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Conserved domains on  [gi|2745580022|gb|XBW51131|]
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cytochrome c oxidase subunit II (mitochondrion) [Lampetra planeri]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-229 5.36e-160

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 441.63  E-value: 5.36e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESWTTDVLES 229
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEE 229
 
Name Accession Description Interval E-value
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-229 5.36e-160

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 441.63  E-value: 5.36e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESWTTDVLES 229
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEE 229
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 1.83e-92

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 267.13  E-value: 1.83e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  93 PHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVIHSWTIPSLGTKV 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2745580022 173 DAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 9.40e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 236.92  E-value: 9.40e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  95 LTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVIHSWTIPSLGTKVDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2745580022 175 VPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 4.24e-59

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 185.80  E-value: 4.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   6 QLGLQDAASPIMEELIHFHDHTLTVVFLISVLIF-YLITLMVTTRFTNKHSLDSQE-----VEIVWTVMPAIVLIMIALP 79
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFgLLLYFAIRYRRRKGDADPAQFhhntkLEIVWTVIPIIIVIVLAVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  80 SLRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEfdsymtpTNELepggirlldvdhriVVPMESPIRMLITSEDV 159
Cdd:COG1622    98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-------VNEL--------------VLPVGRPVRFLLTSADV 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2745580022 160 IHSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:COG1622   157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 3.43e-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: 152.15  E-value: 3.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  12 AASPIMEELIHFHDHTLTVVFLISVLIFYLITLmVTTRFTNKHSLD-------SQEVEIVWTVMPA-IVLIMIALPSLRI 83
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAY-VVWKFRRKGDEEkpsqihgNRRLEYVWTVIPLiIVVGLFAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  84 LYLTDEISDPHLTIKAVGHQWYWSYEYTDYNqiefdsyMTPTNELepggirlldvdhriVVPMESPIRMLITSEDVIHSW 163
Cdd:TIGR02866  80 LYLERPIPKDALKVKVTGYQWWWDFEYPESG-------FTTVNEL--------------VLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2745580022 164 TIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-229 5.36e-160

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 441.63  E-value: 5.36e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESWTTDVLES 229
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEE 229
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-224 1.15e-153

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 425.48  E-value: 1.15e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESWTT 224
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSS 224
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-229 1.89e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 409.87  E-value: 1.89e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESWTTDVLES 229
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLED 229
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 1.55e-141

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 394.86  E-value: 1.55e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESWTTDVL 227
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-222 9.00e-140

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 390.34  E-value: 9.00e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 3.11e-136

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 381.43  E-value: 3.11e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESWTTDVLE 228
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 6.40e-136

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 380.48  E-value: 6.40e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESWTT 224
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 4.58e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 355.93  E-value: 4.58e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESWTTDVLES 229
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-222 2.44e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 346.16  E-value: 2.44e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKW 222
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 1.44e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 336.69  E-value: 1.44e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-224 6.87e-111

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 317.57  E-value: 6.87e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  81 LRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVI 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2745580022 161 HSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESWTT 224
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-222 5.80e-103

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 297.82  E-value: 5.80e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   6 QLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPSLRILY 85
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  86 LTDEISDPHLTIKAVGHQWYWSYEYTDYNQ--IEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVIHSW 163
Cdd:MTH00023   95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2745580022 164 TIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:MTH00023  175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 233
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-222 1.23e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 294.38  E-value: 1.23e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   6 QLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTTRFTNKHSLDSQEVEIVWTVMPAIVLIMIALPSLRILY 85
Cdd:MTH00051    8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  86 LTDEISDPHLTIKAVGHQWYWSYEYTDY--NQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVIHSW 163
Cdd:MTH00051   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2745580022 164 TIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:MTH00051  168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINW 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 1.83e-92

