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Conserved domains on  [gi|5881421|ref|NP_007758|]
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cytochrome c oxidase subunit II (mitochondrion) [Branchiostoma floridae]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475937)

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 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 4.83e-150

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 416.30  E-value: 4.83e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCD 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
 
Name Accession Description Interval E-value
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 4.83e-150

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 416.30  E-value: 4.83e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCD 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 1.74e-93

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: 269.83  E-value: 1.74e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   93 PQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKM 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 5881421  173 DAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.48e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 230.76  E-value: 3.48e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     95 LTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 5881421    175 VPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-222 4.05e-62

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 193.51  E-value: 4.05e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    1 MATPAQLGLMDAASPVMEEMIYFHDhVMLVLILITCLIFYSMLVLISSKYIYR-------FLTDGHVIETVWTVIPAIIL 73
Cdd:COG1622  13 LLLSGQLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVLVFGLLLYFAIRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIV 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   74 VVVALPSLKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYyDIEfdsymlplgdlskgdarlleVDNRVVLPVDTSVRVL 153
Cdd:COG1622  92 IVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQ-GIA--------------------TVNELVLPVGRPVRFL 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5881421  154 VTAADVIHSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGW 222
Cdd:COG1622 151 LTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 1.40e-48

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: 158.31  E-value: 1.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     12 AASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLI------SSKYIYRFLTDGHVIETVWTVIPAIILVVV-ALPSLKLL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLfAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     85 YLTDELDNPQLTIKSVGHQWYWSYEYTDYydiefdsymlplgdlskgdarLLEVDNRVVLPVDTSVRVLVTAADVIHSWT 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5881421    165 VPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 4.83e-150

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 416.30  E-value: 4.83e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCD 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 9.16e-144

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 400.36  E-value: 9.16e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCDMML 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 1.55e-138

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 387.52  E-value: 1.55e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCDMMLDE 229
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.12e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 367.32  E-value: 1.12e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCDMML 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-229 6.34e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 350.55  E-value: 6.34e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCDMMLDE 229
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLED 229
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-223 4.56e-123

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 348.25  E-value: 4.56e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWC 223
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 3.47e-122

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 345.94  E-value: 3.47e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCDMML 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 6.66e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 345.39  E-value: 6.66e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCDMM 226
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-229 5.64e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 338.01  E-value: 5.64e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCDMMLDE 229
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEE 229
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 1.98e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 326.35  E-value: 1.98e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCDMMLD 228
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-222 2.36e-114

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 326.43  E-value: 2.36e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVI 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5881421   161 HSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGW 222
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-222 8.47e-114

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 325.17  E-value: 8.47e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     2 ATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPSL 81
Cdd:MTH00023  11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    82 KLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYYD--IEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADV 159
Cdd:MTH00023  91 KLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADV 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5881421   160 IHSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGW 222
Cdd:MTH00023 171 LHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 233
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-229 3.72e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 315.95  E-value: 3.72e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     4 PAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPSLKL 83
Cdd:MTH00051   6 PWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    84 LYLTDELDNPQLTIKSVGHQWYWSYEYTDY--YDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVIH 161
Cdd:MTH00051  86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5881421   162 SWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCDMMLDE 229
Cdd:MTH00051 166 SFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 1.74e-93

