NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1778128408|ref|YP_009711014|]
View 

cytochrome c oxidase subunit II (mitochondrion) [Acosmetura nigrogeniculata]

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
 1-227 1.41e-153

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 425.01  E-value: 1.41e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFVTPhEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWIINS 227
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 1.41e-153

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 425.01  E-value: 1.41e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFVTPhEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWIINS 227
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-223 2.30e-86

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: 251.34  E-value: 2.30e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  93 PIITVKTVGHQWYWSYEYTDFVTpHEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADVLHSWTIPAMGVK 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1778128408 173 VDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINW 223
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-215 1.83e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 221.13  E-value: 1.83e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  95 ITVKTVGHQWYWSYEYTDFVTPhEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADVLHSWTIPAMGVKVD 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDL-EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1778128408 175 ATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESV 215
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-224 3.49e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 160.38  E-value: 3.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   6 DLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAyIMLTLFFNKYTHR-------YLLEGQTIEVIWTILPAITLIFIAL 78
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVF-GLLLYFAIRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  79 PSLRLLYLLDESMDPIITVKTVGHQWYWSYEYTDfvtphefdsymipYNEmsnngfrllDVDNRTILPFNTQIRMLITAA 158
Cdd:COG1622    97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-------------QGI---------ATVNELVLPVGRPVRFLLTSA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778128408 159 DVLHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWI 224
Cdd:COG1622   155 DVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-224 9.71e-39

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: 132.89  E-value: 9.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  13 ASPLMEQLIFFHDHTLLILLMITVLV-AYIMLTLFfnKYTHR-------YLLEGQTIEVIWTILPAITLIFIALPSLRLL 84
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVW--KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  85 YLLDESMDP-IITVKTVGHQWYWSYEYtdfvtphefdsymipynemSNNGFRlldVDNRTILPFNTQIRMLITAADVLHS 163
Cdd:TIGR02866  80 LYLERPIPKdALKVKVTGYQWWWDFEY-------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778128408 164 WTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWI 224
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 1.41e-153

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 425.01  E-value: 1.41e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFVTPhEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWIINS 227
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 1.22e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 339.39  E-value: 1.22e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFvTPHEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDF-KNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWIIN 226
Cdd:MTH00139  160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-227 5.76e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 337.68  E-value: 5.76e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFVTpHEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWIINS 227
Cdd:MTH00140  160 IHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-226 9.74e-115

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 327.20  E-value: 9.74e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFVTPhEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNL-EFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWIIN 226
Cdd:MTH00008  160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-226 2.14e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 323.47  E-value: 2.14e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFVTpHEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWIIN 226
Cdd:MTH00168  160 LHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-224 8.55e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 322.25  E-value: 8.55e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFvTPHEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDY-KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWI 224
Cdd:MTH00117  160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWS 223
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-226 4.85e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 320.11  E-value: 4.85e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFvTPHEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY-NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWIIN 226
Cdd:MTH00038  160 LHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-223 8.99e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 297.01  E-value: 8.99e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFvTPHEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINW 223
Cdd:MTH00129  160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-226 1.21e-102

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 297.05  E-value: 1.21e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   7 LNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYL 86
Cdd:MTH00023   16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  87 LDESMDPIITVKTVGHQWYWSYEYTDFVTPH-EFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADVLHSWT 165
Cdd:MTH00023   96 MDEVVSPALTIKAIGHQWYWSYEYSDYEGETlEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778128408 166 IPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWIIN 226
Cdd:MTH00023  176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-223 8.84e-101

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 291.62  E-value: 8.84e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFvTPHEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY-EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINW 223
Cdd:MTH00098  160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-224 1.56e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 291.30  E-value: 1.56e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   7 LNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYL 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  87 LDESMDPIITVKTVGHQWYWSYEYTDFVTPH-EFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADVLHSWT 165
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYGTDTiEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1778128408 166 IPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWI 224
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-223 3.99e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 290.25  E-value: 3.99e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFVTpHEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQ-LEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINW 223
Cdd:MTH00185  160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-227 1.78e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 283.21  E-value: 1.78e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  81 LRLLYLLDESMDPIITVKTVGHQWYWSYEYTDFvTPHEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADV 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDY-EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1778128408 161 LHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWIINS 227
Cdd:MTH00076  160 LHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-223 2.30e-86

