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Conserved domains on  [gi|1919576460|ref|YP_009943799|]
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cytochrome c oxidase subunit II (mitochondrion) [Acanthisitta chloris]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475905)

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 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 3.24e-168

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 462.08  E-value: 3.24e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLS-SDTVDAQEVELIWTILPAIVLIMLALPS 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVL 159
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1919576460 160 HSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSSLLS 226
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 3.24e-168

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 462.08  E-value: 3.24e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLS-SDTVDAQEVELIWTILPAIVLIMLALPS 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVL 159
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1919576460 160 HSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSSLLS 226
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 4.05e-95

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: 273.68  E-value: 4.05e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  92 PDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVLHSWAVPSLGVKT 171
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1919576460 172 DAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENW 221
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-212 1.67e-85

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 248.86  E-value: 1.67e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  94 LTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVLHSWAVPSLGVKTDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1919576460 174 IPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVES 212
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
60-221 8.36e-55

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 175.02  E-value: 8.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  60 VELIWTILPAIVLIMLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLsfdsymvptaelplghfrlleVDH 139
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460 140 RVVIPMESPIRIIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFE 219
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                  ..
gi 1919576460 220 NW 221
Cdd:COG1622   218 AW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-221 6.52e-42

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: 140.98  E-value: 6.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  12 ASSPIMEELVEFHDHALMVALAICSLVLYLLT-------LMLAEKLSSDTVDAQEVELIWTILPA-IVLIMLALPSLQIL 83
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAyvvwkfrRKGDEEKPSQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  84 YMMDEIDEPDLTLKAIGHQWYWSYEYTDFkdlsfdsymvptaelplghfrLLEVDHRVVIPMESPIRIIVTADDVLHSWA 163
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1919576460 164 VPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENW 221
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 3.24e-168

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 462.08  E-value: 3.24e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLS-SDTVDAQEVELIWTILPAIVLIMLALPS 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVL 159
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1919576460 160 HSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSSLLS 226
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-225 6.29e-135

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 377.91  E-value: 6.29e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLS-SDTVDAQEVELIWTILPAIVLIMLALPS 79
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLThTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVL 159
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1919576460 160 HSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSSLL 225
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-225 4.99e-133

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 373.28  E-value: 4.99e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLSSD-TVDAQEVELIWTILPAIVLIMLALPS 79
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKyILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVL 159
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1919576460 160 HSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSSLL 225
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 1.95e-132

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 371.80  E-value: 1.95e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLSS-DTVDAQEVELIWTILPAIVLIMLALPS 79
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNtNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVL 159
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1919576460 160 HSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSSL 224
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 7.59e-131

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 367.62  E-value: 7.59e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLSSDTV-DAQEVELIWTILPAIVLIMLALPS 79
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLlEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVL 159
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1919576460 160 HSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSSLLS 226
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 1.18e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 351.98  E-value: 1.18e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLSSDTV-DAQEVELIWTILPAIVLIMLALPS 79
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLlDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVL 159
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1919576460 160 HSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSS 223
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-225 4.53e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 350.72  E-value: 4.53e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLSSD-TVDAQEVELIWTILPAIVLIMLALPS 79
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKyILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVL 159
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1919576460 160 HSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSSLL 225
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-227 2.77e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 343.46  E-value: 2.77e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLSSDTV-DAQEVELIWTILPAIVLIMLALPS 79
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTIlEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVL 159
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1919576460 160 HSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSSLLSS 227
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMSE 228
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-223 7.08e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 337.44  E-value: 7.08e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLaekLSSDT----VDAQEVELIWTILPAIVLIMLA 76
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLL---FSSPTnrffLEGQELETIWTIVPAFILIFIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  77 LPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTAD 156
Cdd:MTH00038   78 LPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1919576460 157 DVLHSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSS 223
Cdd:MTH00038  158 DVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-221 2.56e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 333.61  E-value: 2.56e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLSSDT-VDAQEVELIWTILPAIVLIMLALPS 79
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSlLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVL 159
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1919576460 160 HSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENW 221
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-227 3.01e-110

