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Conserved domains on  [gi|2255172717|gb|USH58037|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Strigops habroptila]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 1000633)

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

CATH:  1.10.287.90
EC:  7.1.1.9
Gene Ontology:  GO:0004129|GO:0005507
PubMed:  6307356|8083153
TCDB:  3.D.4.6.2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 super family cl31800
cytochrome c oxidase subunit II; Provisional
 1-226 1.80e-65

cytochrome c oxidase subunit II; Provisional


The actual alignment was detected with superfamily member MTH00117:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 202.07  E-value: 1.80e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLS-SNTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  80 LQ********DEPDLTLKAIGHQWYWS************************HFRLLEA********************** 159
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255172717 160 ***********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSSLLS 226
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 1.80e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 202.07  E-value: 1.80e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLS-SNTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  80 LQ********DEPDLTLKAIGHQWYWS************************HFRLLEA********************** 159
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255172717 160 ***********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSSLLS 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 ...
 183-221 6.01e-22

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: 87.24  E-value: 6.01e-22
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2255172717 183 FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENW 221
Cdd:cd13912    92 FFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 1.07e-16

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 73.21  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  94 LTLKAIGHQWYWS************************HFRLLEA************************************ 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2255172717 174 *********FIATRPGIFYGQCSEICGANHSFMPIVVEST 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
60-221 2.16e-11

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 61.38  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  60 VELIWTILPAIVLILLALPSLQ********DEPDLTLKAIGHQWYWs************************HFRLLEA** 139
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKW-------------------------LFRYPDQGI 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717 140 ***********************----********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPL 215
Cdd:COG1622   134 ATVnelvlpvgrpvrflltsadvihsfwvpalggkqdaipgrvtelwFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213


                  ....*.
gi 2255172717 216 IHFENW 221
Cdd:COG1622   214 EEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 183-221 1.83e-06

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: 46.99  E-value: 1.83e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2255172717 183 FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENW 221
Cdd:TIGR02866 159 FNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 1.80e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 202.07  E-value: 1.80e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLS-SNTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  80 LQ********DEPDLTLKAIGHQWYWS************************HFRLLEA********************** 159
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255172717 160 ***********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSSLLS 226
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 1.47e-56

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 179.20  E-value: 1.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLSS-NTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNtNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  80 LQ********DEPDLTLKAIGHQWYWS************************HFRLLEA********************** 159
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255172717 160 ***********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSSL 224
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-225 7.42e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 172.59  E-value: 7.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLSS-NTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNkYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  80 LQ********DEPDLTLKAIGHQWYWS************************HFRLLEA********************** 159
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2255172717 160 ***********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSSLL 225
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-225 4.82e-53

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 170.28  E-value: 4.82e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLS-SNTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLThTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  80 LQ********DEPDLTLKAIGHQWYWS************************HFRLLEA********************** 159
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2255172717 160 ***********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSSLL 225
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-225 5.15e-52

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 167.75  E-value: 5.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLSSN-TVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKyILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  80 LQ********DEPDLTLKAIGHQWYWS************************HFRLLEA********************** 159
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2255172717 160 ***********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSSLL 225
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-223 4.96e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 152.55  E-value: 4.96e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************kLSSNT----VDAQEVELIWTILPAIVLILLA 76
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLL---FSSPTnrffLEGQELETIWTIVPAFILIFIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  77 LPSLQ********DEPDLTLKAIGHQWYWS************************HFRLLEA******************* 156
Cdd:MTH00038   78 LPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255172717 157 **************************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSS 223
Cdd:MTH00038  158 DVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 2.54e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 147.82  E-value: 2.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLSSNTV-DAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLlDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  80 LQ********DEPDLTLKAIGHQWYWS************************HFRLLEA********************** 159
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2255172717 160 ***********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSS 223
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 3.38e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 139.96  E-value: 3.38e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLSS-NTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNrFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  80 LQ********DEPDLTLKAIGHQWYWS************************HFRLLE----------------------- 136
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDvdnrlvlpmntqirilitaadvi 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717 137 -------------A*********************************************FIATRPGIFYGQCSEICGANH 203
Cdd:MTH00154  161 hswtvpslgvkvdA------------------------------------VPGRLNQLNFLINRPGLFFGQCSEICGANH 204

                         250       260
                  ....*....|....*....|...
gi 2255172717 204 SFMPIVVESTPLIHFENWSSLLS 226
Cdd:MTH00154  205 SFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-226 5.61e-41

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 139.61  E-value: 5.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLSSNTV-DAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYIlEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  80 LQ********DEPDLTLKAIGHQWYWS************************HFRLLEA********************** 159
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255172717 160 ***********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSSLLS 226
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-221 8.43e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 139.08  E-value: 8.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLSSNT-VDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSlLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  80 LQ********DEPDLTLKAIGHQWYWS************************HFRLLEA********************** 159
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255172717 160 ***********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENW 221
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 2.94e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 129.67  E-value: 2.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLSSNTV-DAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTIlEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  80 LQ********DEPDLTLKAIGHQWYWS************************HFRLLEA********************** 159
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255172717 160 ***********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSSLLS 226
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMS 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-226 1.56e-34

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 123.32  E-value: 1.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   6 QLGFQDASSPIMEELVEFHD***********************K-LSSNTVDAQEVELIWTILPAIVLILLALPSLQ*** 84
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKfYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  85 *****DEPDLTLKAIGHQWYWS************--************HFRLLEA************************* 162
Cdd:MTH00023   95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEfdSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2255172717 163 ********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSSLLS 226
Cdd:MTH00023  175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-226 6.51e-33

