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Conserved domains on  [gi|27371984|gb|AAN87876|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Microcebus murinus]

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
 1-169 6.41e-124

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: 347.86  E-value: 6.41e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00098  59 QEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00098 139 DNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKY 218


                 ....*....
gi 27371984  161 FEEWLLSTL 169
Cdd:MTH00098 219 FEKWSASML 227
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-169 6.41e-124

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 347.86  E-value: 6.41e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00098  59 QEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00098 139 DNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKY 218


                 ....*....
gi 27371984  161 FEEWLLSTL 169
Cdd:MTH00098 219 FEKWSASML 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 35-164 1.17e-90

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: 259.81  E-value: 1.17e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984  35 PTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKT 114
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 27371984 115 DAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKHFEEW 164
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
37-156 1.54e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 233.84  E-value: 1.54e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    37 LTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDA 116
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 27371984   117 IPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELV 156
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-165 1.00e-51

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 164.62  E-value: 1.00e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   3 VETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLcfdsymtppleldpgelrlleVDN 82
Cdd:COG1622  79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984  83 RVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKHFE 162
Cdd:COG1622 138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                ...
gi 27371984 163 EWL 165
Cdd:COG1622 218 AWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 3-165 8.63e-43

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: 140.98  E-value: 8.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984     3 VETVWTI*PAVILI-LIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYenlcfdsymtppleldpgelrLLEVD 81
Cdd:TIGR02866  56 LEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    82 NRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKHF 161
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194


                  ....
gi 27371984   162 EEWL 165
Cdd:TIGR02866 195 DAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-169 6.41e-124

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 347.86  E-value: 6.41e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00098  59 QEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00098 139 DNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKY 218


                 ....*....
gi 27371984  161 FEEWLLSTL 169
Cdd:MTH00098 219 FEKWSASML 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-169 1.56e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 334.19  E-value: 1.56e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00117  59 QEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00117 139 DHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKH 218


                 ....*....
gi 27371984  161 FEEWLLSTL 169
Cdd:MTH00117 219 FENWSSLLS 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-167 3.01e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 315.61  E-value: 3.01e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00154  59 QEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00154 139 DNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNN 218


                 ....*..
gi 27371984  161 FEEWLLS 167
Cdd:MTH00154 219 FINWIKN 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-169 4.08e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 300.09  E-value: 4.08e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00129  59 QEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEA 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00129 139 DHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEH 218


                 ....*....
gi 27371984  161 FEEWLLSTL 169
Cdd:MTH00129 219 FENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-169 8.55e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 296.69  E-value: 8.55e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00076  59 QEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00076 139 DNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNN 218


                 ....*....
gi 27371984  161 FEEWLLSTL 169
Cdd:MTH00076 219 FLNWSSSML 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-167 1.33e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 293.81  E-value: 1.33e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00168  59 QMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00168 139 DNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWET 218


                 ....*..
gi 27371984  161 FEEWLLS 167
Cdd:MTH00168 219 FENWVDS 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-168 7.44e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 284.14  E-value: 7.44e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00140  59 QKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00140 139 DNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLED 218


                 ....*...
gi 27371984  161 FEEWLLST 168
Cdd:MTH00140 219 FVKWLELM 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-169 1.02e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 284.09  E-value: 1.02e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00185  59 QEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLET 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00185 139 DHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEH 218


                 ....*....
gi 27371984  161 FEEWLLSTL 169
Cdd:MTH00185 219 FENWSSLML 227
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-164 1.01e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 281.59  E-value: 1.01e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00038  59 QELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00038 139 DNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNT 218


                 ....
gi 27371984  161 FEEW 164
Cdd:MTH00038 219 FENW 222
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-167 1.08e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 278.91  E-value: 1.08e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00139  59 QEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00139 139 DNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKF 218


                 ....*..
gi 27371984  161 FEEWLLS 167
Cdd:MTH00139 219 FLEWILE 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-167 4.71e-93

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 269.80  E-value: 4.71e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00008  59 QQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00008 139 DNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKS 218


