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Conserved domains on  [gi|1063639017|gb|AOO35100|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Arcyptera sp. ISS-2016]

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 2.97e-136

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 379.94  E-value: 2.97e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQ 195
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-195 2.97e-136

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 379.94  E-value: 2.97e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 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 ...
 95-195 3.22e-62

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: 188.93  E-value: 3.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  95 ITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVLHSWTVPAIGIKIDA 174
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|.
gi 1063639017 175 TPGRLNQGTFTINRPGLFFGQ 195
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQ 103
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-195 1.60e-58

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 179.53  E-value: 1.60e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  95 ITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVLHSWTVPAIGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|.
gi 1063639017 175 TPGRLNQGTFTINRPGLFFGQ 195
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQ 101
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-195 2.47e-39

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 134.19  E-value: 2.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   6 NLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGySLMYMLIIKYTNRN-------MLHGHLIETVWTALPAITLIFIAM 78
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVF-GLLLYFAIRYRRRKgdadpaqFHHNTKLEIVWTVIPIIIVIVLAV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  79 PSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYsdfidvefdvymipemdlENEGFrllDVDNRTILPMNTEVRILTSASD 158
Cdd:COG1622    97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY------------------PDQGI---ATVNELVLPVGRPVRFLLTSAD 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1063639017 159 VLHSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:COG1622   156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-195 8.90e-31

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: 111.32  E-value: 8.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  13 ASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMlIIKYTNRN------MLHGH-LIETVWTALPA-ITLIFIAMPSLRLL 84
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYV-VWKFRRKGdeekpsQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  85 YLLDDSVDAMITIKTIGRQWYWSYEYsdfidvefdvymipemdlENEGFRlldVDNRTILPMNTEVRILTSASDVLHSWT 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063639017 165 VPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGF 170
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-195 2.97e-136

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 379.94  E-value: 2.97e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQ 195
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-195 2.84e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 286.42  E-value: 2.84e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQ 195
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-195 4.43e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 283.53  E-value: 4.43e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQ 195
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-195 1.33e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 282.21  E-value: 1.33e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQ 195
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-195 7.68e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 275.43  E-value: 7.68e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQ 195
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-195 1.37e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 269.54  E-value: 1.37e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQ 195
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-195 1.91e-92

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 269.42  E-value: 1.91e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQ 195
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-195 1.25e-83

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 246.94  E-value: 1.25e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQ 195
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-195 1.97e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 246.34  E-value: 1.97e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQ 195
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-195 6.98e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 245.01  E-value: 6.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQ 195
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-195 1.61e-82

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 244.66  E-value: 1.61e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   7 LSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPSLRLLYL 86
Cdd:MTH00023   16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  87 LDDSVDAMITIKTIGRQWYWSYEYSDFID--VEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVLHSWT 164
Cdd:MTH00023   96 MDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063639017 165 VPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00023  176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQ 206
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-195 5.96e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 240.07  E-value: 5.96e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVL 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063639017 161 HSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQ 195
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-195 9.11e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 240.07  E-value: 9.11e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   7 LSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPSLRLLYL 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  87 LDDSVDAMITIKTIGRQWYWSYEYSDF--IDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVLHSWT 164
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063639017 165 VPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 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 ...
 95-195 3.22e-62

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: 188.93  E-value: 3.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  95 ITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVLHSWTVPAIGIKIDA 174
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|.
gi 1063639017 175 TPGRLNQGTFTINRPGLFFGQ 195
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQ 103
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-195 1.56e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 189.47  E-value: 1.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   7 LSLQDGASPMMEQLSFFHDHtmiVLLMITVIVGYSLMYMLIIKYTNR------NMLHGHLIETVWTALPAITLIFIAMPS 80
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQ---ILFILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  81 LRLLYLLDDSV-DAMITIKTIGRQWYWSYEYSDF--IDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSAS 157
Cdd:MTH00027  112 LRLLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063639017 158 DVLHSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:MTH00027  192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQ 229
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-195 1.60e-58

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 179.53  E-value: 1.60e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  95 ITIKTIGRQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVLHSWTVPAIGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|.
gi 1063639017 175 TPGRLNQGTFTINRPGLFFGQ 195
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQ 101
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-195 7.55e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 158.63  E-value: 7.55e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  23 FHDHTMIVLLMITVIVGYSLMYMLIIKYTNRNMLHGHLIETVWTALPAITLIFIAMPSLRLLYLLD-DSVDAMITIKTIG 101
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017 102 RQWYWSYEYSDFIDVEFDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVLHSWTVPAIGIKIDATPGRLNQ 181
Cdd:MTH00080  105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                         170
                  ....*....|....
gi 1063639017 182 GTFTINRPGLFFGQ 195
Cdd:MTH00080  185 LCYSFPMPGVFYGQ 198
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-195 2.47e-39

