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Conserved domains on  [gi|568780657|dbj|BAO24795|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Drosophila watanabei]

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
 1-215 6.38e-154

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 425.40  E-value: 6.38e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVS 215
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-215 6.38e-154

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 425.40  E-value: 6.38e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVS 215
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-215 4.66e-92

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 265.59  E-value: 4.66e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  93 PSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKV 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568780657 173 DGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVS 123
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 2.92e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 237.69  E-value: 2.92e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   96 TLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGT 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568780657  176 PGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESV 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-215 1.97e-51

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 165.77  E-value: 1.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   6 NLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLM--FMLFF----NNYVNRFLLHGQLIEMIWTILPAIILLFIALP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLlyFAIRYrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  80 SLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIefdsymiptnelstdgfrlldVDNRIVLPMNSQIRILVTAADV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568780657 160 IHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-215 1.21e-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: 134.82  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   13 ASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFF------NNYVNRFLLHGQLIEMIWTILPAIILL-FIALPSLRLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkgDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   86 LLDEINEPSVTLKSIGHQWYWSYEYSDFnniefdsymiptnelstdGFRlldVDNRIVLPMNSQIRILVTAADVIHSWTI 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568780657  166 PALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVP 190
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-215 6.38e-154

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 425.40  E-value: 6.38e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVS 215
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-215 4.90e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 352.70  E-value: 4.90e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVP 215
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-215 2.31e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 350.94  E-value: 2.31e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAIS 215
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-215 5.86e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 339.76  E-value: 5.86e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVP 215
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-215 1.06e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 338.88  E-value: 1.06e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVP 215
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-215 3.26e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 337.66  E-value: 3.26e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVP 215
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-214 8.98e-119

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 336.83  E-value: 8.98e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESV 214
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAV 214
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-215 8.35e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 311.65  E-value: 8.35e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVP 215
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-215 3.65e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 307.58  E-value: 3.65e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVP 215
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-214 1.12e-105

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 303.98  E-value: 1.12e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   7 LGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYL 86
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  87 LDEINEPSVTLKSIGHQWYWSYEYSDFN--NIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWT 164
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568780657 165 IPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESV 214
Cdd:MTH00023 176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAV 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-215 2.43e-105

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 302.79  E-value: 2.43e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVP 215
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-215 1.31e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 298.23  E-value: 1.31e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATP 215
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-214 5.86e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 292.07  E-value: 5.86e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   7 LGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYL 86
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  87 LDEINEPSVTLKSIGHQWYWSYEYSDF--NNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWT 164
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568780657 165 IPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESV 214
Cdd:MTH00051 169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGV 218
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-215 4.66e-92

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 265.59  E-value: 4.66e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  93 PSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKV 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568780657 173 DGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVS 123
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 2.92e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 237.69  E-value: 2.92e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   96 TLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGT 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568780657  176 PGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESV 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-214 1.07e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 231.45  E-value: 1.07e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   7 LGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMF-MLFFNNYVNRFL--LHGQLIEMIWTILPAIILLFIALPSLRL 83
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  84 LYLLDE-INEPSVTLKSIGHQWYWSYEYSDF--NNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00027 115 LYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568780657 161 HSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESV 214
Cdd:MTH00027 195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESV 248
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-213 6.46e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 202.93  E-value: 6.46e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  23 FHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEIN-EPSVTLKSIG 101
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657 102 HQWYWSYEYSDFNNIEFDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQ 181
Cdd:MTH00080 105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568780657 182 TNFFINRPGLFYGQCSEICGANHSFMPIVIES 213
Cdd:MTH00080 185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEV 216
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-215 1.97e-51

