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Conserved domains on  [gi|343409384|gb|AEM23903|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Coptotermes curvignathus]

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
 1-184 1.38e-128

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 359.91  E-value: 1.38e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00154  15 PLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00154  95 ITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00154 175 VPGRLNQLNFLINRPGLFFGQCSE 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-184 1.38e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 359.91  E-value: 1.38e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00154  15 PLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00154  95 ITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00154 175 VPGRLNQLNFLINRPGLFFGQCSE 198
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 79-184 9.07e-74

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 217.82  E-value: 9.07e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  79 PTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKT 158
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100
                 ....*....|....*....|....*.
gi 343409384 159 DATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSE 106
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
81-184 1.63e-67

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 201.87  E-value: 1.63e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....
gi 343409384  161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSE 104
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-184 3.24e-42

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 141.12  E-value: 3.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITT-TVSYMMITLIR-----NKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMD 74
Cdd:COG1622   27 PIAEEIDDLFWVSLIIMLVIFVlVFGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  75 EVQTPTLTLKAVGHQWYWSYEYsdftklefdsymiPQEEQqestfrllDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSL 154
Cdd:COG1622  107 DAPEDPLTVEVTGYQWKWLFRY-------------PDQGI--------ATVNELVLPVGRPVRFLLTSADVIHSFWVPAL 165

                        170       180       190
                 ....*....|....*....|....*....|
gi 343409384 155 GVKTDATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:COG1622  166 GGKQDAIPGRVTELWFTADKPGTYRGQCAE 195
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-184 1.90e-35

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: 122.87  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384    1 PLMEQLIFFHDHVLMIMLMITTTV-SYMMITLIRNKQTSRFML-----EGQMIETTWTIAPAIILV-FIAMPSLRLLYLM 73
Cdd:TIGR02866   4 EIAQQIAFLFLFVLAVSTLISLLVaALLAYVVWKFRRKGDEEKpsqihGNRRLEYVWTVIPLIIVVgLFAATAKGLLYLE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   74 DEVQTPTLTLKAVGHQWYWSYEYSdftklefdsymipqeeqqESTFRlldTDNRIVLPMNSPIRLIVTAADVLHSWTIPS 153
Cdd:TIGR02866  84 RPIPKDALKVKVTGYQWWWDFEYP------------------ESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPE 142

                         170       180       190
                  ....*....|....*....|....*....|.
gi 343409384  154 LGVKTDATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:TIGR02866 143 LGGKIDAIPGQTNALWFNADEPGVYYGFCAE 173
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-184 1.38e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 359.91  E-value: 1.38e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00154  15 PLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00154  95 ITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00154 175 VPGRLNQLNFLINRPGLFFGQCSE 198
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-184 8.85e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 302.60  E-value: 8.85e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00117  15 PIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00117  95 LTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00117 175 VPGRLNQTSFITTRPGVFYGQCSE 198
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-184 1.42e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 299.55  E-value: 1.42e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00140  15 PLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00140  95 LTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00140 175 IPGRLNQLSFEPKRPGVFYGQCSE 198
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-184 1.04e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 297.40  E-value: 1.04e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00139  15 PLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00139  95 LTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00139 175 VPGRLNQVGFFINRPGVFYGQCSE 198
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-184 4.99e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 293.04  E-value: 4.99e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00168  15 PVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00168  95 LTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00168 175 VPGRLNQLAFLSSRPGSFYGQCSE 198
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-184 9.09e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 282.36  E-value: 9.09e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00038  15 PLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00038  95 LTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00038 175 VPGRLNQTTFFISRTGLFYGQCSE 198
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-184 2.09e-97

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 281.36  E-value: 2.09e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00008  15 PVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00008  95 ITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00008 175 VPGRLNQIGFTITRPGVFYGQCSE 198
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-184 1.37e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 274.28  E-value: 1.37e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00129  15 PVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00129  95 LTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00129 175 VPGRLNQTAFIASRPGVFYGQCSE 198
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-184 1.14e-91

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 267.39  E-value: 1.14e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00023  24 PVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTK--LEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKT 158
Cdd:MTH00023 104 LTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKI 183

