NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|158526685|gb|ABW71540|]
View 

cytochrome oxidase subunit II, partial (mitochondrion) [Lamprotornis fischeri]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475905)

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 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 1.01e-158

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 438.19  E-value: 1.01e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLS-SNSVDAQAIELVWTILPAVVLITLALPS 79
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  80 LRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVL 159
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158526685 160 HSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLS 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 1.01e-158

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 438.19  E-value: 1.01e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLS-SNSVDAQAIELVWTILPAVVLITLALPS 79
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  80 LRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVL 159
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158526685 160 HSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLS 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 1.29e-94

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: 272.52  E-value: 1.29e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  92 PDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVLHSWAVPSLGVKT 171
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 158526685 172 DAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 1.12e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 241.93  E-value: 1.12e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   94 LTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVLHSWAVPSLGVKTDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 158526685  174 IPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVEST 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
60-221 5.44e-58

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 183.11  E-value: 5.44e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  60 IELVWTILPAVVLITLALPSLRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTfdsymiptsdlplghfrllevDH 139
Cdd:COG1622   79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT---------------------VN 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685 140 RVIVPTSSKVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFE 219
Cdd:COG1622  138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                 ..
gi 158526685 220 NW 221
Cdd:COG1622  218 AW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 59-221 3.56e-42

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: 141.75  E-value: 3.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   59 AIELVWTILPAVVLITL-ALPSLRILYMMDEINEPDLTLKAIGHQWYWTYEYtdlKELTFDSymiptsdlplghfrllev 137
Cdd:TIGR02866  55 RLEYVWTVIPLIIVVGLfAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEY---PESGFTT------------------ 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  138 DHRVIVPTSSKVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLAN 217
Cdd:TIGR02866 114 VNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEE 193


                  ....
gi 158526685  218 FENW 221
Cdd:TIGR02866 194 FDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 1.01e-158

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 438.19  E-value: 1.01e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLS-SNSVDAQAIELVWTILPAVVLITLALPS 79
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  80 LRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVL 159
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158526685 160 HSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLS 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-225 3.34e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 366.35  E-value: 3.34e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLSSNSV-DAQAIELVWTILPAVVLITLALPS 79
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYIlDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  80 LRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVL 159
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158526685 160 HSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLL 225
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 1.17e-129

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 364.87  E-value: 1.17e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLSS-NSVDAQAIELVWTILPAVVLITLALPS 79
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNtNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  80 LRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVL 159
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158526685 160 HSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSL 224
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-225 1.81e-129

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 364.42  E-value: 1.81e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLS-SNSVDAQAIELVWTILPAVVLITLALPS 79
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLThTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  80 LRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVL 159
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158526685 160 HSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLL 225
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 3.03e-127

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 358.76  E-value: 3.03e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLSS-NSVDAQAIELVWTILPAVVLITLALPS 79
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNrFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  80 LRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVL 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158526685 160 HSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLS 226
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 9.12e-123

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 347.35  E-value: 9.12e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAI-CSLVLYLLTTLLTEKLSSNSVDAQAIELVWTILPAVVLITLALPS 79
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLIlTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  80 LRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVL 159
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158526685 160 HSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSS 223
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-225 2.62e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 341.48  E-value: 2.62e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLSSN-SVDAQAIELVWTILPAVVLITLALPS 79
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKyILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  80 LRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVL 159
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158526685 160 HSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLL 225
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-227 1.49e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 339.22  E-value: 1.49e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLSSNSV-DAQAIELVWTILPAVVLITLALPS 79
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTIlEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  80 LRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVL 159
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158526685 160 HSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLSS 227
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMSE 228
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-223 6.97e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 337.44  E-value: 6.97e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAIcslVLYLLTTLLTEKLSSNS----VDAQAIELVWTILPAVVLITLA 76
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLI---TILVFYGLASLLFSSPTnrffLEGQELETIWTIVPAFILIFIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  77 LPSLRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTAD 156
Cdd:MTH00038  78 LPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158526685 157 DVLHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSS 223
Cdd:MTH00038 158 DVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-221 3.01e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 325.90  E-value: 3.01e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLSSNS-VDAQAIELVWTILPAVVLITLALPS 79
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSlLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  80 LRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVL 159
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158526685 160 HSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-227 1.03e-106

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 306.78  E-value: 1.03e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLSSNSV-DAQAIELVWTILPAVVLITLALPS 79
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYIlEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  80 LRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVL 159
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158526685 160 HSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLSS 227
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-227 2.06e-101

