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Conserved domains on  [gi|218937717|gb|ACL13019|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Coptotermes formosanus]

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
 1-210 2.20e-149

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 413.84  E-value: 2.20e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   1 MTTWLNMSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  81 LRLLYLMDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 218937717 161 HSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIV 210
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-210 2.20e-149

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 413.84  E-value: 2.20e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   1 MTTWLNMSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  81 LRLLYLMDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 218937717 161 HSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIV 210
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-209 1.81e-85

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: 248.64  E-value: 1.81e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  93 PTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKT 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 218937717 173 DATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPI 117
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-209 5.46e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 229.22  E-value: 5.46e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   95 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 218937717  175 TPGRLNQTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPI 115
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-210 8.96e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 176.56  E-value: 8.96e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   6 NMSLQDGASPIMEQLVFFHDHVLMIMLMITT-TVSYMMVTLIR-----NKQTSRFMLEGQMIETTWTIAPAIILVFIAMP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVlVFGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  80 SLRLLYLMDEVHNPTLTLKAVGHQWYWSYEYsdftklefdsymiPQEEQqestfrllDTDNRIVLPINSPIRLIVTAADV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGI--------ATVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 218937717 160 LHSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFK 207
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-210 2.34e-44

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: 146.76  E-value: 2.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   13 ASPIMEQLVFFHDHVLMIMLMITTTV-SYMMVTLIRNKQTSRFML-----EGQMIETTWTIAPAIILV-FIAMPSLRLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVWKFRRKGDEEKpsqihGNRRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   86 LMDEVHNPTLTLKAVGHQWYWSYEYSdftklefdsymipqeeqqESTFRlldTDNRIVLPINSPIRLIVTAADVLHSWTI 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYP------------------ESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 218937717  166 PSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFK 185
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-210 2.20e-149

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 413.84  E-value: 2.20e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   1 MTTWLNMSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  81 LRLLYLMDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 218937717 161 HSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIV 210
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-210 6.01e-123

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 346.93  E-value: 6.01e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   1 MTTWLNMSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  81 LRLLYLMDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 218937717 161 HSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIV 210
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 7-210 3.30e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 344.98  E-value: 3.30e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   7 MSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYL 86
Cdd:MTH00117   7 LGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  87 MDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWTIP 166
Cdd:MTH00117  87 MDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVP 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 218937717 167 SLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:MTH00117 167 SLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIV 210
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-210 3.51e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 340.16  E-value: 3.51e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   1 MTTWLNMSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  81 LRLLYLMDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 218937717 161 HSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIV 210
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-210 2.11e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 338.11  E-value: 2.11e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   1 MTTWLNMSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  81 LRLLYLMDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 218937717 161 HSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIV 210
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-209 9.23e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 331.67  E-value: 9.23e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   1 MTTWLNMSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  81 LRLLYLMDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 218937717 161 HSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPI 209
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-209 3.46e-113

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 322.58  E-value: 3.46e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   1 MTTWLNMSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  81 LRLLYLMDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 218937717 161 HSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPI 209
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-210 4.79e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 314.34  E-value: 4.79e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   1 MTTWLNMSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  81 LRLLYLMDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 218937717 161 HSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIV 210
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-209 1.72e-107

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 308.60  E-value: 1.72e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   7 MSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYL 86
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  87 MDEVHNPTLTLKAVGHQWYWSYEYSDFTK--LEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWT 164
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 218937717 165 IPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:MTH00023 176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPI 220
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-210 1.10e-106

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 305.87  E-value: 1.10e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   1 MTTWLNMSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  81 LRLLYLMDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 218937717 161 HSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIV 210
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 7-209 3.76e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 302.19  E-value: 3.76e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   7 MSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYL 86
Cdd:MTH00185   7 LGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  87 MDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWTIP 166
Cdd:MTH00185  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVP 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 218937717 167 SLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:MTH00185 167 ALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPI 209
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 7-209 8.21e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 301.31  E-value: 8.21e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   7 MSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYL 86
Cdd:MTH00076   7 LGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  87 MDEVHNPTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWTIP 166
Cdd:MTH00076  87 MDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVP 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 218937717 167 SLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:MTH00076 167 SLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPI 209
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-209 4.89e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 294.38  E-value: 4.89e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   7 MSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYL 86
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  87 MDEVHNPTLTLKAVGHQWYWSYEYSDF--TKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWT 164
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 218937717 165 IPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:MTH00051 169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPI 213
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-209 1.81e-85

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: 248.64  E-value: 1.81e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  93 PTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKT 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 218937717 173 DATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPI 117
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-209 5.46e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 229.22  E-value: 5.46e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   95 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 218937717  175 TPGRLNQTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPI 115
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-209 2.64e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 232.61  E-value: 2.64e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   7 MSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMV-TLIRNKQTSRF--MLEGQMIETTWTIAPAIILVFIAMPSLRL 83
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYYwnKLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  84 LYLMDE-VHNPTLTLKAVGHQWYWSYEYSDFTK--LEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVL 160
Cdd:MTH00027 115 LYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEknIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 218937717 161 HSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:MTH00027 195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPI 243
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-209 1.66e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 216.80  E-value: 1.66e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  23 FHDHVLMIMLMITTTVSYMMVTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMdEVHN--PTLTLKAV 100
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYY-GLMNldSNLTVKVT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717 101 GHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLN 180
Cdd:MTH00080 104 GHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILS 183

