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Conserved domains on  [gi|1922070864|gb|QOU10082|]
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cytochrome c oxidase subunit II (mitochondrion) [Otomys sp. Mount Kenya]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 1000132)

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

CATH:  1.10.287.90
EC:  7.1.1.9
Gene Ontology:  GO:0004129|GO:0005507
PubMed:  6307356|8083153
TCDB:  3.D.4.6.2

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
COX2 super family cl31796
cytochrome c oxidase subunit II; Validated
 1-227 3.54e-102

cytochrome c oxidase subunit II; Validated


The actual alignment was detected with superfamily member MTH00098:

Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 295.09  E-value: 3.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1922070864 161 HAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTSMI 227
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 3.54e-102

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 295.09  E-value: 3.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1922070864 161 HAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTSMI 227
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 1.44e-58

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: 181.23  E-value: 1.44e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  93 PVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVLHAWAVPSLGLKT 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1922070864 173 DAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-210 1.63e-53

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 167.97  E-value: 1.63e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  95 LTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1922070864 175 IPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV 210
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIV 116
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
61-210 2.36e-42

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 143.05  E-value: 2.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  61 VETIWTILPAVILILIALPSLRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDN 140
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864 141 RVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV 210
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFK 207
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 61-222 5.34e-36

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: 125.57  E-value: 5.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  61 VETIWTILPAVILI-LIALPSLRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VD 139
Cdd:TIGR02866  56 LEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFT---------------------TV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864 140 NRVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHF 219
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194


                  ...
gi 1922070864 220 ENW 222
Cdd:TIGR02866 195 DAY 197
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 3.54e-102

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 295.09  E-value: 3.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1922070864 161 HAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTSMI 227
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 9.46e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 276.41  E-value: 9.46e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1922070864 161 HAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTSM 226
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 8.69e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 248.86  E-value: 8.69e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1922070864 161 HAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTSMI 227
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 61-227 4.06e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 246.66  E-value: 4.06e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  61 VETIWTILPAVILILIALPSLRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDN 140
Cdd:MTH00154   61 IEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDN 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864 141 RVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFE 220
Cdd:MTH00154  141 RLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFI 220


                  ....*..
gi 1922070864 221 NWSTSMI 227
Cdd:MTH00154  221 NWIKNMS 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 4.99e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 244.30  E-value: 4.99e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1922070864 161 HAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTSM 226
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-227 1.03e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 240.76  E-value: 1.03e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1922070864 161 HAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTSMI 227
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 3.86e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 239.40  E-value: 3.86e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1922070864 161 HAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTSMI 227
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 9.72e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 233.33  E-value: 9.72e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1922070864 161 HAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTS 225
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 5.05e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 221.13  E-value: 5.05e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1922070864 161 HAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTSM 226
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 1.59e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 217.50  E-value: 1.59e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1922070864 161 HAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTSM 226
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 1.31e-68

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 210.10  E-value: 1.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVL 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1922070864 161 HAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTS 225
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 4-227 2.17e-63

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 197.28  E-value: 2.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   4 PLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPSLRI 83
Cdd:MTH00023   13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  84 LYMMDEINNPVLTVKTMGHQWYWSY************************--*****VDNRVVLPMELPIRMLISSEDVLH 161
Cdd:MTH00023   93 LYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSgdFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1922070864 162 AWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTSMI 227
Cdd:MTH00023  173 SFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-226 2.70e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 194.23  E-value: 2.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   4 PLQLGLQDATSPIME******************************************VETIWTILPAVILILIALPSLRI 83
Cdd:MTH00051    6 PWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  84 LYMMDEINNPVLTVKTMGHQWYWSY***********--******************VDNRVVLPMELPIRMLISSEDVLH 161
Cdd:MTH00051   86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEfdSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1922070864 162 AWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENWSTSM 226
Cdd:MTH00051  166 SFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 1.44e-58

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: 181.23  E-value: 1.44e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  93 PVLTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVLHAWAVPSLGLKT 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1922070864 173 DAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-210 1.63e-53

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 167.97  E-value: 1.63e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  95 LTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1922070864 175 IPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV 210
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIV 116
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 62-223 2.88e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 163.26  E-value: 2.88e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  62 ETIWTILPAVILILIALPSLRILYMMDEIN-NPVLTVKTMGHQWYWSY*****************************VDN 140
Cdd:MTH00080   64 ELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDN 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864 141 RVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFE 220
Cdd:MTH00080  144 RCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFK 223


