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Conserved domains on  [gi|594707480|gb|AHM24816|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Vespa basalis]

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
 1-194 9.89e-103

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 295.20  E-value: 9.89e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   1 MQTWMSFYIQDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  81 LKILYMTEEFFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 594707480 161 HSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFG 194
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-194 9.89e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 295.20  E-value: 9.89e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   1 MQTWMSFYIQDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  81 LKILYMTEEFFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 594707480 161 HSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFG 194
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-194 4.07e-60

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: 183.54  E-value: 4.07e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  93 PSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKI 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100
                 ....*....|....*....|..
gi 594707480 173 DASPGRMNQTFIQMIRPGIFFG 194
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYG 102
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-194 1.45e-53

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 166.82  E-value: 1.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   95 LTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|
gi 594707480  175 SPGRMNQTFIQMIRPGIFFG 194
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYG 100
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
59-194 1.05e-32

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 116.85  E-value: 1.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  59 HFIETIWTITPMLTLLMIAIPSLKILYMTEEFFNPSLTVKTIGHQWYWSYELTDYKNVyfdsymipynknnksqfrlldV 138
Cdd:COG1622   77 TKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------T 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 594707480 139 DNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:COG1622  136 VNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRG 191
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 61-194 1.22e-25

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: 97.84  E-value: 1.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   61 IETIWTITPM-LTLLMIAIPSLKILYMTEEFFNPSLTVKTIGHQWYWSYeltDYKNVYFDSymipynknnksqfrlldvD 139
Cdd:TIGR02866  56 LEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDF---EYPESGFTT------------------V 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 594707480  140 NRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYG 169
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-194 9.89e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 295.20  E-value: 9.89e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   1 MQTWMSFYIQDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  81 LKILYMTEEFFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 594707480 161 HSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFG 194
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-194 3.20e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 253.36  E-value: 3.20e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   1 MQTWMSFYIQDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  81 LKILYMTEEFFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVI 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 594707480 161 HSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYG 194
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-194 2.90e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 248.48  E-value: 2.90e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   1 MQTWMSFYIQDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  81 LKILYMTEEFFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVI 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 594707480 161 HSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYG 194
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-194 9.13e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 244.46  E-value: 9.13e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   1 MQTWMSFYIQDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  81 LKILYMTEEFFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVI 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 594707480 161 HSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYG 194
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 10-194 1.08e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 239.43  E-value: 1.08e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  10 QDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPSLKILYMTEE 89
Cdd:MTH00117  10 QDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  90 FFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPALG 169
Cdd:MTH00117  90 INNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLG 169

                        170       180
                 ....*....|....*....|....*
gi 594707480 170 IKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00117 170 VKTDAVPGRLNQTSFITTRPGVFYG 194
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-194 3.40e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 238.06  E-value: 3.40e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   1 MQTWMSFYIQDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  81 LKILYMTEEFFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVI 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 594707480 161 HSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYG 194
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-194 8.15e-77

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 229.74  E-value: 8.15e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   1 MQTWMSFYIQDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  81 LKILYMTEEFFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVI 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 594707480 161 HSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYG 194
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-194 1.46e-74

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 223.83  E-value: 1.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   1 MQTWMSFYIQDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  81 LKILYMTEEFFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVI 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 594707480 161 HSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYG 194
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 10-194 6.44e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 222.28  E-value: 6.44e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  10 QDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPSLKILYMTEE 89
Cdd:MTH00129  10 QDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  90 FFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPALG 169
Cdd:MTH00129  90 INDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALG 169

                        170       180
                 ....*....|....*....|....*
gi 594707480 170 IKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00129 170 VKMDAVPGRLNQTAFIASRPGVFYG 194
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 9-194 7.86e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 217.06  E-value: 7.86e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   9 IQDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPSLKILYMTE 88
Cdd:MTH00185   9 LQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  89 EFFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPAL 168
Cdd:MTH00185  89 EINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPAL 168

                        170       180
                 ....*....|....*....|....*.
gi 594707480 169 GIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00185 169 GVKMDAVPGRLNQATFIISRPGLYYG 194
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 9-194 3.46e-71