                        170       180
                 ....*....|....*....|....*.
gi 343409384 159 DATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00023 184 DAVPGRLNQTGFFIKRPGVFYGQCSE 209
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-184 1.41e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 264.05  E-value: 1.41e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00185  15 PVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00185  95 LTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00185 175 VPGRLNQATFIISRPGLYYGQCSE 198
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-184 2.50e-90

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 263.50  E-value: 2.50e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00098  15 PIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00098  95 LTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00098 175 IPGRLNQTTLMSTRPGLYYGQCSE 198
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-184 7.98e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 262.02  E-value: 7.98e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00076  15 PIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:MTH00076  95 LTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDA 174

                        170       180
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00076 175 IPGRLNQTSFIASRPGVYYGQCSE 198
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-184 3.84e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 253.16  E-value: 3.84e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT 80
Cdd:MTH00051  17 PVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDF--TKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKT 158
Cdd:MTH00051  97 LTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKI 176

                        170       180
                 ....*....|....*....|....*.
gi 343409384 159 DATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00051 177 DAVPGRLNQTSFFIKRPGVFYGQCSE 202
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 79-184 9.07e-74

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 217.82  E-value: 9.07e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  79 PTLTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKT 158
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100
                 ....*....|....*....|....*.
gi 343409384 159 DATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSE 106
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
81-184 1.63e-67

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 201.87  E-value: 1.63e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   81 LTLKAVGHQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....
gi 343409384  161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSE 104
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-184 4.73e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 200.64  E-value: 4.73e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITTTVSYMMI-TLIRNKQTSRF--MLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDE-V 76
Cdd:MTH00027  43 PVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYYwnKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEcG 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  77 QTPTLTLKAVGHQWYWSYEYSDFTK--LEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSL 154
Cdd:MTH00027 123 FSANITIKVTGHQWYWSYSYEDYGEknIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSL 202

                        170       180       190
                 ....*....|....*....|....*....|
gi 343409384 155 GVKTDATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00027 203 AVKMDAVPGRINETGFLIKRPGIFYGQCSE 232
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 9-184 1.41e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 190.61  E-value: 1.41e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   9 FHDHVLMIMLMITTTVSYMMITLIRNKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMDEVQTPT-LTLKAVG 87
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNLDSnLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  88 HQWYWSYEYSDFTKLEFDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQ 167
Cdd:MTH00080 105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                        170
                 ....*....|....*..
gi 343409384 168 TSFSISRPGILYGQCSE 184
Cdd:MTH00080 185 LCYSFPMPGVFYGQCSE 201
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-184 3.24e-42

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 141.12  E-value: 3.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   1 PLMEQLIFFHDHVLMIMLMITT-TVSYMMITLIR-----NKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRLLYLMD 74
Cdd:COG1622   27 PIAEEIDDLFWVSLIIMLVIFVlVFGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  75 EVQTPTLTLKAVGHQWYWSYEYsdftklefdsymiPQEEQqestfrllDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSL 154
Cdd:COG1622  107 DAPEDPLTVEVTGYQWKWLFRY-------------PDQGI--------ATVNELVLPVGRPVRFLLTSADVIHSFWVPAL 165

                        170       180       190
                 ....*....|....*....|....*....|
gi 343409384 155 GVKTDATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:COG1622  166 GGKQDAIPGRVTELWFTADKPGTYRGQCAE 195
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-184 1.90e-35

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: 122.87  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384    1 PLMEQLIFFHDHVLMIMLMITTTV-SYMMITLIRNKQTSRFML-----EGQMIETTWTIAPAIILV-FIAMPSLRLLYLM 73
Cdd:TIGR02866   4 EIAQQIAFLFLFVLAVSTLISLLVaALLAYVVWKFRRKGDEEKpsqihGNRRLEYVWTVIPLIIVVgLFAATAKGLLYLE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   74 DEVQTPTLTLKAVGHQWYWSYEYSdftklefdsymipqeeqqESTFRlldTDNRIVLPMNSPIRLIVTAADVLHSWTIPS 153
Cdd:TIGR02866  84 RPIPKDALKVKVTGYQWWWDFEYP------------------ESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPE 142

