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Conserved domains on  [gi|194359452|gb|ACF57651|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Microcebus sp. Anjiahely]

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

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List of domain hits

 Name Accession Description Interval E-value
COX2 super family cl31796
cytochrome c oxidase subunit II; Validated
 1-176 1.63e-127

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: 357.11  E-value: 1.63e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00098  27 TLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00098 107 SYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMS 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00098 187 TRPGLYYGQCSEICGS 202
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-176 1.63e-127

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 357.11  E-value: 1.63e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00098  27 TLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00098 107 SYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMS 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00098 187 TRPGLYYGQCSEICGS 202
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 67-176 4.60e-74

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: 218.21  E-value: 4.60e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  67 PSLTLKTMGHQWYWSYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKT 146
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 194359452 147 DAIPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGA 110
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
69-176 9.80e-69

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 204.57  E-value: 9.80e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   69 LTLKTMGHQWYWSYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDA 148
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*...
gi 194359452  149 IPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGI 108
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
35-176 1.08e-43

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 144.59  E-value: 1.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  35 VETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYENLcfdsymtspleldpgelrlleVDN 114
Cdd:COG1622   79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194359452 115 RVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:COG1622  138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGT 199
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 35-176 4.01e-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: 124.42  E-value: 4.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   35 VETVWTILPAVILI-LIALPSLRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYenlcfdsymtspleldpgelrLLEVD 113
Cdd:TIGR02866  56 LEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTV 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194359452  114 NRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGA 177
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-176 1.63e-127

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 357.11  E-value: 1.63e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00098  27 TLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00098 107 SYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMS 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00098 187 TRPGLYYGQCSEICGS 202
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-176 3.29e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 333.42  E-value: 3.29e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00117  27 ALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00117 107 SYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFIT 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00117 187 TRPGVFYGQCSEICGA 202
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-176 9.44e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 302.08  E-value: 9.44e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00076  27 ALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00076 107 SYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIA 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00076 187 SRPGVYYGQCSEICGA 202
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-176 3.08e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 295.85  E-value: 3.08e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00129  27 ALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00129 107 SYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIA 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00129 187 SRPGVFYGQCSEICGA 202
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-176 1.12e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 291.73  E-value: 1.12e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00154  27 TMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00154 107 SYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLI 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00154 187 NRPGLFFGQCSEICGA 202
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-176 2.26e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 281.00  E-value: 2.26e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00185  27 TLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00185 107 SYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFII 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00185 187 SRPGLYYGQCSEICGA 202
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-176 4.45e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 269.93  E-value: 4.45e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00168  27 ALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00168 107 SYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLS 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00168 187 SRPGSFYGQCSEICGA 202
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-176 2.35e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 262.95  E-value: 2.35e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00140  27 AMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00140 107 SYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEP 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00140 187 KRPGVFYGQCSEICGA 202
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-176 6.89e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 259.26  E-value: 6.89e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00139  27 AMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00139 107 SYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFI 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00139 187 NRPGVFYGQCSEICGA 202
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-176 1.62e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 258.48  E-value: 1.62e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00038  27 ALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00038 107 SYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFI 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00038 187 SRTGLFYGQCSEICGA 202
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-176 2.92e-83

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 245.15  E-value: 2.92e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   1 TLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYW 80
Cdd:MTH00008  27 ALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00008 107 SYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTI 186

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00008 187 TRPGVFYGQCSEICGA 202
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-176 2.01e-77

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 230.79  E-value: 2.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   2 LMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYWS 81
Cdd:MTH00023  37 MFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWS 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  82 YEYTDY--ENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLM 159
Cdd:MTH00023 117 YEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFF 196

                        170
                 ....*....|....*..
gi 194359452 160 TSRPGIYYGQCSEICGA 176
Cdd:MTH00023 197 IKRPGVFYGQCSEICGA 213
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-176 2.08e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 223.12  E-value: 2.08e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   2 LMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYWS 81
Cdd:MTH00051  30 MFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  82 YEYTDY--ENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLM 159
Cdd:MTH00051 110 YEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFF 189

                        170
                 ....*....|....*..
gi 194359452 160 TSRPGIYYGQCSEICGA 176
Cdd:MTH00051 190 IKRPGVFYGQCSEICGA 206
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 67-176 4.60e-74

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: 218.21  E-value: 4.60e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  67 PSLTLKTMGHQWYWSYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKT 146
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 194359452 147 DAIPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGA 110
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
69-176 9.80e-69

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 204.57  E-value: 9.80e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   69 LTLKTMGHQWYWSYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDA 148
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*...
gi 194359452  149 IPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGI 108
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 2-176 2.80e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 194.46  E-value: 2.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   2 LMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPS-LTLKTMGHQWYW 80
Cdd:MTH00080  30 LFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNLDSnLTVKVTGHQWYW 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  81 SYEYTDYENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMT 160
Cdd:MTH00080 110 SYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSF 189

                        170
                 ....*....|....*.
gi 194359452 161 SRPGIYYGQCSEICGA 176
Cdd:MTH00080 190 PMPGVFYGQCSEICGA 205
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-176 5.21e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 189.85  E-value: 5.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   2 LMIVFLISSLVLYIISLMLTTELTHT---STMDAQEVETVWTILPAVILILIALPSLRILYMMDE-ITTPSLTLKTMGHQ 77
Cdd:MTH00027  56 LFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEcGFSANITIKVTGHQ 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  78 WYWSYEYTDY--ENLCFDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQ 155
Cdd:MTH00027 136 WYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINE 215

