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Conserved domains on  [gi|1863128842|ref|YP_009865060|]
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cytochrome c oxidase subunit II (mitochondrion) [Scarturus williamsi]

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
 1-226 2.03e-172

cytochrome c oxidase subunit II; Validated


:

Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 472.67  E-value: 2.03e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLSM 226
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 2.03e-172

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 472.67  E-value: 2.03e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLSM 226
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 6.41e-94

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: 270.60  E-value: 6.41e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  93 PSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVLHSWAMPSLGIKT 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1863128842 173 DAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 7.43e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 239.62  E-value: 7.43e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  95 LTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVLHSWAMPSLGIKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1863128842 175 IPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 2.33e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 178.87  E-value: 2.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   6 QLGLQDASSPIMEELMNFHdhtlMIVFLISTLVLYIISAML--------------TTKLTHTSTMdaqeVETIWTILPAI 71
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLF----WVSLIIMLVIFVLVFGLLlyfairyrrrkgdaDPAQFHHNTK----LEIVWTVIPII 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  72 ILVLIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTfdsymipttdlpsgglrllevDNRVVLPMELPIR 151
Cdd:COG1622    90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT---------------------VNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1863128842 152 MLISSEDVLHSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENW 222
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 7.55e-46

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: 150.99  E-value: 7.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  12 ASSPIMEELMNFHDHTLMIVFLISTLVL-YIISAML----------TTKLTHTSTMdaqevETIWTILPAIILV-LIALP 79
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAaLLAYVVWkfrrkgdeekPSQIHGNRRL-----EYVWTVIPLIIVVgLFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  80 SLRILYMMDEINNPSLTVKTMGHQWYWSYEYtdyedltfdsymipttdlPSGGLRlleVDNRVVLPMELPIRMLISSEDV 159
Cdd:TIGR02866  76 AKGLLYLERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863128842 160 LHSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENW 222
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 2.03e-172

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 472.67  E-value: 2.03e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLSM 226
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 1.48e-165

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 455.53  E-value: 1.48e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLSM 226
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 5.76e-146

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 406.02  E-value: 5.76e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLSMV 227
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 2.60e-143

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 399.15  E-value: 2.60e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLSM 226
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 7.34e-137

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 383.08  E-value: 7.34e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLSMV 227
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 4.69e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 378.40  E-value: 4.69e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLSM 226
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 2.82e-129

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 363.53  E-value: 2.82e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLS 225
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-222 5.95e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 360.56  E-value: 5.95e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENW 222
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 8.13e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 345.00  E-value: 8.13e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLSM 226
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 4.73e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 335.53  E-value: 4.73e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLSM 226
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 2.71e-112

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 321.04  E-value: 2.71e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863128842 161 HSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLS 225
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 4-226 5.40e-107

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 307.83  E-value: 5.40e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   4 PFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPSLRI 83
Cdd:MTH00023   13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  84 LYMMDEINNPSLTVKTMGHQWYWSYEYTDYED--LTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVLH 161
Cdd:MTH00023   93 LYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863128842 162 SWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLSM 226
Cdd:MTH00023  173 SFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSL 237
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-222 2.53e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 303.63  E-value: 2.53e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   4 PFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPSLRI 83
Cdd:MTH00051    6 PWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  84 LYMMDEINNPSLTVKTMGHQWYWSYEYTDY--EDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVLH 161
Cdd:MTH00051   86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1863128842 162 SWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENW 222
Cdd:MTH00051  166 SFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINW 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 6.41e-94

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: 270.60  E-value: 6.41e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  93 PSLTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVLHSWAMPSLGIKT 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1863128842 173 DAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 3.11e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 246.09  E-value: 3.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   4 PFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHT---STMDAQEVETIWTILPAIILVLIALPS 80
Cdd:MTH00027   32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  81 LRILYMMDE-INNPSLTVKTMGHQWYWSYEYTDY--EDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSE 157
Cdd:MTH00027  112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863128842 158 DVLHSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENW 222
Cdd:MTH00027  192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 7.43e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 239.62  E-value: 7.43e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  95 LTVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVLHSWAMPSLGIKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1863128842 175 IPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 17-227 1.67e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 225.27  E-value: 1.67e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  17 MEELMNFHDHTLMIVFLISTLVLYIISAMLTTKLTHTSTMDAQEVETIWTILPAIILVLIALPSLRILYMMDEINNPS-L 95
Cdd:MTH00080   19 MDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNLDSnL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  96 TVKTMGHQWYWSYEYTDYEDLTFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVLHSWAMPSLGIKTDAI 175
Cdd:MTH00080   99 TVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1863128842 176 PGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENWSLSMV 227
Cdd:MTH00080  179 SGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLL 230
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 2.33e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 178.87  E-value: 2.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   6 QLGLQDASSPIMEELMNFHdhtlMIVFLISTLVLYIISAML--------------TTKLTHTSTMdaqeVETIWTILPAI 71
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLF----WVSLIIMLVIFVLVFGLLlyfairyrrrkgdaDPAQFHHNTK----LEIVWTVIPII 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  72 ILVLIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLTfdsymipttdlpsgglrllevDNRVVLPMELPIR 151
Cdd:COG1622    90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT---------------------VNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1863128842 152 MLISSEDVLHSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENW 222
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 7.55e-46

