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Conserved domains on  [gi|440655457|gb|AGC22350|]
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cytochrome c oxidase subunit II (mitochondrion) [Paramastax nigra]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 7.39e-131

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 367.62  E-value: 7.39e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWMFKLI 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 7.39e-131

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 367.62  E-value: 7.39e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWMFKLI 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-222 2.98e-81

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: 238.62  E-value: 2.98e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  95 LTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDA 174
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 440655457 175 TPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKW 222
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.40e-71

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 213.81  E-value: 1.40e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   95 LTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 440655457  175 TPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIEST 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
57-223 7.29e-46

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 151.90  E-value: 7.29e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  57 HGHTIETIWTILPTITLIFIAFPSIRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDfinmefdsfmisnNNIpmnsfrlm 136
Cdd:COG1622   75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-------------QGI-------- 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457 137 EVDNRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSN 216
Cdd:COG1622  134 ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213


                 ....*..
gi 440655457 217 NLFMKWM 223
Cdd:COG1622  214 EEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-223 5.21e-38

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: 130.96  E-value: 5.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   14 SPLMEQLMFFHDHAMIILIMITMIVSYFMIYLI------KNNMSNKMLLHGHTIETIWTILP-TITLIFIAFPSIRMLYL 86
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIPlIIVVGLFAATAKGLLYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   87 ---IDDNSnmmLTIKTIGRQWYWSYEYSDFinmefdsfmisnnnipmnsfrLMEVDNRMMMPMNTAIRIMATASDVIHSW 163
Cdd:TIGR02866  83 erpIPKDA---LKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  164 TIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWM 223
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 7.39e-131

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 367.62  E-value: 7.39e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWMFKLI 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 6.44e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 312.26  E-value: 6.44e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWMFKL 226
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 7.59e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 301.83  E-value: 7.59e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWMFKL 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 1.28e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 298.94  E-value: 1.28e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKW 222
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-228 5.25e-102

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 294.84  E-value: 5.25e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWMFKLIS 228
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-228 3.21e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 290.45  E-value: 3.21e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWMFKLIS 228
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLE 228
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-222 7.36e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 281.87  E-value: 7.36e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKW 222
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-222 2.43e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 267.74  E-value: 2.43e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKW 222
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-222 1.72e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 263.18  E-value: 1.72e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKW 222
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 9-228 1.81e-89

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 263.53  E-value: 1.81e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   9 FQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPSIRMLYLID 88
Cdd:MTH00023  18 FQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  89 DNSNMMLTIKTIGRQWYWSYEYSDFI--NMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVIHSWTIP 166
Cdd:MTH00023  98 EVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVP 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440655457 167 SLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWMFKLIS 228
Cdd:MTH00023 178 SLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-222 5.10e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 262.13  E-value: 5.10e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKW 222
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-222 3.64e-87

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 257.34  E-value: 3.64e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  81 IRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVI 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440655457 161 HSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKW 222
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 9-223 1.25e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 251.24  E-value: 1.25e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   9 FQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAFPSIRMLYLID 88
Cdd:MTH00051  11 FQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  89 DNSNMMLTIKTIGRQWYWSYEYSDF--INMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVIHSWTIP 166
Cdd:MTH00051  91 EVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVP 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 440655457 167 SLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWM 223
Cdd:MTH00051 171 SLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-222 2.98e-81

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: 238.62  E-value: 2.98e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  95 LTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDA 174
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 440655457 175 TPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKW 222
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.40e-71

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 213.81  E-value: 1.40e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   95 LTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 440655457  175 TPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIEST 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 9-223 1.10e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 209.11  E-value: 1.10e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   9 FQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMI-YLIKNNMSNKML--LHGHTIETIWTILPTITLIFIAFPSIRMLY 85
Cdd:MTH00027  37 FQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRLLY 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  86 LIDDNS-NMMLTIKTIGRQWYWSYEYSDF--INMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVIHS 162
Cdd:MTH00027 117 IMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHS 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440655457 163 WTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWM 223
Cdd:MTH00027 197 WTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 7-224 4.36e-64

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 198.70  E-value: 4.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   7 MYFQDGNSPLMEQLMF--------FHDHAMIILIMITMIVSYFMIYLIKNNMSNKMLLHGHTIETIWTILPTITLIFIAF 78
Cdd:MTH00080   1 NYFQGYNLNFSNSLFSsymdwfhnFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  79 PSIRMLYLID-DNSNMMLTIKTIGRQWYWSYEYSDFINMEFDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATAS 157
Cdd:MTH00080  81 PSLSLLYYYGlMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 440655457 158 DVIHSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWMF 224
Cdd:MTH00080 161 DVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCK 227
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
57-223 7.29e-46

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 151.90  E-value: 7.29e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  57 HGHTIETIWTILPTITLIFIAFPSIRMLYLIDDNSNMMLTIKTIGRQWYWSYEYSDfinmefdsfmisnNNIpmnsfrlm 136
Cdd:COG1622   75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-------------QGI-------- 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457 137 EVDNRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSN 216
Cdd:COG1622  134 ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213