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: 251.34  E-value: 2.30e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  93 PIITVKTVGHQWYWSYEYTDFVTpHEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADVLHSWTIPAMGVK 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1778128408 173 VDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINW 223
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-215 1.83e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 221.13  E-value: 1.83e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  95 ITVKTVGHQWYWSYEYTDFVTPhEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADVLHSWTIPAMGVKVD 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDL-EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1778128408 175 ATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESV 215
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-224 4.42e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 225.29  E-value: 4.42e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   7 LNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYL---LEGQTIEVIWTILPAITLIFIALPSLRL 83
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  84 LYLLDES-MDPIITVKTVGHQWYWSYEYTDFVTPH-EFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADVL 161
Cdd:MTH00027  115 LYIMDECgFSANITIKVTGHQWYWSYSYEDYGEKNiEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778128408 162 HSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWI 224
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-226 7.13e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 195.61  E-value: 7.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   6 DLNLQNSA-SPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLL 84
Cdd:MTH00080    7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  85 YLLD-ESMDPIITVKTVGHQWYWSYEYTDFVTPhEFDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADVLHS 163
Cdd:MTH00080   87 YYYGlMNLDSNLTVKVTGHQWYWSYEFSDIPGL-EFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHS 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778128408 164 WTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWIIN 226
Cdd:MTH00080  166 WALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKL 228
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-224 3.49e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 160.38  E-value: 3.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   6 DLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAyIMLTLFFNKYTHR-------YLLEGQTIEVIWTILPAITLIFIAL 78
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVF-GLLLYFAIRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  79 PSLRLLYLLDESMDPIITVKTVGHQWYWSYEYTDfvtphefdsymipYNEmsnngfrllDVDNRTILPFNTQIRMLITAA 158
Cdd:COG1622    97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-------------QGI---------ATVNELVLPVGRPVRFLLTSA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778128408 159 DVLHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWI 224
Cdd:COG1622   155 DVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-215 7.92e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 135.47  E-value: 7.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  17 MEQLIFFHDHTLLILLMITVLVAYIMLTLFFNKYTHRYLL----EGQTIEVIWTILPAItLIFIALPSLRLLYLLDESMD 92
Cdd:MTH00047    1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSGNGSVnfgsENQVLELLWTVVPTL-LVLVLCFLNLNFITSDLDCF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  93 PIITVKTVGHQWYWSYEYTDfvtPHEFDSYMIPYNEMSNNGFRLLdvdnrtilpFNTQIRMLITAADVLHSWTIPAMGVK 172
Cdd:MTH00047   80 SSETIKVIGHQWYWSYEYSF---GGSYDSFMTDDIFGVDKPLRLV---------YGVPYHLLVTSSDVIHSFSVPDLNLK 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1778128408 173 VDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESV 215
Cdd:MTH00047  148 MDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 119-220 2.47e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 133.02  E-value: 2.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408 119 FDSYMIPYNEMSNNGFRLLDVDNRTILPFNTQIRMLITAADVLHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCS 198
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 1778128408 199 EICGTNHSFMPIVLESVNTKTF 220
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-224 9.71e-39

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: 132.89  E-value: 9.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  13 ASPLMEQLIFFHDHTLLILLMITVLV-AYIMLTLFfnKYTHR-------YLLEGQTIEVIWTILPAITLIFIALPSLRLL 84
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVW--KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  85 YLLDESMDP-IITVKTVGHQWYWSYEYtdfvtphefdsymipynemSNNGFRlldVDNRTILPFNTQIRMLITAADVLHS 163
Cdd:TIGR02866  80 LYLERPIPKdALKVKVTGYQWWWDFEY-------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778128408 164 WTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWI 224
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-213 8.39e-27

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: 98.91  E-value: 8.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  95 ITVKTVGHQWYWSYEYTDFVTPHEFdsymipynemsnngfrlldvdnrtILPFNTQIRMLITAADVLHSWTIPAMGVKVD 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVRTPNEI------------------------VVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1778128408 175 ATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLE 213
Cdd:cd13842    57 AVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 3.41e-24