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 134.19  E-value: 2.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   6 NLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGySLMYMLIIKYTNRN-------MLHGHLIETVWTALPAITLIFIAM 78
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVF-GLLLYFAIRYRRRKgdadpaqFHHNTKLEIVWTVIPIIIVIVLAV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  79 PSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYsdfidvefdvymipemdlENEGFrllDVDNRTILPMNTEVRILTSASD 158
Cdd:COG1622    97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY------------------PDQGI---ATVNELVLPVGRPVRFLLTSAD 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1063639017 159 VLHSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:COG1622   156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-195 8.90e-31

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: 111.32  E-value: 8.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  13 ASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMlIIKYTNRN------MLHGH-LIETVWTALPA-ITLIFIAMPSLRLL 84
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYV-VWKFRRKGdeekpsQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  85 YLLDDSVDAMITIKTIGRQWYWSYEYsdfidvefdvymipemdlENEGFRlldVDNRTILPMNTEVRILTSASDVLHSWT 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063639017 165 VPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGF 170
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 60-194 9.14e-27

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 100.80  E-value: 9.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  60 LIETVWTALPaiTLIFIAMPSLRLLYLLDDSVDAMI-TIKTIGRQWYWSYEYSDfiDVEFDVYMIPEMDLENEGFRLLdv 138
Cdd:MTH00047   48 VLELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFGVDKPLRLV-- 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063639017 139 dnrtilpMNTEVRILTSASDVLHSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFG 194
Cdd:MTH00047  122 -------YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVG 170
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 5.40e-24

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: 90.47  E-value: 5.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017   1 MATWSNLSLQDGASPMMEQLSFFHDHTMIVLLMITVIVGYSLMYMLI------IKYTNRNMLHGHLIETVWTALPAITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1063639017  75 FIAMPSLRL 83
Cdd:pfam02790  81 LIALPSFKL 89
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-195 8.55e-23

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 89.49  E-value: 8.55e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063639017 118 FDVYMIPEMDLENEGFRLLDVDNRTILPMNTEVRILTSASDVLHSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-195 9.24e-16

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: 69.25  E-value: 9.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  95 ITIKTIGRQWYWSYEYSDfidvefdvymipemdlenegfrlLDVDNRTILPMNTEVRILTSASDVLHSWTVPAIGIKIDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100
                  ....*....|....*....|.
gi 1063639017 175 TPGRLNQGTFTINRPGLFFGQ 195
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTII 78
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-195 8.76e-15

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: 66.87  E-value: 8.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  95 ITIKTIGRQWYWSYEYSDfidvefdvymipemdLENEGFRLLdvdNRTILPMNTEVRILTSASDVLHSWTVPAIGIKIDA 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPD---------------EPGRGIVTA---NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100
                  ....*....|....*....|.
gi 1063639017 175 TPGRLNQGTFTINRPGLFFGQ 195
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQ 84
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-192 5.84e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 64.57  E-value: 5.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  95 ITIKTIGRQWYWSYEYSDfidvefdvymipemdleneGFRlldVDNRTILPMNTEVRILTSASDVLHSWTVPAIGIKIDA 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90
                  ....*....|....*...
gi 1063639017 175 TPGRLNQGTFTINRPGLF 192
Cdd:cd13915    60 VPGRYTYLWFEATKPGEY 77
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-195 3.13e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 63.04  E-value: 3.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  95 ITIKTIGRQWYWSYEYsdfidvefdvymiPEMDlENEGFRLLDVDNRTILPMNTEVRILTSASDVLHSWTVPAIGIKIDA 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRY-------------PGGD-GKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100
                  ....*....|....*....|.
gi 1063639017 175 TPGRLNQGTFTINRPGLFFGQ 195
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVR 88
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-180 6.66e-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: 54.34  E-value: 6.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  95 ITIKTIGRQWYWSYEYSDfidvefdvymipemdlENegfrlLDVDNRTILPMNTEVRILTSASDVLHSWTVPAIGIKIDA 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPE----------------AN-----VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                  ....*.
gi 1063639017 175 TPGRLN 180
Cdd:cd13914    60 FPGQYN 65
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-190 5.62e-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: 5.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639017  83 LLYLLD---DSVDAMITIKTIGRQWYWSYEYSdfidvefdvymipemdleNEGFRLldvdNRTILPMNTEVRILTSASDV 159
Cdd:cd13918    18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYP------------------NGVTTG----NTLRVPADTPIALRVTSTDV 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063639017 160 LHSWTVPAIGIKIDATPGRLNQGTFTINRPG 190
Cdd:cd13918    76 FHTFGIPELRVKADAIPGEYTSTWFEADEPG 106
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 144-192 2.16e-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: 36.01  E-value: 2.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1063639017 144 LPMNTEVRILTSASDVLHSWTVPAIGIKIDATPGRLNQGTFTINRPGLF 192
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEY 77
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-195 8.92e-03

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 34.45  E-value: 8.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063639017 140 NRTILPMNTEVRILTSASDVLHSWTVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 195
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80
 
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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