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: 269.83  E-value: 1.74e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   93 PQLTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKM 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 5881421  173 DAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 1.22e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 254.95  E-value: 1.22e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     4 PAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSML-VLISSKYIYRFLT--DGHVIETVWTVIPAIILVVVALPS 80
Cdd:MTH00027  32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYYWNklDGSLIEVIWTLIPAFILILIAFPS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    81 LKLLYLTDE-LDNPQLTIKSVGHQWYWSYEYTDY--YDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAA 157
Cdd:MTH00027 112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5881421   158 DVIHSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGW 222
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-228 1.36e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 245.69  E-value: 1.36e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    23 FHDHVMLVLILITCLIFYSMLVLISSKYIYRFLTDGHVIETVWTVIPAIILVVVALPSLKLLYLTdELDNPQ--LTIKSV 100
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYY-GLMNLDsnLTVKVT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   101 GHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDAVPGRLN 180
Cdd:MTH00080 104 GHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILS 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 5881421   181 QLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGWCDMMLD 228
Cdd:MTH00080 184 TLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.48e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 230.76  E-value: 3.48e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     95 LTIKSVGHQWYWSYEYTDYYDIEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 5881421    175 VPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-222 4.05e-62

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 193.51  E-value: 4.05e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    1 MATPAQLGLMDAASPVMEEMIYFHDhVMLVLILITCLIFYSMLVLISSKYIYR-------FLTDGHVIETVWTVIPAIIL 73
Cdd:COG1622  13 LLLSGQLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVLVFGLLLYFAIRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIV 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   74 VVVALPSLKLLYLTDELDNPQLTIKSVGHQWYWSYEYTDYyDIEfdsymlplgdlskgdarlleVDNRVVLPVDTSVRVL 153
Cdd:COG1622  92 IVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQ-GIA--------------------TVNELVLPVGRPVRFL 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5881421  154 VTAADVIHSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGW 222
Cdd:COG1622 151 LTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 26-214 3.06e-52

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 167.44  E-value: 3.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    26 HVMLVLILITCLIFYSML-VLISSKYIYRFLTDGHVIETVWTVIPAIILVVvaLPSLKLLYLTDELD-NPQLTIKSVGHQ 103
Cdd:MTH00047  13 YILALCVFIPCWVYIMLCwQVVSGNGSVNFGSENQVLELLWTVVPTLLVLV--LCFLNLNFITSDLDcFSSETIKVIGHQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   104 WYWSYEYTDyyDIEFDSYMLPLGDLskgdarlleVDNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDAVPGRLNQLA 183
Cdd:MTH00047  91 WYWSYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLF 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 5881421   184 LQCSRVGTFYGQCSEICGANHSFMPIVIEAV 214
Cdd:MTH00047 160 FCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 1.40e-48

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: 158.31  E-value: 1.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     12 AASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLI------SSKYIYRFLTDGHVIETVWTVIPAIILVVV-ALPSLKLL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLfAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421     85 YLTDELDNPQLTIKSVGHQWYWSYEYTDYydiefdsymlplgdlskgdarLLEVDNRVVLPVDTSVRVLVTAADVIHSWT 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5881421    165 VPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 113-219 2.12e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 138.41  E-value: 2.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   113 YYdiEFDSYMLPLGDLSKGDARLLEVDNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDAVPGRLNQLALQCSRVGTF 192
Cdd:PTZ00047  48 YY--SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVF 125

                         90       100
                 ....*....|....*....|....*..
gi 5881421   193 YGQCSEICGANHSFMPIVIEAVPVEVF 219
Cdd:PTZ00047 126 YGQCSEMCGTLHGFMPIVVEAVSPEAY 152
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 1.68e-31

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: 111.17  E-value: 1.68e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   95 LTIKSVGHQWYWSYEYTDYydiefdsymlplgdlskgDARLLEVDNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDA 174
Cdd:cd04213   2 LTIEVTGHQWWWEFRYPDE------------------PGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                        90       100       110
                ....*....|....*....|....*....|...
gi 5881421  175 VPGRLNQLALQCSRVGTFYGQCSEICGANHSFM 207
Cdd:cd04213  64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 2.11e-27

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: 100.45  E-value: 2.11e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   95 LTIKSVGHQWYWSYEYTDyydiefdsymlplgdlskgdarlLEVDNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDA 174
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 5881421  175 VPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIE 212
Cdd:cd13842  58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.11e-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: 93.17  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421      1 MATPAQLGLMDAASPVMEEMIYFHDHVMLVLILITCLIFYSMLVLI------SSKYIYRFLTDGHVIETVWTVIPAIILV 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 5881421     75 VVALPSLKL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 1.89e-24