                  ...
gi 1922070864 221 NWS 223
Cdd:MTH00080  224 EWC 226
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 3.10e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 156.72  E-value: 3.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   4 PLQLGLQDATSPIME************************************---******VETIWTILPAVILILIALPS 80
Cdd:MTH00027   32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYywnKLDGSLIEVIWTLIPAFILILIAFPS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  81 LRILYMMDE-INNPVLTVKTMGHQWYWSY************************--*****VDNRVVLPMELPIRMLISSE 157
Cdd:MTH00027  112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKNIEFDSYMIPTADLEFgdLRLLEVDNRLILPVDTNVRVLITAA 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1922070864 158 DVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENW 222
Cdd:MTH00027  192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
61-210 2.36e-42

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 143.05  E-value: 2.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  61 VETIWTILPAVILILIALPSLRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VDN 140
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864 141 RVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV 210
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFK 207
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 61-222 5.34e-36

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: 125.57  E-value: 5.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  61 VETIWTILPAVILI-LIALPSLRILYMMDEINNPVLTVKTMGHQWYWSY*****************************VD 139
Cdd:TIGR02866  56 LEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFT---------------------TV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864 140 NRVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHF 219
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194


                  ...
gi 1922070864 220 ENW 222
Cdd:TIGR02866 195 DAY 197
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 61-210 1.11e-31

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 114.28  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  61 VETIWTILPAVI-LILIALPSLRILYMMDEINNPvlTVKTMGHQWYWSY*****************************VD 139
Cdd:MTH00047   49 LELLWTVVPTLLvLVLCFLNLNFITSDLDCFSSE--TIKVIGHQWYWSYEYSFGGSYDSFMTDDIFG-----------VD 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1922070864 140 NRVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV 210
Cdd:MTH00047  116 KPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIV 186
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 138-210 1.89e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 107.60  E-value: 1.89e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1922070864 138 VDNRVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV 210
Cdd:PTZ00047   71 VDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIV 143
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-208 1.73e-28

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: 103.14  E-value: 1.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  95 LTVKTMGHQWYWSY*****************************VDNRVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1922070864 175 IPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMP 208
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYML 91
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 4.63e-22

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: 86.90  E-value: 4.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  95 LTVKTMGHQWYW--SY*****************************vdNRVVLPMELPIRMLISSEDVLHAWAVPSLGLKT 172
Cdd:cd04213     2 LTIEVTGHQWWWefRYPDEPGRGIVTA--------------------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKM 61

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1922070864 173 DAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFM 207
Cdd:cd04213    62 DMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 1.97e-18

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: 77.30  E-value: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  95 LTVKTMGHQWYWSY*****************************vdNRVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDA 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTS--------------PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1922070864 175 IPGRLNQATVTSNRPGLFYGQCSEICGSNHSFM 207
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 139-207 1.28e-17

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: 74.97  E-value: 1.28e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1922070864 139 DNRVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFM 207
Cdd:cd13915    24 INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-222 2.85e-17

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: 75.18  E-value: 2.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  67 ILPAVILI-LIALPSLRILYMMD---EINNPVLTVKTMGHQWYWSY*****************************vdNRV 142
Cdd:cd13918     1 GLSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTG----------------------NTL 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864 143 VLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIV*****LKHFENW 222
Cdd:cd13918    59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 139-207 4.77e-16

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: 71.29  E-value: 4.77e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1922070864 139 DNRVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFM 207
Cdd:cd13914    24 SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 2.47e-08

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 50.26  E-value: 2.47e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1922070864 140 NRVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFM 207
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 6.38e-07

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: 46.17  E-value: 6.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864   1 MAYPLQLGLQDATSPIME***------***************************************VETIWTILPAVILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLelhdyiMFILTLILILVLYILVTCLIRFNRRKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1922070864  75 LIALPSLRI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 1.28e-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: 42.37  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864  96 TVKTMGHQWYWSY*****************************vdNRVVLPMELPIRMLISSEDVLHAWAV--PSLGL--K 171
Cdd:cd13916     2 VVAVTGHQWYWEL-------------------------------SRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQ 50

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1922070864 172 TDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFM 207
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-207 3.84e-05

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 41.38  E-value: 3.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1922070864 140 NRVVLPMELPIRMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFM 207
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 151-207 9.15e-04

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 37.35  E-value: 9.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1922070864 151 RMLISSEDVLHAWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFM 207
Cdd:cd13917    25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 138-210 3.58e-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: 36.05  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922070864 138 VDNRVVLPMELPIRMLISSE-DVLHAWAVPSLGLKTDAI---------------PGRLNQATVTSNRPGLFYGQCSEIcG 201
Cdd:cd00920    21 GPPVLVVPVGDTVRVQFVNKlGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYWFYCTIP-G 99


                  ....*....
gi 1922070864 202 SNHSFMPIV 210
Cdd:cd00920   100 HNHAGMVGT 108
 
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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