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Conserved domains on  [gi|1494814688|gb|AYN25043|]
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cytochrome oxidase subunit 2, partial (mitochondrion) [Phaner electromontis]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475897)

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 MTH00098
cytochrome c oxidase subunit II; Validated
 1-215 1.07e-147

cytochrome c oxidase subunit II; Validated


:

Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 409.88  E-value: 1.07e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   1 VQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRIL 80
Cdd:MTH00098    5 FQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  81 YLMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWT 160
Cdd:MTH00098   85 YMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWA 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1494814688 161 VPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00098  165 VPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYF 219
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-215 1.07e-147

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 409.88  E-value: 1.07e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   1 VQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRIL 80
Cdd:MTH00098    5 FQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  81 YLMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWT 160
Cdd:MTH00098   85 YMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWA 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1494814688 161 VPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00098  165 VPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYF 219
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 89-215 1.07e-90

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: 262.12  E-value: 1.07e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  89 PSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKT 168
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1494814688 169 DAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDF 127
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
91-210 6.04e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 239.62  E-value: 6.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  91 LTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKTDA 170
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1494814688 171 IPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELV 210
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-215 1.51e-41

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 140.35  E-value: 1.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELmyfhDHTLMIVFLISSLV-LYIISLML-------------TTKLTHTSTMdaqeMETVWTILPAI 67
Cdd:COG1622    18 QLSLPDPAGPIAEEI----DDLFWVSLIIMLVIfVLVFGLLLyfairyrrrkgdaDPAQFHHNTK----LEIVWTVIPII 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  68 ILILIALPSLRILYLMDEITTPSLTLKTMGHQWYWSYEYTDYEDLnfdsymipslelnpgelrlleVDNRIVLPTEMPIR 147
Cdd:COG1622    90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVR 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1494814688 148 VLISSEDVLHSWTVPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEF 216
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 8-215 5.79e-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: 127.88  E-value: 5.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   8 AASPIMEELMYFHDHTLMIVFLISSLVLYIISLM-----------LTTKLTHTStmdaqEMETVWTIL-PAIILILIALP 75
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVvwkfrrkgdeeKPSQIHGNR-----RLEYVWTVIpLIIVVGLFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  76 SLRILYLMDEITTPSLTLKTMGHQWYWSYEYTDYedlnfdsymipslelnpgelrLLEVDNRIVLPTEMPIRVLISSEDV 155
Cdd:TIGR02866  76 AKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688 156 LHSWTVPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-215 1.07e-147

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 409.88  E-value: 1.07e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   1 VQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRIL 80
Cdd:MTH00098    5 FQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  81 YLMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWT 160
Cdd:MTH00098   85 YMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWA 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1494814688 161 VPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00098  165 VPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYF 219
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 2-215 2.48e-139

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 388.50  E-value: 2.48e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILY 81
Cdd:MTH00117    6 QLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  82 LMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTV 161
Cdd:MTH00117   86 LMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAV 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1494814688 162 PSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00117  166 PSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHF 219
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 2-215 3.80e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 355.24  E-value: 3.80e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILY 81
Cdd:MTH00076    6 QLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  82 LMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTV 161
Cdd:MTH00076   86 LMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAV 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1494814688 162 PSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00076  166 PSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNF 219
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-215 4.31e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 352.86  E-value: 4.31e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILY 81
Cdd:MTH00129    6 QLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  82 LMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTV 161
Cdd:MTH00129   86 LMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAV 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1494814688 162 PSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00129  166 PALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHF 219
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 2-215 4.70e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 337.19  E-value: 4.70e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILY 81
Cdd:MTH00154    6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  82 LMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTV 161
Cdd:MTH00154   86 LLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTV 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1494814688 162 PSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00154  166 PSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNF 219
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-215 4.28e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 335.32  E-value: 4.28e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILY 81
Cdd:MTH00185    6 QLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  82 LMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTV 161
Cdd:MTH00185   86 LMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTV 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1494814688 162 PSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00185  166 PALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHF 219
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 2-215 7.53e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 321.54  E-value: 7.53e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILY 81
Cdd:MTH00168    6 QLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  82 LMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTV 161
Cdd:MTH00168   86 LMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTL 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1494814688 162 PSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00168  166 PSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETF 219
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 2-215 3.97e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 314.95  E-value: 3.97e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILY 81
Cdd:MTH00140    6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  82 LMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTV 161
Cdd:MTH00140   86 LLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTV 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1494814688 162 PSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00140  166 PSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDF 219
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 2-215 2.49e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 312.79  E-value: 2.49e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILY 81
Cdd:MTH00038    6 QLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  82 LMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTV 161
Cdd:MTH00038   86 LMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAV 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1494814688 162 PSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00038  166 PSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTF 219
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 2-215 1.74e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 300.48  E-value: 1.74e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILY 81
Cdd:MTH00139    6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  82 LMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTV 161
Cdd:MTH00139   86 LMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTV 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1494814688 162 PSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00139  166 PSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFF 219
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-215 4.03e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 287.14  E-value: 4.03e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILY 81
Cdd:MTH00008    6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  82 LMDEITTPSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTV 161
Cdd:MTH00008   86 LMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTV 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1494814688 162 PSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00008  166 PSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSF 219
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-215 1.97e-94

