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Conserved domains on  [gi|1052488259|ref|YP_009271143|]
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cytochrome c oxidase subunit II (mitochondrion) [Sitophilus oryzae]

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
 1-225 7.17e-129

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 362.61  E-value: 7.17e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   1 MSTWKTLFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  81 LRLLYILDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWIIS 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 7.17e-129

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 362.61  E-value: 7.17e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   1 MSTWKTLFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  81 LRLLYILDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWIIS 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 2.21e-84

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: 246.33  E-value: 2.21e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  93 PSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKI 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1052488259 173 DSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.68e-72

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 215.35  E-value: 3.68e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  95 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1052488259 175 TPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
82-223 5.52e-35

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 123.79  E-value: 5.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  82 RLLYILDEINNPSITIKIIGHQWYWSYEYSDYkNIEFDSYM-IPTkelnsfnfrllevdNRTpfpyktqIRLLVTSADVI 160
Cdd:COG1622   100 RVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQ-GIATVNELvLPV--------------GRP-------VRFLLTSADVI 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWI 223
Cdd:COG1622   158 HSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 83-223 3.33e-32

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: 115.94  E-value: 3.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  83 LLYILDEINNPSITIKIIGHQWYWSYEYSDYkniefdsymiptkelnsfnfrLLEVDNRTPFPYKTQIRLLVTSADVIHS 162
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHS 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052488259 163 WTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWI 223
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 7.17e-129

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 362.61  E-value: 7.17e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   1 MSTWKTLFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  81 LRLLYILDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWIIS 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-225 2.44e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 313.41  E-value: 2.44e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   1 MSTWKTLFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  81 LRLLYILDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVI 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWIIS 225
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 6.13e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 309.73  E-value: 6.13e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   1 MSTWKTLFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  81 LRLLYILDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVI 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWIISK 226
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-223 3.29e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 295.46  E-value: 3.29e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   1 MSTWKTLFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  81 LRLLYILDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVI 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWI 223
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWV 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 7-225 3.87e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 294.90  E-value: 3.87e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   7 LFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYI 86
Cdd:MTH00117    7 LGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  87 LDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVP 166
Cdd:MTH00117   87 MDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVP 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052488259 167 SMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWIIS 225
Cdd:MTH00117  167 SLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 5.74e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 291.88  E-value: 5.74e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   1 MSTWKTLFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  81 LRLLYILDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVI 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWIIS 225
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-227 3.71e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 287.52  E-value: 3.71e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   1 MSTWKTLFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  81 LRLLYILDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVI 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWIISKT 227
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-227 9.97e-93

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 271.62  E-value: 9.97e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   7 LFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYI 86
Cdd:MTH00023   16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  87 LDEINNPSITIKIIGHQWYWSYEYSDYK--NIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWT 164
Cdd:MTH00023   96 MDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052488259 165 VPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWIISKT 227
Cdd:MTH00023  176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 7-225 1.82e-92

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 270.44  E-value: 1.82e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   7 LFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYI 86
Cdd:MTH00098    7 LGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  87 LDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVP 166
Cdd:MTH00098   87 MDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVP 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052488259 167 SMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWIIS 225
Cdd:MTH00098  167 SLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSAS 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-222 7.21e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 266.58  E-value: 7.21e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   1 MSTWKTLFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  81 LRLLYILDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVI 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNW 222
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 7-225 6.38e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 259.33  E-value: 6.38e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   7 LFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYI 86
Cdd:MTH00076    7 LGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  87 LDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVP 166
Cdd:MTH00076   87 MDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVP 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052488259 167 SMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWIIS 225
Cdd:MTH00076  167 SLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-222 7.46e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 259.05  E-value: 7.46e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   1 MSTWKTLFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  81 LRLLYILDEINNPSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVI 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNW 222
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-227 4.12e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 252.39  E-value: 4.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   4 WKTLFlQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRL 83
Cdd:MTH00051    7 WQLGF-QDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  84 LYILDEINNPSITIKIIGHQWYWSYEYSDY--KNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIH 161
Cdd:MTH00051   86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052488259 162 SWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWIISKT 227
Cdd:MTH00051  166 SFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 2.21e-84

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: 246.33  E-value: 2.21e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  93 PSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKI 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1052488259 173 DSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.68e-72