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 293.97  E-value: 2.06e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   6 QLGFQDASSPIMEELMQFHDHALMVALAICSLVL-YLLTTLLTEKLSSNSVDAQAIELVWTILPAVVLITLALPSLRILY 84
Cdd:MTH00023  15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLwLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  85 MMDEINEPDLTLKAIGHQWYWTYEYTDLKE--LTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVLHSW 162
Cdd:MTH00023  95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158526685 163 AVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLSS 227
Cdd:MTH00023 175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-228 1.06e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 286.68  E-value: 1.06e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   6 QLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLSSNSV-DAQAIELVWTILPAVVLITLALPSLRILY 84
Cdd:MTH00051   8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLfEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  85 MMDEINEPDLTLKAIGHQWYWTYEYTDL--KELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVLHSW 162
Cdd:MTH00051  88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158526685 163 AVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENWSSLLSSQ 228
Cdd:MTH00051 168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 1.29e-94

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: 272.52  E-value: 1.29e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  92 PDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVLHSWAVPSLGVKT 171
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 158526685 172 DAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-221 3.61e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 248.40  E-value: 3.61e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   6 QLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLSS----NSVDAQAIELVWTILPAVVLITLALPSLR 81
Cdd:MTH00027  34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYsyywNKLDGSLIEVIWTLIPAFILILIAFPSLR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  82 ILYMMDE-INEPDLTLKAIGHQWYWTYEYTDL--KELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDV 158
Cdd:MTH00027 114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158526685 159 LHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:MTH00027 194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 1.12e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 241.93  E-value: 1.12e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   94 LTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVLHSWAVPSLGVKTDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 158526685  174 IPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVEST 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 52-225 5.30e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 231.44  E-value: 5.30e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  52 SNSVDAQAIELVWTILPAVVLITLALPSLRILYMMDEIN-EPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSDLPLG 130
Cdd:MTH00080  55 SKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685 131 HFRLLEVDHRVIVPTSSKVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVV 210
Cdd:MTH00080 135 EPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAV 214

                        170
                 ....*....|....*
gi 158526685 211 ESTPLANFENWSSLL 225
Cdd:MTH00080 215 EVTLLDNFKEWCKLL 229
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
60-221 5.44e-58

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 183.11  E-value: 5.44e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  60 IELVWTILPAVVLITLALPSLRILYMMDEINEPDLTLKAIGHQWYWTYEYTDLKELTfdsymiptsdlplghfrllevDH 139
Cdd:COG1622   79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT---------------------VN 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685 140 RVIVPTSSKVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFE 219
Cdd:COG1622  138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                 ..
gi 158526685 220 NW 221
Cdd:COG1622  218 AW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 56-211 7.18e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 148.56  E-value: 7.18e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  56 DAQAIELVWTILPAVVLITLALPSLR-ILYMMDeiNEPDLTLKAIGHQWYWTYEYTDlkELTFDSYM---IPTSDLPLgh 131
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVLCFLNLNfITSDLD--CFSSETIKVIGHQWYWSYEYSF--GGSYDSFMtddIFGVDKPL-- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685 132 frllevdhRVIVPTSskVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVE 211
Cdd:MTH00047 119 --------RLVYGVP--YHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 59-221 3.56e-42

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: 141.75  E-value: 3.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685   59 AIELVWTILPAVVLITL-ALPSLRILYMMDEINEPDLTLKAIGHQWYWTYEYtdlKELTFDSymiptsdlplghfrllev 137
Cdd:TIGR02866  55 RLEYVWTVIPLIIVVGLfAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEY---PESGFTT------------------ 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  138 DHRVIVPTSSKVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLAN 217
Cdd:TIGR02866 114 VNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEE 193


                  ....
gi 158526685  218 FENW 221
Cdd:TIGR02866 194 FDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 116-212 8.91e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 134.18  E-value: 8.91e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685 116 TFDSYMIPTSDLPLGHFRLLEVDHRVIVPTSSKVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQC 195
Cdd:PTZ00047  50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                         90
                 ....*....|....*..
gi 158526685 196 SEICGANHSFMPIVVES 212
Cdd:PTZ00047 130 SEMCGTLHGFMPIVVEA 146
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 94-211 4.59e-31

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: 109.69  E-value: 4.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  94 LTLKAIGHQWYWTYEYTDLkeltfdsymiptsdlplghfrllEVDHRVIVPTSSKVRVIVTADDVLHSWAVPSLGVKTDA 173
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNV-----------------------RTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 158526685 174 IPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVE 211
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 93-206 2.62e-30

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: 108.09  E-value: 2.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  93 DLTLKAIGHQWYWTYEYTDLKELTFDSymipTSDLplghfrllevdhrvIVPTSSKVRVIVTADDVLHSWAVPSLGVKTD 172
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPGRGIVT----ANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 158526685 173 AIPGRLNQTAFLASRPGVYYGQCSEICGANHSFM 206
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 66-221 4.75e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 95.60  E-value: 4.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  66 ILPAVVLITLALPSL-RILYMMD---EINEPDLTLKAIGHQWYWTYEYTDlkELTFDSYMIptsdlplghfrllevdhrv 141
Cdd:cd13918    1 GLSAIIVISLIVWTYgMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTLR------------------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685 142 iVPTSSKVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:cd13918   60 -VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-211 8.84e-24

