NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|225012910|ref|YP_002650707|]
View 

cytochrome c oxidase subunit II (mitochondrion) [Dermatophagoides pteronyssinus]

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
 1-236 7.69e-110

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 315.61  E-value: 7.69e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  81 MKVLYFMEDVKTPSLSFKVIAHQWYWSYVVPLFKNFSFKvngtsllsSYEYDSlLEDDVNAPRLLGCSSDLVIPLNSVSR 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFD--------SYMIPT-NELENNGFRLLDVDNRLVLPMNTQIR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225012910 161 LLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQFSKTYL 236
Cdd:MTH00154 152 ILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-236 7.69e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 315.61  E-value: 7.69e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  81 MKVLYFMEDVKTPSLSFKVIAHQWYWSYVVPLFKNFSFKvngtsllsSYEYDSlLEDDVNAPRLLGCSSDLVIPLNSVSR 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFD--------SYMIPT-NELENNGFRLLDVDNRLVLPMNTQIR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225012910 161 LLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQFSKTYL 236
Cdd:MTH00154 152 ILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-231 1.04e-52

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: 166.98  E-value: 1.04e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  93 PSLSFKVIAHQWYWSYVVPLFKNFSFkvngtsllssyeyDSLL--EDDVNA--PRLLGCSSDLVIPLNSVSRLLISSTDV 168
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEF-------------DSYMipEDDLEKgqLRLLEVDNRLVVPVNTHIRVLVTSADV 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225012910 169 IHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQF 231
Cdd:cd13912   68 IHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-231 6.10e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 160.76  E-value: 6.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   6 SLNFQDSSSPSMGELSVFHDHVVVVMSGVIILIsyiMIYMLYSVKFY---------KNLSEGTFIETIWSIVPAFLLIIL 76
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIRYrrrkgdadpAQFHHNTKLEIVWTVIPIIIVIVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  77 VLPSMKVLYFMEDVKTPSLSFKVIAHQWYWSYvvplfknfsfkvngtsllssyEYDSLLEDDVNaprllgcssDLVIPLN 156
Cdd:COG1622   95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLF---------------------RYPDQGIATVN---------ELVLPVG 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225012910 157 SVSRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQF 231
Cdd:COG1622  145 RPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-223 2.37e-44

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 145.25  E-value: 2.37e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   95 LSFKVIAHQWYWSYVVPLFKNFSFkvngtsllSSYEY-DSLLEDdvNAPRLLGCSSDLVIPLNSVSRLLISSTDVIHSFA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEF--------DSYMIpTEDLEE--GQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWA 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 225012910  174 VPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVV 223
Cdd:pfam00116  71 VPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-231 1.35e-35

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 125.57  E-value: 1.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   14 SPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYsvKFYKN--------LSEGTFIETIWSIVPAFLLIILVLPS-MKVL 84
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVW--KFRRKgdeekpsqIHGNRRLEYVWTVIPLIIVVGLFAATaKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   85 YFMEDVKTPSLSFKVIAHQWYWSYVVPlfkNFSFKVNGTsllssyeydslleddvnaprllgcssdLVIPLNSVSRLLIS 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYP---ESGFTTVNE---------------------------LVLPAGTPVELQVT 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225012910  165 STDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQF 231
Cdd:TIGR02866 131 SKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-236 7.69e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 315.61  E-value: 7.69e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  81 MKVLYFMEDVKTPSLSFKVIAHQWYWSYVVPLFKNFSFKvngtsllsSYEYDSlLEDDVNAPRLLGCSSDLVIPLNSVSR 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFD--------SYMIPT-NELENNGFRLLDVDNRLVLPMNTQIR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225012910 161 LLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQFSKTYL 236
Cdd:MTH00154 152 ILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-228 2.72e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 238.30  E-value: 2.72e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  81 MKVLYFMEDVKTPSLSFKVIAHQWYWSYVVPLFKNFsfkvngtsllssyEYDSLL--EDDVNA--PRLLGCSSDLVIPLN 156
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVI-------------EFDSYMvpENELELgdFRLLEVDNRLVLPYS 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225012910 157 SVSRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIF 228
Cdd:MTH00140 148 VDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDF 219
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-228 4.56e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 237.69  E-value: 4.56e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  81 MKVLYFMEDVKTPSLSFKVIAHQWYWSYVVPLFKNFSFkvngtsllSSYEY--DSLLEDDVnapRLLGCSSDLVIPLNSV 158
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSF--------DSYMIptEDLSSGEF---RLLEVDNRLVLPYKSN 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910 159 SRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIF 228
Cdd:MTH00139 150 IRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFF 219
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-234 4.04e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 235.19  E-value: 4.04e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  81 MKVLYFMEDVKTPSLSFKVIAHQWYWSYVVPLFKNFSFkvngtsllssyeyDSLLEDDVN----APRLLGCSSDLVIPLN 156
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSF-------------DSYMIPTQDlpngHFRLLEVDHRMVIPME 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225012910 157 SVSRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQFSKT 234
Cdd:MTH00117 148 SPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-228 6.37e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 234.49  E-value: 6.37e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  81 MKVLYFMEDVKTPSLSFKVIAHQWYWSYVVPLFKNFSFKvngtsllssyEYDSLLEDDVN-APRLLGCSSDLVIPLNSVS 159
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFD----------SYMVPTQDLSPgQFRLLEVDNRLVLPMDSKI 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225012910 160 RLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIF 228
Cdd:MTH00168 151 RVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETF 219
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-236 3.99e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 232.67  E-value: 3.99e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  81 MKVLYFMEDVKTPSLSFKVIAHQWYWSYVVPLFKNFSFKvngtsllssyEYDSLLED-DVNAPRLLGCSSDLVIPLNSVS 159
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFD----------SYMVPTSDlSTGLPRLLEVDNRLVLPYQTPI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225012910 160 RLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQFSKTYL 236
Cdd:MTH00038 151 RVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-223 3.33e-71

