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Conserved domains on  [gi|160415267|gb|ABX38970|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Manthichorula grandis]

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
 1-195 3.25e-126

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 354.52  E-value: 3.25e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQ 195
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-195 3.25e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 354.52  E-value: 3.25e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQ 195
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-195 1.85e-63

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: 192.01  E-value: 1.85e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  93 PLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKV 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100
                 ....*....|....*....|...
gi 160415267 173 DATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQ 103
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-195 3.19e-58

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 178.76  E-value: 3.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   95 ITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|.
gi 160415267  175 TPGRLNQVSFTPIRSSIMYGQ 195
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQ 101
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
60-195 9.03e-33

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 117.24  E-value: 9.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  60 LIEVIWTILPAITLIFIALPSLRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVefdsymipmtemnnfnfrlldVD 139
Cdd:COG1622   78 KLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TV 136

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 160415267 140 NRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:COG1622  137 NELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 57-195 1.02e-24

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: 95.53  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   57 EGQLIEVIWTILPA-ITLIFIALPSLRLIYILDETNNPLITVKTIGHQWYWSYEYSDFknvefdsymipmtemnnfnfrL 135
Cdd:TIGR02866  52 GNRRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------G 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  136 LDVDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:TIGR02866 111 FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGF 170
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-195 3.25e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 354.52  E-value: 3.25e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQ 195
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-195 1.00e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 285.07  E-value: 1.00e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQ 195
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-195 1.12e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 282.60  E-value: 1.12e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQ 195
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-195 1.13e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 272.17  E-value: 1.13e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQ 195
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-195 1.33e-92

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 269.80  E-value: 1.33e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQ 195
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-195 1.92e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 269.16  E-value: 1.92e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQ 195
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-195 9.92e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 260.02  E-value: 9.92e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQ 195
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-195 1.17e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 241.93  E-value: 1.17e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQ 195
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-195 8.57e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 239.79  E-value: 8.57e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQ 195
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-195 3.61e-80

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 238.08  E-value: 3.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQ 195
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-195 7.91e-80

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 237.73  E-value: 7.91e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   7 LLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPSLRLIYI 86
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  87 LDETNNPLITVKTIGHQWYWSYEYSDFK--NVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVIHSWT 164
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                        170       180       190
                 ....*....|....*....|....*....|.
gi 160415267 165 VPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00023 176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQ 206
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-195 1.21e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 234.29  E-value: 1.21e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  81 LRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQ 195
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-195 1.19e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 224.27  E-value: 1.19e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   7 LLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPSLRLIYI 86
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  87 LDETNNPLITVKTIGHQWYWSYEYSDF--KNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVIHSWT 164
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                        170       180       190
                 ....*....|....*....|....*....|.
gi 160415267 165 VPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00051 169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQ 199
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-195 1.85e-63

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: 192.01  E-value: 1.85e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  93 PLITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKV 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100
                 ....*....|....*....|...
gi 160415267 173 DATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQ 103
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-195 3.19e-58

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 178.76  E-value: 3.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   95 ITVKTIGHQWYWSYEYSDFKNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|.
gi 160415267  175 TPGRLNQVSFTPIRSSIMYGQ 195
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQ 101
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-195 8.66e-56

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 177.52  E-value: 8.66e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   7 LLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFFNKFIHRFL---LEGQLIEVIWTILPAITLIFIALPSLRL 83
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  84 IYILDETN-NPLITVKTIGHQWYWSYEYSDF--KNVEFDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVI 160
Cdd:MTH00027 115 LYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160415267 161 HSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00027 195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQ 229
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 45-195 1.70e-48

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 157.48  E-value: 1.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  45 LFFNKFIHRFLLEGQLIEVIWTILPAITLIFIALPSLRLIYILDETN-NPLITVKTIGHQWYWSYEYSDFKNVEFDSYMI 123
Cdd:MTH00080  47 ISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMK 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160415267 124 PMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:MTH00080 127 SLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQ 198
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-188 4.74e-34

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 119.29  E-value: 4.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  57 EGQLIEVIWTILPaiTLIFIALPSLRLIYIL-DETNNPLITVKTIGHQWYWSYEYSDfkNVEFDSYMIPMTEMnnfnfrl 135
Cdd:MTH00047  45 ENQVLELLWTVVP--TLLVLVLCFLNLNFITsDLDCFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG------- 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 160415267 136 ldVDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDATPGRLNQVSFTPIR 188
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDR 164
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
60-195 9.03e-33

