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Conserved domains on  [gi|308745779|ref|YP_003934124|]
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cytochrome c oxidase subunit II (mitochondrion) [Culex quinquefasciatus]

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 1.64e-161

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 445.43  E-value: 1.64e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSS 225
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 1.64e-161

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 445.43  E-value: 1.64e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSS 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 1.68e-90

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: 262.12  E-value: 1.68e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  93 PLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVLHSWTVPSLGVKI 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 308745779 173 DATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.94e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 230.37  E-value: 3.94e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   95 ITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVLHSWTVPSLGVKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 308745779  175 TPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-226 8.17e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 172.32  E-value: 8.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHdhtVLILIMITVMITYVMGMLFF---------NKFTNRYLLHGQTIEIIWTILPTI 71
Cdd:COG1622   13 LLLSGQLSLPDPAGPIAEEIDDLF---WVSLIIMLVIFVLVFGLLLYfairyrrrkGDADPAQFHHNTKLEIVWTVIPII 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  72 ILMFIAFPSLRLLYLLDEINSPLITLKAIGHQWYWSYEYsnfmnlefdsymiptneLDLNGfrllDVDNRIILPLNNQIR 151
Cdd:COG1622   90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-----------------PDQGI----ATVNELVLPVGRPVR 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308745779 152 ILVTATDVLHSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSSQ 226
Cdd:COG1622  149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-224 1.32e-43

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 145.22  E-value: 1.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   14 SPLMEQLNFFHdhTVLILIMITVMITYVMGM-LFFNKFTNR-------YLLHGQTIEIIWTILPTIILM-FIAFPSLRLL 84
Cdd:TIGR02866   3 GEIAQQIAFLF--LFVLAVSTLISLLVAALLaYVVWKFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   85 YLLDEINSPLITLKAIGHQWYWSYEYSNFmnlefdsymiptneldlnGFRlldVDNRIILPLNNQIRILVTATDVLHSWT 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  165 VPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVS 224
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 1.64e-161

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 445.43  E-value: 1.64e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSS 225
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-225 1.76e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 366.96  E-value: 1.76e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSS 225
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 7.74e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 354.99  E-value: 7.74e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSSQL 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-225 3.74e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 353.25  E-value: 3.74e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSS 225
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-228 1.29e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 352.08  E-value: 1.29e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSSQLN 228
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLE 228
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 5.02e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 340.42  E-value: 5.02e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSS 225
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 3.45e-118

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 336.06  E-value: 3.45e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSS 225
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 6.01e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 327.83  E-value: 6.01e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSSQL 227
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 1.60e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 321.45  E-value: 1.60e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSSQL 227
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 3.06e-111

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 318.20  E-value: 3.06e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSSQL 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-225 1.47e-109

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 314.38  E-value: 1.47e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   7 LGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPSLRLLYL 86
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  87 LDEINSPLITLKAIGHQWYWSYEYSNFM--NLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVLHSWT 164
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 308745779 165 VPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSS 225
Cdd:MTH00023 176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 3.01e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 313.25  E-value: 3.01e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  81 LRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSSQLN 228
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-226 3.65e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 303.24  E-value: 3.65e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   7 LGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPTIILMFIAFPSLRLLYL 86
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  87 LDEINSPLITLKAIGHQWYWSYEYSNF--MNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVLHSWT 164
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 308745779 165 VPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSSQ 226
Cdd:MTH00051 169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 1.68e-90

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: 262.12  E-value: 1.68e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  93 PLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVLHSWTVPSLGVKI 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 308745779 173 DATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-226 3.34e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 246.09  E-value: 3.34e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   7 LGLQNSSSPLMEQLNFFHDHTVLIL-IMITVMITYVMGMLFFNKFTNRYL--LHGQTIEIIWTILPTIILMFIAFPSLRL 83
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQILFILtIIVGVVLWLIIRILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  84 LYLLDE-INSPLITLKAIGHQWYWSYEYSNF--MNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVL 160
Cdd:MTH00027 115 LYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 308745779 161 HSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSSQ 226
Cdd:MTH00027 195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGRE 260
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.94e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 230.37  E-value: 3.94e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   95 ITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVLHSWTVPSLGVKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 308745779  175 TPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-222 8.14e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 218.34  E-value: 8.14e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   6 NLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFF---NKFTNRYLLHGQTIEIIWTILPTIILMFIAFPSLR 82
Cdd:MTH00080   5 GYNLNFSNSLFSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLisnNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  83 LLYLLDEIN-SPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVLH 161
Cdd:MTH00080  85 LLYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIH 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 308745779 162 SWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKW 222
Cdd:MTH00080 165 SWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW 225
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-226 8.17e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 172.32  E-value: 8.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   1 MATWANLGLQNSSSPLMEQLNFFHdhtVLILIMITVMITYVMGMLFF---------NKFTNRYLLHGQTIEIIWTILPTI 71
Cdd:COG1622   13 LLLSGQLSLPDPAGPIAEEIDDLF---WVSLIIMLVIFVLVFGLLLYfairyrrrkGDADPAQFHHNTKLEIVWTVIPII 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  72 ILMFIAFPSLRLLYLLDEINSPLITLKAIGHQWYWSYEYsnfmnlefdsymiptneLDLNGfrllDVDNRIILPLNNQIR 151
Cdd:COG1622   90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-----------------PDQGI----ATVNELVLPVGRPVR 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308745779 152 ILVTATDVLHSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSSQ 226
Cdd:COG1622  149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 23-214 5.95e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 151.26  E-value: 5.95e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  23 FHDHTVLILIMITVMITYVMGMLFFNKFT-NRYLLHG---QTIEIIWTILPTIILMFIAFPSLR-LLYLLDEINSPLItl 97
Cdd:MTH00047   7 YYDIVCYILALCVFIPCWVYIMLCWQVVSgNGSVNFGsenQVLELLWTVVPTLLVLVLCFLNLNfITSDLDCFSSETI-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  98 KAIGHQWYWSYEYSNfmNLEFDSYMIPtnelDLNGfrlldVDNRIILPLNNQIRILVTATDVLHSWTVPSLGVKIDATPG 177
Cdd:MTH00047  85 KVIGHQWYWSYEYSF--GGSYDSFMTD----DIFG-----VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPG 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 308745779 178 RLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESI 214
Cdd:MTH00047 154 RINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-224 1.32e-43