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 215.77  E-value: 3.46e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   9 IQDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPSLKILYMTE 88
Cdd:MTH00023  18 FQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  89 EFFNPSLTVKTIGHQWYWSYELTDYK--NVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVP 166
Cdd:MTH00023  98 EVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVP 177

                        170       180
                 ....*....|....*....|....*...
gi 594707480 167 ALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00023 178 SLGLKIDAVPGRLNQTGFFIKRPGVFYG 205
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 10-194 3.99e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 205.01  E-value: 3.99e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  10 QDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPSLKILYMTEE 89
Cdd:MTH00076  10 QDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  90 FFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPALG 169
Cdd:MTH00076  90 INDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLG 169

                        170       180
                 ....*....|....*....|....*
gi 594707480 170 IKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00076 170 IKTDAIPGRLNQTSFIASRPGVYYG 194
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 10-194 1.40e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 201.16  E-value: 1.40e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  10 QDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNEHFIETIWTITPMLTLLMIAIPSLKILYMTEE 89
Cdd:MTH00051  12 QDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  90 FFNPSLTVKTIGHQWYWSYELTDY--KNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPA 167
Cdd:MTH00051  92 VIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS 171

                        170       180
                 ....*....|....*....|....*..
gi 594707480 168 LGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00051 172 LSVKIDAVPGRLNQTSFFIKRPGVFYG 198
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-194 4.07e-60

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: 183.54  E-value: 4.07e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  93 PSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKI 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100
                 ....*....|....*....|..
gi 594707480 173 DASPGRMNQTFIQMIRPGIFFG 194
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYG 102
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-194 1.45e-53

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 166.82  E-value: 1.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   95 LTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|
gi 594707480  175 SPGRMNQTFIQMIRPGIFFG 194
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYG 100
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 10-194 7.59e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 162.12  E-value: 7.59e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  10 QDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLISNKITNRFLTNE---HFIETIWTITPMLTLLMIAIPSLKILYM 86
Cdd:MTH00027  38 QDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYWNKldgSLIEVIWTLIPAFILILIAFPSLRLLYI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  87 TEE-FFNPSLTVKTIGHQWYWSYELTDY--KNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSW 163
Cdd:MTH00027 118 MDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSW 197

                        170       180       190
                 ....*....|....*....|....*....|.
gi 594707480 164 AVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00027 198 TVPSLAVKMDAVPGRINETGFLIKRPGIFYG 228
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 7-194 1.02e-48

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 158.25  E-value: 1.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   7 FYIQDSNTPNMNQLVM-----FHDY--SMLMIITITSIITYMFLFLIS-NKITNRFLTNEHFIETIWTITPMLTLLMIAI 78
Cdd:MTH00080   1 NYFQGYNLNFSNSLFSsymdwFHNFncSLLFGEFVLAFVVFLFLYLISnNFYFKSKKIEYQFGELLCSVFPVLILLMQMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  79 PSLKILYMTE-EFFNPSLTVKTIGHQWYWSYELTDYKNVYFDSYMIPYNKNNKSQFRLLDVDNRLILPFNTQIRVLTTST 157
Cdd:MTH00080  81 PSLSLLYYYGlMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSS 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 594707480 158 DVIHSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00080 161 DVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYG 197
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
59-194 1.05e-32

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 116.85  E-value: 1.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  59 HFIETIWTITPMLTLLMIAIPSLKILYMTEEFFNPSLTVKTIGHQWYWSYELTDYKNVyfdsymipynknnksqfrlldV 138
Cdd:COG1622   77 TKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------T 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 594707480 139 DNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:COG1622  136 VNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRG 191
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 60-194 2.82e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 106.96  E-value: 2.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  60 FIETIWTITPmlTLLMIAIPSLKILYMTEEF-FNPSLTVKTIGHQWYWSYELTDykNVYFDSYMIPYNKNnksqfrlldV 138
Cdd:MTH00047  48 VLELLWTVVP--TLLVLVLCFLNLNFITSDLdCFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------V 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 594707480 139 DNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:MTH00047 115 DKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVG 170
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 61-194 1.22e-25

