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Conserved domains on  [gi|745999808|ref|YP_009114617|]
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cytochrome c oxidase subunit II (mitochondrion) [Varecia variegata]

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 1.57e-161

cytochrome c oxidase subunit II; Validated


:

Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 445.32  E-value: 1.57e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 745999808 161 HSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSML 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 1.57e-161

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 445.32  E-value: 1.57e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 745999808 161 HSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSML 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 9.47e-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: 265.20  E-value: 9.47e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  93 PSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVLHSWTVPSLGVKT 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 745999808 173 DAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.18e-79

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 234.23  E-value: 1.18e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   95 LTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVLHSWTVPSLGVKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 745999808  175 IPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-223 2.69e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 158.07  E-value: 2.69e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   6 QLGFQDAASPTMEELLYFHDHTLMIMFLISSLVlyiISLML-------------TTKLTHTSTMdaqeVETVWTILPAAI 72
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLyfairyrrrkgdaDPAQFHHNTK----LEIVWTVIPIII 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  73 LI********ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLcfdsymipcsdlkpgelrlleVDNRVVLPTELSIRT 152
Cdd:COG1622   91 VIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRF 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 745999808 153 LISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWL 223
Cdd:COG1622  150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 2.84e-42

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 141.75  E-value: 2.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   12 AASPTMEELLYFHDHTLMIMFLISSLVLYIISLM-----------LTTKLTHTSTMdaqevETVWTILPAAILI****** 80
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVvwkfrrkgdeeKPSQIHGNRRL-----EYVWTVIPLIIVVGLFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   81 **-ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYenlcfdsymipcsdlkpgelrLLEVDNRVVLPTELSIRTLISSEDV 159
Cdd:TIGR02866  76 AKgLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 745999808  160 LHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWL 223
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 1.57e-161

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 445.32  E-value: 1.57e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 745999808 161 HSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSML 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 2.04e-153

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 424.71  E-value: 2.04e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 745999808 161 HSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSML 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 3.55e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 378.67  E-value: 3.55e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 745999808 161 HSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSML 227
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-227 3.85e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 378.74  E-value: 3.85e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 745999808 161 HSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSML 227
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 1.67e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 354.58  E-value: 1.67e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 745999808 161 HSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSML 227
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 3.54e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 353.36  E-value: 3.54e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 745999808 161 HSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSML 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 1.39e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 344.27  E-value: 1.39e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 745999808 161 HSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLS 225
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-227 9.60e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 334.75  E-value: 9.60e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 745999808 161 HSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSML 227
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 6-226 2.35e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 328.44  E-value: 2.35e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   6 QLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI********ILY 85
Cdd:MTH00140   6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  86 MMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVLHSWTV 165
Cdd:MTH00140  86 LLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 745999808 166 PSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSM 226
Cdd:MTH00140 166 PSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 6.15e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 322.44  E-value: 6.15e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 745999808 161 HSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSM 226
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 5.56e-107

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 307.55  E-value: 5.56e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 745999808 161 HSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLS 225
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-226 2.64e-101

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 293.58  E-value: 2.64e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   2 AHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI******* 81
Cdd:MTH00023  11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  82 *ILYMMDEITSPSLTLKTMGHQWYWSYEYTDY--ENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDV 159
Cdd:MTH00023  91 KLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADV 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 745999808 160 LHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSM 226
Cdd:MTH00023 171 LHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSL 237
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-226 5.67e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 289.76  E-value: 5.67e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   2 AHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI******* 81
Cdd:MTH00051   4 PEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  82 *ILYMMDEITSPSLTLKTMGHQWYWSYEYTDY--ENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDV 159
Cdd:MTH00051  84 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADV 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 745999808 160 LHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSM 226
Cdd:MTH00051 164 LHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 9.47e-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: 265.20  E-value: 9.47e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  93 PSLTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVLHSWTVPSLGVKT 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 745999808 173 DAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-223 3.43e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 240.70  E-value: 3.43e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   4 PVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTTKLTHT---STMDAQEVETVWTILPAAILI****** 80
Cdd:MTH00027  32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  81 **ILYMMDE-ITSPSLTLKTMGHQWYWSYEYTDY--ENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSE 157
Cdd:MTH00027 112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 745999808 158 DVLHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWL 223
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.18e-79

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 234.23  E-value: 1.18e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   95 LTLKTMGHQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVLHSWTVPSLGVKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 745999808  175 IPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-227 3.32e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 219.50  E-value: 3.32e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  23 FHDHTLMIMFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAAILI********ILYMMDEITSPS-LTLKTMG 101
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNLDSnLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808 102 HQWYWSYEYTDYENLCFDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVLHSWTVPSLGVKTDAIPGRLNQ 181
Cdd:MTH00080 105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 745999808 182 ATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWLLSML 227
Cdd:MTH00080 185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLL 230
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-223 2.69e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 158.07  E-value: 2.69e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   6 QLGFQDAASPTMEELLYFHDHTLMIMFLISSLVlyiISLML-------------TTKLTHTSTMdaqeVETVWTILPAAI 72
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLyfairyrrrkgdaDPAQFHHNTK----LEIVWTVIPIII 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  73 LI********ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYENLcfdsymipcsdlkpgelrlleVDNRVVLPTELSIRT 152
Cdd:COG1622   91 VIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRF 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 745999808 153 LISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWL 223
Cdd:COG1622  150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 2.84e-42

