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Conserved domains on  [gi|1575635774|gb|QBE85411|]
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cytochrome oxidase subunit 2, partial (mitochondrion) [Panorpa bashanicola]

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
 1-184 8.54e-130

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 362.99  E-value: 8.54e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00154   30 ILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00154  110 YSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRP 189

                         170       180
                  ....*....|....*....|....
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00154  190 GLFFGQCSEICGANHSFMPIVIES 213
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-184 8.54e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 362.99  E-value: 8.54e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00154   30 ILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00154  110 YSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRP 189

                         170       180
                  ....*....|....*....|....
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00154  190 GLFFGQCSEICGANHSFMPIVIES 213
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-184 4.18e-89

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: 256.73  E-value: 4.18e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  64 PAITLKTIGHQWYWSYEYSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKV 143
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1575635774 144 DATPGRLNQTSFLINRPGLFFGQCSEICGANHSFMPIVIES 184
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEA 121
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
66-184 1.82e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 234.61  E-value: 1.82e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  66 ITLKTIGHQWYWSYEYSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDA 145
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1575635774 146 TPGRLNQTSFLINRPGLFFGQCSEICGANHSFMPIVIES 184
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
28-183 8.87e-45

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 147.67  E-value: 8.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  28 ESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYEYSDFIALEfdsymipSNELetdgfrll 107
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-------VNEL-------- 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1575635774 108 dvdnraVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRPGLFFGQCSEICGANHSFMPIVIE 183
Cdd:COG1622   140 ------VLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-183 2.42e-34

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: 119.79  E-value: 2.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVlVGYMMSSLFfnTYTNR-------YLLESQGIEVIWTILPA-ITLIFIALPSLRLLYLLDEVSDPAITLKTIG 72
Cdd:TIGR02866  21 TLISLLV-AALLAYVVW--KFRRKgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  73 HQWYWSYEYSDFialefdsymipsneletdGFRlldVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQ 152
Cdd:TIGR02866  98 YQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNA 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1575635774 153 TSFLINRPGLFFGQCSEICGANHSFMPIVIE 183
Cdd:TIGR02866 157 LWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-184 8.54e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 362.99  E-value: 8.54e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00154   30 ILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00154  110 YSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRP 189

                         170       180
                  ....*....|....*....|....
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00154  190 GLFFGQCSEICGANHSFMPIVIES 213
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-184 8.16e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 302.63  E-value: 8.16e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00140   30 VLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00140  110 YSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRP 189

                         170       180
                  ....*....|....*....|....
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00140  190 GVFYGQCSEICGANHSFMPIVVEA 213
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-184 4.41e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 295.47  E-value: 4.41e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00139   30 ILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00139  110 YSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRP 189

                         170       180
                  ....*....|....*....|....
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00139  190 GVFYGQCSEICGANHSFMPIVVEA 213
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-184 1.36e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 291.82  E-value: 1.36e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00117   30 VALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00117  110 YTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRP 189

                         170       180
                  ....*....|....*....|....
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00117  190 GVFYGQCSEICGANHSFMPIVVES 213
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-183 2.28e-101

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 291.37  E-value: 2.28e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00008   30 ILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00008  110 YSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRP 189

                         170       180
                  ....*....|....*....|...
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIE 183
Cdd:MTH00008  190 GVFYGQCSEICGANHSFMPIVLE 212
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-184 1.54e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 284.29  E-value: 1.54e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00038   30 ILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00038  110 YTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRT 189

                         170       180
                  ....*....|....*....|....
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00038  190 GLFYGQCSEICGANHSFMPIVIES 213
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-183 5.20e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 280.33  E-value: 5.20e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00168   30 ILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00168  110 YTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRP 189

                         170       180
                  ....*....|....*....|...
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIE 183
Cdd:MTH00168  190 GSFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-184 2.89e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 268.51  E-value: 2.89e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00129   30 IVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00129  110 YTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRP 189

                         170       180
                  ....*....|....*....|....
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00129  190 GVFYGQCSEICGANHSFMPIVVEA 213
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-184 1.43e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 266.75  E-value: 1.43e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00185   30 IVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00185  110 YTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRP 189

                         170       180
                  ....*....|....*....|....
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00185  190 GLYYGQCSEICGANHSFMPIVVEA 213
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-183 2.34e-90

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 263.50  E-value: 2.34e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00098   30 IVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00098  110 YTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRP 189