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 93.09  E-value: 1.89e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   95 LTIKSVGHQWYWSYEYtdyydiefdsymlPLGDLSKGDARLLEVdNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDA 174
Cdd:cd13919   2 LVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 5881421  175 VPGRLNQLALQCSRVGTFYGQCSEICGANHSFM 207
Cdd:cd13919  68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 8.50e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 88.45  E-value: 8.50e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   95 LTIKSVGHQWYWSYEYtdyydiefdsymlPLGDlskgdarllEVDNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDA 174
Cdd:cd13915   2 LEIQVTGRQWMWEFTY-------------PNGK---------REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                        90       100       110
                ....*....|....*....|....*....|...
gi 5881421  175 VPGRLNQLALQCSRVGTFYGQCSEICGANHSFM 207
Cdd:cd13915  60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 1.45e-22

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 88.23  E-value: 1.45e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   96 TIKSVGHQWYWSYEYtdyydiefdsymlplgdlskGDARLLEvDNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDAV 175
Cdd:cd13914   2 EIEVEAYQWGWEFSY--------------------PEANVTT-SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 5881421  176 PGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGW 222
Cdd:cd13914  61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 68-222 2.58e-21

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 85.97  E-value: 2.58e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   68 IPAIILV-VVALPSLKLLYLTDELDNPQ---LTIKSVGHQWYWSYEYTDYYdiefdsymlplgdlskgdarllEVDNRVV 143
Cdd:cd13918   2 LSAIIVIsLIVWTYGMLLYVEDPPDEADedaLEVEVEGFQFGWQFEYPNGV----------------------TTGNTLR 59

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5881421  144 LPVDTSVRVLVTAADVIHSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVPVEVFEGW 222
Cdd:cd13918  60 VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 5.65e-10

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: 54.50  E-value: 5.65e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5881421  140 NRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFM 207
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-214 9.79e-09

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: 51.39  E-value: 9.79e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5881421  140 NRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAV 214
Cdd:cd04212  25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 64-222 1.31e-04

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 42.09  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421    64 VWTViPAIILVVVALPSLKLlylTDELDNPQ--------LTIKSVGHQWYWSYEYTDyydiefdsymlplgdlsKGDARL 135
Cdd:PRK10525  92 VWTV-PILIIIFLAVLTWKT---THALEPSKplahdekpITIEVVSMDWKWFFIYPE-----------------QGIATV 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   136 levdNRVVLPVDTSVRVLVTAADVIHSWTVPSLGLKMDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFMPIVIEAVP 215
Cdd:PRK10525 151 ----NEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATP 226


                 ....*...
gi 5881421   216 V-EVFEGW 222
Cdd:PRK10525 227 DrAEFDQW 234
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 135-212 1.33e-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: 37.21  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421  135 LLEVDNRVVLPVDTSVRV-LVTAADVIHSWTVPSLGLKMDA---------------VPGRLNQLALQCSRVGTFYGQCSE 198
Cdd:cd00920  18 LLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYWFYCTI 97

                        90
                ....*....|....
gi 5881421  199 ICGaNHSFMPIVIE 212
Cdd:cd00920  98 PGH-NHAGMVGTIN 110
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 1.65e-03

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 36.59  E-value: 1.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5881421   96 TIKSVGHQWYWSYeytdyydiefdsymlplgdlskgdarllevdNRVVLPVDTSVRVLVTAADVIHSWTV--PSLGL--K 171
Cdd:cd13916   2 VVAVTGHQWYWEL-------------------------------SRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQ 50

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 5881421  172 MDAVPGRLNQLALQCSRVGTFYGQCSEICGANHSFM 207
Cdd:cd13916  51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
 
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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