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: 150.99  E-value: 7.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  12 ASSPIMEELMNFHDHTLMIVFLISTLVL-YIISAML----------TTKLTHTSTMdaqevETIWTILPAIILV-LIALP 79
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAaLLAYVVWkfrrkgdeekPSQIHGNRRL-----EYVWTVIPLIIVVgLFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  80 SLRILYMMDEINNPSLTVKTMGHQWYWSYEYtdyedltfdsymipttdlPSGGLRlleVDNRVVLPMELPIRMLISSEDV 159
Cdd:TIGR02866  76 AKGLLYLERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863128842 160 LHSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENW 222
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-214 3.41e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 146.64  E-value: 3.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  57 DAQEVETIWTILPA-IILVLIALPSLRILYMMDeiNNPSLTVKTMGHQWYWSYEYTDyeDLTFDSYMiptTDLPSGglrl 135
Cdd:MTH00047   45 ENQVLELLWTVVPTlLVLVLCFLNLNFITSDLD--CFSSETIKVIGHQWYWSYEYSF--GGSYDSFM---TDDIFG---- 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1863128842 136 leVDNRVVLPMELPIRMLISSEDVLHSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVV 214
Cdd:MTH00047  114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-214 3.13e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 130.33  E-value: 3.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842 117 TFDSYMIPTTDLPSGGLRLLEVDNRVVLPMELPIRMLISSEDVLHSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQC 196
Cdd:PTZ00047   50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                          90
                  ....*....|....*...
gi 1863128842 197 SEICGSNHSFMPIVLEVV 214
Cdd:PTZ00047  130 SEMCGTLHGFMPIVVEAV 147
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 4.52e-32

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 112.39  E-value: 4.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  95 LTVKTMGHQWYWSYEYTDyedltfdsymipttdlpsgglrlLEVDNRVVLPMELPIRMLISSEDVLHSWAMPSLGIKTDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1863128842 175 IPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLE 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 1.23e-28

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: 103.85  E-value: 1.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  94 SLTVKTMGHQWYWSYEYtdyedltfdsymipttdlPSGGLRLLEVDNRVVLPMELPIRMLISSEDVLHSWAMPSLGIKTD 173
Cdd:cd04213     1 ALTIEVTGHQWWWEFRY------------------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1863128842 174 AIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFM 207
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 4.60e-28

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: 101.64  E-value: 4.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842   1 MAYPFQLGLQDASSPIMEELMNFHDHTLMIVFLISTLVLYIISAMLTT------KLTHTSTMDAQEVETIWTILPAIILV 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1863128842  75 LIALPSLRI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-214 4.49e-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: 91.93  E-value: 4.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  95 LTVKTMGHQWYWSYEYTDYedltfDSYMIPTTDLPSGGLrllevdnrvVLPMELPIRMLISSEDVLHSWAMPSLGIKTDA 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPEL---------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1863128842 175 IPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVV 214
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKVV 107
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-222 4.83e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 90.59  E-value: 4.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  67 ILPAIILV-LIALPSLRILYMMD---EINNPSLTVKTMGHQWYWSYEYtdyedltfdsymipttdlPSGGLRLlevdNRV 142
Cdd:cd13918     1 GLSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEY------------------PNGVTTG----NTL 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842 143 VLPMELPIRMLISSEDVLHSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENW 222
Cdd:cd13918    59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-213 1.19e-22

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: 88.07  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  94 SLTVKTMGHQWYWSYEYtdyedltfdsymipttdlPSGglrlLEVDNRVVLPMELPIRMLISSEDVLHSWAMPSLGIKTD 173
Cdd:cd13915     1 ALEIQVTGRQWMWEFTY------------------PNG----KREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1863128842 174 AIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEV 213
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 6.19e-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: 81.30  E-value: 6.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  96 TVKTMGHQWYWSYEYTDYEDLTFdsymipttdlpsgglrllevdNRVVLPMELPIRMLISSEDVLHSWAMPSLGIKTDAI 175
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1863128842 176 PGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVPLKHFENW 222
Cdd:cd13914    61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-214 9.07e-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: 48.72  E-value: 9.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863128842 140 NRVVLPMELPIRMLISSEDVLHSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVV 214
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-214 1.19e-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: 42.75  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842  96 TVKTMGHQWYWSyeytdyedltfdsymIPTTDLPSGGlrllevdnrvvlpmelPIRMLISSEDVLHSWAM--PSLGI--K 171
Cdd:cd13916     2 VVAVTGHQWYWE---------------LSRTEIPAGK----------------PVEFRVTSADVNHGFGIydPDMRLlaQ 50

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1863128842 172 TDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVV 214
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTVV 93
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 129-212 2.16e-05

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: 42.22  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863128842 129 PSGGLRLLEVDNRVVLPMELPIRMLISSE-DVLHSWAMPSLGIKTDAI---------------PGRLNQATLTSTRPGLF 192
Cdd:cd00920    12 FTYNGVLLFGPPVLVVPVGDTVRVQFVNKlGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVY 91

                          90       100
                  ....*....|....*....|
gi 1863128842 193 YGQCSEIcGSNHSFMPIVLE 212
Cdd:cd00920    92 WFYCTIP-GHNHAGMVGTIN 110
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-214 1.45e-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: 1.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863128842 140 NRVVLPMELPIRMLISSEDVLHSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVV 214
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 157-215 1.01e-03

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: 37.21  E-value: 1.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1863128842 157 EDVLHSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFMPIVLEVVP 215
Cdd:cd04223    37 EDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLIVEP 95
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 151-207 1.18e-03

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 36.97  E-value: 1.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1863128842 151 RMLISSEDVLHSWAMPSLGIKTDAIPGRLNQATLTSTRPGLFYGQCSEICGSNHSFM 207
Cdd:cd13917    25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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