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Conserved domains on  [gi|2732679556|gb|XAT91336|]
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cytochrome c oxidase subunit II (mitochondrion) [Yoldia hyperborea]

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
 1-229 4.49e-94

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 274.78  E-value: 4.49e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556   1 MNLWwwqSYTWLKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMG 80
Cdd:MTH00154    1 MATW---SNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  81 YTSLHLLYIMDEVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGM 160
Cdd:MTH00154   78 LPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2732679556 161 DVIHSWALPSLGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVENY 229
Cdd:MTH00154  158 DVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-229 4.49e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 274.78  E-value: 4.49e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556   1 MNLWwwqSYTWLKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMG 80
Cdd:MTH00154    1 MATW---SNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  81 YTSLHLLYIMDEVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGM 160
Cdd:MTH00154   78 LPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2732679556 161 DVIHSWALPSLGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVENY 229
Cdd:MTH00154  158 DVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 98-225 1.15e-78

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: 232.08  E-value: 1.15e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  98 LTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSLGFKLDC 177
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2732679556 178 IPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKW 225
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
98-215 7.00e-64

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 194.55  E-value: 7.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  98 LTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSLGFKLDC 177
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2732679556 178 IPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVE 215
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
11-231 2.59e-47

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 155.76  E-value: 2.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  11 WLKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLW-----AGYADGVSF-GSQIAEGCWTMGPILILLYMGYTSL 84
Cdd:COG1622    20 SLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIryrrrKGDADPAQFhHNTKLEIVWTVIPIIIVIVLAVPTL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  85 HLLYIMDEVKGCRLTFKILGRQWYWSYEYTDNGVisfdsylvqegdlqvggfrlaEVDNRVVLPEGYNIRALTLGMDVIH 164
Cdd:COG1622   100 RVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI---------------------ATVNELVLPVGRPVRFLLTSADVIH 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2732679556 165 SWALPSLGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVENYKE 231
Cdd:COG1622   159 SFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKA 225
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 16-227 5.13e-38

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: 130.96  E-value: 5.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  16 ASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADG-VSFGSQIAEGCW------TMGPILILLYMGYTSLHLLY 88
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGdEEKPSQIHGNRRleyvwtVIPLIIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  89 IMDEVKGCRLTFKILGRQWYWSYEYTDNGVISfdsylvqegdlqvggfrlaevDNRVVLPEGYNIRALTLGMDVIHSWAL 168
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPESGFTT---------------------VNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2732679556 169 PSLGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVE 227
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-229 4.49e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 274.78  E-value: 4.49e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556   1 MNLWwwqSYTWLKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMG 80
Cdd:MTH00154    1 MATW---SNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  81 YTSLHLLYIMDEVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGM 160
Cdd:MTH00154   78 LPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2732679556 161 DVIHSWALPSLGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVENY 229
Cdd:MTH00154  158 DVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 12-228 9.18e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 266.46  E-value: 9.18e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  12 LKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSLHLLYIMD 91
Cdd:MTH00168    9 LQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  92 EVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSL 171
Cdd:MTH00168   89 EIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2732679556 172 GFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVEN 228
Cdd:MTH00168  169 GLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 12-229 1.58e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 263.12  E-value: 1.58e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  12 LKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSLHLLYIMD 91
Cdd:MTH00139    9 FQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  92 EVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSL 171
Cdd:MTH00139   89 EVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2732679556 172 GFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVENY 229
Cdd:MTH00139  169 GVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 5-228 9.97e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 261.41  E-value: 9.97e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556   5 WWQSYtwLKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSL 84
Cdd:MTH00140    4 WGQLG--FQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  85 HLLYIMDEVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIH 164
Cdd:MTH00140   82 RLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIH 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2732679556 165 SWALPSLGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVEN 228
Cdd:MTH00140  162 SWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 12-228 5.73e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 254.45  E-value: 5.73e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  12 LKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSLHLLYIMD 91
Cdd:MTH00117    9 FQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  92 EVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSL 171
Cdd:MTH00117   89 EINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2732679556 172 GFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVEN 228
Cdd:MTH00117  169 GVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 12-225 3.90e-82

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 244.63  E-value: 3.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  12 LKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSLHLLYIMD 91
Cdd:MTH00098    9 FQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  92 EVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSL 171
Cdd:MTH00098   89 EINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2732679556 172 GFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKW 225
Cdd:MTH00098  169 GLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 12-231 5.02e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 244.23  E-value: 5.02e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  12 LKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSLHLLYIMD 91
Cdd:MTH00038    9 LQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  92 EVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSL 171
Cdd:MTH00038   89 EVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556 172 GFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVENYKE 231
Cdd:MTH00038  169 GVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLE 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 98-225 1.15e-78

