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Conserved domains on  [gi|2316637351|gb|UYE91456|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Coptotermes intermedius]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-173 1.31e-115

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 326.79  E-value: 1.31e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00154   20 LIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179

                         170
                  ....*....|...
gi 2316637351 161 NQTSFSISRPGIM 173
Cdd:MTH00154  180 NQLNFLINRPGLF 192
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-173 1.31e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 326.79  E-value: 1.31e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00154   20 LIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179

                         170
                  ....*....|...
gi 2316637351 161 NQTSFSISRPGIM 173
Cdd:MTH00154  180 NQLNFLINRPGLF 192
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 74-172 5.54e-67

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: 200.10  E-value: 5.54e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  74 PALTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKT 153
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90
                  ....*....|....*....
gi 2316637351 154 DATPGRLNQTSFSISRPGI 172
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGV 99
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
76-172 4.58e-61

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 184.92  E-value: 4.58e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  76 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 155
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*..
gi 2316637351 156 TPGRLNQTSFSISRPGI 172
Cdd:pfam00116  81 VPGRLNQTSFSIDREGV 97
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-172 7.54e-38

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 129.56  E-value: 7.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   6 DHVLMIMLMITT-----TVSYMMITLIR-----NKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPA 75
Cdd:COG1622    33 DDLFWVSLIIMLvifvlVFGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  76 LTLKAVGHQWYWSYEYsdftklefdsymiPQEEQqestfrllDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 155
Cdd:COG1622   113 LTVEVTGYQWKWLFRY-------------PDQGI--------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDA 171

                         170
                  ....*....|....*..
gi 2316637351 156 TPGRLNQTSFSISRPGI 172
Cdd:COG1622   172 IPGRVTELWFTADKPGT 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 42-172 7.81e-31

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: 110.55  E-value: 7.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  42 IETTWTIAPAIILV-FIAMPSLRLLYLMDEIHNPALTLKAVGHQWYWSYEYSdftklefdsymipqeeqqESTFRlldTD 120
Cdd:TIGR02866  56 LEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYP------------------ESGFT---TV 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2316637351 121 NRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPGI 172
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGV 166
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-173 1.31e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 326.79  E-value: 1.31e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00154   20 LIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179

                         170
                  ....*....|...
gi 2316637351 161 NQTSFSISRPGIM 173
Cdd:MTH00154  180 NQLNFLINRPGLF 192
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-172 4.32e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 277.57  E-value: 4.32e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00117   20 LLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00117  100 IGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRL 179

                         170
                  ....*....|..
gi 2316637351 161 NQTSFSISRPGI 172
Cdd:MTH00117  180 NQTSFITTRPGV 191
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-173 5.09e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 272.20  E-value: 5.09e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00140   20 LIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00140  100 IGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRL 179

                         170
                  ....*....|...
gi 2316637351 161 NQTSFSISRPGIM 173
Cdd:MTH00140  180 NQLSFEPKRPGVF 192
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-173 2.08e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 270.82  E-value: 2.08e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00139   20 LIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00139  100 VGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRL 179

                         170
                  ....*....|...
gi 2316637351 161 NQTSFSISRPGIM 173
Cdd:MTH00139  180 NQVGFFINRPGVF 192
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-173 2.90e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 267.62  E-value: 2.90e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00168   20 LILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00168  100 VGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRL 179

                         170
                  ....*....|...
gi 2316637351 161 NQTSFSISRPGIM 173
Cdd:MTH00168  180 NQLAFLSSRPGSF 192
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-172 4.35e-88

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 257.48  E-value: 4.35e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00008   20 LISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00008  100 IGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRL 179

                         170
                  ....*....|..
gi 2316637351 161 NQTSFSISRPGI 172
Cdd:MTH00008  180 NQIGFTITRPGV 191
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-172 1.31e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 256.17  E-value: 1.31e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00038   20 LIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00038  100 IGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRL 179

                         170
                  ....*....|..
gi 2316637351 161 NQTSFSISRPGI 172
Cdd:MTH00038  180 NQTTFFISRTGL 191
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-172 1.08e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 251.17  E-value: 1.08e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00129   20 LLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00129  100 MGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRL 179

