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Conserved domains on  [gi|2283858885|gb|UUT08524|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Drosophila alei]

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
 1-209 3.69e-147

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.45  E-value: 3.69e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00154   18 EQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPG 160
Cdd:MTH00154   98 KTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2283858885 161 RLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISNN 209
Cdd:MTH00154  178 RLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-209 3.69e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.45  E-value: 3.69e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00154   18 EQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPG 160
Cdd:MTH00154   98 KTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2283858885 161 RLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISNN 209
Cdd:MTH00154  178 RLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 76-205 1.03e-93

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: 269.83  E-value: 1.03e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  76 PSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKV 155
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2283858885 156 DGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 205
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
79-197 3.91e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 235.00  E-value: 3.91e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  79 TLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGT 158
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2283858885 159 PGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESV 197
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-208 2.95e-47

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 155.37  E-value: 2.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVgylMFMLFFNSYINR---------FLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLD 71
Cdd:COG1622    30 EEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  72 EINEPSVTLKSIGHQWYWSYEYSDFNNVefdsymiptnelsndgfrlldVDNRIVLPMNSQIRILVTAADVIHSWTIPAL 151
Cdd:COG1622   107 DAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPAL 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2283858885 152 GVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 208
Cdd:COG1622   166 GGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-207 7.99e-39

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: 132.50  E-value: 7.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFF------NSYINRFLLHGQLIEMIWTILPAIILL-FIALPSLRLLYLLDEI 73
Cdd:TIGR02866   7 QQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkgDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  74 NEPSVTLKSIGHQWYWSYEYSdfnnvefdsymiptnelsNDGFRlldVDNRIVLPMNSQIRILVTAADVIHSWTIPALGV 153
Cdd:TIGR02866  87 PKDALKVKVTGYQWWWDFEYP------------------ESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGG 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2283858885 154 KVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWIS 207
Cdd:TIGR02866 146 KIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-209 3.69e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.45  E-value: 3.69e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00154   18 EQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPG 160
Cdd:MTH00154   98 KTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2283858885 161 RLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISNN 209
Cdd:MTH00154  178 RLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-208 1.03e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 334.21  E-value: 1.03e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00140   18 EELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPG 160
Cdd:MTH00140   98 KAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPG 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2283858885 161 RLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 208
Cdd:MTH00140  178 RLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-208 2.85e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 332.84  E-value: 2.85e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00139   18 EQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPG 160
Cdd:MTH00139   98 KAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPG 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2283858885 161 RLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 208
Cdd:MTH00139  178 RLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-208 5.27e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 332.26  E-value: 5.27e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGY-LMFMLFFNSYINRfLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVT 79
Cdd:MTH00117   18 EELLFFHDHALMVALLISSLVLYlLTLMLTTKLTHTN-TVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  80 LKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTP 159
Cdd:MTH00117   97 IKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVP 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2283858885 160 GRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 208
Cdd:MTH00117  177 GRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-209 4.63e-115

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 327.58  E-value: 4.63e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   2 QLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLK 81
Cdd:MTH00008   19 QLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  82 SIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGR 161
Cdd:MTH00008   99 TIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2283858885 162 LNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISNN 209
Cdd:MTH00008  179 LNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSF 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-208 5.37e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 321.93  E-value: 5.37e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00168   18 EELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPG 160
Cdd:MTH00168   98 KAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPG 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2283858885 161 RLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 208
Cdd:MTH00168  178 RLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-212 2.70e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 315.49  E-value: 2.70e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00038   18 EELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPG 160
Cdd:MTH00038   98 KAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPG 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2283858885 161 RLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISNNVNS 212
Cdd:MTH00038  178 RLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-207 4.39e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 297.40  E-value: 4.39e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00129   18 EELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPG 160
Cdd:MTH00129   98 KAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPG 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2283858885 161 RLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWIS 207
Cdd:MTH00129  178 RLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-207 2.61e-101