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 217.80  E-value: 3.33e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  81 MKVLYFMEDVKTPSLSFKVIAHQWYWSYVVPLFKNFSFK--VNGTSLLSSYEYdslleddvnapRLLGCSSDLVIPLNSV 158
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDsyMLPTSDLSPGQF-----------RLLEVDNRAVLPMQTE 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225012910 159 SRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVV 223
Cdd:MTH00008 150 IRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAV 214
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-236 5.42e-71

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 216.89  E-value: 5.42e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  81 MKVLYFMEDVKTPSLSFKVIAHQWYWSYVVPLFKNFSFK--VNGTSLLSSYEYdslleddvnapRLLGCSSDLVIPLNSV 158
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDsyMIPTSDLKPGEL-----------RLLEVDNRVVLPMEMP 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225012910 159 SRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQFSKTYL 236
Cdd:MTH00098 150 IRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-225 7.99e-66

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 204.21  E-value: 7.99e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   7 LNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPSMKVLYF 86
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  87 MEDVKTPSLSFKVIAHQWYWSYVVPLFKNfsfkvngtsllSSYEYDSLL--EDDVNAP--RLLGCSSDLVIPLNSVSRLL 162
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEG-----------ETLEFDSYMvpTSDLNSGdfRLLEVDNRLVVPINTHVRIL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225012910 163 ISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPL 225
Cdd:MTH00023 165 VTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSL 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 7-238 2.87e-64

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 199.94  E-value: 2.87e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   7 LNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPSMKVLYF 86
Cdd:MTH00129   7 LGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  87 MEDVKTPSLSFKVIAHQWYWSYVVPLFKNFSFK--VNGTSLLSSYEYdslleddvnapRLLGCSSDLVIPLNSVSRLLIS 164
Cdd:MTH00129  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDsyMIPTQDLTPGQF-----------RLLEADHRMVVPVESPIRVLVS 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225012910 165 STDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQFSKTYLLD 238
Cdd:MTH00129 156 AEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLED 229
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-225 6.24e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 196.93  E-value: 6.24e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   7 LNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPSMKVLYF 86
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  87 MEDVKTPSLSFKVIAHQWYWSYVVPLFknfsfkvnGTSLLssyEYDSLL--EDDVNAP--RLLGCSSDLVIPLNSVSRLL 162
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDY--------GTDTI---EFDSYMipTSDLNSGdlRLLEVDNRLIVPIQTQVRVL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225012910 163 ISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPL 225
Cdd:MTH00051 158 VTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSL 220
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 7-234 7.18e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 196.54  E-value: 7.18e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   7 LNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPSMKVLYF 86
Cdd:MTH00076   7 LGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  87 MEDVKTPSLSFKVIAHQWYWSYVVPLFKNFSFkvngtsllSSYEYDSlleDDVNAP--RLLGCSSDLVIPLNSVSRLLIS 164
Cdd:MTH00076  87 MDEINDPHLTVKAIGHQWYWSYEYTDYEDLSF--------DSYMIPT---QDLTPGqfRLLEVDNRMVVPMESPIRMLIT 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910 165 STDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQFSKT 234
Cdd:MTH00076 156 AEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 7-236 9.52e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 196.26  E-value: 9.52e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   7 LNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPSMKVLYF 86
Cdd:MTH00185   7 LGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  87 MEDVKTPSLSFKVIAHQWYWSYVVPLFKNFSFKvngtsllssyEYDSLLED-DVNAPRLLGCSSDLVIPLNSVSRLLISS 165
Cdd:MTH00185  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFD----------SYMTPTQDlTPGQFRLLETDHRMVVPMESPIRVLITA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225012910 166 TDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQFSKTYL 236
Cdd:MTH00185 157 EDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-231 1.04e-52