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 315.64  E-value: 3.01e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLSSDTV-DAQEVELIWTILPAIVLIMLALPS 79
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYIlEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  80 LQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVL 159
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1919576460 160 HSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSSLLSS 227
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-227 4.27e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 287.80  E-value: 4.27e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   6 QFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEK-LSSDTVDAQEVELIWTILPAIVLIMLALPSLQILY 84
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKfYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  85 MMDEIDEPDLTLKAIGHQWYWSYEYTDFKD--LSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVLHSW 162
Cdd:MTH00023   95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1919576460 163 AVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSSLLSS 227
Cdd:MTH00023  175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-226 2.20e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 278.20  E-value: 2.20e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   6 QFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLSSDTV-DAQEVELIWTILPAIVLIMLALPSLQILY 84
Cdd:MTH00051    8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLfEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  85 MMDEIDEPDLTLKAIGHQWYWSYEYTDF--KDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVLHSW 162
Cdd:MTH00051   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1919576460 163 AVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENWSSLLS 226
Cdd:MTH00051  168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 4.05e-95

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: 273.68  E-value: 4.05e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  92 PDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVLHSWAVPSLGVKT 171
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1919576460 172 DAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENW 221
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-212 1.67e-85

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 248.86  E-value: 1.67e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  94 LTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVLHSWAVPSLGVKTDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1919576460 174 IPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVES 212
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-221 3.50e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 240.70  E-value: 3.50e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   6 QFGFQDASSPIMEELVEFHDHALMVALAICSLVL-YLLTLMLAEKLSS---DTVDAQEVELIWTILPAIVLIMLALPSLQ 81
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLwLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPSLR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  82 ILYMMDE-IDEPDLTLKAIGHQWYWSYEYTDF--KDLSFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDV 158
Cdd:MTH00027  114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1919576460 159 LHSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENW 221
Cdd:MTH00027  194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 56-225 3.36e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 224.50  E-value: 3.36e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  56 DAQEVELIWTILPAIVLIMLALPSLQILYMMDEID-EPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMVPTAELPLGHFRL 134
Cdd:MTH00080   59 EYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460 135 LEVDHRVVIPMESPIRIIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAP 214
Cdd:MTH00080  139 LEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTL 218

                         170
                  ....*....|.
gi 1919576460 215 LKYFENWSSLL 225
Cdd:MTH00080  219 LDNFKEWCKLL 229
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
60-221 8.36e-55

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 175.02  E-value: 8.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  60 VELIWTILPAIVLIMLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLsfdsymvptaelplghfrlleVDH 139
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460 140 RVVIPMESPIRIIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFE 219
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                  ..
gi 1919576460 220 NW 221
Cdd:COG1622   218 AW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 56-211 5.98e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 153.57  E-value: 5.98e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  56 DAQEVELIWTILPA-IVLIMLALPSLQILYMMDeiDEPDLTLKAIGHQWYWSYEYTDfkDLSFDSYMVPTAELplghfrl 134
Cdd:MTH00047   45 ENQVLELLWTVVPTlLVLVLCFLNLNFITSDLD--CFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG------- 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1919576460 135 leVDHRVVIPMESPIRIIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVE 211
Cdd:MTH00047  114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-221 6.52e-42

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: 140.98  E-value: 6.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  12 ASSPIMEELVEFHDHALMVALAICSLVLYLLT-------LMLAEKLSSDTVDAQEVELIWTILPA-IVLIMLALPSLQIL 83
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAyvvwkfrRKGDEEKPSQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  84 YMMDEIDEPDLTLKAIGHQWYWSYEYTDFkdlsfdsymvptaelplghfrLLEVDHRVVIPMESPIRIIVTADDVLHSWA 163
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1919576460 164 VPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENW 221
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 116-217 1.53e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 131.10  E-value: 1.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460 116 SFDSYMVPTAELPLGHFRLLEVDHRVVIPMESPIRIIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQC 195
Cdd:PTZ00047   50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                          90       100
                  ....*....|....*....|...
gi 1919576460 196 SEICGANHSYMPIVVES-APLKY 217
Cdd:PTZ00047  130 SEMCGTLHGFMPIVVEAvSPEAY 152
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 94-211 2.31e-32

