NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|148728387|gb|ABR08668|]
View 

cytochrome oxidase subunit II, partial (mitochondrion) [Conocephalus percaudatus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-176 5.29e-118

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 332.95  E-value: 5.29e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00154  27 TMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFSEpYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00154 107 SYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFL 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00154 186 INRPGLFFGQCSEICG 201
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-176 5.29e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 332.95  E-value: 5.29e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00154  27 TMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFSEpYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00154 107 SYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFL 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00154 186 INRPGLFFGQCSEICG 201
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 67-176 1.25e-73

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: 217.05  E-value: 1.25e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  67 PMITVKTVGHQWYWSYEYTDFsEPYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVK 146
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDF-NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 148728387 147 VDATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:cd13912   80 VDAVPGRLNQTSFFIERPGVYYGQCSEICG 109
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
69-176 3.39e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 195.32  E-value: 3.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   69 ITVKTVGHQWYWSYEYTDFsEPYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVD 148
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDF-GDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100
                  ....*....|....*....|....*...
gi 148728387  149 ATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICG 107
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-176 2.68e-37

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 128.02  E-value: 2.68e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMtsLFFNK---------FTHRFllegqTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITV 71
Cdd:COG1622   43 MLVIFVLVFGLLLYFA--IRYRRrkgdadpaqFHHNT-----KLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  72 KTVGHQWYWSYEYTDFSEpyefdsymipynemasdgfrllDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATP 151
Cdd:COG1622  116 EVTGYQWKWLFRYPDQGI----------------------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIP 173

                        170       180
                 ....*....|....*....|....*
gi 148728387 152 GRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:COG1622  174 GRVTELWFTADKPGTYRGQCAELCG 198
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-176 8.24e-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: 107.85  E-value: 8.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387    1 ALMILLMITVlVAYIMTSLFfnKFTHR-------FLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDP-MITVK 72
Cdd:TIGR02866  18 AVSTLISLLV-AALLAYVVW--KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYLERPIPKdALKVK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   73 TVGHQWYWSYEYTDFsepyefdsymipynemasdGFRlldVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPG 152
Cdd:TIGR02866  95 VTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPG 152

                         170       180
                  ....*....|....*....|....
gi 148728387  153 RLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:TIGR02866 153 QTNALWFNADEPGVYYGFCAELCG 176
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-176 5.29e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 332.95  E-value: 5.29e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00154  27 TMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFSEpYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00154 107 SYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFL 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00154 186 INRPGLFFGQCSEICG 201
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-176 1.10e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 266.42  E-value: 1.10e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00140  27 AMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFSEpYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00140 107 SYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFE 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00140 186 PKRPGVFYGQCSEICG 201
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-176 1.97e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 263.12  E-value: 1.97e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00139  27 AMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFsEPYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00139 107 SYEYSDF-KNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFF 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00139 186 INRPGVFYGQCSEICG 201
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-176 2.57e-88

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 257.86  E-value: 2.57e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00008  27 ALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFSEpYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00008 107 SYEYSDFSN-LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFT 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00008 186 ITRPGVFYGQCSEICG 201
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-176 1.84e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 255.78  E-value: 1.84e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00038  27 ALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFSEpYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00038 107 SYEYTDYND-LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFF 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00038 186 ISRTGLFYGQCSEICG 201
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-176 4.04e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 254.84  E-value: 4.04e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00117  27 ALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFsEPYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00117 107 SYEYTDY-KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFI 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00117 186 TTRPGVFYGQCSEICG 201
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-176 1.67e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 248.36  E-value: 1.67e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00168  27 ALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFSEpYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00168 107 SYEYTDYND-LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFL 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00168 186 SSRPGSFYGQCSEICG 201
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-176 2.61e-83

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 245.82  E-value: 2.61e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   2 LMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYWS 81
Cdd:MTH00023  37 MFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWS 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  82 YEYTDF-SEPYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00023 117 YEYSDYeGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFF 196

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00023 197 IKRPGVFYGQCSEICG 212
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-176 5.38e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 239.62  E-value: 5.38e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00129  27 ALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFsEPYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00129 107 SYEYTDY-EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFI 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00129 186 ASRPGVFYGQCSEICG 201
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-176 1.10e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 236.32  E-value: 1.10e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00185  27 TLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFsEPYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00185 107 SYEYTDY-EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFI 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00185 186 ISRPGLYYGQCSEICG 201
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-176 3.90e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 235.06  E-value: 3.90e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   2 LMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYWS 81
Cdd:MTH00051  30 MFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  82 YEYTDF-SEPYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00051 110 YEYSDYgTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFF 189