                         170
                  ....*....|..
gi 2316637351 161 NQTSFSISRPGI 172
Cdd:MTH00129  180 NQTAFIASRPGV 191
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-172 2.07e-82

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 243.50  E-value: 2.07e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00023   29 IIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTK--LEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPG 158
Cdd:MTH00023  109 IGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPG 188

                         170
                  ....*....|....
gi 2316637351 159 RLNQTSFSISRPGI 172
Cdd:MTH00023  189 RLNQTGFFIKRPGV 202
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-172 3.77e-82

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 242.32  E-value: 3.77e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00098   20 LLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00098  100 MGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRL 179

                         170
                  ....*....|..
gi 2316637351 161 NQTSFSISRPGI 172
Cdd:MTH00098  180 NQTTLMSTRPGL 191
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-172 3.83e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 242.48  E-value: 3.83e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00185   20 LIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00185  100 MGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRL 179

                         170
                  ....*....|..
gi 2316637351 161 NQTSFSISRPGI 172
Cdd:MTH00185  180 NQATFIISRPGL 191
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-172 1.12e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 238.53  E-value: 1.12e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00076   20 LLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRL 160
Cdd:MTH00076  100 IGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRL 179

                         170
                  ....*....|..
gi 2316637351 161 NQTSFSISRPGI 172
Cdd:MTH00076  180 NQTSFIASRPGV 191
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-172 3.98e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 229.67  E-value: 3.98e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPALTLKA 80
Cdd:MTH00051   22 IIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  81 VGHQWYWSYEYSDF--TKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPG 158
Cdd:MTH00051  102 IGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPG 181

                         170
                  ....*....|....
gi 2316637351 159 RLNQTSFSISRPGI 172
Cdd:MTH00051  182 RLNQTSFFIKRPGV 195
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 74-172 5.54e-67

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: 200.10  E-value: 5.54e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  74 PALTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKT 153
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90
                  ....*....|....*....
gi 2316637351 154 DATPGRLNQTSFSISRPGI 172
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGV 99
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
76-172 4.58e-61

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 184.92  E-value: 4.58e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  76 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 155
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*..
gi 2316637351 156 TPGRLNQTSFSISRPGI 172
Cdd:pfam00116  81 VPGRLNQTSFSIDREGV 97
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-172 9.93e-56

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 176.37  E-value: 9.93e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMI-TLIRNKQTSRF--MLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDE-IHNPAL 76
Cdd:MTH00027   48 IIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYYwnKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEcGFSANI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  77 TLKAVGHQWYWSYEYSDFTK--LEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTD 154
Cdd:MTH00027  128 TIKVTGHQWYWSYSYEDYGEknIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMD 207

                         170
                  ....*....|....*...
gi 2316637351 155 ATPGRLNQTSFSISRPGI 172
Cdd:MTH00027  208 AVPGRINETGFLIKRPGI 225
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 4-172 3.78e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 173.66  E-value: 3.78e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   4 FHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMdEIHN--PALTLKAV 81
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYY-GLMNldSNLTVKVT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  82 GHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLN 161
Cdd:MTH00080  104 GHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILS 183

                         170
                  ....*....|.
gi 2316637351 162 QTSFSISRPGI 172
Cdd:MTH00080  184 TLCYSFPMPGV 194
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-172 7.54e-38

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 129.56  E-value: 7.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   6 DHVLMIMLMITT-----TVSYMMITLIR-----NKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEIHNPA 75
Cdd:COG1622    33 DDLFWVSLIIMLvifvlVFGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  76 LTLKAVGHQWYWSYEYsdftklefdsymiPQEEQqestfrllDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 155
Cdd:COG1622   113 LTVEVTGYQWKWLFRY-------------PDQGI--------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDA 171

                         170
                  ....*....|....*..
gi 2316637351 156 TPGRLNQTSFSISRPGI 172
Cdd:COG1622   172 IPGRVTELWFTADKPGT 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 42-172 7.81e-31