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 267.13  E-value: 1.83e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  93 PHLTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVIHSWTIPSLGTKV 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2745580022 173 DAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-222 5.72e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 243.01  E-value: 5.72e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   6 QLGLQDAASPIMEELIHFHDHTLTVV-FLISVLIFYLITLMVTTRFTNKH--SLDSQEVEIVWTVMPAIVLIMIALPSLR 82
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFILtIIVGVVLWLIIRILLGNNYYSYYwnKLDGSLIEVIWTLIPAFILILIAFPSLR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  83 ILYLTDE-ISDPHLTIKAVGHQWYWSYEYTDYNQ--IEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDV 159
Cdd:MTH00027  114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEknIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2745580022 160 IHSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:MTH00027  194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 9.40e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 236.92  E-value: 9.40e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  95 LTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVIHSWTIPSLGTKVDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2745580022 175 VPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-222 8.87e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 226.04  E-value: 8.87e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  23 FHDHTLTVVFLISVLIF----YLITLMVTTRFTNKHSlDSQEVEIVWTVMPAIVLIMIALPSLRILYLTDEIS-DPHLTI 97
Cdd:MTH00080   22 FHNFNCSLLFGEFVLAFvvflFLYLISNNFYFKSKKI-EYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  98 KAVGHQWYWSYEYTDYNQIEFDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVIHSWTIPSLGTKVDAVPG 177
Cdd:MTH00080  101 KVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSG 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2745580022 178 RLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:MTH00080  181 ILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW 225
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 4.24e-59

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 185.80  E-value: 4.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   6 QLGLQDAASPIMEELIHFHDHTLTVVFLISVLIF-YLITLMVTTRFTNKHSLDSQE-----VEIVWTVMPAIVLIMIALP 79
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFgLLLYFAIRYRRRKGDADPAQFhhntkLEIVWTVIPIIIVIVLAVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  80 SLRILYLTDEISDPHLTIKAVGHQWYWSYEYTDYNQIEfdsymtpTNELepggirlldvdhriVVPMESPIRMLITSEDV 159
Cdd:COG1622    98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-------VNEL--------------VLPVGRPVRFLLTSADV 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2745580022 160 IHSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:COG1622   157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 3.43e-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: 152.15  E-value: 3.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  12 AASPIMEELIHFHDHTLTVVFLISVLIFYLITLmVTTRFTNKHSLD-------SQEVEIVWTVMPA-IVLIMIALPSLRI 83
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAY-VVWKFRRKGDEEkpsqihgNRRLEYVWTVIPLiIVVGLFAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  84 LYLTDEISDPHLTIKAVGHQWYWSYEYTDYNqiefdsyMTPTNELepggirlldvdhriVVPMESPIRMLITSEDVIHSW 163
Cdd:TIGR02866  80 LYLERPIPKDALKVKVTGYQWWWDFEYPESG-------FTTVNEL--------------VLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2745580022 164 TIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-214 3.67e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 149.33  E-value: 3.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  57 DSQEVEIVWTVMPAivLIMIALPSLRILYLTDEISD-PHLTIKAVGHQWYWSYEYTdyNQIEFDSYMTptnelepGGIRL 135
Cdd:MTH00047   45 ENQVLELLWTVVPT--LLVLVLCFLNLNFITSDLDCfSSETIKVIGHQWYWSYEYS--FGGSYDSFMT-------DDIFG 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2745580022 136 LDVDHRIVvpMESPIRMLITSEDVIHSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAV 214
Cdd:MTH00047  114 VDKPLRLV--YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-218 8.61e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 129.17  E-value: 8.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022 118 FDSYMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSEDVIHSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 2745580022 198 EICGANHSFMPIALEAV-PLSY 218
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVsPEAY 152
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.95e-31

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 110.85  E-value: 1.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  95 LTIKAVGHQWYWSYEYTDYNqiefdsymtptnelepggirlldVDHRIVVPMESPIRMLITSEDVIHSWTIPSLGTKVDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2745580022 175 VPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALE 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 7.90e-30

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: 106.94  E-value: 7.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  94 HLTIKAVGHQWYWSYEYTDYNQIEFdsymTPTNElepggirlldvdhrIVVPMESPIRMLITSEDVIHSWTIPSLGTKVD 173
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGI----VTANE--------------LHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2745580022 174 AVPGRLNQATFITIRPGLYFGQCSEICGANHSFM 207
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 1.08e-25

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 96.16  E-value: 1.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  95 LTIKAVGHQWYWSYEYtdynqiefdsymtptnelePGGIRLLDVdhrIVVPMESPIRMLITSEDVIHSWTIPSLGTKVDA 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTY-------------------PNGKREINE---LHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2745580022 175 VPGRLNQATFITIRPGLYFGQCSEICGANHSFM 207
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 1.73e-25

