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Conserved domains on  [gi|52788748|ref|YP_054533|]
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cytochrome c oxidase subunit II (mitochondrion) [Thermobia domestica]

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
 1-227 5.24e-145

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 403.83  E-value: 5.24e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKMM 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 5.24e-145

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 403.83  E-value: 5.24e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKMM 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 1.14e-86

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: 252.49  E-value: 1.14e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748  93 PAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVLHSWAMPAFGIKA 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 52788748 173 DATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 1.34e-73

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 218.82  E-value: 1.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    95 ITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVLHSWAMPAFGIKADA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 52788748   175 TPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEA 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-226 1.29e-50

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 164.23  E-value: 1.29e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLV-GYLLASLL-----PNTYINRNLLEGQTLETIWTILPAITLI 74
Cdd:COG1622  13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfGLLLYFAIryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVI 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748  75 FIALPSLRLLYLLDEIHQPAITLKTIGHQWYWSYEYsdfsltefdsymipineMNPNSfrllDVDNRIVLPINIDIRILI 154
Cdd:COG1622  93 VLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-----------------PDQGI----ATVNELVLPVGRPVRFLL 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52788748 155 TAADVLHSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKM 226
Cdd:COG1622 152 TSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 1.25e-38

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 132.50  E-value: 1.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    12 AASPVMEQMTFFHDHTMLIVTMITVLVGYLLA------------SLLPNTYINRnllegqTLETIWTILPA-ITLIFIAL 78
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAyvvwkfrrkgdeEKPSQIHGNR------RLEYVWTVIPLiIVVGLFAA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    79 PSLRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTefdsymipinemnpnsfrlldVDNRIVLPINIDIRILITAAD 158
Cdd:TIGR02866  75 TAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFT---------------------TVNELVLPAGTPVELQVTSKD 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52788748   159 VLHSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWM 223
Cdd:TIGR02866 134 VIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 5.24e-145

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 403.83  E-value: 5.24e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKMM 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 4.78e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 340.76  E-value: 4.78e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKM 226
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 3.06e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 330.91  E-value: 3.06e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKM 226
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 7.01e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 330.13  E-value: 7.01e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKMMQE 229
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 6.87e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 324.94  E-value: 6.87e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKM 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 8.59e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 324.63  E-value: 8.59e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMT 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 1.34e-112

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 321.81  E-value: 1.34e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTK 225
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 6.50e-107

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 307.42  E-value: 6.50e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKMM 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-229 7.48e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 294.87  E-value: 7.48e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKMMQE 229
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEE 229
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 5-229 1.02e-101

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 294.74  E-value: 1.02e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    5 NQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPSLRLL 84
Cdd:MTH00023  14 WQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   85 YLLDEIHQPAITLKTIGHQWYWSYEYSDF--SLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVLHS 162
Cdd:MTH00023  94 YLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHS 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52788748  163 WAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKMMQE 229
Cdd:MTH00023 174 FAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSND 240
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 2.04e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 293.61  E-value: 2.04e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKM 226
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-229 9.88e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 291.62  E-value: 9.88e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   81 LRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52788748  161 HSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKMMQE 229
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLED 229
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-230 1.37e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 276.28  E-value: 1.37e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    6 QLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPSLRLLY 85
Cdd:MTH00051   8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   86 LLDEIHQPAITLKTIGHQWYWSYEYSDF--SLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVLHSW 163
Cdd:MTH00051  88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52788748  164 AMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKMMQEL 230
Cdd:MTH00051 168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 1.14e-86

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: 252.49  E-value: 1.14e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748  93 PAITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVLHSWAMPAFGIKA 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 52788748 173 DATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 1.34e-73

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 218.82  E-value: 1.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    95 ITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVLHSWAMPAFGIKADA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 52788748   175 TPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEA 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-225 1.69e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 218.74  E-value: 1.69e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    6 QLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLA-SLLPNTYINR--NLLEGQTLETIWTILPAITLIFIALPSLR 82
Cdd:MTH00027  34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYywNKLDGSLIEVIWTLIPAFILILIAFPSLR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   83 LLYLLDE-IHQPAITLKTIGHQWYWSYEYSDFSLT--EFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADV 159
Cdd:MTH00027 114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKniEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52788748  160 LHSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTK 225
Cdd:MTH00027 194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-223 3.29e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 201.78  E-value: 3.29e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   23 FHDHTMLIVTMITVLVGYLLASLLPNTYINRNLLEGQTLETIWTILPAITLIFIALPSLRLLYLLDEIH-QPAITLKTIG 101
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748  102 HQWYWSYEYSDFSLTEFDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVLHSWAMPAFGIKADATPGRLNQ 181
Cdd:MTH00080 105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 52788748  182 VAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWM 223
Cdd:MTH00080 185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-226 1.29e-50

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 164.23  E-value: 1.29e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLV-GYLLASLL-----PNTYINRNLLEGQTLETIWTILPAITLI 74
Cdd:COG1622  13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfGLLLYFAIryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVI 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748  75 FIALPSLRLLYLLDEIHQPAITLKTIGHQWYWSYEYsdfsltefdsymipineMNPNSfrllDVDNRIVLPINIDIRILI 154
Cdd:COG1622  93 VLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-----------------PDQGI----ATVNELVLPVGRPVRFLL 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52788748 155 TAADVLHSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWMTKM 226
Cdd:COG1622 152 TSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-212 1.25e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 135.08  E-value: 1.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748   57 EGQTLETIWTILP--------AITLIFIALPSLRLLYLldeihqpaiTLKTIGHQWYWSYEYSDFSltEFDSYMIPINEM 128
Cdd:MTH00047  45 ENQVLELLWTVVPtllvlvlcFLNLNFITSDLDCFSSE---------TIKVIGHQWYWSYEYSFGG--SYDSFMTDDIFG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748  129 npnsfrlldVDNRIVLPINIDIRILITAADVLHSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMP 208
Cdd:MTH00047 114 ---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMP 184