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 292.78  E-value: 2.61e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00098   18 EELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPG 160
Cdd:MTH00098   98 KTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPG 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2283858885 161 RLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWIS 207
Cdd:MTH00098  178 RLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSA 224
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-207 5.73e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 291.79  E-value: 5.73e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00185   18 EELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPG 160
Cdd:MTH00185   98 KAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPG 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2283858885 161 RLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWIS 207
Cdd:MTH00185  178 RLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-212 2.27e-100

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 290.88  E-value: 2.27e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00023   27 EEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDFN--NVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGT 158
Cdd:MTH00023  107 KAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAV 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2283858885 159 PGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISNNVNS 212
Cdd:MTH00023  187 PGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSND 240
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-211 4.96e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 287.06  E-value: 4.96e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00076   18 EELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPG 160
Cdd:MTH00076   98 KAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPG 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2283858885 161 RLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISNNVN 211
Cdd:MTH00076  178 RLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-212 9.47e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 278.97  E-value: 9.47e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTL 80
Cdd:MTH00051   20 EEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  81 KSIGHQWYWSYEYSDF--NNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGT 158
Cdd:MTH00051  100 KAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAV 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2283858885 159 PGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISNNVNS 212
Cdd:MTH00051  180 PGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 76-205 1.03e-93

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: 269.83  E-value: 1.03e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  76 PSVTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKV 155
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2283858885 156 DGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 205
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
79-197 3.91e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 235.00  E-value: 3.91e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  79 TLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGT 158
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2283858885 159 PGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESV 197
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-206 3.92e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 217.20  E-value: 3.92e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMF-MLFFNSYINRFL--LHGQLIEMIWTILPAIILLFIALPSLRLLYLLDE-INEP 76
Cdd:MTH00027   46 EEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEcGFSA 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  77 SVTLKSIGHQWYWSYEYSDF--NNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVK 154
Cdd:MTH00027  126 NITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVK 205

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2283858885 155 VDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWI 206
Cdd:MTH00027  206 MDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-211 1.78e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 204.47  E-value: 1.78e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   6 FHDHALLILVMITVLVGYLMFMLFFNSYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEIN-EPSVTLKSIG 84
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  85 HQWYWSYEYSDFNNVEFDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQ 164
Cdd:MTH00080  105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2283858885 165 TNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISNNVN 211
Cdd:MTH00080  185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-208 2.95e-47

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 155.37  E-value: 2.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVgylMFMLFFNSYINR---------FLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLD 71
Cdd:COG1622    30 EEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  72 EINEPSVTLKSIGHQWYWSYEYSDFNNVefdsymiptnelsndgfrlldVDNRIVLPMNSQIRILVTAADVIHSWTIPAL 151
Cdd:COG1622   107 DAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPAL 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2283858885 152 GVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWISN 208
Cdd:COG1622   166 GGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 6-201 4.46e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 151.26  E-value: 4.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   6 FHDHALLILVMITVLVGYLMFMLFFNSYI-NRFLLHG---QLIEMIWTILPAIILLFIALPSLRLLYLlDEINEPSVTLK 81
Cdd:MTH00047    7 YYDIVCYILALCVFIPCWVYIMLCWQVVSgNGSVNFGsenQVLELLWTVVPTLLVLVLCFLNLNFITS-DLDCFSSETIK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  82 SIGHQWYWSYEYSDfnNVEFDSYMiptnelSNDGFrllDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGR 161
Cdd:MTH00047   86 VIGHQWYWSYEYSF--GGSYDSFM------TDDIF---GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGR 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2283858885 162 LNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNY 201
Cdd:MTH00047  155 INHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 101-197 5.51e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 136.87  E-value: 5.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885 101 FDSYMIPTNELSNDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCS 180
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*..
gi 2283858885 181 EICGANHSFMPIVIESV 197
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAV 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-207 7.99e-39