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: 110.55  E-value: 7.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  42 IETTWTIAPAIILV-FIAMPSLRLLYLMDEIHNPALTLKAVGHQWYWSYEYSdftklefdsymipqeeqqESTFRlldTD 120
Cdd:TIGR02866  56 LEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYP------------------ESGFT---TV 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2316637351 121 NRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPGI 172
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGV 166
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 4-172 1.39e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 107.35  E-value: 1.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   4 FHDHVLMIMLMITTTVSYMMITLIRN----KQTSRFMLEGQMIETTWTIAPAIILVFIAmpSLRLLYLMDEIH-NPALTL 78
Cdd:MTH00047    7 YYDIVCYILALCVFIPCWVYIMLCWQvvsgNGSVNFGSENQVLELLWTVVPTLLVLVLC--FLNLNFITSDLDcFSSETI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  79 KAVGHQWYWSYEYSDftKLEFDSYMipqeeqqesTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPG 158
Cdd:MTH00047   85 KVIGHQWYWSYEYSF--GGSYDSFM---------TDDIFGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPG 153

                         170
                  ....*....|....
gi 2316637351 159 RLNQTSFSISRPGI 172
Cdd:MTH00047  154 RINHLFFCPDRHGV 167
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 99-172 1.38e-20

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 82.95  E-value: 1.38e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316637351  99 FDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPGI 172
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGV 124
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 76-171 7.14e-20

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: 79.26  E-value: 7.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  76 LTLKAVGHQWYWSYEYSDFTklefdsymipqeeqqestfrlldTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 155
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90
                  ....*....|....*.
gi 2316637351 156 TPGRLNQTSFSISRPG 171
Cdd:cd13842    58 VPGYTSELWFVADKPG 73
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 75-172 1.61e-19

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: 78.43  E-value: 1.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  75 ALTLKAVGHQWYWSYEYSDftklefdsymipqeeqqeSTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTD 154
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPD------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90
                  ....*....|....*...
gi 2316637351 155 ATPGRLNQTSFSISRPGI 172
Cdd:cd04213    63 MIPGRTNRLWLQADEPGV 80
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 75-171 4.63e-17

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 72.29  E-value: 4.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  75 ALTLKAVGHQWYWSYEYsdftklefdsymiPQEEQQESTFRLLDTdNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTD 154
Cdd:cd13919     1 ALVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90
                  ....*....|....*..
gi 2316637351 155 ATPGRLNQTSFSISRPG 171
Cdd:cd13919    67 AVPGRTTRLWFTPTREG 83
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-64 8.31e-17

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: 71.21  E-value: 8.31e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351   1 LVFFHDHVLMIMLMITTTVSYMMITLIR------NKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRL 64
Cdd:pfam02790  20 LLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIALPSFKL 89
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 75-171 1.20e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 68.42  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  75 ALTLKAVGHQWYWSYEYSDFTKlefdsymipqeeqqestfrlldTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTD 154
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKR----------------------EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90
                  ....*....|....*..
gi 2316637351 155 ATPGRLNQTSFSISRPG 171
Cdd:cd13915    59 VVPGRYTYLWFEATKPG 75
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 51-171 1.67e-13

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: 64.01  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  51 AIILV-FIAMPSLRLLYLMD---EIHNPALTLKAVGHQWYWSYEYsdftklefdsymiPQEEQQESTFRLldtdnrivlP 126
Cdd:cd13918     4 AIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEY-------------PNGVTTGNTLRV---------P 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2316637351 127 MNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPG 171
Cdd:cd13918    62 ADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPG 106
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 77-161 2.03e-12

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: 60.50  E-value: 2.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316637351  77 TLKAVGHQWYWSYEYsdftklefdsymiPQEEqqestfrlLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDAT 156
Cdd:cd13914     2 EIEVEAYQWGWEFSY-------------PEAN--------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60


                  ....*
gi 2316637351 157 PGRLN 161
Cdd:cd13914    61 PGQYN 65
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 119-171 3.32e-05

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: 41.02  E-value: 3.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2316637351 119 TDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPG 171
Cdd:cd13913    23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPG 75
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 119-173 8.84e-04

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: 36.76  E-value: 8.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2316637351 119 TDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPGIM 173
Cdd:cd04212    23 TVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTY 77
 
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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