                 ....*..
gi 27371984  161 FEEWLLS 167
Cdd:MTH00008 219 FMKWVSS 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 35-164 1.17e-90

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: 259.81  E-value: 1.17e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984  35 PTLTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKT 114
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 27371984 115 DAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKHFEEW 164
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 3-167 5.57e-88

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 257.37  E-value: 5.57e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    3 VETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDY--ENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00023  70 LEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEV 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00023 150 DNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDK 229


                 ....*..
gi 27371984  161 FEEWLLS 167
Cdd:MTH00023 230 YINWLLS 236
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 3-167 1.34e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 240.84  E-value: 1.34e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    3 VETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDY--ENLCFDSYMTPPLELDPGELRLLEV 80
Cdd:MTH00051  63 IEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEV 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   81 DNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKH 160
Cdd:MTH00051 143 DNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDK 222


                 ....*..
gi 27371984  161 FEEWLLS 167
Cdd:MTH00051 223 YINWVAT 229
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
37-156 1.54e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 233.84  E-value: 1.54e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    37 LTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDA 116
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 27371984   117 IPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELV 156
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-169 1.19e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 220.65  E-value: 1.19e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVILILIALPSLRILYMMDEITTPT-LTLKTMGHQWYWSYEYTDYENLCFDSYMTPPLELDPGELRLLE 79
Cdd:MTH00080  61 QFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNLDSnLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   80 VDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLK 159
Cdd:MTH00080 141 VDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLD 220

                        170
                 ....*....|
gi 27371984  160 HFEEWLLSTL 169
Cdd:MTH00080 221 NFKEWCKLLL 230
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 3-165 1.06e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 214.12  E-value: 1.06e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    3 VETVWTI*PAVILILIALPSLRILYMMDE-ITTPTLTLKTMGHQWYWSYEYTDY--ENLCFDSYMTPPLELDPGELRLLE 79
Cdd:MTH00027  92 IEVIWTLIPAFILILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLE 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   80 VDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLK 159
Cdd:MTH00027 172 VDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLS 251


                 ....*.
gi 27371984  160 HFEEWL 165
Cdd:MTH00027 252 KYIDWI 257
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-165 1.00e-51

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 164.62  E-value: 1.00e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   3 VETVWTI*PAVILILIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYENLcfdsymtppleldpgelrlleVDN 82
Cdd:COG1622  79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984  83 RVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKHFE 162
Cdd:COG1622 138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                ...
gi 27371984 163 EWL 165
Cdd:COG1622 218 AWL 220
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 1-156 3.26e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 142.02  E-value: 3.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    1 QEVETVWTI*PAVI-LILIALPSLRILYMMDeiTTPTLTLKTMGHQWYWSYEYTDyeNLCFDSYMTPPLELdpgelrlle 79
Cdd:MTH00047  47 QVLELLWTVVPTLLvLVLCFLNLNFITSDLD--CFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG--------- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27371984   80 VDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELV 156
Cdd:MTH00047 114 VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 3-165 8.63e-43

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: 140.98  E-value: 8.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984     3 VETVWTI*PAVILI-LIALPSLRILYMMDEITTPTLTLKTMGHQWYWSYEYTDYenlcfdsymtppleldpgelrLLEVD 81
Cdd:TIGR02866  56 LEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984    82 NRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKHF 161
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194


                  ....
gi 27371984   162 EEWL 165
Cdd:TIGR02866 195 DAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 60-156 2.22e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 133.79  E-value: 2.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984   60 FDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCS 139
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*..
gi 27371984  140 EICGANHSFMPIVLELV 156
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAV 147
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 37-154 1.49e-31

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 108.92  E-value: 1.49e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984  37 LTLKTMGHQWYWSYEYTDyenlcfdsymtppleldpgelrlLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDA 116
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 27371984 117 IPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 154
Cdd:cd13842  58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 36-149 1.39e-29

