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Conserved domains on  [gi|18182658|gb|AAL65222|]
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cytochrome oxidase subunit 2, partial (mitochondrion) [Kawanaphila nartee]

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
 1-186 9.77e-126

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 352.98  E-value: 9.77e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00154  15 PLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00154  95 ITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVD 173

                        170       180
                 ....*....|....*....|....*.
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00154 174 AVPGRLNQLNFLINRPGLFFGQCSEI 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-186 9.77e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 352.98  E-value: 9.77e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00154  15 PLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00154  95 ITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVD 173

                        170       180
                 ....*....|....*....|....*.
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00154 174 AVPGRLNQLNFLINRPGLFFGQCSEI 199
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 79-186 2.62e-70

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: 209.35  E-value: 2.62e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658  79 PIITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVK 158
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                        90       100
                ....*....|....*....|....*...
gi 18182658 159 VDATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:cd13912  80 VDAVPGRLNQTSFFIERPGVYYGQCSEI 107
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
81-186 9.92e-63

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 189.54  E-value: 9.92e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100
                  ....*....|....*....|....*.
gi 18182658   161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEI 105
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-186 6.53e-35

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 122.24  E-value: 6.53e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   1 PLMEQLTFFHDHTLLILLMITVLV-AYIMASLFF-----NKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLD 74
Cdd:COG1622  27 PIAEEIDDLFWVSLIIMLVIFVLVfGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALD 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658  75 ESMDPIITVKTVGHQWYWSYEYTDfttpyefdaymipYNEmnlngfrllDVDNRTVLPMSTQVRMLVTAADVLHSWTVPA 154
Cdd:COG1622 107 DAPEDPLTVEVTGYQWKWLFRYPD-------------QGI---------ATVNELVLPVGRPVRFLLTSADVIHSFWVPA 164

                       170       180       190
                ....*....|....*....|....*....|..
gi 18182658 155 LGVKVDATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:COG1622 165 LGGKQDAIPGRVTELWFTADKPGTYRGQCAEL 196
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-185 5.75e-30

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: 109.01  E-value: 5.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658     1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFnKFTHR-------YLLEGQTIEVIWTILPAITLIFIALPSLRLLYLL 73
Cdd:TIGR02866   4 EIAQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    74 DESMDP-IITVKTVGHQWYWSYEYTDFTTpyefdaymipynemnlngfrllDVDNRTVLPMSTQVRMLVTAADVLHSWTV 152
Cdd:TIGR02866  83 ERPIPKdALKVKVTGYQWWWDFEYPESGF----------------------TTVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190
                  ....*....|....*....|....*....|...
gi 18182658   153 PALGVKVDATPGRLNQTSFFMNRPGLFYGQCSE 185
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAE 173
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-186 9.77e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 352.98  E-value: 9.77e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00154  15 PLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00154  95 ITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVD 173

                        170       180
                 ....*....|....*....|....*.
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00154 174 AVPGRLNQLNFLINRPGLFFGQCSEI 199
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-186 3.62e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 278.14  E-value: 3.62e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00139  15 PLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00139  95 LTFKAVGHQWYWSYEYSDFKN-LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKID 173

                        170       180
                 ....*....|....*....|....*.
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00139 174 AVPGRLNQVGFFINRPGVFYGQCSEI 199
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-186 3.63e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 275.66  E-value: 3.63e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00140  15 PLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00140  95 LTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVD 173

                        170       180
                 ....*....|....*....|....*.
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00140 174 AIPGRLNQLSFEPKRPGVFYGQCSEI 199
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-186 6.17e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 267.55  E-value: 6.17e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00117  15 PIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00117  95 LTIKAIGHQWYWSYEYTDYKD-LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTD 173

                        170       180
                 ....*....|....*....|....*.
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00117 174 AVPGRLNQTSFITTRPGVFYGQCSEI 199
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-186 1.09e-90

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 264.41  E-value: 1.09e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00008  15 PVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00008  95 ITLKTIGHQWYWSYEYSDFSN-LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVD 173

                        170       180
                 ....*....|....*....|....*.
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00008 174 AVPGRLNQIGFTITRPGVFYGQCSEI 199
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-186 2.11e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 261.17  E-value: 2.11e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00038  15 PLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00038  95 LTIKAIGHQWYWSYEYTDYND-LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMD 173

                        170       180
                 ....*....|....*....|....*.
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00038 174 AVPGRLNQTTFFISRTGLFYGQCSEI 199
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-186 9.34e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 256.83  E-value: 9.34e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00168  15 PVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00168  95 LTIKAVGHQWYWSYEYTDYND-LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMD 173

                        170       180
                 ....*....|....*....|....*.
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00168 174 AVPGRLNQLAFLSSRPGSFYGQCSEI 199
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-186 3.27e-85

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 251.21  E-value: 3.27e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00023  24 PVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTP-YEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKV 159
Cdd:MTH00023 104 LTIKAIGHQWYWSYEYSDYEGEtLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKI 183