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: 166.98  E-value: 1.04e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  93 PSLSFKVIAHQWYWSYVVPLFKNFSFkvngtsllssyeyDSLL--EDDVNA--PRLLGCSSDLVIPLNSVSRLLISSTDV 168
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEF-------------DSYMipEDDLEKgqLRLLEVDNRLVVPVNTHIRVLVTSADV 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225012910 169 IHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQF 231
Cdd:cd13912   68 IHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 7-237 7.08e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 163.26  E-value: 7.08e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   7 LNFQDSSSPS-MGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNLSEGTFIETIWSIVPAFLLIILVLPSMKVLY 85
Cdd:MTH00080   8 LNFSNSLFSSyMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  86 FMEDVKTPS-LSFKVIAHQWYWSYVVPLFKNFSFKvngtSLLSSYEYDSLLEddvnaPRLLGCSSDLVIPLNSVSRLLIS 164
Cdd:MTH00080  88 YYGLMNLDSnLTVKVTGHQWYWSYEFSDIPGLEFD----SYMKSLDQLRLGE-----PRLLEVDNRCVLPCDTNIRFCIT 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225012910 165 STDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQFSKTYLL 237
Cdd:MTH00080 159 SSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-225 2.61e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 162.89  E-value: 2.61e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   7 LNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYK---NLSEGTFIETIWSIVPAFLLIILVLPSMKV 83
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  84 LYFMED-VKTPSLSFKVIAHQWYWSYVvplFKNFSFKvngtsllsSYEYDSLL----EDDVNAPRLLGCSSDLVIPLNSV 158
Cdd:MTH00027 115 LYIMDEcGFSANITIKVTGHQWYWSYS---YEDYGEK--------NIEFDSYMiptaDLEFGDLRLLEVDNRLILPVDTN 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225012910 159 SRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPL 225
Cdd:MTH00027 184 VRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSL 250
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-231 6.10e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 160.76  E-value: 6.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   6 SLNFQDSSSPSMGELSVFHDHVVVVMSGVIILIsyiMIYMLYSVKFY---------KNLSEGTFIETIWSIVPAFLLIIL 76
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIRYrrrkgdadpAQFHHNTKLEIVWTVIPIIIVIVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  77 VLPSMKVLYFMEDVKTPSLSFKVIAHQWYWSYvvplfknfsfkvngtsllssyEYDSLLEDDVNaprllgcssDLVIPLN 156
Cdd:COG1622   95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLF---------------------RYPDQGIATVN---------ELVLPVG 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225012910 157 SVSRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQF 231
Cdd:COG1622  145 RPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-223 2.37e-44

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 145.25  E-value: 2.37e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   95 LSFKVIAHQWYWSYVVPLFKNFSFkvngtsllSSYEY-DSLLEDdvNAPRLLGCSSDLVIPLNSVSRLLISSTDVIHSFA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEF--------DSYMIpTEDLEE--GQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWA 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 225012910  174 VPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVV 223
Cdd:pfam00116  71 VPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-223 9.01e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 136.24  E-value: 9.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  17 MGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKFYKNL----SEGTFIETIWSIVPAflLIILVLPSMKVLYFMED-VK 91
Cdd:MTH00047   1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSGNGSvnfgSENQVLELLWTVVPT--LLVLVLCFLNLNFITSDlDC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  92 TPSLSFKVIAHQWYWSYVVPlfknfsfkvngtsllSSYEYDSLLEDDVNaprllGCSSDLVIPLNSVSRLLISSTDVIHS 171
Cdd:MTH00047  79 FSSETIKVIGHQWYWSYEYS---------------FGGSYDSFMTDDIF-----GVDKPLRLVYGVPYHLLVTSSDVIHS 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 225012910 172 FAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVV 223
Cdd:MTH00047 139 FSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-231 1.35e-35