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: 232.08  E-value: 1.15e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  98 LTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSLGFKLDC 177
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2732679556 178 IPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKW 225
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 12-231 1.64e-78

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 235.52  E-value: 1.64e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  12 LKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSLHLLYIMD 91
Cdd:MTH00008    9 FQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  92 EVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSL 171
Cdd:MTH00008   89 EVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556 172 GFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVENYKE 231
Cdd:MTH00008  169 GVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 12-225 9.29e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 231.14  E-value: 9.29e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  12 LKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSLHLLYIMD 91
Cdd:MTH00129    9 FQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  92 EVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSL 171
Cdd:MTH00129   89 EINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPAL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2732679556 172 GFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKW 225
Cdd:MTH00129  169 GVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 7-225 5.39e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 229.00  E-value: 5.39e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556   7 QSYTWLKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSLHL 86
Cdd:MTH00185    4 PSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  87 LYIMDEVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSW 166
Cdd:MTH00185   84 LYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSW 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2732679556 167 ALPSLGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKW 225
Cdd:MTH00185  164 TVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 12-225 3.43e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 226.97  E-value: 3.43e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  12 LKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSLHLLYIMD 91
Cdd:MTH00076    9 FQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  92 EVKGCRLTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSL 171
Cdd:MTH00076   89 EINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2732679556 172 GFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKW 225
Cdd:MTH00076  169 GIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 13-231 8.37e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 226.20  E-value: 8.37e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  13 KDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSLHLLYIMDE 92
Cdd:MTH00051   12 QDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  93 VKGCRLTFKILGRQWYWSYEYTDNG--VISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPS 170
Cdd:MTH00051   92 VIDPALTIKAIGHQWYWSYEYSDYGtdTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2732679556 171 LGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVENYKE 231
Cdd:MTH00051  172 LSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSE 232
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 12-228 3.09e-71

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 217.31  E-value: 3.09e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  12 LKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSLHLLYIMD 91
Cdd:MTH00023   18 FQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  92 EVKGCRLTFKILGRQWYWSYEYTD--NGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALP 169
Cdd:MTH00023   98 EVVSPALTIKAIGHQWYWSYEYSDyeGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVP 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2732679556 170 SLGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVEN 228
Cdd:MTH00023  178 SLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
98-215 7.00e-64

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 194.55  E-value: 7.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  98 LTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSLGFKLDC 177
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2732679556 178 IPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVE 215
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 26-231 4.99e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 193.69  E-value: 4.99e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  26 FYDIVMFIVFSIGFLVALCMFYVLWAGYADGVSFGSQIAEGCWTMGPILILLYMGYTSLHLLYIMDEVK-GCRLTFKILG 104
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556 105 RQWYWSYEYTDNGVISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSLGFKLDCIPGRLNQ 184
Cdd:MTH00080  105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2732679556 185 GLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVENYKE 231
Cdd:MTH00080  185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 12-226 1.66e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 177.91  E-value: 1.66e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  12 LKDSASPVFQQMQYFYDIVMFIV-FSIGFLVALCMFYVLWAGYADGV--SFGSQIAEGCWTMGPILILLYMGYTSLHLLY 88
Cdd:MTH00027   37 FQDAGSPVMEEIIMLHDQILFILtIIVGVVLWLIIRILLGNNYYSYYwnKLDGSLIEVIWTLIPAFILILIAFPSLRLLY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  89 IMDE-VKGCRLTFKILGRQWYWSYEYTDNGV--ISFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHS 165
Cdd:MTH00027  117 IMDEcGFSANITIKVTGHQWYWSYSYEDYGEknIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHS 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2732679556 166 WALPSLGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWV 226
Cdd:MTH00027  197 WTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
11-231 2.59e-47