                 ....
gi 52788748  209 IVVE 212
Cdd:MTH00047 185 IVIE 188
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-213 1.94e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 133.41  E-value: 1.94e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748  118 FDSYMIPINEMNPNSFRLLDVDNRIVLPINIDIRILITAADVLHSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*.
gi 52788748  198 EICGANHSFMPIVVEA 213
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEA 146
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 1.25e-38

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 132.50  E-value: 1.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    12 AASPVMEQMTFFHDHTMLIVTMITVLVGYLLA------------SLLPNTYINRnllegqTLETIWTILPA-ITLIFIAL 78
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAyvvwkfrrkgdeEKPSQIHGNR------RLEYVWTVIPLiIVVGLFAA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748    79 PSLRLLYLLDEIHQPAITLKTIGHQWYWSYEYSDFSLTefdsymipinemnpnsfrlldVDNRIVLPINIDIRILITAAD 158
Cdd:TIGR02866  75 TAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFT---------------------TVNELVLPAGTPVELQVTSKD 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52788748   159 VLHSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWM 223
Cdd:TIGR02866 134 VIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 3.52e-25

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: 94.67  E-value: 3.52e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748  95 ITLKTIGHQWYWSYEYSDfsltefdsymipinemnpnsfrlLDVDNRIVLPINIDIRILITAADVLHSWAMPAFGIKADA 174
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 52788748 175 TPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVE 212
Cdd:cd13842  58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 3.79e-22

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


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 86.62  E-value: 3.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748     1 MAIWNQLGLQDAASPVMEQMTFFHDHTMLIVTMITVLVGYLLASLL------PNTYINRNLLEGQTLETIWTILPAITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 52788748    75 FIA 77
Cdd:pfam02790  81 LIA 83
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-213 8.97e-22

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: 85.76  E-value: 8.97e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748  94 AITLKTIGHQWYWSYEYsdfsltefdsymipinemnPNSFRlldVDNRIVLPINIDIRILITAADVLHSWAMPAFGIKAD 173
Cdd:cd13915   1 ALEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 52788748 174 ATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEA 213
Cdd:cd13915  59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-212 1.42e-21

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 85.77  E-value: 1.42e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748  94 AITLKTIGHQWYWSYEYSDFSLTEFDSYMIPINEMnpnsfrlldvdnriVLPINIDIRILITAADVLHSWAMPAFGIKAD 173
Cdd:cd13919   1 ALVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 52788748 174 ATPGRLNQVAANITRTGLFFGQCSEICGANHSFM--PIVVE 212
Cdd:cd13919  67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-213 4.84e-21

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: 84.21  E-value: 4.84e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748  94 AITLKTIGHQWYWSYEYSDFSLTEFDSymipINEmnpnsfrlldvdnrIVLPINIDIRILITAADVLHSWAMPAFGIKAD 173
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPDEPGRGIVT----ANE--------------LHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 52788748 174 ATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEA 213
Cdd:cd04213  63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIA 102
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-223 2.11e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 82.84  E-value: 2.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748 101 GHQWYWSYEYSDFSLTEFdsymipinemnpnsfrlldvdNRIVLPINIDIRILITAADVLHSWAMPAFGIKADATPGRLN 180
Cdd:cd13914   7 AYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 52788748 181 QVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWM 223
Cdd:cd13914  66 TIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-223 9.09e-15

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: 68.64  E-value: 9.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748  88 DEIHQPAITLKTIGHQWYWSYEYSDFSLTefdsymipINEMnpnsfrlldvdnriVLPINIDIRILITAADVLHSWAMPA 167
Cdd:cd13918  26 DEADEDALEVEVEGFQFGWQFEYPNGVTT--------GNTL--------------RVPADTPIALRVTSTDVFHTFGIPE 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 52788748 168 FGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEACPHSVFIKWM 223
Cdd:cd13918  84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-212 9.03e-07

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: 46.02  E-value: 9.03e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52788748 140 NRIVLPINIDIRILITAADVLHSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFM--PIVVE 212
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 120-212 7.56e-03

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 35.28  E-value: 7.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788748 120 SYMIPINEMNPNSFrlldVDNRIVLPINIDIRILIT-AADVLHSWAMPAFGIKADATPGRLN-----------QVAANIT 187
Cdd:cd00920   7 DWGWSFTYNGVLLF----GPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAMAGGANpglvntlvigpGESAEVT 82

                        90       100
                ....*....|....*....|....*....
gi 52788748 188 ----RTGLFFGQCSEICGaNHSFMPIVVE 212
Cdd:cd00920  83 fttdQAGVYWFYCTIPGH-NHAGMVGTIN 110
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-213 8.74e-03

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: 34.83  E-value: 8.74e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52788748 140 NRIVLPINIDIRILITAADVLHSWAMPAFGIKADATPGRLNQVAANITRTGLFFGQCSEICGANHSFMPIVVEA 213
Cdd:cd04212  25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLA 98
 
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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