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: 132.50  E-value: 7.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFF------NSYINRFLLHGQLIEMIWTILPAIILL-FIALPSLRLLYLLDEI 73
Cdd:TIGR02866   7 QQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkgDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  74 NEPSVTLKSIGHQWYWSYEYSdfnnvefdsymiptnelsNDGFRlldVDNRIVLPMNSQIRILVTAADVIHSWTIPALGV 153
Cdd:TIGR02866  87 PKDALKVKVTGYQWWWDFEYP------------------ESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGG 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2283858885 154 KVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWIS 207
Cdd:TIGR02866 146 KIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 78-195 2.12e-26

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 97.37  E-value: 2.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  78 VTLKSIGHQWYWSYEYSDFNnvefdsymiptnelsndgfrlldVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 157
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2283858885 158 TPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIE 195
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), ...
 77-190 2.69e-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: 92.30  E-value: 2.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  77 SVTLKSIGHQWYWSYEYSDFNNVEFdsymiptnELSNDgfrlldvdnrIVLPMNSQIRILVTAADVIHSWTIPALGVKVD 156
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGI--------VTANE----------LHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2283858885 157 GTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFM 190
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 78-190 1.86e-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: 82.30  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  78 VTLKSIGHQWYWSYEYSDFNNVEFDSYMIPTNELsndgfrlldvdnriVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 157
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2283858885 158 TPGRLNQTNFFMNRPGLFYGQCSEICGANHSFM 190
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 71-205 7.25e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 79.42  E-value: 7.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  71 DEINEPSVTLKSIGHQWYWSYEYSdfNNVEFDSYMiptnelsndgfrlldvdnriVLPMNSQIRILVTAADVIHSWTIPA 150
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYP--NGVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2283858885 151 LGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 205
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 78-206 1.37e-18

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 77.45  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  78 VTLKSIGHQWYWSYEYSDFNNVEFdsymiptnelsndgfrlldvdNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 157
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2283858885 158 TPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKWI 206
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-190 4.83e-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: 4.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  83 IGHQWYWSYEYSDfnnvefdsymiptnelsndGFRlldVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 162
Cdd:cd13915     7 TGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRY 64

                          90       100
                  ....*....|....*....|....*...
gi 2283858885 163 NQTNFFMNRPGLFYGQCSEICGANHSFM 190
Cdd:cd13915    65 TYLWFEATKPGEYDLFCTEYCGTGHSGM 92
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-60 3.45e-15

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


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 68.13  E-value: 3.45e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2283858885   1 EQLIFFHDHALLILVMITVLVGYLMFMLFF------NSYINRFLLHGQLIEMIWTILPAIILLFIA 60
Cdd:pfam02790  18 EGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 123-190 3.57e-11

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: 57.58  E-value: 3.57e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2283858885 123 NRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFM 190
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 123-190 6.52e-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: 43.31  E-value: 6.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2283858885 123 NRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFM 190
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 84-190 3.30e-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: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  84 GHQWYWsyeysdfnnvefdsymiptnELSndgfrlldvdnRIVLPMNSQIRILVTAADVIHSWTI--PALGV--KVDGTP 159
Cdd:cd13916     7 GHQWYW--------------------ELS-----------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMP 55

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2283858885 160 GRLNQTNFFMNRPGLFYGQCSEICGANHSFM 190
Cdd:cd13916    56 GYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 98-195 5.43e-04

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: 38.37  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2283858885  98 NVEFDSYMIPTNELSNDGFrlldVDNRIVLPMNSQIR-ILVTAADVIHSWTIPALGVKVDG---------------TPGR 161
Cdd:cd00920     2 TVTASDWGWSFTYNGVLLF----GPPVLVVPVGDTVRvQFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGE 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2283858885 162 LNQTNFFMNRPGLFYGQCSEICGaNHSFMPIVIE 195
Cdd:cd00920    78 SAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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