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: 104.24  E-value: 1.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984  36 TLTLKTMGHQWYWSYEYTDYENlcfdsymtppleldpgelRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTD 115
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPDEPG------------------RGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                        90       100       110
                ....*....|....*....|....*....|....
gi 27371984 116 AIPGRLNQATLMTSRPGIYYGQCSEICGANHSFM 149
Cdd:cd04213  63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 36-149 9.07e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 84.23  E-value: 9.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984  36 TLTLKTMGHQWYWSYEYTDYenlcfDSYMTPPLELDPGELRLlEVDNRVvlptemsiRMLISSEDVLHSWTVPSLGVKTD 115
Cdd:cd13919   1 ALVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL-PVGRPV--------LFNLRSKDVIHSFWVPEFRVKQD 66

                        90       100       110
                ....*....|....*....|....*....|....
gi 27371984 116 AIPGRLNQATLMTSRPGIYYGQCSEICGANHSFM 149
Cdd:cd13919  67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 12-165 1.50e-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: 84.81  E-value: 1.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984  12 AVILI-LIALPSLRILYMMDEITTP---TLTLKTMGHQWYWSYEYtdyenlcfdsymtppleldPGELrllEVDNRVVLP 87
Cdd:cd13918   4 AIIVIsLIVWTYGMLLYVEDPPDEAdedALEVEVEGFQFGWQFEY-------------------PNGV---TTGNTLRVP 61

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27371984  88 TEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLELVPLKHFEEWL 165
Cdd:cd13918  62 ADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 43-165 6.43e-21

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 82.07  E-value: 6.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984  43 GHQWYWSYEYTDYENlcfdsymtppleldpgelrllEVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLN 122
Cdd:cd13914   7 AYQWGWEFSYPEANV---------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 27371984 123 qaTLMTS--RPGIYYGQCSEICGANHSFMPIVLELVPLKHFEEWL 165
Cdd:cd13914  66 --TIKTEatEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 36-149 3.10e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 77.67  E-value: 3.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984  36 TLTLKTMGHQWYWSYEYtdyenlcfdsymtppleldPGELRlleVDNRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTD 115
Cdd:cd13915   1 ALEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                        90       100       110
                ....*....|....*....|....*....|....
gi 27371984 116 AIPGRLNQATLMTSRPGIYYGQCSEICGANHSFM 149
Cdd:cd13915  59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 82-149 3.33e-08

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 48.72  E-value: 3.33e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27371984  82 NRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFM 149
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 72-154 7.83e-08

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: 48.00  E-value: 7.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984  72 PGELRLLEVDNRVVLPTEMSIRMLISSE-DVLHSWTVPSLGVKTDAI---------------PGRLNQATLMTSRPGIYY 135
Cdd:cd00920  13 TYNGVLLFGPPVLVVPVGDTVRVQFVNKlGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYW 92

                        90
                ....*....|....*....
gi 27371984 136 GQCSEICGaNHSFMPIVLE 154
Cdd:cd00920  93 FYCTIPGH-NHAGMVGTIN 110
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-25 1.72e-06

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: 43.86  E-value: 1.72e-06
                          10        20
                  ....*....|....*....|....*
gi 27371984     1 QEVETVWTI*PAVILILIALPSLRI 25
Cdd:pfam02790  65 QTIEIIWTIIPAVILILIALPSFKL 89
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 82-149 7.16e-06

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: 42.54  E-value: 7.16e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27371984  82 NRVVLPTEMSIRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFM 149
Cdd:cd04212  25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 43-149 1.91e-04

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 38.52  E-value: 1.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371984  43 GHQWYWsyeytdyenlcfdsymtpplELDPGELRLLE-VDNRVvlptemsirmliSSEDVLHSWTVPS----LGVKTDAI 117
Cdd:cd13916   7 GHQWYW--------------------ELSRTEIPAGKpVEFRV------------TSADVNHGFGIYDpdmrLLAQTQAM 54

                        90       100       110
                ....*....|....*....|....*....|..
gi 27371984 118 PGRLNQATLMTSRPGIYYGQCSEICGANHSFM 149
Cdd:cd13916  55 PGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 99-149 4.65e-03

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 34.90  E-value: 4.65e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 27371984  99 EDVLHSWTVPSLGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFM 149
Cdd:cd04223  37 EDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
 
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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