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 125.57  E-value: 1.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   14 SPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYsvKFYKN--------LSEGTFIETIWSIVPAFLLIILVLPS-MKVL 84
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVW--KFRRKgdeekpsqIHGNRRLEYVWTVIPLIIVVGLFAATaKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910   85 YFMEDVKTPSLSFKVIAHQWYWSYVVPlfkNFSFKVNGTsllssyeydslleddvnaprllgcssdLVIPLNSVSRLLIS 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYP---ESGFTTVNE---------------------------LVLPAGTPVELQVT 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225012910  165 STDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQF 231
Cdd:TIGR02866 131 SKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-223 4.12e-25

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: 95.40  E-value: 4.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  98 KVIAHQWYWSYVVPLfknfsfkvngtsllssyeydsllEDDVNAPRLLGCSSDLVIPLNSVSRLLISSTDVIHSFAVPSL 177
Cdd:cd13919    5 EVTAQQWAWTFRYPG-----------------------GDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEF 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 225012910 178 GLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVV 223
Cdd:cd13919   62 RVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKVV 107
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 143-238 8.58e-25

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 96.43  E-value: 8.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910 143 RLLGCSSDLVIPLNSVSRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKV 222
Cdd:PTZ00047  67 RQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEA 146

                         90
                 ....*....|....*.
gi 225012910 223 VPLGIFDQFSKTYLLD 238
Cdd:PTZ00047 147 VSPEAYAAHAKKYYKD 162
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-223 4.86e-24

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 92.68  E-value: 4.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  94 SLSFKVIAHQWYWSYVVPlfknfsfkvngtsllssyeyDSLLEDDVNAprllgcsSDLVIPLNSVSRLLISSTDVIHSFA 173
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYP--------------------DEPGRGIVTA-------NELHIPVGRPVRLRLTSADVIHSFW 53

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 225012910 174 VPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMpiSMKVV 223
Cdd:cd04213   54 VPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM--RFKVI 101
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 98-221 6.10e-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: 86.97  E-value: 6.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  98 KVIAHQWYWSYVVPLfknfsfkvngtsllssyeydslleddvnaprlLGCSSDLVIPLNSVSRLLISSTDVIHSFAVPSL 177
Cdd:cd13842    4 YVTGVQWSWTFIYPN--------------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNL 51

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 225012910 178 GLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMK 221
Cdd:cd13842   52 GVKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-231 1.22e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 83.61  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  99 VIAHQWYWSYVVPlfknfsfkvngtsllssyeydsllEDDVNAprllgcSSDLVIPLNSVSRLLISSTDVIHSFAVPSLG 178
Cdd:cd13914    5 VEAYQWGWEFSYP------------------------EANVTT------SEQLVIPADRPVYFRITSRDVIHAFHVPELG 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 225012910 179 LKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVVPLGIFDQF 231
Cdd:cd13914   55 LKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-222 8.60e-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: 81.14  E-value: 8.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  98 KVIAHQWYWSYVVPlfknfsfkvNGTsllssyeydslleddvnaprllGCSSDLVIPLNSVSRLLISSTDVIHSFAVPSL 177
Cdd:cd13915    5 QVTGRQWMWEFTYP---------NGK----------------------REINELHVPVGKPVRLILTSKDVIHSFYVPAF 53

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 225012910 178 GLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKV 222
Cdd:cd13915   54 RIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 5.55e-19

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: 78.91  E-value: 5.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910    1 MPSWMSLNFQDSSSPSMGELSVFHDHVVVVMSGVIILISYIMIYMLYSVKF------YKNLSEGTFIETIWSIVPAFLLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 225012910   75 ILVLPSMKV 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-229 4.53e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 72.49  E-value: 4.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910  67 IVPAFLLIILVLPSMKVLYFMEDVKTPS----LSFKVIAHQWYWsyvvplfkNFSFKVNGTSLlssyeydslleddvnap 142
Cdd:cd13918    1 GLSAIIVISLIVWTYGMLLYVEDPPDEAdedaLEVEVEGFQFGW--------QFEYPNGVTTG----------------- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225012910 143 rllgcsSDLVIPLNSVSRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKV 222
Cdd:cd13918   56 ------NTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIV 129


                 ....*..
gi 225012910 223 VPLGIFD 229
Cdd:cd13918  130 MDEEEFE 136
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 149-223 3.45e-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: 52.96  E-value: 3.45e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225012910 149 SDLVIPLNSVSRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVV 223
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 151-216 1.84e-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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 39.28  E-value: 1.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225012910 151 LVIPLNSVSRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFM 216
Cdd:cd13917   16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 151-223 1.18e-03

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 37.14  E-value: 1.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225012910 151 LVIPLNSVSRLLISSTDVIHSFAVPSLGLKVDAFPGRINQLFVNPVRLGNFYGQCSEICGSNHSFMPISMKVV 223
Cdd:cd04212   27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
 
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