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Conserved domains on  [gi|2215610882|dbj|BCI57496|]
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cytochrome c oxidase II, partial (mitochondrion) [Mycodrosophila separata]

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
 1-222 2.83e-169

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 464.69  E-value: 2.83e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINW 222
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-222 2.83e-169

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 464.69  E-value: 2.83e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINW 222
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 2.81e-95

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: 273.68  E-value: 2.81e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  93 PSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKV 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2215610882 173 DGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 1.76e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 236.15  E-value: 1.76e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  96 TLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGT 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2215610882 176 PGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESV 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 8.02e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 177.33  E-value: 8.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   6 NLGLQDSASPLMEQLIFFHDHALLILVMITVLVgylMFMLFFNSFINR---------NLLHGQLIEMIWTILPAIILLFI 76
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIVL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  77 AFPSLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIefdsymiptnelntdsfrlldVDNRIVLPMNSQIRILVTA 156
Cdd:COG1622    95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTS 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2215610882 157 ADVIHSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:COG1622   154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-222 2.29e-43

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: 144.45  E-value: 2.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  13 ASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNsFINRN-------LLHGQLIEMIWTILPAIILL-FIAFPSLRLL 84
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWK-FRRKGdeekpsqIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  85 YLLDEINEPSVTLKSIGHQWYWSYEYSDFnniefdsymiptnelntdsfrLLDVDNRIVLPMNSQIRILVTAADVIHSWT 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2215610882 165 IPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-222 2.83e-169

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 464.69  E-value: 2.83e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINW 222
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-222 3.94e-138

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 385.83  E-value: 3.94e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKW 222
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 7.54e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 377.52  E-value: 7.54e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-222 6.91e-134

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 375.02  E-value: 6.91e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENW 222
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-222 4.99e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 365.46  E-value: 4.99e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENW 222
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-222 7.17e-129

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 362.48  E-value: 7.17e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-222 2.15e-128

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 361.48  E-value: 2.15e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-222 3.29e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 335.53  E-value: 3.29e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-222 1.15e-117

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 334.38  E-value: 1.15e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-222 3.30e-116

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 330.94  E-value: 3.30e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   7 LGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPSLRLLYL 86
Cdd:MTH00023   16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  87 LDEINEPSVTLKSIGHQWYWSYEYSDFN--NIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVIHSWT 164
Cdd:MTH00023   96 MDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2215610882 165 IPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00023  176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 233
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-222 7.98e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 329.54  E-value: 7.98e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-222 1.03e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 329.43  E-value: 1.03e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  81 LRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-222 5.99e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 314.80  E-value: 5.99e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   7 LGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPSLRLLYL 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  87 LDEINEPSVTLKSIGHQWYWSYEYSDF--NNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVIHSWT 164
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2215610882 165 IPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINW 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 2.81e-95

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: 273.68  E-value: 2.81e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  93 PSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKV 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2215610882 173 DGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-222 1.03e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 252.25  E-value: 1.03e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   7 LGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMF-MLFFNSFINR--NLLHGQLIEMIWTILPAIILLFIAFPSLRL 83
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYywNKLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  84 LYLLDE-INEPSVTLKSIGHQWYWSYEYSDF--NNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVI 160
Cdd:MTH00027  115 LYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2215610882 161 HSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 1.76e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 236.15  E-value: 1.76e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  96 TLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGT 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2215610882 176 PGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESV 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-222 1.50e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 219.88  E-value: 1.50e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  23 FHDHALLILVMITVLVGYLMFMLFFNSFINRNLLHGQLIEMIWTILPAIILLFIAFPSLRLLYLLDEIN-EPSVTLKSIG 101
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882 102 HQWYWSYEYSDFNNIEFDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQ 181
Cdd:MTH00080  105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2215610882 182 TNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:MTH00080  185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW 225
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 8.02e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 177.33  E-value: 8.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   6 NLGLQDSASPLMEQLIFFHDHALLILVMITVLVgylMFMLFFNSFINR---------NLLHGQLIEMIWTILPAIILLFI 76
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIVL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  77 AFPSLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIefdsymiptnelntdsfrlldVDNRIVLPMNSQIRILVTA 156
Cdd:COG1622    95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTS 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2215610882 157 ADVIHSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:COG1622   154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-218 2.97e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 162.05  E-value: 2.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  17 MEQLIFFHDHALLILVMITVLVGYLMFMLFFNSFI-NRNLLHG---QLIEMIWTILPAIILLFIAFpsLRLLYLLDEIN- 91
Cdd:MTH00047    1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSgNGSVNFGsenQVLELLWTVVPTLLVLVLCF--LNLNFITSDLDc 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  92 EPSVTLKSIGHQWYWSYEYSDfnNIEFDSYMiptnelnTDSFRLldVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVK 171
Cdd:MTH00047   79 FSSETIKVIGHQWYWSYEYSF--GGSYDSFM-------TDDIFG--VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2215610882 172 VDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNY 218
Cdd:MTH00047  148 MDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-222 2.29e-43

