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Conserved domains on  [gi|426405935|ref|YP_007025024|]
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cytochrome c oxidase subunit II (mitochondrion) [Peponocephala electra]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475897)

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 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 4.82e-174

cytochrome c oxidase subunit II; Validated


:

Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 476.90  E-value: 4.82e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASML 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 4.82e-174

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 476.90  E-value: 4.82e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASML 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 5.76e-96

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: 275.99  E-value: 5.76e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  93 PSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVLHSWAVPSLGLKT 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 426405935 173 DAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.05e-84

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 246.94  E-value: 1.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   95 LTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVLHSWAVPSLGLKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 426405935  175 IPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 2.38e-57

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 181.57  E-value: 2.38e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   6 QLGLQDAASPVMEELLQFHdhalMIVFLISSLVLYIITLML--------------TTKLTHTNTMdaqeVETIWTVLPAV 71
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLF----WVSLIIMLVIFVLVFGLLlyfairyrrrkgdaDPAQFHHNTK----LEIVWTVIPII 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  72 ILITIALPSLRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLnfdsymiptsdlkpgelrlleVDNRMILPMQMTIR 151
Cdd:COG1622   90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVR 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 426405935 152 MLVSSEDVLHSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASM 226
Cdd:COG1622  149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 7.84e-44

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: 145.99  E-value: 7.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   12 AASPVMEELLQFHDHALMIVFLISSLVLYIITLM-----------LTTKLTHTNTMdaqevETIWTVLPAVILIT-IALP 79
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVvwkfrrkgdeeKPSQIHGNRRL-----EYVWTVIPLIIVVGlFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   80 SLRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYedlnfdsymiptsdlkpgelrLLEVDNRMILPMQMTIRMLVSSEDV 159
Cdd:TIGR02866  76 AKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426405935  160 LHSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKW 222
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 4.82e-174

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 476.90  E-value: 4.82e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASML 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 3.85e-164

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 452.06  E-value: 3.85e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASML 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 8.26e-149

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 413.34  E-value: 8.26e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASML 227
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-227 3.20e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 409.17  E-value: 3.20e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASML 227
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 2.74e-138

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 386.93  E-value: 2.74e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASML 227
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 1.73e-134

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 376.86  E-value: 1.73e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASML 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 3.52e-132

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 370.85  E-value: 3.52e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSAS 225
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-227 1.03e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 367.49  E-value: 1.03e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASML 227
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 5.89e-127

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 358.10  E-value: 5.89e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASM 226
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 4.45e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 342.85  E-value: 4.45e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKW 222
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 8.87e-117

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 332.21  E-value: 8.87e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 426405935 161 HSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSAS 225
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 4-226 1.96e-111

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 319.00  E-value: 1.96e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   4 PFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPSLRI 83
Cdd:MTH00023  13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  84 LYMMDEINNPSLTVKAMGHQWYWSYEYTDYED--LNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVLH 161
Cdd:MTH00023  93 LYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 426405935 162 SWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASM 226
Cdd:MTH00023 173 SFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSL 237
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-226 3.23e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 313.26  E-value: 3.23e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   4 PFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPSLRI 83
Cdd:MTH00051   6 PWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  84 LYMMDEINNPSLTVKAMGHQWYWSYEYTDY--EDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVLH 161
Cdd:MTH00051  86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 426405935 162 SWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASM 226
Cdd:MTH00051 166 SFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 5.76e-96

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: 275.99  E-value: 5.76e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  93 PSLTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVLHSWAVPSLGLKT 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 426405935 173 DAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 1.62e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 254.18  E-value: 1.62e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   4 PFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTTKLTHT---NTMDAQEVETIWTVLPAVILITIALPS 80
Cdd:MTH00027  32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  81 LRILYMMDE-INNPSLTVKAMGHQWYWSYEYTDY--EDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSE 157
Cdd:MTH00027 112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 426405935 158 DVLHSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKW 222
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.05e-84

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 246.94  E-value: 1.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   95 LTVKAMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVLHSWAVPSLGLKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 426405935  175 IPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-227 1.55e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 230.28  E-value: 1.55e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  23 FHDHALMIVFLISSLVLYIITLMLTTKLTHTNTMDAQEVETIWTVLPAVILITIALPSLRILYMMDEINNPS-LTVKAMG 101
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNLDSnLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935 102 HQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVLHSWAVPSLGLKTDAIPGRLNQ 181
Cdd:MTH00080 105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 426405935 182 TTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASML 227
Cdd:MTH00080 185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLL 230
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 2.38e-57

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 181.57  E-value: 2.38e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   6 QLGLQDAASPVMEELLQFHdhalMIVFLISSLVLYIITLML--------------TTKLTHTNTMdaqeVETIWTVLPAV 71
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLF----WVSLIIMLVIFVLVFGLLlyfairyrrrkgdaDPAQFHHNTK----LEIVWTVIPII 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  72 ILITIALPSLRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYEDLnfdsymiptsdlkpgelrlleVDNRMILPMQMTIR 151
Cdd:COG1622   90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVR 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 426405935 152 MLVSSEDVLHSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKWSASM 226
Cdd:COG1622  149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 7.84e-44