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 275.48  E-value: 1.97e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILY 81
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  82 LMDEITTPSLTLKTMGHQWYWSYEYTDYED--LNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSW 159
Cdd:MTH00023   95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1494814688 160 TVPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00023  175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKY 230
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-215 1.11e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 273.58  E-value: 1.11e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILY 81
Cdd:MTH00051    8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  82 LMDEITTPSLTLKTMGHQWYWSYEYTDY--EDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSW 159
Cdd:MTH00051   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1494814688 160 TVPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00051  168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKY 223
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 89-215 1.07e-90

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: 262.12  E-value: 1.07e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  89 PSLTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKT 168
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1494814688 169 DAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDF 127
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
91-210 6.04e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 239.62  E-value: 6.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  91 LTLKTMGHQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKTDA 170
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1494814688 171 IPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELV 210
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-215 1.08e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 226.45  E-value: 1.08e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTKLTHT---STMDAQEMETVWTILPAIILILIALPSLR 78
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPSLR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  79 ILYLMDE-ITTPSLTLKTMGHQWYWSYEYTDY--EDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDV 155
Cdd:MTH00027  114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688 156 LHSWTVPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00027  194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKY 253
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 19-215 3.69e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 196.00  E-value: 3.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  19 FHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEMETVWTILPAIILILIALPSLRILYLMDEITTPS-LTLKTMG 97
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNLDSnLTVKVTG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  98 HQWYWSYEYTDYEDLNFDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKTDAIPGRLNQ 177
Cdd:MTH00080  105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1494814688 178 TTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:MTH00080  185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNF 222
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-215 1.51e-41

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 140.35  E-value: 1.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   2 QLGFQDAASPIMEELmyfhDHTLMIVFLISSLV-LYIISLML-------------TTKLTHTSTMdaqeMETVWTILPAI 67
Cdd:COG1622    18 QLSLPDPAGPIAEEI----DDLFWVSLIIMLVIfVLVFGLLLyfairyrrrkgdaDPAQFHHNTK----LEIVWTVIPII 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  68 ILILIALPSLRILYLMDEITTPSLTLKTMGHQWYWSYEYTDYEDLnfdsymipslelnpgelrlleVDNRIVLPTEMPIR 147
Cdd:COG1622    90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVR 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1494814688 148 VLISSEDVLHSWTVPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEF 216
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 114-210 1.09e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 136.10  E-value: 1.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688 114 FDSYMIPSLELNPGELRLLEVDNRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCS 193
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*..
gi 1494814688 194 EICGANHSFMPIVLELV 210
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAV 147
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 88-210 6.98e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 130.07  E-value: 6.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  88 TPSLTLKTMGHQWYWSYEYTDyeDLNFDSYMIPSLELnpgelrlleVDNRIVLPTEMPIRVLISSEDVLHSWTVPSLGVK 167
Cdd:MTH00047   79 FSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1494814688 168 TDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELV 210
Cdd:MTH00047  148 MDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 8-215 5.79e-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: 127.88  E-value: 5.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688   8 AASPIMEELMYFHDHTLMIVFLISSLVLYIISLM-----------LTTKLTHTStmdaqEMETVWTIL-PAIILILIALP 75
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVvwkfrrkgdeeKPSQIHGNR-----RLEYVWTVIpLIIVVGLFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  76 SLRILYLMDEITTPSLTLKTMGHQWYWSYEYTDYedlnfdsymipslelnpgelrLLEVDNRIVLPTEMPIRVLISSEDV 155
Cdd:TIGR02866  76 AKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688 156 LHSWTVPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 90-203 2.27e-32