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 165.77  E-value: 1.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   6 NLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLM--FMLFF----NNYVNRFLLHGQLIEMIWTILPAIILLFIALP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLlyFAIRYrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  80 SLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIefdsymiptnelstdgfrlldVDNRIVLPMNSQIRILVTAADV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568780657 160 IHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-214 5.99e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 153.19  E-value: 5.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  17 MEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYV-NRFLLHG---QLIEMIWTILPAIILLFIALPSLRLLYLlDEINE 92
Cdd:MTH00047   1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSgNGSVNFGsenQVLELLWTVVPTLLVLVLCFLNLNFITS-DLDCF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  93 PSVTLKSIGHQWYWSYEYSdfNNIEFDSYMiptnelSTDGFrllDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKV 172
Cdd:MTH00047  80 SSETIKVIGHQWYWSYEYS--FGGSYDSFM------TDDIF---GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKM 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568780657 173 DGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESV 214
Cdd:MTH00047 149 DAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-214 8.35e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 139.18  E-value: 8.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657 118 FDSYMIPTNELSTDGFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*..
gi 568780657 198 EICGANHSFMPIVIESV 214
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAV 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-215 1.21e-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: 134.82  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   13 ASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFF------NNYVNRFLLHGQLIEMIWTILPAIILL-FIALPSLRLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkgDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657   86 LLDEINEPSVTLKSIGHQWYWSYEYSDFnniefdsymiptnelstdGFRlldVDNRIVLPMNSQIRILVTAADVIHSWTI 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568780657  166 PALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVP 190
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.38e-27

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: 100.45  E-value: 1.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  95 VTLKSIGHQWYWSYEYSDFNniefdsymiptnelstdgfrlldVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568780657 175 TPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIE 212
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 1.84e-24

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: 92.01  E-value: 1.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657    1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYV------NRFLLHGQLIEMIWTILPAIILL 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 568780657   75 FIA 77
Cdd:pfam02790  81 LIA 83
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-207 2.70e-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: 2.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  94 SVTLKSIGHQWYWSYEYSDfnniefdsymiptnelsTDGFRLLDVdNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVD 173
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPD-----------------EPGRGIVTA-NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568780657 174 GTPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 207
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 6.44e-21

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: 83.46  E-value: 6.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  95 VTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELstdgfrlldvdnriVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 174
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568780657 175 TPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 207
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-207 9.92e-19

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 77.67  E-value: 9.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657 100 IGHQWYWSYEYSDfnniefdsymiptnelstdGFRlldVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 179
Cdd:cd13915    7 TGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRY 64

                         90       100
                 ....*....|....*....|....*...
gi 568780657 180 NQTNFFINRPGLFYGQCSEICGANHSFM 207
Cdd:cd13915   65 TYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-215 3.82e-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: 76.29  E-value: 3.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  95 VTLKSIGHQWYWSYEYSDFNNIEFdsymiptnelstdgfrlldvdNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 174
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568780657 175 TPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVP 215
Cdd:cd13914   60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVS 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-207 5.67e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 76.73  E-value: 5.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657  88 DEINEPSVTLKSIGHQWYWSYEYSdfnniefdsymiptNELSTDgfrlldvdNRIVLPMNSQIRILVTAADVIHSWTIPA 167
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYP--------------NGVTTG--------NTLRVPADTPIALRVTSTDVFHTFGIPE 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568780657 168 LGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 207
Cdd:cd13918   84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 1.37e-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: 1.37e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568780657 140 NRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 207
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-207 1.41e-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: 45.23  E-value: 1.41e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568780657 140 NRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFM 207
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-207 1.14e-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: 39.67  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657 101 GHQWYWsyeysdfnniefdsymiptnELSTDgfrlldvdnriVLPMNSQIRILVTAADVIHSWTI--PALGV--KVDGTP 176
Cdd:cd13916    7 GHQWYW--------------------ELSRT-----------EIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMP 55

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568780657 177 GRLNQTNFFINRPGLFYGQCSEICGANHSFM 207
Cdd:cd13916   56 GYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 125-212 1.25e-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: 37.21  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568780657 125 TNELSTDGFRLLDVDNRIVLPMNSQIR-ILVTAADVIHSWTIPALGVKVDG---------------TPGRLNQTNFFINR 188
Cdd:cd00920    8 WGWSFTYNGVLLFGPPVLVVPVGDTVRvQFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQ 87

                         90       100
                 ....*....|....*....|....
gi 568780657 189 PGLFYGQCSEICGaNHSFMPIVIE 212
Cdd:cd00920   88 AGVYWFYCTIPGH-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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