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Conserved domains on  [gi|1238858212|ref|XP_022245860|]
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LOW QUALITY PROTEIN: uncharacterized protein LOC106462804 [Limulus polyphemus]

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
 1-220 1.93e-114

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 326.02  E-value: 1.93e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFI 220
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFI 220
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-220 1.93e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 326.02  E-value: 1.93e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFI 220
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFI 220
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-221 7.76e-74

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: 219.36  E-value: 7.76e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  93 PTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVIHA*TVLALGIKI 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1238858212 173 DAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFIE 221
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLS 129
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 6.58e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 196.48  E-value: 6.58e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  95 LTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVIHA*TVLALGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1238858212 175 IPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
67-214 1.75e-36

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 127.64  E-value: 1.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  67 IIPALILIFITLPSLRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDftsiefdsyiisetEGSsasfrllDVDDRTGLPI 146
Cdd:COG1622    85 VIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD--------------QGI-------ATVNELVLPV 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238858212 147 NTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESV 214
Cdd:COG1622   144 GRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVV 211
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 67-219 2.34e-28

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: 105.93  E-value: 2.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  67 IIPALILIFITLPS-LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTsiefdsyiisetegssasfrlLDVDDRTGLP 145
Cdd:TIGR02866  62 VIPLIIVVGLFAATaKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESG---------------------FTTVNELVLP 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238858212 146 INTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSF 219
Cdd:TIGR02866 121 AGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-220 1.93e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 326.02  E-value: 1.93e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFI 220
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFI 220
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-221 1.58e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 285.84  E-value: 1.58e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFIE 221
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLE 221
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-221 1.68e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 280.67  E-value: 1.68e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFIE 221
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVK 221
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-219 1.86e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 275.25  E-value: 1.86e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSF 219
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHF 219
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-221 1.59e-92

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 270.57  E-value: 1.59e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFIE 221
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMK 221
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-220 1.98e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 264.92  E-value: 1.98e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFI 220
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFE 220
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-219 6.44e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 261.56  E-value: 6.44e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSF 219
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTF 219
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-220 1.15e-84

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 251.21  E-value: 1.15e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   6 HLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPSLRLLY 85
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  86 LIDEISNPTLTVK*IGHQGY*SYEYSDFTS--IEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVIHA* 163
Cdd:MTH00023   95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1238858212 164 TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFI 220
Cdd:MTH00023  175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYI 231
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-219 2.54e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 247.32  E-value: 2.54e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSF 219
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHF 219
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-219 1.80e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 245.18  E-value: 1.80e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSF 219
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHF 219
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-220 4.36e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 241.61  E-value: 4.36e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFI 220
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFL 220
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-219 5.78e-81

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 241.16  E-value: 5.78e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVI 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1238858212 161 HA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSF 219
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYF 219
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-221 6.12e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 233.90  E-value: 6.12e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   7 LLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKIINTIYNSFTNRVLLEEQETETL*TIIPALILIFITLPSLRLLYL 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  87 IDEISNPTLTVK*IGHQGY*SYEYSDF--TSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVIHA*T 164
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1238858212 165 VLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFIE 221
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYIN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-221 7.76e-74

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: 219.36  E-value: 7.76e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  93 PTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVIHA*TVLALGIKI 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1238858212 173 DAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFIE 221
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLS 129
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 6.58e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 196.48  E-value: 6.58e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  95 LTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVIHA*TVLALGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1238858212 175 IPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-221 7.25e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 188.70  E-value: 7.25e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   6 HLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKII-----NTIYNSFTNRVLLEEQETETL*tIIPALILIFITLPS 80
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrillgNNYYSYYWNKLDGSLIEVIWT--LIPAFILILIAFPS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  81 LRLLYLIDE-ISNPTLTVK*IGHQGY*SYEYSDF--TSIEFDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAA 157
Cdd:MTH00027  112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238858212 158 DVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFIE 221
Cdd:MTH00027  192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYID 255
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 67-221 3.28e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 180.98  E-value: 3.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  67 IIPALILIFITLPSLRLLYLIdEISN--PTLTVK*IGHQGY*SYEYSDFTSIEFDSYIISETEGSSASFRLLDVDDRTGL 144
Cdd:MTH00080   69 VFPVLILLMQMVPSLSLLYYY-GLMNldSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVL 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238858212 145 PINTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSFIE 221
Cdd:MTH00080  148 PCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKE 224
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
67-214 1.75e-36