                         170       180
                  ....*....|....*....|...
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIE 183
Cdd:MTH00098  190 GLYYGQCSEICGSNHSFMPIVLE 212
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-184 4.79e-90

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 263.15  E-value: 4.79e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00023   39 LLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIA--LEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLIN 158
Cdd:MTH00023  119 YSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIK 198

                         170       180
                  ....*....|....*....|....*.
gi 1575635774 159 RPGLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00023  199 RPGVFYGQCSEICGANHSFMPIVIEA 224
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-184 2.38e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 260.87  E-value: 2.38e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00076   30 AVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00076  110 YTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRP 189

                         170       180
                  ....*....|....*....|....
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00076  190 GVYYGQCSEICGANHSFMPIVVEA 213
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-184 4.18e-89

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: 256.73  E-value: 4.18e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  64 PAITLKTIGHQWYWSYEYSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKV 143
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1575635774 144 DATPGRLNQTSFLINRPGLFFGQCSEICGANHSFMPIVIES 184
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEA 121
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-183 2.24e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 251.24  E-value: 2.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00051   32 ILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIA--LEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLIN 158
Cdd:MTH00051  112 YSDYGTdtIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIK 191

                         170       180
                  ....*....|....*....|....*
gi 1575635774 159 RPGLFFGQCSEICGANHSFMPIVIE 183
Cdd:MTH00051  192 RPGVFYGQCSEICGANHSFMPIVIE 216
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
66-184 1.82e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 234.61  E-value: 1.82e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  66 ITLKTIGHQWYWSYEYSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDA 145
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1575635774 146 TPGRLNQTSFLINRPGLFFGQCSEICGANHSFMPIVIES 184
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-184 2.68e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 201.02  E-value: 2.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNTYTNRYL--LESQGIEVIWTILPAITLIFIALPSLRLLYLLDE-VSDPAITLKTIGHQWYW 77
Cdd:MTH00027   59 LTIIVGVVLWLIIRILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYW 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  78 SYEYSDF--IALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSF 155
Cdd:MTH00027  139 SYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGF 218

                         170       180
                  ....*....|....*....|....*....
gi 1575635774 156 LINRPGLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00027  219 LIKRPGIFYGQCSEICGANHSFMPIVVES 247
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 2-184 1.04e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 196.00  E-value: 1.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   2 VIMITVLVgyMMSSLFFNTYTNRYLLESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVS-DPAITLKTIGHQWYWSYE 80
Cdd:MTH00080   35 VLAFVVFL--FLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDFIALEFDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00080  113 FSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMP 192

                         170       180
                  ....*....|....*....|....
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIES 184
Cdd:MTH00080  193 GVFYGQCSEICGANHSFMPIAVEV 216
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
28-183 8.87e-45

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 147.67  E-value: 8.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  28 ESQGIEVIWTILPAITLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYEYSDFIALEfdsymipSNELetdgfrll 107
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-------VNEL-------- 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1575635774 108 dvdnraVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRPGLFFGQCSEICGANHSFMPIVIE 183
Cdd:COG1622   140 ------VLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 1-183 1.82e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 140.47  E-value: 1.82e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVLVGYMMSSLFFNtytnryllESQGIEVIWTILPAItLIFIALPSLRLLYLLDEVSDPAITLKTIGHQWYWSYE 80
Cdd:MTH00047   26 YIMLCWQVVSGNGSVNFGS--------ENQVLELLWTVVPTL-LVLVLCFLNLNFITSDLDCFSSETIKVIGHQWYWSYE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  81 YSDfiALEFDSYMipsneleTDGFRLldVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRP 160
Cdd:MTH00047   97 YSF--GGSYDSFM-------TDDIFG--VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRH 165

                         170       180
                  ....*....|....*....|...
gi 1575635774 161 GLFFGQCSEICGANHSFMPIVIE 183
Cdd:MTH00047  166 GVFVGYCSELCGVGHSYMPIVIE 188
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 89-184 1.78e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 129.55  E-value: 1.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  89 FDSYMIPSNELETDGFRLLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRPGLFFGQCS 168
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*.
gi 1575635774 169 EICGANHSFMPIVIES 184
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEA 146
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-183 2.42e-34

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: 119.79  E-value: 2.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774   1 IVIMITVlVGYMMSSLFfnTYTNR-------YLLESQGIEVIWTILPA-ITLIFIALPSLRLLYLLDEVSDPAITLKTIG 72
Cdd:TIGR02866  21 TLISLLV-AALLAYVVW--KFRRKgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  73 HQWYWSYEYSDFialefdsymipsneletdGFRlldVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQ 152
Cdd:TIGR02866  98 YQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNA 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1575635774 153 TSFLINRPGLFFGQCSEICGANHSFMPIVIE 183
Cdd:TIGR02866 157 LWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 66-183 3.67e-28