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: 91.16  E-value: 8.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  93 DLTLKAIGHQWYWTYEY--TDLKELTFDSYMIPTSDLPLGHfrllevdhrvivptssKVRVIVTADDVLHSWAVPSLGVK 170
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYpgGDGKLGTDDDVTSPELHLPVGR----------------PVLFNLRSKDVIHSFWVPEFRVK 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 158526685 171 TDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFM--PIVVE 211
Cdd:cd13919   65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-210 1.48e-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: 82.68  E-value: 1.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  93 DLTLKAIGHQWYWTYEYTDLKEltfdsymiptsdlplghfrlleVDHRVIVPTSSKVRVIVTADDVLHSWAVPSLGVKTD 172
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYPNGKR----------------------EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 158526685 173 AIPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVV 210
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-82 3.17e-20

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 81.61  E-value: 3.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685    1 MANHSQLGFQDASSPIMEELMQFHDHALMVALAICSLVLYLLTTLLTEKLSSNS-------VDAQAIELVWTILPAVVLI 73
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNpitarytTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 158526685   74 TLALPSLRI 82
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-221 1.64e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 80.14  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  95 TLKAIGHQWYWTYEYTDLKELTFDsymiptsdlplghfrllevdhRVIVPTSSKVRVIVTADDVLHSWAVPSLGVKTDAI 174
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEANVTTSE---------------------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 158526685 175 PGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVESTPLANFENW 221
Cdd:cd13914   61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 143-211 4.44e-10

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: 54.88  E-value: 4.44e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158526685 143 VPTSSKVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFM--PIVVE 211
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 148-206 5.76e-07

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 46.46  E-value: 5.76e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158526685 148 KVRVIVT----ADDVLHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFM 206
Cdd:cd04223   25 EVTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 3.68e-06

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: 43.91  E-value: 3.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  95 TLKAIGHQWYWTyeytdlkeltfdsymIPTSDLPLGhfrllevdhrvivptsSKVRVIVTADDVLHSWAVPS----LGVK 170
Cdd:cd13916    2 VVAVTGHQWYWE---------------LSRTEIPAG----------------KPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 158526685 171 TDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFM 206
Cdd:cd13916   51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 52-221 1.33e-05

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 45.18  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  52 SNSVDAqaieLVWTIlPAVVLITLALPSLRILYMMDEI-----NEPDLTLKAIGHQWYWTYEYTDLKELTFDSYMIPTSd 126
Cdd:PRK10525  85 SNKVEA----VVWTV-PILIIIFLAVLTWKTTHALEPSkplahDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPAN- 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685 127 lplghfrllevdhrviVPTSSKVrvivTADDVLHSWAVPSLGVKTDAIPGRLNQTAFLASRPGVYYGQCSEICGANHSFM 206
Cdd:PRK10525 159 ----------------VPVYFKV----TSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGM 218

                        170
                 ....*....|....*.
gi 158526685 207 PIVVESTP-LANFENW 221
Cdd:PRK10525 219 KFKAIATPdRAEFDQW 234
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 94-213 5.16e-05

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 40.99  E-value: 5.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685  94 LTLKAIGHQWYWTYEYTDLKELTFDSYMIPTsDLPLgHFRLlevdhrvivptsskvrvivTADDVLHSWAVPSLGVKTDA 173
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPV-GRPV-NFRL-------------------TSDSVMNSFFIPQLGGQIYA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 158526685 174 IPGRLNQTAFLASRPGVYYGQCSEICGANHSFMPIVVEST 213
Cdd:cd04212   60 MAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 120-206 9.53e-05

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 43.04  E-value: 9.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685 120 YMipTSDLP---LGHFRLLEVDHrvivptsskVRVIVT----ADDVLHSWAVPSLGVKTDAIPgrlNQTA---FLASRPG 189
Cdd:PRK02888 544 YM--TSQAPafgLREFTVKQGDE---------VTVIVTnldkVEDLTHGFAIPNYGVNMEVAP---QATAsvtFTADKPG 609

                         90
                 ....*....|....*..
gi 158526685 190 VYYGQCSEICGANHSFM 206
Cdd:PRK02888 610 VYWYYCTWFCHALHMEM 626
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 132-211 1.40e-04

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: 39.91  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158526685 132 FRLLEVDHRVIVPTSSKVRVIVT-ADDVLHSWAVPSLGVKTDAI---------------PGRLNQTAFLASRPGVYYGQC 195
Cdd:cd00920   16 GVLLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYWFYC 95

                         90
                 ....*....|....*.
gi 158526685 196 SEICGaNHSFMPIVVE 211
Cdd:cd00920   96 TIPGH-NHAGMVGTIN 110
 
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