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 145.22  E-value: 1.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   14 SPLMEQLNFFHdhTVLILIMITVMITYVMGM-LFFNKFTNR-------YLLHGQTIEIIWTILPTIILM-FIAFPSLRLL 84
Cdd:TIGR02866   3 GEIAQQIAFLF--LFVLAVSTLISLLVAALLaYVVWKFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779   85 YLLDEINSPLITLKAIGHQWYWSYEYSNFmnlefdsymiptneldlnGFRlldVDNRIILPLNNQIRILVTATDVLHSWT 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  165 VPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVS 224
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-214 2.99e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 133.02  E-value: 2.99e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779 118 FDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVLHSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*..
gi 308745779 198 EICGANHSFMPIVIESI 214
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAV 147
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 4.23e-27

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: 99.33  E-value: 4.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779    1 MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFF------NKFTNRYLLHGQTIEIIWTILPTIILM 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 308745779   75 FIAFPSLRL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 8.68e-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: 93.51  E-value: 8.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  95 ITLKAIGHQWYWSYEYSNfmnlefdsymiptneldlngfrlLDVDNRIILPLNNQIRILVTATDVLHSWTVPSLGVKIDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 308745779 175 TPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIE 212
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 1.72e-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: 93.07  E-value: 1.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  95 ITLKAIGHQWYWSYEYsnfmnlefdsymiptneLDLNGFRLLDVdNRIILPLNNQIRILVTATDVLHSWTVPSLGVKIDA 174
Cdd:cd04213    2 LTIEVTGHQWWWEFRY-----------------PDEPGRGIVTA-NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90       100       110
                 ....*....|....*....|....*....|...
gi 308745779 175 TPGRLNQTNFLINQSGLFFGQCSEICGANHSFM 207
Cdd:cd04213   64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 6.04e-20

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 81.53  E-value: 6.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  95 ITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELdlngfrlldvdnriILPLNNQIRILVTATDVLHSWTVPSLGVKIDA 174
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 308745779 175 TPGRLNQTNFLINQSGLFFGQCSEICGANHSFM 207
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 71-223 1.83e-19

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 80.96  E-value: 1.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  71 IILMFIAFPSLRLLYLLD---EINSPLITLKAIGHQWYWSYEYSNFMNlefdsymiptnelDLNGFRLldvdnriilPLN 147
Cdd:cd13918    6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVT-------------TGNTLRV---------PAD 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 308745779 148 NQIRILVTATDVLHSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWV 223
Cdd:cd13918   64 TPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 1.06e-18

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 77.67  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  95 ITLKAIGHQWYWSYEYsnfmnlefdsymiptneldLNGFRlldVDNRIILPLNNQIRILVTATDVLHSWTVPSLGVKIDA 174
Cdd:cd13915    2 LEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90       100       110
                 ....*....|....*....|....*....|...
gi 308745779 175 TPGRLNQTNFLINQSGLFFGQCSEICGANHSFM 207
Cdd:cd13915   60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-223 2.91e-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: 71.67  E-value: 2.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308745779  95 ITLKAIGHQWYWSYEYsnfmnlefdsymiptNELDLNGFrlldvdNRIILPLNNQIRILVTATDVLHSWTVPSLGVKIDA 174
Cdd:cd13914    1 VEIEVEAYQWGWEFSY---------------PEANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 308745779 175 TPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWV 223
Cdd:cd13914   60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 1.05e-06

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: 45.64  E-value: 1.05e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 308745779 140 NRIILPLNNQIRILVTATDVLHSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFM 207
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 151-207 9.85e-03

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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 34.27  E-value: 9.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 308745779 151 RILVTATDVLHSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFM 207
Cdd:cd13917   25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
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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