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: 113.16  E-value: 2.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  94 LTLKAIGHQWYWSYEYTDfkdlsfdsymvptaelplghfrlLEVDHRVVIPMESPIRIIVTADDVLHSWAVPSLGVKTDA 173
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1919576460 174 IPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVE 211
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 93-206 1.37e-29

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: 106.16  E-value: 1.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  93 DLTLKAIGHQWYWSYEYTDFKDLSFdsymVPTAELplghfrllevdhrvVIPMESPIRIIVTADDVLHSWAVPSLGVKTD 172
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGI----VTANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1919576460 173 AIPGRLNQTSFITTRPGIFYGQCSEICGANHSYM 206
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-211 5.70e-25

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: 94.24  E-value: 5.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  93 DLTLKAIGHQWYWSYEY--TDFKDLSFDSYMVPTAELPLGHfrllevdhrvvipmesPIRIIVTADDVLHSWAVPSLGVK 170
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYpgGDGKLGTDDDVTSPELHLPVGR----------------PVLFNLRSKDVIHSFWVPEFRVK 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1919576460 171 TDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYM--PIVVE 211
Cdd:cd13919    65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 66-221 3.20e-24

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: 93.67  E-value: 3.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  66 ILPAIVLIMLALPSL-QILYMMD---EIDEPDLTLKAIGHQWYWSYEYTDfkDLSFDSYMVptaelplghfrllevdhrv 141
Cdd:cd13918     1 GLSAIIVISLIVWTYgMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTLR------------------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460 142 vIPMESPIRIIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENW 221
Cdd:cd13918    60 -VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-82 5.64e-22

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: 86.23  E-value: 5.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLAEKLSSD-------TVDAQEVELIWTILPAIVLI 73
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKnpitaryTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1919576460  74 MLALPSLQI 82
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-210 1.23e-21

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 85.37  E-value: 1.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  93 DLTLKAIGHQWYWSYEYTDFKdlsfdsymvptaelplghfrllEVDHRVVIPMESPIRIIVTADDVLHSWAVPSLGVKTD 172
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGK----------------------REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1919576460 173 AIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVV 210
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-221 1.07e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 78.22  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  95 TLKAIGHQWYWSYEYTDFKDLSFDsymvptaelplghfrllevdhRVVIPMESPIRIIVTADDVLHSWAVPSLGVKTDAI 174
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTTSE---------------------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1919576460 175 PGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESAPLKYFENW 221
Cdd:cd13914    61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 141-211 8.35e-10

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: 54.11  E-value: 8.35e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1919576460 141 VVIPMESPIRIIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYM--PIVVE 211
Cdd:cd13913    27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 7.94e-06

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: 43.14  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460  95 TLKAIGHQWYWSyeytdfkdLSfdsymvptaelplghfrllevdhRVVIPMESPIRIIVTADDVLHSWAVPS----LGVK 170
Cdd:cd13916     2 VVAVTGHQWYWE--------LS-----------------------RTEIPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1919576460 171 TDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYM 206
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 141-206 1.36e-05

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: 42.54  E-value: 1.36e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1919576460 141 VVIPMESPIRIIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYM 206
Cdd:cd04212    27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 149-206 1.37e-04

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 39.53  E-value: 1.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1919576460 149 IRIIVT----ADDVLHSWAVPSLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYM 206
Cdd:cd04223    26 VTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 132-211 1.62e-03

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 37.21  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576460 132 FRLLEVDHRVVIPMESPIRIIVT-ADDVLHSWAVPSLGVKTDAI---------------PGRLNQTSFITTRPGIFYGQC 195
Cdd:cd00920    16 GVLLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYWFYC 95

                          90
                  ....*....|....*.
gi 1919576460 196 SEICGaNHSYMPIVVE 211
Cdd:cd00920    96 TIPGH-NHAGMVGTIN 110
 
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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