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: 113.10  E-value: 2.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  90 SLTLKTMGHQWYWSYEYTDYEDLNFdsymipslelnpgelrllEVDNRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKTD 169
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGI------------------VTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1494814688 170 AIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFM 203
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 91-208 6.74e-32

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: 111.62  E-value: 6.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  91 LTLKTMGHQWYWSYEYTDyedlnfdsymipslelnpgelrlLEVDNRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKTDA 170
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1494814688 171 IPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLE 208
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 91-203 1.42e-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: 87.70  E-value: 1.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  91 LTLKTMGHQWYWSYEYTDYedlnfDSYMIPSLELNPGELrllevdnriVLPTEMPIRVLISSEDVLHSWTVPSLGVKTDA 170
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPEL---------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1494814688 171 IPGRLNQTTLMTSRPGIYYGQCSEICGANHSFM 203
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 79-215 1.95e-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: 1.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  79 ILYLMDEITTP---SLTLKTMGHQWYWSYEYTdyedlnfdsymipslelNPGELRllevdNRIVLPTEMPIRVLISSEDV 155
Cdd:cd13918    18 LLYVEDPPDEAdedALEVEVEGFQFGWQFEYP-----------------NGVTTG-----NTLRVPADTPIALRVTSTDV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688 156 LHSWTVPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKQF 215
Cdd:cd13918    76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEF 135
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 90-203 1.39e-19

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 79.98  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  90 SLTLKTMGHQWYWSYEYtdyedlnfdsymipslelnPGELRlleVDNRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKTD 169
Cdd:cd13915     1 ALEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1494814688 170 AIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFM 203
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 97-211 8.04e-19

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 78.22  E-value: 8.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  97 GHQWYWSYEYTDYEdlnfdsymipslelnpgelrlLEVDNRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKTDAIPGRLN 176
Cdd:cd13914     7 AYQWGWEFSYPEAN---------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1494814688 177 qtTLMTS--RPGIYYGQCSEICGANHSFMPIVLELVP 211
Cdd:cd13914    66 --TIKTEatEEGEYQLYCAEYCGAGHSQMLSTVTVVS 100
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 2-62 1.29e-17

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 74.29  E-value: 1.29e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1494814688   2 QLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTT------KLTHTSTMDAQEMETVWT 62
Cdd:pfam02790   6 GLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWT 72
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 136-203 2.06e-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: 50.26  E-value: 2.06e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1494814688 136 NRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFM 203
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 125-208 4.18e-07

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: 46.84  E-value: 4.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688 125 NPGELRLLEVDNRIVLPTEMPIRVLISSE-DVLHSWTVPSLGVKTDAI---------------PGRLNQTTLMTSRPGIY 188
Cdd:cd00920    12 FTYNGVLLFGPPVLVVPVGDTVRVQFVNKlGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVY 91

                          90       100
                  ....*....|....*....|
gi 1494814688 189 YGQCSEICGaNHSFMPIVLE 208
Cdd:cd00920    92 WFYCTIPGH-NHAGMVGTIN 110
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 136-203 2.28e-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: 2.28e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1494814688 136 NRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFM 203
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 97-203 3.00e-04

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: 38.52  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494814688  97 GHQWYWsyeytdyedlnfdsymipslELNPGElrllevdnrivLPTEMPIRVLISSEDVLHSWTVPS----LGVKTDAIP 172
Cdd:cd13916     7 GHQWYW--------------------ELSRTE-----------IPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQTQAMP 55

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1494814688 173 GRLNQTTLMTSRPGIYYGQCSEICGANHSFM 203
Cdd:cd13916    56 GYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 136-203 1.98e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 38.24  E-value: 1.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1494814688 136 NRIVLPTEMPIRVLISSEDVLHSWTVPSLGVKTDAIPGRLNQTTLMTSRPGIYYGQCSEICGANHSFM 203
Cdd:PRK10525  151 NEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGM 218
 
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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