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Conserved domains on  [gi|1776829131|gb|QGL05007|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Zygothrica aff. vittimaculosa 1 TBG-2019]

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
 1-201 2.72e-141

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 393.04  E-value: 2.72e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00154   20 LIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:MTH00154  180 NQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFI 220
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-201 2.72e-141

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 393.04  E-value: 2.72e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00154   20 LIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:MTH00154  180 NQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFI 220
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 74-201 6.38e-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: 264.43  E-value: 6.38e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  74 PSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKV 153
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1776829131 154 DGTPGRLNQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFL 128
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
77-195 6.20e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 236.54  E-value: 6.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  77 TLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGT 156
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1776829131 157 PGRLNQTNFFINRPGLFFGQCSEICGANHSFMPIVIESV 195
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
4-196 8.42e-46

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 150.75  E-value: 8.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   4 FHDHALLILVMITVLVgylMFMLFFNSYVNR---------FLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEP 74
Cdd:COG1622    35 LFWVSLIIMLVIFVLV---FGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPED 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  75 SVTLKSIGHQWYWSYEYSDFNNVefdsymiptnelsndgfrlldVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVD 154
Cdd:COG1622   112 PLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1776829131 155 GTPGRLNQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVP 196
Cdd:COG1622   171 AIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 8-196 3.57e-36

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 125.19  E-value: 3.57e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   8 ALLILVMITVLVGYLMFMLFFNSYVNRFL----LHGQLIEMIWTILPAIILL-FIALPSLRLLYLLDEINEPSVTLKSIG 82
Cdd:TIGR02866  18 AVSTLISLLVAALLAYVVWKFRRKGDEEKpsqiHGNRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  83 HQWYWSYEYSdfnnvefdsymiptnelsNDGFRlldVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQ 162
Cdd:TIGR02866  98 YQWWWDFEYP------------------ESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNA 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1776829131 163 TNFFINRPGLFFGQCSEICGANHSFMPIVIESVP 196
Cdd:TIGR02866 157 LWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVP 190
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-201 2.72e-141

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 393.04  E-value: 2.72e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00154   20 LIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:MTH00154  180 NQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFI 220
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-201 2.51e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 324.97  E-value: 2.51e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00140   20 LIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00140  100 IGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:MTH00140  180 NQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFV 220
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-200 1.08e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 320.71  E-value: 1.08e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGY-LMFMLFFNSYVNRfLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLK 79
Cdd:MTH00117   20 LLFFHDHALMVALLISSLVLYlLTLMLTTKLTHTN-TVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  80 SIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGR 159
Cdd:MTH00117   99 AIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1776829131 160 LNQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYF 200
Cdd:MTH00117  179 LNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHF 219
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-201 1.05e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 318.20  E-value: 1.05e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00139   20 LIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00139  100 VGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:MTH00139  180 NQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFL 220
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-201 1.65e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 309.99  E-value: 1.65e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00168   20 LILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00168  100 VGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:MTH00168  180 NQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFE 220
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-201 1.74e-108

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 310.25  E-value: 1.74e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00008   20 LISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00008  100 IGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:MTH00008  180 NQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFM 220
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-200 7.86e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 303.55  E-value: 7.86e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00038   20 LIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00038  100 IGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYF 200
Cdd:MTH00038  180 NQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTF 219
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-200 4.27e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 286.61  E-value: 4.27e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00129   20 LLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00129  100 MGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYF 200
Cdd:MTH00129  180 NQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHF 219
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-200 7.97e-98

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 283.15  E-value: 7.97e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00098   20 LLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00098  100 MGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYF 200
Cdd:MTH00098  180 NQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYF 219
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-200 1.14e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 282.93  E-value: 1.14e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00185   20 LIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00185  100 MGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYF 200
Cdd:MTH00185  180 NQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHF 219
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-201 1.14e-96

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 280.48  E-value: 1.14e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00023   29 IIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFN--NVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPG 158
Cdd:MTH00023  109 IGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPG 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1776829131 159 RLNQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:MTH00023  189 RLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYI 231
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-201 1.00e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 275.12  E-value: 1.00e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKS 80
Cdd:MTH00076   20 LLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00076  100 IGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:MTH00076  180 NQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFL 220
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 74-201 6.38e-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: 264.43  E-value: 6.38e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  74 PSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKV 153
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1776829131 154 DGTPGRLNQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFL 128
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 3-201 1.11e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 267.80  E-value: 1.11e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   3 FFHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKSIG 82
Cdd:MTH00051   24 FFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  83 HQWYWSYEYSDF--NNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:MTH00051  104 HQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRL 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:MTH00051  184 NQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYI 224
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
77-195 6.20e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 236.54  E-value: 6.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  77 TLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGT 156
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1776829131 157 PGRLNQTNFFINRPGLFFGQCSEICGANHSFMPIVIESV 195
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-201 2.60e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 209.50  E-value: 2.60e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMF-MLFFNSYVNRFL--LHGQLIEMIWTILPAIILLFIALPSLRLLYLLDE-INEPSV 76
Cdd:MTH00027   48 IIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEcGFSANI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  77 TLKSIGHQWYWSYEYSDF--NNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVD 154
Cdd:MTH00027  128 TIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMD 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1776829131 155 GTPGRLNQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:MTH00027  208 AVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYI 254
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 4-201 2.04e-64

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 198.31  E-value: 2.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   4 FHDHALLILVMITVLVGYLMFMLFFNSYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEIN-EPSVTLKSIG 82
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  83 HQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQ 162
Cdd:MTH00080  105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1776829131 163 TNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNYFI 201
Cdd:MTH00080  185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFK 223
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
4-196 8.42e-46