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00051 190 IKRPGVFYGQCSEICG 205
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-176 4.30e-79

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 234.61  E-value: 4.30e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00098  27 TLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFsEPYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00098 107 SYEYTDY-EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLM 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00098 186 STRPGLYYGQCSEICG 201
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-176 2.42e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 227.74  E-value: 2.42e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYW 80
Cdd:MTH00076  27 ALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFSEpYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00076 107 SYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFI 185

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00076 186 ASRPGVYYGQCSEICG 201
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 67-176 1.25e-73

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: 217.05  E-value: 1.25e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  67 PMITVKTVGHQWYWSYEYTDFsEPYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVK 146
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDF-NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 148728387 147 VDATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:cd13912   80 VDAVPGRLNQTSFFIERPGVYYGQCSEICG 109
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
69-176 3.39e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 195.32  E-value: 3.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   69 ITVKTVGHQWYWSYEYTDFsEPYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVD 148
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDF-GDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100
                  ....*....|....*....|....*...
gi 148728387  149 ATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICG 107
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-176 3.40e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 180.22  E-value: 3.40e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMTSLFFNKfthrflLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDES-MDPMITVKTVGHQWY 79
Cdd:MTH00027  64 GVVLWLIIRILLGNNYYSYYWNK------LDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECgFSANITIKVTGHQWY 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  80 WSYEYTDFSEP-YEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTN 158
Cdd:MTH00027 138 WSYSYEDYGEKnIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETG 217

                        170
                 ....*....|....*...
gi 148728387 159 FFMNRPGLFYGQCSEICG 176
Cdd:MTH00027 218 FLIKRPGIFYGQCSEICG 235
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 2-176 1.35e-48

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 157.09  E-value: 1.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   2 LMILLMITVLVAYIMTSLFFNKFTHRFLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLD-ESMDPMITVKTVGHQWYW 80
Cdd:MTH00080  30 LFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTGHQWYW 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  81 SYEYTDFSEpYEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00080 110 SYEFSDIPG-LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYS 188

                        170
                 ....*....|....*.
gi 148728387 161 MNRPGLFYGQCSEICG 176
Cdd:MTH00080 189 FPMPGVFYGQCSEICG 204
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-176 2.68e-37

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 128.02  E-value: 2.68e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   1 ALMILLMITVLVAYIMtsLFFNK---------FTHRFllegqTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPMITV 71
Cdd:COG1622   43 MLVIFVLVFGLLLYFA--IRYRRrkgdadpaqFHHNT-----KLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  72 KTVGHQWYWSYEYTDFSEpyefdsymipynemasdgfrllDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATP 151
Cdd:COG1622  116 EVTGYQWKWLFRYPDQGI----------------------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIP 173

                        170       180
                 ....*....|....*....|....*
gi 148728387 152 GRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:COG1622  174 GRVTELWFTADKPGTYRGQCAELCG 198
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 31-176 1.84e-33

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 117.36  E-value: 1.84e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  31 EGQTIEVIWTILPAItLIFIALPSLRLLYLLDESMDPMITVKTVGHQWYWSYEYtdfSEPYEFDSYMIpynemaSDGFrl 110
Cdd:MTH00047  45 ENQVLELLWTVVPTL-LVLVLCFLNLNFITSDLDCFSSETIKVIGHQWYWSYEY---SFGGSYDSFMT------DDIF-- 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148728387 111 lDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:MTH00047 113 -GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCG 177
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 91-176 1.12e-32

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 114.15  E-value: 1.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  91 YEFDSYMIPYNEMASDGFRLLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFFMNRPGLFYGQ 170
Cdd:PTZ00047  49 YSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128


                 ....*.
gi 148728387 171 CSEICG 176
Cdd:PTZ00047 129 CSEMCG 134
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-176 8.24e-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: 107.85  E-value: 8.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387    1 ALMILLMITVlVAYIMTSLFfnKFTHR-------FLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDP-MITVK 72
Cdd:TIGR02866  18 AVSTLISLLV-AALLAYVVW--KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYLERPIPKdALKVK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   73 TVGHQWYWSYEYTDFsepyefdsymipynemasdGFRlldVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPG 152
Cdd:TIGR02866  95 VTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPG 152

                         170       180
                  ....*....|....*....|....
gi 148728387  153 RLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:TIGR02866 153 QTNALWFNADEPGVYYGFCAELCG 176
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 69-176 1.12e-22