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 95.79  E-value: 1.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  95 LTIKAVGHQWYWSYEYTDYNQIEFDSYMTPTNELepggirlldvdhriVVPMESPIRMLITSEDVIHSWTIPSLGTKVDA 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2745580022 175 VPGRLNQATFITIRPGLYFGQCSEICGANHSFM 207
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 2.83e-24

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: 92.01  E-value: 2.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022   1 MAQQAQLGLQDAASPIMEELIHFHDHTLTVVFLISVLIFYLITLMVTT------RFTNKHSLDSQEVEIVWTVMPAIVLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 2745580022  75 MIALPSLRI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 71-222 5.18e-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: 90.21  E-value: 5.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  71 IVLIMIALPSLRILYLTD---EISDPHLTIKAVGHQWYWSYEYTdyNQIEFDSYMtptnelepggirlldvdhriVVPME 147
Cdd:cd13918     6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYP--NGVTTGNTL--------------------RVPAD 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2745580022 148 SPIRMLITSEDVIHSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:cd13918    64 TPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 5.94e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 84.00  E-value: 5.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  96 TIKAVGHQWYWSYEYTDYNQIEFDsymtptnelepggirlldvdhRIVVPMESPIRMLITSEDVIHSWTIPSLGTKVDAV 175
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTTSE---------------------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2745580022 176 PGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAVPLSYFESW 222
Cdd:cd13914    61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 95-214 3.76e-10

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: 55.25  E-value: 3.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  95 LTIKAVGHQWYWSYEYTDYNqIEfdsymtPTNELepggirlldvdhriVVPMESPIRMLITSEDVIHSWTIPSLGTKVDA 174
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQG-IA------TVNEL--------------VIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYA 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2745580022 175 VPGRLNQATFITIRPGLYFGQCSEICGANHSFMPIALEAV 214
Cdd:cd04212    60 MAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 142-207 1.22e-09

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: 53.73  E-value: 1.22e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2745580022 142 IVVPMESPIRMLITSEDVIHSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFM 207
Cdd:cd13913    27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 1.01e-06

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 45.45  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  96 TIKAVGHQWYWSyeytdynqiefdsyMTPTnelepggirlldvdhriVVPMESPIRMLITSEDVIHSWTIPS----LGTK 171
Cdd:cd13916     2 VVAVTGHQWYWE--------------LSRT-----------------EIPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2745580022 172 VDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFM 207
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 58-229 2.40e-06

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 47.49  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022  58 SQEVE-IVWTVmPAIVLIMIALpslrILYLTDEISDPH---------LTIKAVGHQWYWSYEYTDYNqiefdsyMTPTNE 127
Cdd:PRK10525   85 SNKVEaVVWTV-PILIIIFLAV----LTWKTTHALEPSkplahdekpITIEVVSMDWKWFFIYPEQG-------IATVNE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022 128 lepggirlldvdhrIVVPMESPIRMLITSEDVIHSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFM 207
Cdd:PRK10525  153 --------------IAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGM 218

                         170       180
                  ....*....|....*....|...
gi 2745580022 208 PIALEAVP-LSYFESWTTDVLES 229
Cdd:PRK10525  219 KFKAIATPdRAEFDQWVAKAKQS 241
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 157-207 5.17e-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: 37.98  E-value: 5.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2745580022 157 EDVIHSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFM 207
Cdd:cd04223    37 EDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 121-209 4.76e-03

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 35.67  E-value: 4.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745580022 121 YMTPTNELEPGGIRLLDVDHRIVVPMESPIRMLITSE-DVIHSWTIPSLGTKVDA---------------VPGRLNQATF 184
Cdd:cd00920     4 TASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVQFVNKlGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTF 83

                          90       100
                  ....*....|....*....|....*
gi 2745580022 185 ITIRPGLYFGQCSEICGaNHSFMPI 209
Cdd:cd00920    84 TTDQAGVYWFYCTIPGH-NHAGMVG 107
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 157-207 7.95e-03

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 36.88  E-value: 7.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2745580022 157 EDVIHSWTIPSLGTKVDAVPGRLNQATFITIRPGLYFGQCSEICGANHSFM 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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