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: 92.01  E-value: 3.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408   1 MATWSDLNLQNSASPLMEQLIFFHDHTLLILLMITVLVAYIMLTLFF------NKYTHRYLLEGQTIEVIWTILPAITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 1778128408  75 FIA 77
Cdd:pfam02790  81 LIA 83
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-208 1.58e-21

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: 85.36  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  95 ITVKTVGHQWYWSYEYTD-----FVTPhefdsymipyNEMsnngfrlldvdnrtILPFNTQIRMLITAADVLHSWTIPAM 169
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDepgrgIVTA----------NEL--------------HIPVGRPVRLRLTSADVIHSFWVPSL 57

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1778128408 170 GVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFM 208
Cdd:cd04213    58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-208 1.81e-21

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 85.38  E-value: 1.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  95 ITVKTVGHQWYWSYEYTDFVTPHEFDSyMIPYNEMsnngfrlldvdnrtILPFNTQIRMLITAADVLHSWTIPAMGVKVD 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDD-DVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1778128408 175 ATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFM 208
Cdd:cd13919    67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-208 1.14e-20

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: 83.06  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  95 ITVKTVGHQWYWSYEYTdfvtphefdsymipynemsnNGFRlldVDNRTILPFNTQIRMLITAADVLHSWTIPAMGVKVD 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTYP--------------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1778128408 175 ATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFM 208
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-223 9.45e-19

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 79.04  E-value: 9.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  88 DESMDPIITVKTVGHQWYWSYEYTDFVTphefdsymipynemSNNGFRLldvdnrtilPFNTQIRMLITAADVLHSWTIP 167
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPNGVT--------------TGNTLRV---------PADTPIALRVTSTDVFHTFGIP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1778128408 168 AMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINW 223
Cdd:cd13918    83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-224 1.15e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 75.52  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  95 ITVKTVGHQWYWSYEYtdfvtphefdsymipyNEMSNNGFrlldvdNRTILPFNTQIRMLITAADVLHSWTIPAMGVKVD 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSY----------------PEANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1778128408 175 ATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESVNTKTFINWI 224
Cdd:cd13914    59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 145-208 3.97e-09

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: 52.19  E-value: 3.97e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1778128408 145 LPFNTQIRMLITAADVLHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFM 208
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-208 5.34e-07

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: 46.22  E-value: 5.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  95 ITVKTVGHQWYWsyeytdfvtphefdsymipynEMSnngfrlldvdnRTILPFNTQIRMLITAADVLHSWTI--PAMGV- 171
Cdd:cd13916     1 QVVAVTGHQWYW---------------------ELS-----------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLl 48

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1778128408 172 -KVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFM 208
Cdd:cd13916    49 aQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 141-215 1.00e-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: 40.22  E-value: 1.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778128408 141 NRTILPFNTQIRMLITAADVLHSWTIPAMGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFMPIVLESV 215
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 154-213 1.49e-03

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 37.21  E-value: 1.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778128408 154 LITAADVLHSWTIPAMGVKVDA---------------TPGRLNQTSFFMNRPGLYYGQCSEICGtNHSFMPIVLE 213
Cdd:cd00920    37 FVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 29-208 2.54e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 38.24  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  29 LIL----LMITVLVAYIMLTLFFN----------KYTHRYLLEGQTIEVIWTIlPAITLIFIALPSLRLLYLLDESmDPI 94
Cdd:PRK10525   43 LILtafgLMLIVVIPAILMAVGFAwkyrasnkdaKYSPNWSHSNKVEAVVWTV-PILIIIFLAVLTWKTTHALEPS-KPL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778128408  95 ------ITVKTVGHQWYWSYEYTDfvtphefdSYMIPYNEMSnngfrlldvdnrtiLPFNTQIRMLITAADVLHSWTIPA 168
Cdd:PRK10525  121 ahdekpITIEVVSMDWKWFFIYPE--------QGIATVNEIA--------------FPANVPVYFKVTSNSVMNSFFIPR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1778128408 169 MGVKVDATPGRLNQTSFFMNRPGLYYGQCSEICGTNHSFM 208
Cdd:PRK10525  179 LGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGM 218
 
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