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: 100.83  E-value: 3.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  66 ITLKTIGHQWYWSYEYSDfialefdsymipsneletdgfrlLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDA 145
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1575635774 146 TPGRLNQTSFLINRPGLFFGQCSEICGANHSFMPIVIE 183
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 65-178 1.60e-24

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 91.91  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  65 AITLKTIGHQWYWSYEYSDFIALEFDSymipSNELetdgfrlldvdnraVLPMNTQIRMLVSAADVLHSWTIPALGVKVD 144
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGIVT----ANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1575635774 145 ATPGRLNQTSFLINRPGLFFGQCSEICGANHSFM 178
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 65-178 1.26e-22

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: 86.93  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  65 AITLKTIGHQWYWSYEYSDFIALEFDSYMIPSNELetdgfrlldvdnraVLPMNTQIRMLVSAADVLHSWTIPALGVKVD 144
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1575635774 145 ATPGRLNQTSFLINRPGLFFGQCSEICGANHSFM 178
Cdd:cd13919    67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 65-178 5.34e-21

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 82.68  E-value: 5.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  65 AITLKTIGHQWYWSYEYSDfialefdsymipsneletdGFRlldVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVD 144
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1575635774 145 ATPGRLNQTSFLINRPGLFFGQCSEICGANHSFM 178
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 59-178 8.18e-18

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 75.57  E-value: 8.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  59 DEVSDPAITLKTIGHQWYWSYEYSdfialefdsymipsNELETDgfrlldvdNRAVLPMNTQIRMLVSAADVLHSWTIPA 138
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYP--------------NGVTTG--------NTLRVPADTPIALRVTSTDVFHTFGIPE 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1575635774 139 LGVKVDATPGRLNQTSFLINRPGLFFGQCSEICGANHSFM 178
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 72-178 7.37e-16

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 69.74  E-value: 7.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  72 GHQWYWSYEYSDfialefdsymipSNeletdgfrlLDVDNRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLN 151
Cdd:cd13914     7 AYQWGWEFSYPE------------AN---------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65

                          90       100
                  ....*....|....*....|....*..
gi 1575635774 152 QTSFLINRPGLFFGQCSEICGANHSFM 178
Cdd:cd13914    66 TIKTEATEEGEYQLYCAEYCGAGHSQM 92
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-48 1.90e-08

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: 49.64  E-value: 1.90e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1575635774   1 IVIMITVLVGYMMSSLFF------NTYTNRYLLESQGIEVIWTILPAITLIFIA 48
Cdd:pfam02790  30 ILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 111-178 8.35e-08

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: 47.95  E-value: 8.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1575635774 111 NRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRPGLFFGQCSEICGANHSFM 178
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 111-178 2.63e-06

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: 44.08  E-value: 2.63e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1575635774 111 NRAVLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRPGLFFGQCSEICGANHSFM 178
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 91-183 2.30e-05

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 41.83  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  91 SYMIPSNELETDGFrlldVDNRAVLPMNTQIRM-LVSAADVLHSWTIPALGVKVDA---------------TPGRLNQTS 154
Cdd:cd00920     7 DWGWSFTYNGVLLF----GPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVT 82

                          90       100
                  ....*....|....*....|....*....
gi 1575635774 155 FLINRPGLFFGQCSEICGaNHSFMPIVIE 183
Cdd:cd00920    83 FTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 66-178 6.53e-04

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 37.36  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575635774  66 ITLKTIGHQWYWsyeysdfialefdsymipsnELETDgfrlldvdnraVLPMNTQIRMLVSAADVLHSWTI--PALGV-- 141
Cdd:cd13916     1 QVVAVTGHQWYW--------------------ELSRT-----------EIPAGKPVEFRVTSADVNHGFGIydPDMRLla 49

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1575635774 142 KVDATPGRLNQTSFLINRPGLFFGQCSEICGANHSFM 178
Cdd:cd13916    50 QTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 114-178 3.96e-03

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 35.04  E-value: 3.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1575635774 114 VLPMNTQIRMLVSAADVLHSWTIPALGVKVDATPGRLNQTSFLINRPGLFFGQCSEICGANHSFM 178
Cdd:cd13917    17 VLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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