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Conserved domains on  [gi|501416511|gb|AGL93590|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Scaptomyza setosiscutellum]

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
 1-224 7.45e-156

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 430.79  E-value: 7.45e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   1 STWSNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSL 80
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIH 160
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416511 161 SWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-224 7.45e-156

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 430.79  E-value: 7.45e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   1 STWSNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSL 80
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIH 160
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416511 161 SWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 1.40e-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: 1.40e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  92 PSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWTVPALGVKV 171
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 501416511 172 DGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKW 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 3.46e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 235.38  E-value: 3.46e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   95 TLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWTVPALGVKVDGT 174
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 501416511  175 PGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESV 213
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
5-222 3.87e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 160.38  E-value: 3.87e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   5 NLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLM--FMLFF----NNYINRFLLHGQLIEMIWTILPAIILLFIALP 78
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLlyFAIRYrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  79 SLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIefdsymiptnelstdgfrlldVDNRIILPMNSQIRILVTAADV 158
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416511 159 IHSWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWI 222
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 1.55e-40

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: 137.51  E-value: 1.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   12 ASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFF------NNYINRFLLHGQLIEMIWTILPAIILL-FIALPSLRLLY 84
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkgDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   85 LLDEINEPSVTLKSIGHQWYWSYEYSDFnniefdsymiptnelstdGFRlldVDNRIILPMNSQIRILVTAADVIHSWTV 164
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 501416511  165 PALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWI 222
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-224 7.45e-156

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 430.79  E-value: 7.45e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   1 STWSNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSL 80
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIH 160
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416511 161 SWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-224 5.91e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 355.18  E-value: 5.91e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   1 STWSNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSL 80
Cdd:MTH00139   2 AYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIH 160
Cdd:MTH00139  82 RLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416511 161 SWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00139 162 SWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-224 1.41e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 351.93  E-value: 1.41e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   1 STWSNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSL 80
Cdd:MTH00140   2 SYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIH 160
Cdd:MTH00140  82 RLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416511 161 SWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00140 162 SWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 4-224 7.91e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 344.98  E-value: 7.91e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   4 SNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLL 83
Cdd:MTH00117   5 SQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  84 YLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWT 163
Cdd:MTH00117  85 YLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWA 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501416511 164 VPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00117 165 VPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-224 2.77e-121

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 343.38  E-value: 2.77e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   1 STWSNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSL 80
Cdd:MTH00008   2 PHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIH 160
Cdd:MTH00008  82 RLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416511 161 SWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00008 162 SWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 1.76e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 338.88  E-value: 1.76e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   1 STWSNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSL 80
Cdd:MTH00168   2 ATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIH 160
Cdd:MTH00168  82 RLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416511 161 SWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00168 162 SWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-224 6.92e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 334.75  E-value: 6.92e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   1 STWSNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSL 80
Cdd:MTH00038   2 ATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  81 RLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIH 160
Cdd:MTH00038  82 QLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416511 161 SWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00038 162 SWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 4-224 1.48e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 313.96  E-value: 1.48e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   4 SNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLL 83
Cdd:MTH00129   5 SQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  84 YLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWT 163
Cdd:MTH00129  85 YLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWA 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501416511 164 VPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00129 165 VPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSL 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-224 4.60e-107

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 307.83  E-value: 4.60e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   6 LSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYL 85
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  86 LDEINEPSVTLKSIGHQWYWSYEYSDFN--NIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWT 163
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501416511 164 VPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00023 176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 4-224 6.88e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 304.50  E-value: 6.88e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   4 SNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLL 83
Cdd:MTH00185   5 SQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  84 YLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWT 163
Cdd:MTH00185  85 YLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWT 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501416511 164 VPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00185 165 VPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSL 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 6-224 3.64e-105

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 302.79  E-value: 3.64e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   6 LSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYL 85
Cdd:MTH00098   7 LGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  86 LDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWTVP 165
Cdd:MTH00098  87 MDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 501416511 166 ALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00098 167 SLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSAS 225
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 4-224 2.95e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 300.54  E-value: 2.95e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   4 SNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLL 83
Cdd:MTH00076   5 SQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  84 YLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWT 163
Cdd:MTH00076  85 YLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWA 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501416511 164 VPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00076 165 VPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-224 8.53e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 294.38  E-value: 8.53e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   6 LSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYL 85
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  86 LDEINEPSVTLKSIGHQWYWSYEYSDF--NNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWT 163
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501416511 164 VPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWITS 224
Cdd:MTH00051 169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVAT 229
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 1.40e-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: 1.40e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  92 PSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWTVPALGVKV 171
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 501416511 172 DGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKW 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 3.46e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 235.38  E-value: 3.46e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   95 TLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWTVPALGVKVDGT 174
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 501416511  175 PGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESV 213
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-222 8.05e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 234.53  E-value: 8.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   6 LSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMF-MLFFNNYINRFL--LHGQLIEMIWTILPAIILLFIALPSLRL 82
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  83 LYLLDE-INEPSVTLKSIGHQWYWSYEYSDF--NNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVI 159
Cdd:MTH00027 115 LYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501416511 160 HSWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWI 222
Cdd:MTH00027 195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 22-222 5.60e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 203.32  E-value: 5.60e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  22 FHDHALLILVMITMLVGYLMFMLFFNNYINRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEIN-EPSVTLKSIG 100
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511 101 HQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQ 180
Cdd:MTH00080 105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 501416511 181 TNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWI 222
Cdd:MTH00080 185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
5-222 3.87e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 160.38  E-value: 3.87e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   5 NLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLM--FMLFF----NNYINRFLLHGQLIEMIWTILPAIILLFIALP 78
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLlyFAIRYrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  79 SLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIefdsymiptnelstdgfrlldVDNRIILPMNSQIRILVTAADV 158
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501416511 159 IHSWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWI 222
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 16-213 1.07e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 152.80  E-value: 1.07e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  16 MEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYI-NRFLLHG---QLIEMIWTILPAIILLFIALPSLRLLYLlDEINE 91
Cdd:MTH00047   1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSgNGSVNFGsenQVLELLWTVVPTLLVLVLCFLNLNFITS-DLDCF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  92 PSVTLKSIGHQWYWSYEYSdfNNIEFDSYMiptnelSTDGFrllDVDNRIILPMNSQIRILVTAADVIHSWTVPALGVKV 171
Cdd:MTH00047  80 SSETIKVIGHQWYWSYEYS--FGGSYDSFM------TDDIF---GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKM 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 501416511 172 DGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESV 213
Cdd:MTH00047 149 DAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-213 6.31e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 137.26  E-value: 6.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511 117 FDSYMIPTNELSTDGFRLLDVDNRIILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCS 196
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*..
gi 501416511 197 EICGANHSFMPIVIESV 213
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAV 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 1.55e-40