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: 145.99  E-value: 7.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   12 AASPVMEELLQFHDHALMIVFLISSLVLYIITLM-----------LTTKLTHTNTMdaqevETIWTVLPAVILIT-IALP 79
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVvwkfrrkgdeeKPSQIHGNRRL-----EYVWTVIPLIIVVGlFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935   80 SLRILYMMDEINNPSLTVKAMGHQWYWSYEYTDYedlnfdsymiptsdlkpgelrLLEVDNRMILPMQMTIRMLVSSEDV 159
Cdd:TIGR02866  76 AKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426405935  160 LHSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKW 222
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-214 3.81e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 143.94  E-value: 3.81e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  57 DAQEVETIWTVLPAVILITIALPSLR-ILYMMDeiNNPSLTVKAMGHQWYWSYEYTDyeDLNFDSYMiptSDLKPGelrl 135
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVLCFLNLNfITSDLD--CFSSETIKVIGHQWYWSYEYSF--GGSYDSFM---TDDIFG---- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 426405935 136 leVDNRMILPMQMTIRMLVSSEDVLHSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELV 214
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-222 1.61e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 138.80  E-value: 1.61e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935 118 FDSYMIPTSDLKPGELRLLEVDNRMILPMQMTIRMLVSSEDVLHSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|....*....
gi 426405935 198 EICGSNHSFMPIVLELVPLENF----EKW 222
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVSPEAYaahaKKY 159
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 4.67e-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: 112.39  E-value: 4.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  95 LTVKAMGHQWYWSYEYTDyedlnfdsymiptsdlkpgelrlLEVDNRMILPMQMTIRMLVSSEDVLHSWAVPSLGLKTDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 426405935 175 IPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLE 212
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 2.11e-29

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: 105.11  E-value: 2.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935    1 MAYPFQLGLQDAASPVMEELLQFHDHALMIVFLISSLVLYIITLMLTT------KLTHTNTMDAQEVETIWTVLPAVILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 426405935   75 TIALPSLRI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-207 3.34e-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: 105.01  E-value: 3.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  94 SLTVKAMGHQWYWSYEYTDYEDLNFdsymiptsdlkpgelrllEVDNRMILPMQMTIRMLVSSEDVLHSWAVPSLGLKTD 173
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPGRGI------------------VTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 426405935 174 AIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFM 207
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 2.52e-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: 95.40  E-value: 2.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  95 LTVKAMGHQWYWSYEYTDYedlnfDSYMIPTSDLKPGELRLlevdnrmilPMQMTIRMLVSSEDVLHSWAVPSLGLKTDA 174
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 426405935 175 IPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFM 207
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-207 4.50e-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: 83.83  E-value: 4.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  94 SLTVKAMGHQWYWSYEYtdyedlnfdsymiptsdlkPGELRlleVDNRMILPMQMTIRMLVSSEDVLHSWAVPSLGLKTD 173
Cdd:cd13915    1 ALEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100       110
                 ....*....|....*....|....*....|....
gi 426405935 174 AIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFM 207
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 68-222 5.63e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 85.20  E-value: 5.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  68 LPAVILIT-IALPSLRILYMMD---EINNPSLTVKAMGHQWYWSYEYtdyedlnfdsymiptsdlkPGElrlLEVDNRMI 143
Cdd:cd13918    2 LSAIIVISlIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEY-------------------PNG---VTTGNTLR 59

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 426405935 144 LPMQMTIRMLVSSEDVLHSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKW 222
Cdd:cd13918   60 VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 1.93e-20

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: 82.84  E-value: 1.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  96 TVKAMGHQWYWSYEYTDYEDLNFDSYMIPTsdlkpgelrllevdNRmilpmQMTIRmlVSSEDVLHSWAVPSLGLKTDAI 175
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEANVTTSEQLVIPA--------------DR-----PVYFR--ITSRDVIHAFHVPELGLKQDAF 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 426405935 176 PGRLNQTTLTSTRPGLFYGQCSEICGSNHSFMPIVLELVPLENFEKW 222
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 ...
 140-207 1.70e-08

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 50.65  E-value: 1.70e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 426405935 140 NRMILPMQMTIRMLVSSEDVLHSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFM 207
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 129-212 1.71e-06

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: 45.30  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935 129 KPGELRLLEVDNRMILPMQMTIRM-LVSSEDVLHSWAVPSLGLKTDAI---------------PGRLNQTTLTSTRPGLF 192
Cdd:cd00920   12 FTYNGVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVY 91

                         90       100
                 ....*....|....*....|
gi 426405935 193 YGQCSEIcGSNHSFMPIVLE 212
Cdd:cd00920   92 WFYCTIP-GHNHAGMVGTIN 110
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 2.65e-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: 44.29  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426405935  96 TVKAMGHQWYWSyeytdyedlnfdsymIPTSDLKPGELrllevdnrmilpmqmtIRMLVSSEDVLHSWAV--PSLGL--K 171
Cdd:cd13916    2 VVAVTGHQWYWE---------------LSRTEIPAGKP----------------VEFRVTSADVNHGFGIydPDMRLlaQ 50

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 426405935 172 TDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFM 207
Cdd:cd13916   51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 149-207 7.66e-04

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 37.35  E-value: 7.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 426405935 149 TIRMLVSSEDVLHSWAVPSLGLKTDAIPGRLNQTTLTSTRPGLFYGQCSEICGSNHSFM 207
Cdd:cd13917   23 TYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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