                        170       180
                 ....*....|....*....|....*....
gi 218937717 181 QTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:MTH00080 184 TLCYSFPMPGVFYGQCSEICGANHSFMPI 212
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-210 8.96e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 176.56  E-value: 8.96e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   6 NMSLQDGASPIMEQLVFFHDHVLMIMLMITT-TVSYMMVTLIR-----NKQTSRFMLEGQMIETTWTIAPAIILVFIAMP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVlVFGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  80 SLRLLYLMDEVHNPTLTLKAVGHQWYWSYEYsdftklefdsymiPQEEQqestfrllDTDNRIVLPINSPIRLIVTAADV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGI--------ATVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 218937717 160 LHSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFK 207
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-210 2.34e-44

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: 146.76  E-value: 2.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   13 ASPIMEQLVFFHDHVLMIMLMITTTV-SYMMVTLIRNKQTSRFML-----EGQMIETTWTIAPAIILV-FIAMPSLRLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVWKFRRKGDEEKpsqihGNRRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717   86 LMDEVHNPTLTLKAVGHQWYWSYEYSdftklefdsymipqeeqqESTFRlldTDNRIVLPINSPIRLIVTAADVLHSWTI 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYP------------------ESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 218937717  166 PSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFK 185
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-209 5.15e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 143.17  E-value: 5.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  17 MEQLVFFHDHVLMIMLM---ITTTVSYMM-VTLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAmpSLRLLYLM-DEVH 91
Cdd:MTH00047   1 MNLSLLYYDIVCYILALcvfIPCWVYIMLcWQVVSGNGSVNFGSENQVLELLWTVVPTLLVLVLC--FLNLNFITsDLDC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  92 NPTLTLKAVGHQWYWSYEYSDftKLEFDSYMipqeeqqesTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVK 171
Cdd:MTH00047  79 FSSETIKVIGHQWYWSYEYSF--GGSYDSFM---------TDDIFGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 218937717 172 TDATPGRLNQTSFSISRPGILYGQCSEICGANHSFMPI 209
Cdd:MTH00047 148 MDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPI 185
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-209 1.82e-34

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 119.92  E-value: 1.82e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717 118 FDSYMIPQEEQQESTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|..
gi 218937717 198 EICGANHSFMPI 209
Cdd:PTZ00047 131 EMCGTLHGFMPI 142
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-207 5.98e-30

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: 106.55  E-value: 5.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  94 TLTLKAVGHQWYWSYEYSDftklefdsymipqeeqqeSTFRLLDTDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKTD 173
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPD------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 218937717 174 ATPGRLNQTSFSISRPGILYGQCSEICGANHSFM 207
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-210 4.08e-29

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: 104.30  E-value: 4.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  95 LTLKAVGHQWYWSYEYSDFTklefdsymipqeeqqestfrlldTDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKTDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 218937717 175 TPGRLNQTSFSISRPGILYGQCSEICGANHSFMPIT 210
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGK 93
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 2.91e-26

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: 96.63  E-value: 2.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717    1 MTTWLNMSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMVTLIR------NKQTSRFMLEGQMIETTWTIAPAIILV 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 218937717   75 FIAMPSLRL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-207 1.95e-24

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: 92.70  E-value: 1.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  94 TLTLKAVGHQWYWSYEYsdftklefdsymiPQEEQQESTFRLLDTdNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKTD 173
Cdd:cd13919    1 ALVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                         90       100       110
                 ....*....|....*....|....*....|....
gi 218937717 174 ATPGRLNQTSFSISRPGILYGQCSEICGANHSFM 207
Cdd:cd13919   67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-207 3.06e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 83.83  E-value: 3.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  94 TLTLKAVGHQWYWSYEYSDFTKlefdsymipqeeqqestfrlldTDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKTD 173
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYPNGKR----------------------EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100       110
                 ....*....|....*....|....*....|....
gi 218937717 174 ATPGRLNQTSFSISRPGILYGQCSEICGANHSFM 207
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 70-207 2.53e-20

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 82.89  E-value: 2.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  70 AIILV-FIAMPSLRLLYLMD---EVHNPTLTLKAVGHQWYWSYEYsdftklefdsymiPQEEQQESTFRLldtdnrivlP 145
Cdd:cd13918    4 AIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEY-------------PNGVTTGNTLRV---------P 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218937717 146 INSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFM 207
Cdd:cd13918   62 ADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 1.26e-18

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 77.45  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  96 TLKAVGHQWYWSYEYsdftklefdsymiPQEEqqestfrlLDTDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKTDAT 175
Cdd:cd13914    2 EIEVEAYQWGWEFSY-------------PEAN--------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                         90       100       110
                 ....*....|....*....|....*....|..
gi 218937717 176 PGRLNQTSFSISRPGILYGQCSEICGANHSFM 207
Cdd:cd13914   61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 138-207 8.64e-10

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 53.73  E-value: 8.64e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717 138 TDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFM 207
Cdd:cd13913   23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 2.74e-06

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 44.29  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717  96 TLKAVGHQWYWSyeysdftklefdsymipqeeqqestfrlLDTDnriVLPINSPIRLIVTAADVLHSWTIPS----LGVK 171
Cdd:cd13916    2 VVAVTGHQWYWE----------------------------LSRT---EIPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 218937717 172 TDATPGRLNQTSFSISRPGILYGQCSEICGANHSFM 207
Cdd:cd13916   51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 138-207 3.34e-05

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: 41.38  E-value: 3.34e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717 138 TDNRIVLPINSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSEICGANHSFM 207
Cdd:cd04212   23 TVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 138-210 9.84e-04

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 37.60  E-value: 9.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218937717 138 TDNRIVLPINSPIRLIVT-AADVLHSWTIPSLGVKTDA---------------TPGRLNQTSFSISRPGILYGQCSEICG 201
Cdd:cd00920   21 GPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGH 100


                 ....*....
gi 218937717 202 aNHSFMPIT 210
Cdd:cd00920  101 -NHAGMVGT 108
 
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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