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: 137.51  E-value: 1.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   12 ASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFF------NNYINRFLLHGQLIEMIWTILPAIILL-FIALPSLRLLY 84
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkgDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511   85 LLDEINEPSVTLKSIGHQWYWSYEYSDFnniefdsymiptnelstdGFRlldVDNRIILPMNSQIRILVTAADVIHSWTV 164
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 501416511  165 PALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWI 222
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 94-211 4.01e-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: 96.98  E-value: 4.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  94 VTLKSIGHQWYWSYEYSDFNniefdsymiptnelstdgfrlldVDNRIILPMNSQIRILVTAADVIHSWTVPALGVKVDG 173
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501416511 174 TPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIE 211
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), ...
 93-206 2.31e-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: 92.68  E-value: 2.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  93 SVTLKSIGHQWYWSYEYSDfnniefdsymiptnelsTDGFRLLDVdNRIILPMNSQIRILVTAADVIHSWTVPALGVKVD 172
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPD-----------------EPGRGIVTA-NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 501416511 173 GTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFM 206
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-76 5.09e-22

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: 86.23  E-value: 5.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511    1 STWSNLSLQDSASPLMEQLIFFHDHALLILVMITMLVGYLMFMLFFNNYI------NRFLLHGQLIEMIWTILPAIILLF 74
Cdd:pfam02790   2 PTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILIL 81


                  ..
gi 501416511   75 IA 76
Cdd:pfam02790  82 IA 83
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-206 1.02e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 80.76  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  94 VTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELstdgfrlldvdnriILPMNSQIRILVTAADVIHSWTVPALGVKVDG 173
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 501416511 174 TPGRLNQTNFFMNRPGLFYGQCSEICGANHSFM 206
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-222 1.08e-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: 78.22  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  94 VTLKSIGHQWYWSYEYSDFNNIEFdsymiptnelstdgfrlldvdNRIILPMNSQIRILVTAADVIHSWTVPALGVKVDG 173
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 501416511 174 TPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKWI 222
Cdd:cd13914   60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-206 7.09e-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: 7.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  99 IGHQWYWSYEYSDfnniefdsymiptnelstdGFRlldVDNRIILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRL 178
Cdd:cd13915    7 TGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRY 64

                         90       100
                 ....*....|....*....|....*...
gi 501416511 179 NQTNFFMNRPGLFYGQCSEICGANHSFM 206
Cdd:cd13915   65 TYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 87-221 1.03e-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: 76.34  E-value: 1.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511  87 DEINEPSVTLKSIGHQWYWSYEYSdfnniefdsymiptNELSTDgfrlldvdNRIILPMNSQIRILVTAADVIHSWTVPA 166
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYP--------------NGVTTG--------NTLRVPADTPIALRVTSTDVFHTFGIPE 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 501416511 167 LGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPTNFFIKW 221
Cdd:cd13918   84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 139-206 1.66e-10

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 56.04  E-value: 1.66e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501416511 139 NRIILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFM 206
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 139-206 9.25e-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: 40.22  E-value: 9.25e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501416511 139 NRIILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFM 206
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-206 5.78e-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: 37.75  E-value: 5.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511 100 GHQWYWsyeysdfnniefdsymiptnELSTDGFrlldvdnriilPMNSQIRILVTAADVIHSWTV--PALGV--KVDGTP 175
Cdd:cd13916    7 GHQWYW--------------------ELSRTEI-----------PAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMP 55

                         90       100       110
                 ....*....|....*....|....*....|.
gi 501416511 176 GRLNQTNFFMNRPGLFYGQCSEICGANHSFM 206
Cdd:cd13916   56 GYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 101-211 1.02e-03

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 37.60  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501416511 101 HQWYWSYEYSDFNNIEFDSYMIPTNelstDGFRLldvdnriilpmnsqirILVTAADVIHSWTVPALGVKVDG------- 173
Cdd:cd00920    6 SDWGWSFTYNGVLLFGPPVLVVPVG----DTVRV----------------QFVNKLGENHSVTIAGFGVPVVAmagganp 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 501416511 174 --------TPGRLNQTNFFMNRPGLFYGQCSEICGaNHSFMPIVIE 211
Cdd:cd00920   66 glvntlviGPGESAEVTFTTDQAGVYWFYCTIPGH-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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