                         170       180       190
                  ....*....|....*....|....*....|.
gi 343409384  154 LGVKTDATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:TIGR02866 143 LGGKIDAIPGQTNALWFNADEPGVYYGFCAE 173
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 3-184 2.27e-34

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 120.06  E-value: 2.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384   3 MEQLIFFHDHVLMIMLMITTTVSYMMITLIRN----KQTSRFMLEGQMIETTWTIAPAIILVFIAmpSLRLLYLM-DEVQ 77
Cdd:MTH00047   1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQvvsgNGSVNFGSENQVLELLWTVVPTLLVLVLC--FLNLNFITsDLDC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  78 TPTLTLKAVGHQWYWSYEYSDftKLEFDSYMipqeeqqesTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVK 157
Cdd:MTH00047  79 FSSETIKVIGHQWYWSYEYSF--GGSYDSFM---------TDDIFGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147

                        170       180
                 ....*....|....*....|....*..
gi 343409384 158 TDATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:MTH00047 148 MDAIPGRINHLFFCPDRHGVFVGYCSE 174
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 104-184 1.11e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 99.12  E-value: 1.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384 104 FDSYMIPQEEQQESTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCS 183
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130


                 .
gi 343409384 184 E 184
Cdd:PTZ00047 131 E 131
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 80-184 1.04e-24

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: 92.30  E-value: 1.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  80 TLTLKAVGHQWYWSYEYSDftklefdsymipqeeqqeSTFRLLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTD 159
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPD------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100
                 ....*....|....*....|....*
gi 343409384 160 ATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAE 87
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 81-184 7.92e-23

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: 87.35  E-value: 7.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  81 LTLKAVGHQWYWSYEYSDFTklefdsymipqeeqqestfrlldTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDA 160
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100
                 ....*....|....*....|....
gi 343409384 161 TPGRLNQTSFSISRPGILYGQCSE 184
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAE 81
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-69 3.07e-20

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: 80.45  E-value: 3.07e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343409384    1 PLMEQLIFFHDHVLMIMLMITTTVSYMMITLIR------NKQTSRFMLEGQMIETTWTIAPAIILVFIAMPSLRL 69
Cdd:pfam02790  15 PLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 80-184 8.44e-19

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 77.30  E-value: 8.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  80 TLTLKAVGHQWYWSYEYsdftklefdsymiPQEEQQESTFRLLDTdNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTD 159
Cdd:cd13919    1 ALVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                         90       100
                 ....*....|....*....|....*
gi 343409384 160 ATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:cd13919   67 AVPGRTTRLWFTPTREGEYEVRCAE 91
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 80-184 1.04e-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: 68.81  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  80 TLTLKAVGHQWYWSYEYSDFTKlefdsymipqeeqqestfrlldTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTD 159
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYPNGKR----------------------EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100
                 ....*....|....*....|....*
gi 343409384 160 ATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCTE 83
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 56-184 1.16e-14

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: 67.48  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  56 AIILV-FIAMPSLRLLYLMD---EVQTPTLTLKAVGHQWYWSYEYsdftklefdsymiPQEEQQESTFRLldtdnrivlP 131
Cdd:cd13918    4 AIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEY-------------PNGVTTGNTLRV---------P 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 343409384 132 MNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQCSE 184
Cdd:cd13918   62 ADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYE 114
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 82-184 2.12e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 63.20  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343409384  82 TLKAVGHQWYWSYEYsdftklefdsymiPQEEqqestfrlLDTDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDAT 161
Cdd:cd13914    2 EIEVEAYQWGWEFSY-------------PEAN--------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                         90       100
                 ....*....|....*....|...
gi 343409384 162 PGRLNQTSFSISRPGILYGQCSE 184
Cdd:cd13914   61 PGQYNTIKTEATEEGEYQLYCAE 83
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 124-176 3.19e-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: 3.19e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 343409384 124 TDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPG 176
Cdd:cd13913   23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPG 75
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 124-181 4.26e-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: 37.91  E-value: 4.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 343409384 124 TDNRIVLPMNSPIRLIVTAADVLHSWTIPSLGVKTDATPGRLNQTSFSISRPGILYGQ 181
Cdd:cd04212   23 TVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80
 
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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