                        170       180
                 ....*....|....*....|.
gi 194359452 156 ATLMTSRPGIYYGQCSEICGA 176
Cdd:MTH00027 216 TGFLIKRPGIFYGQCSEICGA 236
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
35-176 1.08e-43

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 144.59  E-value: 1.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  35 VETVWTILPAVILILIALPSLRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYENLcfdsymtspleldpgelrlleVDN 114
Cdd:COG1622   79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194359452 115 RVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:COG1622  138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGT 199
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 35-176 4.01e-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: 124.42  E-value: 4.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452   35 VETVWTILPAVILI-LIALPSLRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYenlcfdsymtspleldpgelrLLEVD 113
Cdd:TIGR02866  56 LEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTV 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194359452  114 NRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGA 177
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 31-176 6.39e-35

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 120.83  E-value: 6.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  31 DAQEVETVWTILPAVI-LILIALPSLRILYMMDeiTTPSLTLKTMGHQWYWSYEYTDyeNLCFDSYMTSPLELdpgelrl 109
Cdd:MTH00047  45 ENQVLELLWTVVPTLLvLVLCFLNLNFITSDLD--CFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG------- 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194359452 110 leVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGV 178
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 92-176 1.09e-33

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 116.84  E-value: 1.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  92 FDSYMTSPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCS 171
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130


                 ....*
gi 194359452 172 EICGA 176
Cdd:PTZ00047 131 EMCGT 135
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 68-176 4.59e-27

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: 98.08  E-value: 4.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  68 SLTLKTMGHQWYWSYEYTDYENlcfdsymtspleldpgelRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTD 147
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPG------------------RGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100
                 ....*....|....*....|....*....
gi 194359452 148 AIPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGA 91
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 69-176 1.18e-26

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: 96.60  E-value: 1.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  69 LTLKTMGHQWYWSYEYTDyenlcfdsymtspleldpgelrlLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDA 148
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100
                 ....*....|....*....|....*...
gi 194359452 149 IPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGL 85
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 69-176 1.71e-19

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 78.84  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  69 LTLKTMGHQWYWSYEYTDYenlcfDSYMTSPLELDPGELRLlEVDNRVvlptemsiRMLISSEDVLHSWTVPSLGVKTDA 148
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL-PVGRPV--------LFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100
                 ....*....|....*....|....*...
gi 194359452 149 IPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGL 95
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 68-175 6.88e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 69.19  E-value: 6.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  68 SLTLKTMGHQWYWSYEYtdyenlcfdsymtspleldPGELRlleVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTD 147
Cdd:cd13915    1 ALEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100
                 ....*....|....*....|....*...
gi 194359452 148 AIPGRLNQATLMTSRPGIYYGQCSEICG 175
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCTEYCG 86
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 75-176 7.11e-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: 69.36  E-value: 7.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  75 GHQWYWSYEYTDYENlcfdsymtspleldpgelrllEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLN 154
Cdd:cd13914    7 AYQWGWEFSYPEANV---------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65

                         90       100
                 ....*....|....*....|....
gi 194359452 155 qaTLMTS--RPGIYYGQCSEICGA 176
Cdd:cd13914   66 --TIKTEatEEGEYQLYCAEYCGA 87
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 41-176 1.56e-15

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: 69.41  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  41 ILPAVILI-LIALPSLRILYMMDEITTP---SLTLKTMGHQWYWSYEYtdyenlcfdsymtspleldPGELrllEVDNRV 116
Cdd:cd13918    1 GLSAIIVIsLIVWTYGMLLYVEDPPDEAdedALEVEVEGFQFGWQFEY-------------------PNGV---TTGNTL 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452 117 VLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:cd13918   59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGS 118
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-57 1.20e-14

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: 65.82  E-value: 1.20e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194359452    1 TLMIVFLISSLVLYIISLMLTT------ELTHTSTMDAQEVETVWTILPAVILILIALPSLRI 57
Cdd:pfam02790  27 IMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWTIIPAVILILIALPSFKL 89
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 114-176 4.15e-06

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: 43.33  E-value: 4.15e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194359452 114 NRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGA 87
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 104-176 8.85e-06

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 42.60  E-value: 8.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452 104 PGELRLLEVDNRVVLPTEMSIRMLISSE-DVLHSWTVPSLGVKTDAI---------------PGRLNQATLMTSRPGIYY 167
Cdd:cd00920   13 TYNGVLLFGPPVLVVPVGDTVRVQFVNKlGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYW 92


                 ....*....
gi 194359452 168 GQCSEICGA 176
Cdd:cd00920   93 FYCTIPGHN 101
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 114-176 4.39e-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: 40.61  E-value: 4.39e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194359452 114 NRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGE 87
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 75-176 3.95e-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: 35.05  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194359452  75 GHQWYWSyeytdyenlcfdsymTSPLELDPGELrlleVDNRVvlptemsirmliSSEDVLHSWTVPS----LGVKTDAIP 150
Cdd:cd13916    7 GHQWYWE---------------LSRTEIPAGKP----VEFRV------------TSADVNHGFGIYDpdmrLLAQTQAMP 55

                         90       100
                 ....*....|....*....|....*.
gi 194359452 151 GRLNQATLMTSRPGIYYGQCSEICGA 176
Cdd:cd13916   56 GYTNVLRYTFDKPGTYTILCLEYCGL 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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