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 141.75  E-value: 2.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   12 AASPTMEELLYFHDHTLMIMFLISSLVLYIISLM-----------LTTKLTHTSTMdaqevETVWTILPAAILI****** 80
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVvwkfrrkgdeeKPSQIHGNRRL-----EYVWTVIPLIIVVGLFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808   81 **-ILYMMDEITSPSLTLKTMGHQWYWSYEYTDYenlcfdsymipcsdlkpgelrLLEVDNRVVLPTELSIRTLISSEDV 159
Cdd:TIGR02866  76 AKgLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 745999808  160 LHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWL 223
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-212 1.28e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 139.18  E-value: 1.28e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808 118 FDSYMIPCSDLKPGELRLLEVDNRVVLPTELSIRTLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*
gi 745999808 198 EICGANHSFMPIVLE 212
Cdd:PTZ00047 131 EMCGTLHGFMPIVVE 145
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-214 1.55e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 137.39  E-value: 1.55e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  57 DAQEVETVWTILPAAI-LI********ILYMMDeiTSPSLTLKTMGHQWYWSYEYTDyeNLCFDSYMipcSDLKPGelrl 135
Cdd:MTH00047  45 ENQVLELLWTVVPTLLvLVLCFLNLNFITSDLD--CFSSETIKVIGHQWYWSYEYSF--GGSYDSFM---TDDIFG---- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 745999808 136 leVDNRVVLPTELSIRTLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELI 214
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.45e-30

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: 108.54  E-value: 1.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  95 LTLKTMGHQWYWSYEYTDyenlcfdsymipcsdlkpgelrlLEVDNRVVLPTELSIRTLISSEDVLHSWTVPSLGVKTDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 745999808 175 IPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLE 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), ...
 94-207 1.18e-29

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


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 106.16  E-value: 1.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  94 SLTLKTMGHQWYWSYEYTDYENlcfdsymipcsdlkpgelRLLEVDNRVVLPTELSIRTLISSEDVLHSWTVPSLGVKTD 173
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPG------------------RGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 745999808 174 AIPGRLNQATLMASRPGVYYGQCSEICGANHSFM 207
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-74 5.16e-23

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: 88.93  E-value: 5.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808    1 MAHPVQLGFQDAASPTMEELLYFHDHTLMIMFLISSLVLYIISLMLTT------KLTHTSTMDAQEVETVWTILPAAILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWTIIPAVILI 80
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 6.16e-23

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: 89.24  E-value: 6.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  95 LTLKTMGHQWYWSYEYTDYenlcfDSYMIPCSDLKPGELRLlEVDNRVVLptelsirtLISSEDVLHSWTVPSLGVKTDA 174
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL-PVGRPVLF--------NLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 745999808 175 IPGRLNQATLMASRPGVYYGQCSEICGANHSFM 207
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-223 2.98e-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: 85.58  E-value: 2.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  83 ILYMMDEITSP---SLTLKTMGHQWYWSYEYtdyenlcfdsymipcsdlkPGELrllEVDNRVVLPTELSIRTLISSEDV 159
Cdd:cd13918   18 LLYVEDPPDEAdedALEVEVEGFQFGWQFEY-------------------PNGV---TTGNTLRVPADTPIALRVTSTDV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 745999808 160 LHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWL 223
Cdd:cd13918   76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-223 2.68e-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: 82.46  E-value: 2.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808 101 GHQWYWSYEYTDYENlcfdsymipcsdlkpgelrllEVDNRVVLPTELSIRTLISSEDVLHSWTVPSLGVKTDAIPGRLN 180
Cdd:cd13914    7 AYQWGWEFSYPEANV---------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 745999808 181 QATLMASRPGVYYGQCSEICGANHSFMPIVLELIPLKHFEEWL 223
Cdd:cd13914   66 TIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-207 1.50e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 79.98  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808  94 SLTLKTMGHQWYWSYEYtdyenlcfdsymipcsdlkPGELRlleVDNRVVLPTELSIRTLISSEDVLHSWTVPSLGVKTD 173
Cdd:cd13915    1 ALEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100       110
                 ....*....|....*....|....*....|....
gi 745999808 174 AIPGRLNQATLMASRPGVYYGQCSEICGANHSFM 207
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 4.34e-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: 49.49  E-value: 4.34e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 745999808 140 NRVVLPTELSIRTLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFM 207
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 129-212 1.46e-07

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: 48.38  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808 129 KPGELRLLEVDNRVVLPTELSIR-TLISSEDVLHSWTVPSLGVKTDAI---------------PGRLNQATLMASRPGVY 192
Cdd:cd00920   12 FTYNGVLLFGPPVLVVPVGDTVRvQFVNKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVY 91

                         90       100
                 ....*....|....*....|
gi 745999808 193 YGQCSEICGaNHSFMPIVLE 212
Cdd:cd00920   92 WFYCTIPGH-NHAGMVGTIN 110
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-207 1.85e-05

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 42.15  E-value: 1.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 745999808 140 NRVVLPTELSIRTLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFM 207
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 157-207 1.39e-04

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


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 39.53  E-value: 1.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 745999808 157 EDVLHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFM 207
Cdd:cd04223   37 EDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-207 6.97e-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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 37.75  E-value: 6.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745999808 101 GHQWYWSyeytdyenlcfdsymIPCSDLKPGELrlleVDNRVvlptelsirtliSSEDVLHSWTVPS----LGVKTDAIP 176
Cdd:cd13916    7 GHQWYWE---------------LSRTEIPAGKP----VEFRV------------TSADVNHGFGIYDpdmrLLAQTQAMP 55

                         90       100       110
                 ....*....|....*....|....*....|.
gi 745999808 177 GRLNQATLMASRPGVYYGQCSEICGANHSFM 207
Cdd:cd13916   56 GYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 157-207 2.99e-03

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 38.42  E-value: 2.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 745999808 157 EDVLHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFM 207
Cdd:PRK02888 576 EDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEM 626
 
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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