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 117.24  E-value: 9.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  60 LIEVIWTILPAITLIFIALPSLRLIYILDETNNPLITVKTIGHQWYWSYEYSDFKNVefdsymipmtemnnfnfrlldVD 139
Cdd:COG1622   78 KLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TV 136

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 160415267 140 NRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:COG1622  137 NELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 57-195 1.02e-24

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: 95.53  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267   57 EGQLIEVIWTILPA-ITLIFIALPSLRLIYILDETNNPLITVKTIGHQWYWSYEYSDFknvefdsymipmtemnnfnfrL 135
Cdd:TIGR02866  52 GNRRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------G 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  136 LDVDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:TIGR02866 111 FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGF 170
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-195 1.15e-22

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 89.11  E-value: 1.15e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160415267 118 FDSYMIPMTEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDATPGRLNQVSFTPIRSSIMYGQ 195
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.78e-17

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: 73.52  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267    1 MATWKLLLLQDSASPLMEQLSFFHDHTLLILVIITILVGQMLAGLFF------NKFIHRFLLEGQLIEVIWTILPAITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 160415267   75 FIALPSLRL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-186 6.23e-15

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: 66.94  E-value: 6.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  95 ITVKTIGHQWYWSYEYSDfknvefdsymipmtemnnfnfrlLDVDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90
                 ....*....|..
gi 160415267 175 TPGRLNQVSFTP 186
Cdd:cd13842   58 VPGYTSELWFVA 69
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-195 2.04e-14

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: 66.10  E-value: 2.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  95 ITVKTIGHQWYWSYEYSDFKNVEFDSymipmtemnnfnfrlldvDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDA 174
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90       100
                 ....*....|....*....|.
gi 160415267 175 TPGRLNQVSFTPIRSSIMYGQ 195
Cdd:cd04213   64 IPGRTNRLWLQADEPGVYRGQ 84
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-188 8.13e-14

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: 64.58  E-value: 8.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  95 ITVKTIGHQWYWSYEYSDfknvefdsymipmtEMNNFNFRLLDVDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDA 174
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPG--------------GDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90
                 ....*....|....
gi 160415267 175 TPGRLNQVSFTPIR 188
Cdd:cd13919   68 VPGRTTRLWFTPTR 81
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-186 8.40e-13

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: 61.49  E-value: 8.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  95 ITVKTIGHQWYWSYEYSDFKnvefdsymipmTEmnnfnfrlldvDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDA 174
Cdd:cd13915    2 LEIQVTGRQWMWEFTYPNGK-----------RE-----------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90
                 ....*....|..
gi 160415267 175 TPGRLNQVSFTP 186
Cdd:cd13915   60 VPGRYTYLWFEA 71
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-182 2.68e-10

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: 55.11  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  95 ITVKTIGHQWYWSYEYSdfknvefdsymipmtEMNNFNFrlldvdNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDA 174
Cdd:cd13914    1 VEIEVEAYQWGWEFSYP---------------EANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                 ....*...
gi 160415267 175 TPGRLNQV 182
Cdd:cd13914   60 FPGQYNTI 67
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 63-185 4.88e-07

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: 47.06  E-value: 4.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415267  63 VIWTILpaiTLIFIALPSlrliyilDETNNPLITVKTIGHQWYWSYEYSDfknvefdsymiPMTEMNNfnfrlldvdnrM 142
Cdd:cd13918   11 IVWTYG---MLLYVEDPP-------DEADEDALEVEVEGFQFGWQFEYPN-----------GVTTGNT-----------L 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 160415267 143 VVPYLSQIRMLITAADVIHSWTVPSLGIKVDATPGRLNQVSFT 185
Cdd:cd13918   59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFE 101
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 117-185 8.75e-04

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 37.16  E-value: 8.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160415267 117 EFDSYMIPMTemnnFNFRlldvDNRMVVPYLSQIRMLITAADVIHSWTVPSLGIKVDATPGRLNQVSFT 185
Cdd:cd13913   10 EYEVYVVAQA----FAFN----PNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYT 70
 
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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