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 155.76  E-value: 2.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  11 WLKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLW-----AGYADGVSF-GSQIAEGCWTMGPILILLYMGYTSL 84
Cdd:COG1622    20 SLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIryrrrKGDADPAQFhHNTKLEIVWTVIPIIIVIVLAVPTL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  85 HLLYIMDEVKGCRLTFKILGRQWYWSYEYTDNGVisfdsylvqegdlqvggfrlaEVDNRVVLPEGYNIRALTLGMDVIH 164
Cdd:COG1622   100 RVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI---------------------ATVNELVLPVGRPVRFLLTSADVIH 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2732679556 165 SWALPSLGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVENYKE 231
Cdd:COG1622   159 SFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKA 225
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 26-217 4.47e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 143.94  E-value: 4.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  26 FYDIVMFIVFSIGFLVALCMFYVLW--AGYADGVSFG--SQIAEGCWTMGPILILLYMGYTSLHLLYiMDEVKGCRLTFK 101
Cdd:MTH00047    7 YYDIVCYILALCVFIPCWVYIMLCWqvVSGNGSVNFGseNQVLELLWTVVPTLLVLVLCFLNLNFIT-SDLDCFSSETIK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556 102 ILGRQWYWSYEYTDNGviSFDSYLVQEGDLqvggfrlaeVDNRVVLPEGYNIRALTLGMDVIHSWALPSLGFKLDCIPGR 181
Cdd:MTH00047   86 VIGHQWYWSYEYSFGG--SYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGR 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2732679556 182 LNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFI 217
Cdd:MTH00047  155 INHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 120-231 9.78e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 134.18  E-value: 9.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556 120 SFDSYLVQEGDLQVGGFRLAEVDNRVVLPEGYNIRALTLGMDVIHSWALPSLGFKLDCIPGRLNQGLLISDRVGVFYGQC 199
Cdd:PTZ00047   50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2732679556 200 SEICGVNHAFMPIVVEFISSEDF----KKWvenYKE 231
Cdd:PTZ00047  130 SEMCGTLHGFMPIVVEAVSPEAYaahaKKY---YKD 162
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 16-227 5.13e-38

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: 130.96  E-value: 5.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  16 ASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGYADG-VSFGSQIAEGCW------TMGPILILLYMGYTSLHLLY 88
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGdEEKPSQIHGNRRleyvwtVIPLIIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  89 IMDEVKGCRLTFKILGRQWYWSYEYTDNGVISfdsylvqegdlqvggfrlaevDNRVVLPEGYNIRALTLGMDVIHSWAL 168
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPESGFTT---------------------VNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2732679556 169 PSLGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWVE 227
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 98-210 1.93e-22

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: 87.68  E-value: 1.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  98 LTFKILGRQWYWSYEYtdngvisfdsylvqeGDLQVGGFRLAevdNRVVLPEGYNIRALTLGMDVIHSWALPSLGFKLDC 177
Cdd:cd04213     2 LTIEVTGHQWWWEFRY---------------PDEPGRGIVTA---NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2732679556 178 IPGRLNQGLLISDRVGVFYGQCSEICGVNHAFM 210
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 98-215 1.11e-19

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: 80.42  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  98 LTFKILGRQWYWSYEYTDNGVisfdsylvqegdlqvggfrlaevDNRVVLPEGYNIRALTLGMDVIHSWALPSLGFKLDC 177
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVRT-----------------------PNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2732679556 178 IPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVE 215
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-215 3.17e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 71.52  E-value: 3.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  98 LTFKILGRQWYWSYEYTDNGVISFDSYLVQEGDLqvggfrlaevdnrvVLPEGYNIRALTLGMDVIHSWALPSLGFKLDC 177
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2732679556 178 IPGRLNQGLLISDRVGVFYGQCSEICGVNHAFM--PIVVE 215
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-214 1.79e-14

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 66.88  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  98 LTFKILGRQWYWSYEYTDNGVIsfdsylvqegdlqvggfrlaevDNRVVLPEGYNIRALTLGMDVIHSWALPSLGFKLDC 177
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPNGKRE----------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2732679556 178 IPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVV 214
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 102-226 8.12e-14

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 65.51  E-value: 8.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556 102 ILGRQWYWSYEYTDNGVISFdsylvqegdlqvggfrlaevdNRVVLPEGYNIRALTLGMDVIHSWALPSLGFKLDCIPGR 181
Cdd:cd13914     5 VEAYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQ 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2732679556 182 LNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWV 226
Cdd:cd13914    64 YNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 86-226 5.98e-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: 61.32  E-value: 5.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556  86 LLYIMD---EVKGCRLTFKILGRQWYWSYEYTdNGVISFdsylvqegdlqvggfrlaevdNRVVLPEGYNIRALTLGMDV 162
Cdd:cd13918    18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYP-NGVTTG---------------------NTLRVPADTPIALRVTSTDV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2732679556 163 IHSWALPSLGFKLDCIPGRLNQGLLISDRVGVFYGQCSEICGVNHAFMPIVVEFISSEDFKKWV 226
Cdd:cd13918    76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 5-86 1.96e-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: 47.33  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679556   5 WWQSYtwLKDSASPVFQQMQYFYDIVMFIVFSIGFLVALCMFYVLWAGY------ADGVSFGSQIAEGCWTMGPILILLY 78
Cdd:pfam02790   4 PWGLG--FQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNrrknpiTARYTTHGQTIEIIWTIIPAVILIL 81


                  ....*...
gi 2732679556  79 MGYTSLHL 86
Cdd:pfam02790  82 IALPSFKL 89
 
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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