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 127.64  E-value: 1.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  67 IIPALILIFITLPSLRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDftsiefdsyiisetEGSsasfrllDVDDRTGLPI 146
Cdd:COG1622    85 VIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD--------------QGI-------ATVNELVLPV 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238858212 147 NTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESV 214
Cdd:COG1622   144 GRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVV 211
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-219 2.25e-33

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 117.61  E-value: 2.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212 118 FDSYIISETEGSSASFRLLDVDDRTGLPINTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 1238858212 198 EICGANHSFIPIVVESVNTSSF 219
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 67-218 2.88e-33

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 118.52  E-value: 2.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  67 IIPALILIFitLPSLRLLYLIDEIS-NPTLTVK*IGHQGY*SYEYSDftSIEFDSYIISETEGssasfrlldVDDRTGLP 145
Cdd:MTH00047   55 VVPTLLVLV--LCFLNLNFITSDLDcFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------VDKPLRLV 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238858212 146 INTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSS 218
Cdd:MTH00047  122 YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 67-219 2.34e-28

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: 105.93  E-value: 2.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  67 IIPALILIFITLPS-LRLLYLIDEISNPTLTVK*IGHQGY*SYEYSDFTsiefdsyiisetegssasfrlLDVDDRTGLP 145
Cdd:TIGR02866  62 VIPLIIVVGLFAATaKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESG---------------------FTTVNELVLP 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238858212 146 INTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSF 219
Cdd:TIGR02866 121 AGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 7.41e-21

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: 83.11  E-value: 7.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  95 LTVK*IGHQGY*SYEYSDFTSiefdsyiisetegssasfrlldvDDRTGLPINTQIRLIITAADVIHA*TVLALGIKIDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVRT-----------------------PNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1238858212 175 IPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 144-205 5.84e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 76.14  E-value: 5.84e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238858212 144 LPINTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHS 205
Cdd:cd13919    37 LPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHY 98
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 144-205 3.81e-17

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


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 73.81  E-value: 3.81e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238858212 144 LPINTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHS 205
Cdd:cd04213    33 IPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHA 94
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 144-205 3.08e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 71.12  E-value: 3.08e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238858212 144 LPINTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHS 205
Cdd:cd13915    29 VPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHS 90
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 139-205 4.94e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 63.20  E-value: 4.94e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238858212 139 DDRTGLPINTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHS 205
Cdd:cd13914    24 SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHS 90
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-219 1.27e-12

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 62.86  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212  67 IIPALILI-FITLPSLRLLYLID---EISNPTLTVK*IGHQGY*SYEYSDftsiefdsyiisetEGSSASFRLLdvddrt 142
Cdd:cd13918     1 GLSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPN--------------GVTTGNTLRV------ 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238858212 143 glPINTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANHSFIPIVVESVNTSSF 219
Cdd:cd13918    61 --PADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEF 135
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 144-204 1.33e-07

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: 1.33e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238858212 144 LPINTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANH 204
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGH 89
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 3.64e-07

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: 46.56  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238858212   1 MAT*SHLLFQDRASPTIE*IIFFHDHTIIILTLITTLVGYKII------NTIYNSFTNRVLLEEQETETL*TIIPALILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVtclirfNRRKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1238858212  75 FITLPSLRL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 144-202 1.41e-04

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 39.84  E-value: 1.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1238858212 144 LPINTQIRLIITAADVIHA*TVLALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGA 202
Cdd:cd04212    29 IPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGE 87
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 140-204 6.08e-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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 35.05  E-value: 6.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238858212 140 DRTGLPINTQIRLIITAADVIHA*TV----LALGIKIDAIPGRLNQYSIIINRPGLFFGQCSEICGANH 204
Cdd:cd13916    15 SRTEIPAGKPVEFRVTSADVNHGFGIydpdMRLLAQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAH 83
 
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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