                 ....*..
gi 440655457 217 NLFMKWM 223
Cdd:COG1622  214 EEFDAWL 220
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 60-217 8.36e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 148.18  E-value: 8.36e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  60 TIETIWTILPTITLIFIAFPSIRMLYLiDDNSNMMLTIKTIGRQWYWSYEYSDfiNMEFDSFMISNNNIpmnsfrlmeVD 139
Cdd:MTH00047  48 VLELLWTVVPTLLVLVLCFLNLNFITS-DLDCFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------VD 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440655457 140 NRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNN 217
Cdd:MTH00047 116 KPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVD 193
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-223 5.21e-38

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: 130.96  E-value: 5.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   14 SPLMEQLMFFHDHAMIILIMITMIVSYFMIYLI------KNNMSNKMLLHGHTIETIWTILP-TITLIFIAFPSIRMLYL 86
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIPlIIVVGLFAATAKGLLYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457   87 ---IDDNSnmmLTIKTIGRQWYWSYEYSDFinmefdsfmisnnnipmnsfrLMEVDNRMMMPMNTAIRIMATASDVIHSW 163
Cdd:TIGR02866  83 erpIPKDA---LKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  164 TIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWM 223
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-215 1.55e-35

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 123.39  E-value: 1.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457 118 FDSFMISNNNIPMNSFRLMEVDNRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*...
gi 440655457 198 EICGINHSFMPIMIESTS 215
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVS 148
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.70e-24

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: 92.74  E-value: 1.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  95 LTIKTIGRQWYWSYEYSDfinmefdsfmisnnnipmnsfrlMEVDNRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 440655457 175 TPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIE 212
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), ...
 95-207 6.87e-23

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: 88.83  E-value: 6.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  95 LTIKTIGRQWYWSYEYsdfinmefdsfmisnnniPMNSFRLMEVDNRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDA 174
Cdd:cd04213    2 LTIEVTGHQWWWEFRY------------------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90       100       110
                 ....*....|....*....|....*....|...
gi 440655457 175 TPGRLNQSSFNINKPGILFGQCSEICGINHSFM 207
Cdd:cd04213   64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 2.82e-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: 2.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457    1 MATWSNMYFQDGNSPLMEQLMFFHDHAMIILIMITMIVSYFMIYLI------KNNMSNKMLLHGHTIETIWTILPTITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 440655457   75 FIAFPSIRM 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 3.55e-20

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 81.52  E-value: 3.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  95 LTIKTIGRQWYWSYEYSdfinmefdsfmisNNNipmnsfrlmEVDNRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDA 174
Cdd:cd13915    2 LEIQVTGRQWMWEFTYP-------------NGK---------REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90       100       110
                 ....*....|....*....|....*....|...
gi 440655457 175 TPGRLNQSSFNINKPGILFGQCSEICGINHSFM 207
Cdd:cd13915   60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 7.28e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 78.45  E-value: 7.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  95 LTIKTIGRQWYWSYEYSDFinmefDSFMISNNNIPMNSFRLmevdnrmmmPMNTAIRIMATASDVIHSWTIPSLGIKIDA 174
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 440655457 175 TPGRLNQSSFNINKPGILFGQCSEICGINHSFM 207
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-223 4.21e-18

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: 77.50  E-value: 4.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  95 LTIKTIGRQWYWSYEYSDFInmefdsfmisnnnipmnsfrlmEVDNRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDA 174
Cdd:cd13918   33 LEVEVEGFQFGWQFEYPNGV----------------------TTGNTLRVPADTPIALRVTSTDVFHTFGIPELRVKADA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 440655457 175 TPGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWM 223
Cdd:cd13918   91 IPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-223 1.31e-17

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 75.14  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  96 TIKTIGRQWYWSYEYSDfinmefdsfmiSNNNipmnsfrlmeVDNRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDAT 175
Cdd:cd13914    2 EIEVEAYQWGWEFSYPE-----------ANVT----------TSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 440655457 176 PGRLNQSSFNINKPGILFGQCSEICGINHSFMPIMIESTSNNLFMKWM 223
Cdd:cd13914   61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 3.16e-07

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 47.18  E-value: 3.16e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440655457 140 NRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFM 207
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-207 8.90e-04

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 37.53  E-value: 8.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440655457 140 NRMMMPMNTAIRIMATASDVIHSWTIPSLGIKIDATPGRLNQSSFNINKPGILFGQCSEICGINHSFM 207
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 2.42e-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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 36.21  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655457  96 TIKTIGRQWYWSyeysdfinmefdsfmISNNNIPMNSfrlmevdnrmmmpmntAIRIMATASDVIHSWTI--PSLGI--K 171
Cdd:cd13916    2 VVAVTGHQWYWE---------------LSRTEIPAGK----------------PVEFRVTSADVNHGFGIydPDMRLlaQ 50

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 440655457 172 IDATPGRLNQSSFNINKPGILFGQCSEICGINHSFM 207
Cdd:cd13916   51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
 
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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