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 118.73  E-value: 6.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   6 QLGFQDASSPIMEELVEFHD***********************KLSSNTV-DAQEVELIWTILPAIVLILLALPSLQ*** 84
Cdd:MTH00051    8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLfEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  85 *****DEPDLTLKAIGHQWYWS************--************HFRLLEA************************* 162
Cdd:MTH00051   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEfdSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2255172717 163 ********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENWSSLLS 226
Cdd:MTH00051  168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-221 1.19e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 103.18  E-value: 1.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   6 QLGFQDASSPIMEELVEFHD**********************----*KLSSNTVDAQEVELIWTILPAIVLILLALPSLQ 81
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLgnnyYSYYWNKLDGSLIEVIWTLIPAFILILIAFPSLR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  82 ********DE----PDLTLKAIGHQWYWS*****--*******************HFRLLEA****************** 155
Cdd:MTH00027  114 LLYIM---DEcgfsANITIKVTGHQWYWSYSYEDygEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITA 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2255172717 156 ***************************FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENW 221
Cdd:MTH00027  191 ADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 183-221 6.01e-22

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: 87.24  E-value: 6.01e-22
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2255172717 183 FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENW 221
Cdd:cd13912    92 FFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 49-225 1.76e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 83.52  E-value: 1.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  49 KLSSNTVDAQEVELIWTILPAIVLILLALPSLQ********D-EPDLTLKAIGHQWYWS********************* 127
Cdd:MTH00080   52 YFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717 128 ***HFRLLEA*********************************************FIATRPGIFYGQCSEICGANHSFMP 207
Cdd:MTH00080  132 RLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMP 211

                         170
                  ....*....|....*...
gi 2255172717 208 IVVESTPLIHFENWSSLL 225
Cdd:MTH00080  212 IAVEVTLLDNFKEWCKLL 229
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 1.07e-16

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 73.21  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  94 LTLKAIGHQWYWS************************HFRLLEA************************************ 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2255172717 174 *********FIATRPGIFYGQCSEICGANHSFMPIVVEST 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-81 2.83e-15

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: 68.51  E-value: 2.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717   1 MANHSQLGFQDASSPIMEELVEFHD***********************KLSS-------NTVDAQEVELIWTILPAIVLI 73
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRknpitarYTTHGQTIEIIWTIIPAVILI 80


                  ....*...
gi 2255172717  74 LLALPSLQ 81
Cdd:pfam02790  81 LIALPSFK 88
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
60-221 2.16e-11

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 61.38  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717  60 VELIWTILPAIVLILLALPSLQ********DEPDLTLKAIGHQWYWs************************HFRLLEA** 139
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKW-------------------------LFRYPDQGI 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255172717 140 ***********************----********************FIATRPGIFYGQCSEICGANHSFMPIVVESTPL 215
Cdd:COG1622   134 ATVnelvlpvgrpvrflltsadvihsfwvpalggkqdaipgrvtelwFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213


                  ....*.
gi 2255172717 216 IHFENW 221
Cdd:COG1622   214 EEFDAW 219
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 187-212 8.88e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 55.60  E-value: 8.88e-10
                          10        20
                  ....*....|....*....|....*.
gi 2255172717 187 RPGIFYGQCSEICGANHSFMPIVVES 212
Cdd:PTZ00047  121 REGVFYGQCSEMCGTLHGFMPIVVEA 146
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 183-211 4.80e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 51.49  E-value: 4.80e-08
                          10        20
                  ....*....|....*....|....*....
gi 2255172717 183 FIATRPGIFYGQCSEICGANHSFMPIVVE 211
Cdd:MTH00047  160 FCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 183-211 1.72e-07

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: 47.68  E-value: 1.72e-07
                          10        20
                  ....*....|....*....|....*....
gi 2255172717 183 FIATRPGIFYGQCSEICGANHSFMPIVVE 211
Cdd:cd13842    67 FVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 183-221 1.83e-06

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: 46.99  E-value: 1.83e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2255172717 183 FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENW 221
Cdd:TIGR02866 159 FNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 185-206 3.00e-06

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: 44.53  E-value: 3.00e-06
                          10        20
                  ....*....|....*....|..
gi 2255172717 185 ATRPGIFYGQCSEICGANHSFM 206
Cdd:cd04213    75 ADEPGVYRGQCAEFCGASHALM 96
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 56-106 2.48e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 43.40  E-value: 2.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2255172717  56 DAQEVELIWTILPAIVLILLALPSLQ********DEPDLTLKAIGHQWYWS 106
Cdd:MTH00047   45 ENQVLELLWTVVPTLLVLVLCFLNLNFITSDLD-CFSSETIKVIGHQWYWS 94
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 60-106 3.20e-05

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: 43.14  E-value: 3.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2255172717  60 VELIWTILPA-IVLILLALPSLQ********DEPDLTLKAIGHQWYWS 106
Cdd:TIGR02866  56 LEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWD 103
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 183-221 5.53e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 38.98  E-value: 5.53e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2255172717 183 FIATRPGIFYGQCSEICGANHSFMPIVVESTPLIHFENW 221
Cdd:cd13918   100 FEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 183-211 9.73e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 37.62  E-value: 9.73e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2255172717 183 FIATRPGIFYGQCSEICGANHSFM--PIVVE 211
Cdd:cd13919    77 FTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 183-210 8.17e-03

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: 34.91  E-value: 8.17e-03
                          10        20
                  ....*....|....*....|....*...
gi 2255172717 183 FIATRPGIFYGQCSEICGANHSFMPIVV 210
Cdd:cd13915    69 FEATKPGEYDLFCTEYCGTGHSGMIGKV 96
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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