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: 86.58  E-value: 1.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  69 ITVKTVGHQWYWSYEYTDfsepyefdsymipynemasdgfrlLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVD 148
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                         90       100
                 ....*....|....*....|....*...
gi 148728387 149 ATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:cd13842   57 AVPGYTSELWFVADKPGTYTIICAEYCG 84
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 69-176 2.94e-20

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: 80.74  E-value: 2.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  69 ITVKTVGHQWYWSYEYTDfSEPYEFDSYmipyNEMasdgfrlldvdnrtILPMNTQVRMLVTAADVLHSWTVPALGVKVD 148
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPD-EPGRGIVTA----NEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100
                 ....*....|....*....|....*...
gi 148728387 149 ATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCG 90
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 69-176 1.61e-17

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 73.44  E-value: 1.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  69 ITVKTVGHQWYWSYEYTDfSEPYEFDSYMIPYNEMasdgfrlldvdnrtILPMNTQVRMLVTAADVLHSWTVPALGVKVD 148
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPG-GDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                         90       100
                 ....*....|....*....|....*...
gi 148728387 149 ATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:cd13919   67 AVPGRTTRLWFTPTREGEYEVRCAELCG 94
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 69-176 8.43e-16

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 68.81  E-value: 8.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  69 ITVKTVGHQWYWSYEYtdfsepyefdsymipynemaSDGFRlldVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVD 148
Cdd:cd13915    2 LEIQVTGRQWMWEFTY--------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100
                 ....*....|....*....|....*...
gi 148728387 149 ATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCTEYCG 86
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 69-176 2.46e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 65.51  E-value: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  69 ITVKTVGHQWYWSYEYTDFSepyefdsymipynemasdgfrlLDVDNRTILPMNTQVRMLVTAADVLHSWTVPALGVKVD 148
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEAN----------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                         90       100
                 ....*....|....*....|....*...
gi 148728387 149 ATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:cd13914   59 AFPGQYNTIKTEATEEGEYQLYCAEYCG 86
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-51 9.57e-13

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: 60.81  E-value: 9.57e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148728387    1 ALMILLMITVLVAYIMTSLFF------NKFTHRFLLEGQTIEVIWTILPAITLIFIA 51
Cdd:pfam02790  27 IMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 62-176 1.53e-12

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 61.70  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  62 DESMDPMITVKTVGHQWYWSYEYtdfSEPYEFDSYMIpynemasdgfrlldvdnrtiLPMNTQVRMLVTAADVLHSWTVP 141
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEY---PNGVTTGNTLR--------------------VPADTPIALRVTSTDVFHTFGIP 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 148728387 142 ALGVKVDATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:cd13918   83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCG 117
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 119-176 7.55e-07

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: 45.25  E-value: 7.55e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148728387 119 LPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCG 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 115-170 1.97e-05

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 41.38  E-value: 1.97e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148728387 115 NRTILPMNTQVRMLVTAADVLHSWTVPALGVKVDATPGRLNQTNFFMNRPGLFYGQ 170
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 69-176 9.52e-04

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 36.59  E-value: 9.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  69 ITVKTVGHQWYWsyeytdfsepyefdsymipynEMasdgfrlldvdNRTILPMNTQVRMLVTAADVLHSWTV--PALGV- 145
Cdd:cd13916    1 QVVAVTGHQWYW---------------------EL-----------SRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLl 48

                         90       100       110
                 ....*....|....*....|....*....|..
gi 148728387 146 -KVDATPGRLNQTNFFMNRPGLFYGQCSEICG 176
Cdd:cd13916   49 aQTQAMPGYTNVLRYTFDKPGTYTILCLEYCG 80
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 5-169 2.35e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 37.47  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387   5 LLMITVLVAYIMTSLFFNKF-------------THRFLLEGqtieVIWTIlPAITLIFIALPSLRLLYLLDESmDPM--- 68
Cdd:PRK10525  50 LMLIVVIPAILMAVGFAWKYrasnkdakyspnwSHSNKVEA----VVWTV-PILIIIFLAVLTWKTTHALEPS-KPLahd 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728387  69 ---ITVKTVGHQWYWSYEYTDFSepyefdsyMIPYNEMAsdgfrlldvdnrtiLPMNTQVRMLVTAADVLHSWTVPALGV 145
Cdd:PRK10525 124 ekpITIEVVSMDWKWFFIYPEQG--------IATVNEIA--------------FPANVPVYFKVTSNSVMNSFFIPRLGS 181

                        170       180
                 ....*....|....*....|....
gi 148728387 146 KVDATPGRLNQTNFFMNRPGLFYG 169
Cdd:PRK10525 182 QIYAMAGMQTRLHLIANEPGTYDG 205
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH