPLITLKSIGHQWYWSYEYSDFN--NIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWT 163
Cdd:MTH00023   96 MDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDlNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172045830 164 IPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINN 224
Cdd:MTH00023  176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-221 6.49e-92

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: 265.59  E-value: 6.49e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  93 PLITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKI 171
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDlEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1172045830 172 DANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINW 221
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 1.80e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 231.14  E-value: 1.80e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  95 ITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKIDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1172045830 174 NPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESI 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-222 5.48e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 214.89  E-value: 5.48e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   7 LNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFF-NNYINRFL--LEGQMIELIWTILPAITLIFIALPSLRL 83
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLgNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  84 LYLLDELN-NPLITLKSIGHQWYWSYEYSDF--NNIEFDSYMIQSNE-NLNNFRLLDVDNRIILPMNNQIRILVTATDVI 159
Cdd:MTH00027  115 LYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADlEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172045830 160 HSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWI 222
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-225 1.36e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 197.54  E-value: 1.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   6 NLNYQNSA-SPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYINRFLLEGQMIELIWTILPAITLIFIALPSLRLL 84
Cdd:MTH00080    7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  85 YLLDELN-NPLITLKSIGHQWYWSYEYSDFNNIEFDSYM-IQSNENLNNFRLLDVDNRIILPMNNQIRILVTATDVIHSW 162
Cdd:MTH00080   87 YYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMkSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSW 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172045830 163 TIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWINNY 225
Cdd:MTH00080  167 ALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
61-224 3.57e-46

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 152.68  E-value: 3.57e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  61 IELIWTILPAITLIFIALPSLRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFNNIefdsymiqsnenlnnfrlldVDNR 140
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA--------------------TVNE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830 141 IILPMNNQIRILVTATDVIHSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFIN 220
Cdd:COG1622   139 LVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDA 218


                  ....
gi 1172045830 221 WINN 224
Cdd:COG1622   219 WLAE 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 40-213 1.87e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 144.71  E-value: 1.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  40 YLMM--NLFFNNYINRFLLEGQMIELIWTILPAItLIFIALPSLRLLYLLDELNNPLITLKSIGHQWYWSYEYSDfnNIE 117
Cdd:MTH00047   26 YIMLcwQVVSGNGSVNFGSENQVLELLWTVVPTL-LVLVLCFLNLNFITSDLDCFSSETIKVIGHQWYWSYEYSF--GGS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830 118 FDSYMIQSNENlnnfrlldVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSE 197
Cdd:MTH00047  103 YDSFMTDDIFG--------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSE 174

                         170
                  ....*....|....*.
gi 1172045830 198 ICGANHSFMPIVIESI 213
Cdd:MTH00047  175 LCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 121-213 9.30e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 136.87  E-value: 9.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830 121 YMIQSN----ENL--NNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQ 194
Cdd:PTZ00047   49 YSFQSNlvtdEDLkpGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128

                          90
                  ....*....|....*....
gi 1172045830 195 CSEICGANHSFMPIVIESI 213
Cdd:PTZ00047  129 CSEMCGTLHGFMPIVVEAV 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-223 5.23e-38

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: 130.96  E-value: 5.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  13 ASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFF------NNYINRFLLEGQMIELIWTILPA-ITLIFIALPSLRLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkgDEEKPSQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  86 LLDELNNPLITLKSIGHQWYWSYEYSDFnniefdsymiqsnenlnnfrLLDVDNRIILPMNNQIRILVTATDVIHSWTIP 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPES--------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVP 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1172045830 166 SLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWIN 223
Cdd:TIGR02866 142 ELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-211 4.58e-28

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 101.99  E-value: 4.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  95 ITLKSIGHQWYWSYEYSDFNniefdsymiqsnenlnnfrlldVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKIDAN 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVR----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAV 58

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1172045830 175 PGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIE 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 4.78e-27

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: 99.62  E-value: 4.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  95 ITLKSIGHQWYWSYEYSDFNNIEFDSymiqSNEnlnnfrlldvdnrIILPMNNQIRILVTATDVIHSWTIPSLGVKIDAN 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT----ANE-------------LHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMI 64

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1172045830 175 PGRLNQTSFFINRPGIYYGQCSEICGANHSFM 206
Cdd:cd04213    65 PGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 6.77e-22

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 86.54  E-value: 6.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  95 ITLKSIGHQWYWSYEYSDFNNIEFDSYMIQSNEnlnnfrlldvdnrIILPMNNQIRILVTATDVIHSWTIPSLGVKIDAN 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPE-------------LHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAV 68

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1172045830 175 PGRLNQTSFFINRPGIYYGQCSEICGANHSFM 206
Cdd:cd13919    69 PGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-221 2.84e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 83.27  E-value: 2.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  95 ITLKSIGHQWYWSYEYSdfNNIEFDSYMIqsnenlnnfrlldvdnriiLPMNNQIRILVTATDVIHSWTIPSLGVKIDAN 174
Cdd:cd13918    33 LEVEVEGFQFGWQFEYP--NGVTTGNTLR-------------------VPADTPIALRVTSTDVFHTFGIPELRVKADAI 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1172045830 175 PGRLNQTSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINW 221
Cdd:cd13918    92 PGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-222 9.56e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 80.92  E-value: 9.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830 101 GHQWYWSYEYSDFNNIEFdsymiqsnenlnnfrlldvdNRIILPMNNQIRILVTATDVIHSWTIPSLGVKIDANPGRLNQ 180
Cdd:cd13914     7 AYQWGWEFSYPEANVTTS--------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNT 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1172045830 181 TSFFINRPGIYYGQCSEICGANHSFMPIVIESIPLKNFINWI 222
Cdd:cd13914    67 IKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 1.35e-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: 77.67  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  95 ITLKSIGHQWYWSYEYsdfnniefdsymiqsnenLNNFRlldVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKIDAN 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTY------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1172045830 175 PGRLNQTSFFINRPGIYYGQCSEICGANHSFM 206
Cdd:cd13915    61 PGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 3.32e-15

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: 68.51  E-value: 3.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830   1 MATWSNLNYQNSASPLMEQIIFFHDHTLIILIMITILVAYLMMNLFFNNYI------NRFLLEGQMIELIWTILPAITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 1172045830  75 FIA 77
Cdd:pfam02790  81 LIA 83
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 139-206 3.18e-10

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: 55.27  E-value: 3.18e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172045830 139 NRIILPMNNQIRILVTATDVIHSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFM 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 4.08e-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: 44.08  E-value: 4.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172045830 139 NRIILPMNNQIRILVTATDVIHSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFM 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 5.92e-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: 5.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830  95 ITLKSIGHQWYWSYeysdfnniefdsymiqsnenlnnfrlldvdNRIILPMNNQIRILVTATDVIHSWTIPS----LGVK 170
Cdd:cd13916     1 QVVAVTGHQWYWEL------------------------------SRTEIPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1172045830 171 IDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFM 206
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 155-206 3.52e-04

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


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 38.37  E-value: 3.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1172045830 155 ATDVIHSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFM 206
Cdd:cd04223    36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 157-206 1.97e-03

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 38.80  E-value: 1.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1172045830 157 DVIHSWTIPSLGVKIDANPGRLNQTSFFINRPGIYYGQCSEICGANHSFM 206
Cdd:PRK02888  577 DLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEM 626
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 131-211 2.84e-03

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 36.44  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172045830 131 NFRLLDVDNRIILPMNNQIRILVTAT-DVIHSWTIPSLGVKIDAN---------------PGRLNQTSFFINRPGIYYGQ 194
Cdd:cd00920    15 NGVLLFGPPVLVVPVGDTVRVQFVNKlGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYWFY 94

                          90
                  ....*....|....*..
gi 1172045830 195 CSEICGaNHSFMPIVIE 211
Cdd:cd00920    95 CTIPGH-NHAGMVGTIN 110
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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