                        170       180
                 ....*....|....*....|....*..
gi 18182658  160 DATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00023 184 DAVPGRLNQTGFFIKRPGVFYGQCSEI 210
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-187 1.64e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 246.34  E-value: 1.64e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00185  15 PVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00185  95 LTIKAMGHQWYWSYEYTDYEQ-LEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMD 173

                        170       180
                 ....*....|....*....|....*..
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEIW 187
Cdd:MTH00185 174 AVPGRLNQATFIISRPGLYYGQCSEIC 200
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-186 1.70e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 246.16  E-value: 1.70e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00129  15 PVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00129  95 LTIKAMGHQWYWSYEYTDYED-LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMD 173

                        170       180
                 ....*....|....*....|....*.
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00129 174 AVPGRLNQTAFIASRPGVFYGQCSEI 199
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-186 2.06e-83

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 246.17  E-value: 2.06e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00098  15 PIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00098  95 LTVKTMGHQWYWSYEYTDYED-LSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTD 173

                        170       180
                 ....*....|....*....|....*.
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00098 174 AIPGRLNQTTLMSTRPGLYYGQCSEI 199
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-186 9.02e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 244.69  E-value: 9.02e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00051  17 PVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDF-TTPYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKV 159
Cdd:MTH00051  97 LTIKAIGHQWYWSYEYSDYgTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKI 176

                        170       180
                 ....*....|....*....|....*..
gi 18182658  160 DATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00051 177 DAVPGRLNQTSFFIKRPGVFYGQCSEI 203
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-186 4.90e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 237.37  E-value: 4.90e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPI 80
Cdd:MTH00076  15 PIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:MTH00076  95 LTVKAIGHQWYWSYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTD 173

                        170       180
                 ....*....|....*....|....*.
gi 18182658  161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00076 174 AIPGRLNQTSFIASRPGVYYGQCSEI 199
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 79-186 2.62e-70

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: 209.35  E-value: 2.62e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658  79 PIITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVK 158
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                        90       100
                ....*....|....*....|....*...
gi 18182658 159 VDATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:cd13912  80 VDAVPGRLNQTSFFIERPGVYYGQCSEI 107
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
81-186 9.92e-63

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 189.54  E-value: 9.92e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    81 ITVKTVGHQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100
                  ....*....|....*....|....*.
gi 18182658   161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEI 105
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-186 1.70e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 184.07  E-value: 1.70e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFNKFTHRYL---LEGQTIEVIWTILPAITLIFIALPSLRLLYLLDES- 76
Cdd:MTH00027  43 PVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECg 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   77 MDPIITVKTVGHQWYWSYEYTDFTTP-YEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPAL 155
Cdd:MTH00027 123 FSANITIKVTGHQWYWSYSYEDYGEKnIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSL 202

                        170       180       190
                 ....*....|....*....|....*....|.
gi 18182658  156 GVKVDATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00027 203 AVKMDAVPGRINETGFLIKRPGIFYGQCSEI 233
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 9-186 3.23e-48

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 156.71  E-value: 3.23e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    9 FHDHTLLILLMITVLVAYIMASLFFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLD-ESMDPIITVKTVG 87
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   88 HQWYWSYEYTDFTTpYEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVDATPGRLN 167
Cdd:MTH00080 105 HQWYWSYEFSDIPG-LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILS 183

                        170
                 ....*....|....*....
gi 18182658  168 QTSFFMNRPGLFYGQCSEI 186
Cdd:MTH00080 184 TLCYSFPMPGVFYGQCSEI 202
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-186 6.53e-35

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 122.24  E-value: 6.53e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   1 PLMEQLTFFHDHTLLILLMITVLV-AYIMASLFF-----NKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLD 74
Cdd:COG1622  27 PIAEEIDDLFWVSLIIMLVIFVLVfGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALD 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658  75 ESMDPIITVKTVGHQWYWSYEYTDfttpyefdaymipYNEmnlngfrllDVDNRTVLPMSTQVRMLVTAADVLHSWTVPA 154
Cdd:COG1622 107 DAPEDPLTVEVTGYQWKWLFRYPD-------------QGI---------ATVNELVLPVGRPVRFLLTSADVIHSFWVPA 164

                       170       180       190
                ....*....|....*....|....*....|..
gi 18182658 155 LGVKVDATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:COG1622 165 LGGKQDAIPGRVTELWFTADKPGTYRGQCAEL 196
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-185 5.75e-30

