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Conserved domains on  [gi|6685354|sp|Q37649|]
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RecName: Full=Cytochrome c oxidase subunit 2; AltName: Full=Cytochrome c oxidase polypeptide II

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 1.68e-167

cytochrome c oxidase subunit II; Validated


:

Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 460.34  E-value: 1.68e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSML 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 1.68e-167

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 460.34  E-value: 1.68e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSML 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 1.13e-92

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: 267.51  E-value: 1.13e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   93 PYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVLHSWAVPSLGLKT 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6685354  173 DAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.01e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 241.93  E-value: 1.01e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     95 LTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVLHSWAVPSLGLKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 6685354    175 IPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 1.41e-50

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 164.23  E-value: 1.41e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    6 QLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQE------VETIWTILPAMILIMIALP 79
Cdd:COG1622  18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPAQfhhntkLEIVWTVIPIIIVIVLAVP 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   80 SLRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDmsfdsymvptqdlkpgelrllEVDNRVVLPMELTIRMLISSEDV 159
Cdd:COG1622  98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI---------------------ATVNELVLPVGRPVRFLLTSADV 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6685354  160 LHSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
Cdd:COG1622 157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 4.69e-40

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: 136.36  E-value: 4.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     12 ATSPIMEELLHFHDHALMIVFLISSLVL-YLISVMLTTSLTHTSTMDAQE-----VETIWTILPAMILI-MIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAaLLAYVVWKFRRKGDEEKPSQIhgnrrLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     85 YMMDEINNPYLTVKTMGHQWYWSYEYTDYedmsfdsymvptqdlkpgelrLLEVDNRVVLPMELTIRMLISSEDVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6685354    165 VPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 1.68e-167

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 460.34  E-value: 1.68e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSML 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 2.01e-159

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 440.12  E-value: 2.01e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSML 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 7.50e-144

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 400.63  E-value: 7.50e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSML 227
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-227 7.53e-141

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 392.99  E-value: 7.53e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSML 227
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 3.80e-133

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 373.84  E-value: 3.80e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSML 227
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 3.23e-131

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 368.77  E-value: 3.23e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSML 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 2.24e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 356.21  E-value: 2.24e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSS 225
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-227 1.32e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 352.08  E-value: 1.32e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSML 227
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 1.63e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 339.22  E-value: 1.63e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSM 226
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 4.91e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 327.83  E-value: 4.91e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSM 226
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 2.70e-110

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 316.03  E-value: 2.70e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6685354   161 HSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSS 225
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 4-226 2.96e-102

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 295.89  E-value: 2.96e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     4 PFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPSLRI 83
Cdd:MTH00023  13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    84 LYMMDEINNPYLTVKTMGHQWYWSYEYTDYED--MSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVLH 161
Cdd:MTH00023  93 LYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6685354   162 SWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSM 226
Cdd:MTH00023 173 SFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSL 237
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-226 1.03e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 294.38  E-value: 1.03e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     4 PFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPSLRI 83
Cdd:MTH00051   6 PWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    84 LYMMDEINNPYLTVKTMGHQWYWSYEYTDY--EDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVLH 161
Cdd:MTH00051  86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6685354   162 SWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSM 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 1.13e-92

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: 267.51  E-value: 1.13e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   93 PYLTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVLHSWAVPSLGLKT 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6685354  173 DAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.01e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 241.93  E-value: 1.01e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     95 LTVKTMGHQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVLHSWAVPSLGLKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 6685354    175 IPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 2.89e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 246.09  E-value: 2.89e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     4 PFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTST---MDAQEVETIWTILPAMILIMIALPS 80
Cdd:MTH00027  32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    81 LRILYMMDE-INNPYLTVKTMGHQWYWSYEYTDY--EDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSE 157
Cdd:MTH00027 112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6685354   158 DVLHSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-227 2.23e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 217.18  E-value: 2.23e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    23 FHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMILIMIALPSLRILYMMDEIN-NPYLTVKTMG 101
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   102 HQWYWSYEYTDYEDMSFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQ 181
Cdd:MTH00080 105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6685354   182 TTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSSSML 227
Cdd:MTH00080 185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLL 230
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 1.41e-50

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 164.23  E-value: 1.41e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    6 QLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHTSTMDAQE------VETIWTILPAMILIMIALP 79
Cdd:COG1622  18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPAQfhhntkLEIVWTVIPIIIVIVLAVP 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   80 SLRILYMMDEINNPYLTVKTMGHQWYWSYEYTDYEDmsfdsymvptqdlkpgelrllEVDNRVVLPMELTIRMLISSEDV 159
Cdd:COG1622  98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI---------------------ATVNELVLPVGRPVRFLLTSADV 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6685354  160 LHSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
Cdd:COG1622 157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-218 4.20e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 140.34  E-value: 4.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   117 SFDSYMVPTQDLKPGELRLLEVDNRVVLPMELTIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQC 196
Cdd:PTZ00047  50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                         90       100
                 ....*....|....*....|...
gi 6685354   197 SEICGSNHSFMPIVLELV-PLKY 218
Cdd:PTZ00047 130 SEMCGTLHGFMPIVVEAVsPEAY 152
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 31-214 3.93e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 138.93  E-value: 3.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354    31 VFLISSLVLYLISVMLTTSLTHTSTMDAQEVETIWTILPAMI-LIMIALPSLRILYMMDeiNNPYLTVKTMGHQWYWSYE 109
Cdd:MTH00047  19 VFIPCWVYIMLCWQVVSGNGSVNFGSENQVLELLWTVVPTLLvLVLCFLNLNFITSDLD--CFSSETIKVIGHQWYWSYE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   110 YTDyeDMSFDSYMVPTQDLkpgelrlleVDNRVVLPMELTIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLLSTRP 189
Cdd:MTH00047  97 YSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRH 165