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: 144.45  E-value: 2.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  13 ASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNsFINRN-------LLHGQLIEMIWTILPAIILL-FIAFPSLRLL 84
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWK-FRRKGdeekpsqIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  85 YLLDEINEPSVTLKSIGHQWYWSYEYSDFnniefdsymiptnelntdsfrLLDVDNRIVLPMNSQIRILVTAADVIHSWT 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2215610882 165 IPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-214 4.93e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 137.26  E-value: 4.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882 118 FDSYMIPTNELNTDSFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*..
gi 2215610882 198 EICGANHSFMPIVIESV 214
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAV 147
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 6.45e-28

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: 101.25  E-value: 6.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882   1 MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFF------NSFINRNLLHGQLIEMIWTILPAIILL 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 2215610882  75 FIAFPSLRL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 6.67e-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: 98.91  E-value: 6.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  95 VTLKSIGHQWYWSYEYSDFNniefdsymiptnelntdsfrlldVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2215610882 175 TPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIE 212
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), ...
 94-207 5.07e-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: 91.53  E-value: 5.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  94 SVTLKSIGHQWYWSYEYSDfnniefdsymiptnelntDSFRLLDVDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVD 173
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPD------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2215610882 174 GTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFM 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 2.67e-20

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 82.30  E-value: 2.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  95 VTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELntdsfrlldvdnriVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2215610882 175 TPGRLNQTNFFMNRPGLFYGQCSEICGANHSFM 207
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-222 3.63e-20

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 82.89  E-value: 3.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  67 ILPAIILL-FIAFPSLRLLYLLD---EINEPSVTLKSIGHQWYWSYEYSdfNNIEFDSYMiptnelntdsfrlldvdnri 142
Cdd:cd13918     1 GLSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYP--NGVTTGNTL-------------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882 143 VLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:cd13918    59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-222 1.63e-18

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 77.45  E-value: 1.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882  95 VTLKSIGHQWYWSYEYSDFNNIEFdsymiptnelntdsfrlldvdNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDG 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2215610882 175 TPGRLNQTNFFMNRPGLFYGQCSEICGANHSFMPIVIESVPVNYFIKW 222
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-207 1.22e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 74.97  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882 100 IGHQWYWSYEYSDFNNIefdsymiptnelntdsfrlldvDNRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRL 179
Cdd:cd13915     7 TGRQWMWEFTYPNGKRE----------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRY 64

                          90       100
                  ....*....|....*....|....*...
gi 2215610882 180 NQTNFFMNRPGLFYGQCSEICGANHSFM 207
Cdd:cd13915    65 TYLWFEATKPGEYDLFCTEYCGTGHSGM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 1.79e-11

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 58.74  E-value: 1.79e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2215610882 140 NRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFM 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 6.82e-06

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 43.31  E-value: 6.82e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2215610882 140 NRIVLPMNSQIRILVTAADVIHSWTIPALGVKVDGTPGRLNQTNFFMNRPGLFYGQCSEICGANHSFM 207
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 120-212 9.23e-05

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: 40.68  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882 120 SYMIPTNELNTDSFrlldVDNRIVLPMNSQIR-ILVTAADVIHSWTIPALGVKVDG---------------TPGRLNQTN 183
Cdd:cd00920     7 DWGWSFTYNGVLLF----GPPVLVVPVGDTVRvQFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVT 82

                          90       100
                  ....*....|....*....|....*....
gi 2215610882 184 FFMNRPGLFYGQCSEICGaNHSFMPIVIE 212
Cdd:cd00920    83 FTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-207 3.28e-04

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 38.52  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2215610882 101 GHQWYWsyeysdfnniefdsymiptnELNTDSFrlldvdnrivlPMNSQIRILVTAADVIHSWTI--PALGV--KVDGTP 176
Cdd:cd13916     7 GHQWYW--------------------ELSRTEI-----------PAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMP 55

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2215610882 177 GRLNQTNFFMNRPGLFYGQCSEICGANHSFM 207
Cdd:cd13916    56 GYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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