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: 109.01  E-value: 5.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658     1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFFnKFTHR-------YLLEGQTIEVIWTILPAITLIFIALPSLRLLYLL 73
Cdd:TIGR02866   4 EIAQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658    74 DESMDP-IITVKTVGHQWYWSYEYTDFTTpyefdaymipynemnlngfrllDVDNRTVLPMSTQVRMLVTAADVLHSWTV 152
Cdd:TIGR02866  83 ERPIPKdALKVKVTGYQWWWDFEYPESGF----------------------TTVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190
                  ....*....|....*....|....*....|...
gi 18182658   153 PALGVKVDATPGRLNQTSFFMNRPGLFYGQCSE 185
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAE 173
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 43-185 3.34e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 106.58  E-value: 3.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658   43 EGQTIEVIWTILPAItLIFIALPSLRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFTtpyEFDAYMIPYNEMnlngfrl 122
Cdd:MTH00047  45 ENQVLELLWTVVPTL-LVLVLCFLNLNFITSDLDCFSSETIKVIGHQWYWSYEYSFGG---SYDSFMTDDIFG------- 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18182658  123 ldVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLFYGQCSE 185
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSE 174
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 103-186 5.93e-28

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 102.59  E-value: 5.93e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658  103 YEFDAYMIPYNEMNLNGFRLLDVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLFYGQ 182
Cdd:PTZ00047  49 YSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128


                 ....
gi 18182658  183 CSEI 186
Cdd:PTZ00047 129 CSEM 132
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 81-186 9.40e-21

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: 81.96  E-value: 9.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658  81 ITVKTVGHQWYWSYEYTDFTTPyefdaymipynemnlngfrlldvdNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPNVRTP------------------------NEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                        90       100
                ....*....|....*....|....*.
gi 18182658 161 ATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:cd13842  57 AVPGYTSELWFVADKPGTYTIICAEY 82
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-63 1.02e-18

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: 76.60  E-value: 1.02e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18182658     1 PLMEQLTFFHDHTLLILLMITVLVAYIMASLFF------NKFTHRYLLEGQTIEVIWTILPAITLIFIA 63
Cdd:pfam02790  15 PLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 81-185 1.83e-17

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: 73.81  E-value: 1.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658  81 ITVKTVGHQWYWSYEYTD-----FTTPyefdaymipyNEMnlngfrlldvdnrtVLPMSTQVRMLVTAADVLHSWTVPAL 155
Cdd:cd04213   2 LTIEVTGHQWWWEFRYPDepgrgIVTA----------NEL--------------HIPVGRPVRLRLTSADVIHSFWVPSL 57

                        90       100       110
                ....*....|....*....|....*....|
gi 18182658 156 GVKVDATPGRLNQTSFFMNRPGLFYGQCSE 185
Cdd:cd04213  58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAE 87
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 81-185 1.66e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 68.82  E-value: 1.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658  81 ITVKTVGHQWYWSYEYTDFTTPYEFDAyMIPYNEMnlngfrlldvdnrtVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGGDGKLGTDD-DVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                        90       100
                ....*....|....*....|....*
gi 18182658 161 ATPGRLNQTSFFMNRPGLFYGQCSE 185
Cdd:cd13919  67 AVPGRTTRLWFTPTREGEYEVRCAE 91
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 81-185 8.53e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 63.80  E-value: 8.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658  81 ITVKTVGHQWYWSYEYtdfttpyefdaymipynemnLNGFRlldVDNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:cd13915   2 LEIQVTGRQWMWEFTY--------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                        90       100
                ....*....|....*....|....*
gi 18182658 161 ATPGRLNQTSFFMNRPGLFYGQCSE 185
Cdd:cd13915  59 VVPGRYTYLWFEATKPGEYDLFCTE 83
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 81-185 2.14e-11

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: 57.80  E-value: 2.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658  81 ITVKTVGHQWYWSYEYtdfttpyefdaymipyNEMNLNGFrlldvdNRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVD 160
Cdd:cd13914   1 VEIEVEAYQWGWEFSY----------------PEANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                        90       100
                ....*....|....*....|....*
gi 18182658 161 ATPGRLNQTSFFMNRPGLFYGQCSE 185
Cdd:cd13914  59 AFPGQYNTIKTEATEEGEYQLYCAE 83
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 74-186 3.05e-10

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: 55.54  E-value: 3.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18182658  74 DESMDPIITVKTVGHQWYWSYEYTdfttpyefdaymipynemnlNGFRLLdvdNRTVLPMSTQVRMLVTAADVLHSWTVP 153
Cdd:cd13918  26 DEADEDALEVEVEGFQFGWQFEYP--------------------NGVTTG---NTLRVPADTPIALRVTSTDVFHTFGIP 82

                        90       100       110
                ....*....|....*....|....*....|...
gi 18182658 154 ALGVKVDATPGRLNQTSFFMNRPGLFYGQCSEI 186
Cdd:cd13918  83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYEL 115
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 127-185 6.11e-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: 40.25  E-value: 6.11e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18182658 127 NRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLFYGQCSE 185
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNE 83
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 127-182 2.51e-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: 38.68  E-value: 2.51e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18182658 127 NRTVLPMSTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLFYGQ 182
Cdd:cd04212  25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 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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