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 215.35  E-value: 3.68e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  95 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1052488259 175 TPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-223 7.51e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 209.50  E-value: 7.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   7 LFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFL---LEGQLIETIWTILPAIILILIALPSLRL 83
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  84 LYILDE-INNPSITIKIIGHQWYWSYEYSDY--KNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVI 160
Cdd:MTH00027  115 LYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWI 223
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 8-223 4.09e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 185.98  E-value: 4.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259   8 FLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYIL 87
Cdd:MTH00080   10 FSNSLFSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  88 DEINNPS-ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVP 166
Cdd:MTH00080   90 GLMNLDSnLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALP 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1052488259 167 SMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWI 223
Cdd:MTH00080  170 SLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-217 2.24e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 144.71  E-value: 2.24e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  57 EGQLIETIWTILPAIILILIALPslRLLYILDEIN-NPSITIKIIGHQWYWSYEYSDykNIEFDSYMipTKELNSfnfrl 135
Cdd:MTH00047   45 ENQVLELLWTVVPTLLVLVLCFL--NLNFITSDLDcFSSETIKVIGHQWYWSYEYSF--GGSYDSFM--TDDIFG----- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259 136 leVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIK 215
Cdd:MTH00047  114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVD 191


                  ..
gi 1052488259 216 PN 217
Cdd:MTH00047  192 VD 193
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-219 1.23e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 128.78  E-value: 1.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259 118 FDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 1052488259 198 EICGANHSFMPIILESIKPNLF 219
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
82-223 5.52e-35

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 123.79  E-value: 5.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  82 RLLYILDEINNPSITIKIIGHQWYWSYEYSDYkNIEFDSYM-IPTkelnsfnfrllevdNRTpfpyktqIRLLVTSADVI 160
Cdd:COG1622   100 RVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQ-GIATVNELvLPV--------------GRP-------VRFLLTSADVI 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052488259 161 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWI 223
Cdd:COG1622   158 HSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 83-223 3.33e-32

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: 115.94  E-value: 3.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  83 LLYILDEINNPSITIKIIGHQWYWSYEYSDYkniefdsymiptkelnsfnfrLLEVDNRTPFPYKTQIRLLVTSADVIHS 162
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHS 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052488259 163 WTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNWI 223
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-207 7.04e-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: 7.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  94 SITIKIIGHQWYWSYEYSDYKNIEFDS---YMIPTKElnsfnfrllevdnrtpfpyktQIRLLVTSADVIHSWTVPSMGI 170
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGIVTaneLHIPVGR---------------------PVRLRLTSADVIHSFWVPSLAG 59

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1052488259 171 KIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFM 207
Cdd:cd04213    60 KMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 3.29e-23

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: 89.28  E-value: 3.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  95 ITIKIIGHQWYWSYEYsdykniefdsymiptkeLNSFNFRLLEVDNRTPfpyktqIRLLVTSADVIHSWTVPSMGIKIDS 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIY-----------------PNVRTPNEIVVPAGTP------VRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1052488259 175 TPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 9.00e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 75.75  E-value: 9.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  95 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNsfnfrlLEVDNRtpfpyktqIRLLVTSADVIHSWTVPSMGIKIDS 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPELH------LPVGRP--------VLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1052488259 175 TPGRLNQANLIANRSSIFFGQCSEICGANHSFM 207
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-207 2.02e-16

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: 71.89  E-value: 2.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  94 SITIKIIGHQWYWSYEYSDYKniefdsymiptkelnsfnfrllEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKID 173
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGK----------------------REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1052488259 174 STPGRLNQANLIANRSSIFFGQCSEICGANHSFM 207
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-222 2.26e-16

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: 72.87  E-value: 2.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  83 LLYILD---EINNPSITIKIIGHQWYWSYEYSDykNIEFDSYMIptkelnsfnfrllevdnrtpFPYKTQIRLLVTSADV 159
Cdd:cd13918    18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTLR--------------------VPADTPIALRVTSTDV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052488259 160 IHSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFMPIILESIKPNLFLNW 222
Cdd:cd13918    76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 4.34e-16

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: 71.29  E-value: 4.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  95 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKelnsfnfrllevdnrtpfpykTQIRLLVTSADVIHSWTVPSMGIKIDS 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEANVTTSEQLVIPAD---------------------RPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1052488259 175 TPGRLNQANLIANRSSIFFGQCSEICGANHSFM 207
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-69 2.94e-11

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: 57.73  E-value: 2.94e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052488259   1 MSTWKTLFLQDSASPLMEHLTLFHDHTILILILITILVSQMLLSMLL------NKLSHRFLLEGQLIETIWTILP 69
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIP 75
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 95-207 6.06e-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: 43.69  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052488259  95 ITIKIIGHQWYWSYEYSDYKniefdsymIPTKelnsfnfrllevdNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 174
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQG--------IATV-------------NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYA 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1052488259 175 TPGRLNQANLIANRSSIFFGQCSEICGANHSFM 207
Cdd:cd04212    60 MAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 145-207 5.49e-04

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: 37.93  E-value: 5.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052488259 145 PYKTQIRLLVTSADVIHSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCSEICGANHSFM 207
Cdd:cd13913    30 PAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
 
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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