                        170       180
                 ....*....|....*....|....*
gi 6685354   190 GLYYGQCSEICGSNHSFMPIVLELV 214
Cdd:MTH00047 166 GVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 4.69e-40

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: 136.36  E-value: 4.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     12 ATSPIMEELLHFHDHALMIVFLISSLVL-YLISVMLTTSLTHTSTMDAQE-----VETIWTILPAMILI-MIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAaLLAYVVWKFRRKGDEEKPSQIhgnrrLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354     85 YMMDEINNPYLTVKTMGHQWYWSYEYTDYedmsfdsymvptqdlkpgelrLLEVDNRVVLPMELTIRMLISSEDVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6685354    165 VPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 5.78e-31

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: 109.31  E-value: 5.78e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   95 LTVKTMGHQWYWSYEYTDyedmsfdsymvptqdlkpgelrlLEVDNRVVLPMELTIRMLISSEDVLHSWAVPSLGLKTDA 174
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6685354  175 IPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLE 212
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), ...
 95-207 1.16e-27

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: 101.16  E-value: 1.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   95 LTVKTMGHQWYWSYEYTDYEDmsfdsymvptqdlkpgelRLLEVDNRVVLPMELTIRMLISSEDVLHSWAVPSLGLKTDA 174
Cdd:cd04213   2 LTIEVTGHQWWWEFRYPDEPG------------------RGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                        90       100       110
                ....*....|....*....|....*....|...
gi 6685354  175 IPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFM 207
Cdd:cd04213  64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.68e-25

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: 95.09  E-value: 1.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354      1 MAYPFQLGFQDATSPIMEELLHFHDHALMIVFLISSLVLYLISVMLTTSLTHT------STMDAQEVETIWTILPAMILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKnpitarYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 6685354     75 MIALPSLRI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 6.13e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 91.55  E-value: 6.13e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   95 LTVKTMGHQWYWSYEYTDYedmsfDSYMVPTQDLKPGELrllevdnrvVLPMELTIRMLISSEDVLHSWAVPSLGLKTDA 174
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPEL---------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 6685354  175 IPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFM 207
Cdd:cd13919  68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 1.87e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 82.29  E-value: 1.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   95 LTVKTMGHQWYWSYEYtdyedmsfdsymvptqdlkPGELRlleVDNRVVLPMELTIRMLISSEDVLHSWAVPSLGLKTDA 174
Cdd:cd13915   2 LEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                        90       100       110
                ....*....|....*....|....*....|...
gi 6685354  175 IPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFM 207
Cdd:cd13915  60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 1.15e-19

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: 80.53  E-value: 1.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   96 TVKTMGHQWYWSYEYTDYEDMSFDSYMVPTqdlkpgelrllevdNRVVlpmelTIRmlISSEDVLHSWAVPSLGLKTDAI 175
Cdd:cd13914   2 EIEVEAYQWGWEFSYPEANVTTSEQLVIPA--------------DRPV-----YFR--ITSRDVIHAFHVPELGLKQDAF 60

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 6685354  176 PGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
Cdd:cd13914  61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-222 9.36e-19

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: 79.04  E-value: 9.36e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   67 ILPAMILI-MIALPSLRILYMMD---EINNPYLTVKTMGHQWYWSYEYtdyedmsfdsymvptqdlkPGElrlLEVDNRV 142
Cdd:cd13918   1 GLSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEY-------------------PNG---VTTGNTL 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354  143 VLPMELTIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
Cdd:cd13918  59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 1.40e-07

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 47.95  E-value: 1.40e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6685354  140 NRVVLPMELTIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFM 207
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 129-212 1.39e-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: 45.68  E-value: 1.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354  129 KPGELRLLEVDNRVVLPMELTIRMLISSE-DVLHSWAVPSLGLKTDAI---------------PGRLNQTTLLSTRPGLY 192
Cdd:cd00920  12 FTYNGVLLFGPPVLVVPVGDTVRVQFVNKlGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVY 91

                        90       100
                ....*....|....*....|
gi 6685354  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 3.23e-05

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: 41.60  E-value: 3.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6685354   96 TVKTMGHQWYWSyeytdyedmsfdsyMVPTQdLKPGELrlleVDNRVvlpmeltirmliSSEDVLHSWAV--PSLGL--K 171
Cdd:cd13916   2 VVAVTGHQWYWE--------------LSRTE-IPAGKP----VEFRV------------TSADVNHGFGIydPDMRLlaQ 50

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 6685354  172 TDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFM 207
Cdd:cd13916  51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-207 1.26e-04

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 39.84  E-value: 1.26e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6685354  140 NRVVLPMELTIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLLSTRPGLYYGQCSEICGSNHSFM 207
Cdd:cd04212  25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
 
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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