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: 97.84  E-value: 1.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480   61 IETIWTITPM-LTLLMIAIPSLKILYMTEEFFNPSLTVKTIGHQWYWSYeltDYKNVYFDSymipynknnksqfrlldvD 139
Cdd:TIGR02866  56 LEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDF---EYPESGFTT------------------V 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 594707480  140 NRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYG 169
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 134-194 3.63e-22

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 87.95  E-value: 3.63e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 594707480 134 RLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDASPGRMNQ--TFIQmiRPGIFFG 194
Cdd:PTZ00047  67 RQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKinTFIL--REGVFYG 127
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-194 8.94e-17

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: 72.27  E-value: 8.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  94 SLTVKTIGHQWYWSYEltdYKNvyfdsymipynknnkSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKID 173
Cdd:cd04213    1 ALTIEVTGHQWWWEFR---YPD---------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100
                 ....*....|....*....|.
gi 594707480 174 ASPGRMNQTFIQMIRPGIFFG 194
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRG 83
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 9.44e-15

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: 66.59  E-value: 9.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480    1 MQTWMSFYIQDSNTPNMNQLVMFHDYSMLMIITITSIITYMFLFLI------SNKITNRFLTNEHFIETIWTITPMLTLL 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 594707480   75 MIAIPSLKI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-192 1.49e-13

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: 63.47  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  95 LTVKTIGHQWYWSYELTDyknvyfdsymipynknnksqfrlLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90
                 ....*....|....*...
gi 594707480 175 SPGRMNQTFIQMIRPGIF 192
Cdd:cd13842   58 VPGYTSELWFVADKPGTY 75
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-192 1.81e-12

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: 60.73  E-value: 1.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  95 LTVKTIGHQWYWSYEltdyknvYFDSymipynkNNKSQFRLLDVDNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDA 174
Cdd:cd13919    2 LVVEVTAQQWAWTFR-------YPGG-------DGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90
                 ....*....|....*...
gi 594707480 175 SPGRMNQTFIQMIRPGIF 192
Cdd:cd13919   68 VPGRTTRLWFTPTREGEY 85
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-192 2.70e-12

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: 60.34  E-value: 2.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  94 SLTVKTIGHQWYWSYEltdyknvyfdsymipYnKNNKSQfrlldvDNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKID 173
Cdd:cd13915    1 ALEIQVTGRQWMWEFT---------------Y-PNGKRE------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90
                 ....*....|....*....
gi 594707480 174 ASPGRMNQTFIQMIRPGIF 192
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEY 77
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-180 2.32e-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: 55.49  E-value: 2.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  96 TVKTIGHQWYWSYEltdyknvyfdsymipYNKNNKSQFrlldvdNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDAS 175
Cdd:cd13914    2 EIEVEAYQWGWEFS---------------YPEANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60


                 ....*
gi 594707480 176 PGRMN 180
Cdd:cd13914   61 PGQYN 65
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-192 2.12e-08

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: 50.92  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594707480  95 LTVKTIGHQWYWSYEltdYKNVYFDSymipynknnksqfrlldvdNRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDA 174
Cdd:cd13918   33 LEVEVEGFQFGWQFE---YPNGVTTG-------------------NTLRVPADTPIALRVTSTDVFHTFGIPELRVKADA 90

                         90
                 ....*....|....*...
gi 594707480 175 SPGRMNQTFIQMIRPGIF 192
Cdd:cd13918   91 IPGEYTSTWFEADEPGTY 108
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-194 2.69e-04

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: 38.68  E-value: 2.69e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 594707480 140 NRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDASPGRMNQTFIQMIRPGIFFG 194
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQG 79
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-192 9.43e-03

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: 34.47  E-value: 9.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 594707480 140 NRLILPFNTQIRVLTTSTDVIHSWAVPALGIKIDASPGRMNQTFIQMIRPGIF 192
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEY 77
 
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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