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 150.75  E-value: 8.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   4 FHDHALLILVMITVLVgylMFMLFFNSYVNR---------FLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEP 74
Cdd:COG1622    35 LFWVSLIIMLVIFVLV---FGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPED 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  75 SVTLKSIGHQWYWSYEYSDFNNVefdsymiptnelsndgfrlldVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVD 154
Cdd:COG1622   112 PLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1776829131 155 GTPGRLNQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVP 196
Cdd:COG1622   171 AIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 4-199 9.46e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 149.72  E-value: 9.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   4 FHDHALLILVMITVLVGYLMFMLFFNSYV-NRFLLHG---QLIEMIWTILPAIILLFIALPSLRLLYLlDEINEPSVTLK 79
Cdd:MTH00047    7 YYDIVCYILALCVFIPCWVYIMLCWQVVSgNGSVNFGsenQVLELLWTVVPTLLVLVLCFLNLNFITS-DLDCFSSETIK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  80 SIGHQWYWSYEYSDfnNVEFDSYMiptnelSNDGFrllDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGR 159
Cdd:MTH00047   86 VIGHQWYWSYEYSF--GGSYDSFM------TDDIF---GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGR 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1776829131 160 LNQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVPVNY 199
Cdd:MTH00047  155 INHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 99-195 7.61e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 136.10  E-value: 7.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  99 FDSYMIPTNELSNDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFFGQCS 178
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*..
gi 1776829131 179 EICGANHSFMPIVIESV 195
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAV 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 8-196 3.57e-36

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 125.19  E-value: 3.57e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131   8 ALLILVMITVLVGYLMFMLFFNSYVNRFL----LHGQLIEMIWTILPAIILL-FIALPSLRLLYLLDEINEPSVTLKSIG 82
Cdd:TIGR02866  18 AVSTLISLLVAALLAYVVWKFRRKGDEEKpsqiHGNRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  83 HQWYWSYEYSdfnnvefdsymiptnelsNDGFRlldVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQ 162
Cdd:TIGR02866  98 YQWWWDFEYP------------------ESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNA 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1776829131 163 TNFFINRPGLFFGQCSEICGANHSFMPIVIESVP 196
Cdd:TIGR02866 157 LWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVP 190
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 76-193 2.04e-25

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: 94.29  E-value: 2.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  76 VTLKSIGHQWYWSYEYSDFNnvefdsymiptnelsndgfrlldVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDG 155
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1776829131 156 TPGRLNQTNFFINRPGLFFGQCSEICGANHSFMPIVIE 193
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 75-188 8.36e-24

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 90.37  E-value: 8.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  75 SVTLKSIGHQWYWSYEYSDFNNVEFDSymipTNELsndgfrlldvdnrvILPMNSQIRILVTAADVIHSWTIPALGVKVD 154
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGIVT----ANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1776829131 155 GTPGRLNQTNFFINRPGLFFGQCSEICGANHSFM 188
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 76-188 5.98e-20

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 80.76  E-value: 5.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  76 VTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELsndgfrlldvdnrvILPMNSQIRILVTAADVIHSWTIPALGVKVDG 155
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1776829131 156 TPGRLNQTNFFINRPGLFFGQCSEICGANHSFM 188
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 81-188 3.43e-18

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 75.74  E-value: 3.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  81 IGHQWYWSYEYSDfnnvefdsymiptnelsndGFRlldVDNRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 160
Cdd:cd13915     7 TGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRY 64

                          90       100
                  ....*....|....*....|....*...
gi 1776829131 161 NQTNFFINRPGLFFGQCSEICGANHSFM 188
Cdd:cd13915    65 TYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 69-188 1.01e-17

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: 75.95  E-value: 1.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  69 DEINEPSVTLKSIGHQWYWSYEYSdfNNVEFDSYMIptnelsndgfrlldvdnrviLPMNSQIRILVTAADVIHSWTIPA 148
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYP--NGVTTGNTLR--------------------VPADTPIALRVTSTDVFHTFGIPE 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1776829131 149 LGVKVDGTPGRLNQTNFFINRPGLFFGQCSEICGANHSFM 188
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 76-196 3.33e-17

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: 73.60  E-value: 3.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  76 VTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNelsndgfrlldvdnrvilpmnSQIRILVTAADVIHSWTIPALGVKVDG 155
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEANVTTSEQLVIPAD---------------------RPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1776829131 156 TPGRLNQTNFFINRPGLFFGQCSEICGANHSFMPIVIESVP 196
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVS 100
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-58 2.78e-14

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: 65.43  E-value: 2.78e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776829131   1 LTFFHDHALLILVMITVLVGYLMFMLFF------NSYVNRFLLHGQLIEMIWTILPAIILLFIA 58
Cdd:pfam02790  20 LLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 121-188 1.74e-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: 1.74e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776829131 121 NRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFFGQCSEICGANHSFM 188
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 121-188 1.06e-05

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: 42.54  E-value: 1.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776829131 121 NRVILPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFFGQCSEICGANHSFM 188
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 82-188 7.70e-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: 37.36  E-value: 7.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776829131  82 GHQWYWsyeysdfnnvefdsymiptnELSndgfrlldvdnRVILPMNSQIRILVTAADVIHSWTI--PALGV--KVDGTP 157
Cdd:cd13916     7 GHQWYW--------------------ELS-----------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMP 55

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1776829131 158 GRLNQTNFFINRPGLFFGQCSEICGANHSFM 188
Cdd:cd13916    56 GYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
 
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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