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Conserved domains on  [gi|338164010|gb|AEI75262|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Roger sp. ccoc164]

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
 6-230 4.59e-144

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 401.13  E-value: 4.59e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   6 ATWKTSLFLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSL 85
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  86 KLIYLIDEIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIH 165
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338164010 166 SWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKSF 230
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 6-230 4.59e-144

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 401.13  E-value: 4.59e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   6 ATWKTSLFLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSL 85
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  86 KLIYLIDEIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIH 165
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338164010 166 SWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKSF 230
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 97-226 1.62e-85

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: 249.41  E-value: 1.62e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  97 PLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKI 176
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 338164010 177 DASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKW 226
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
99-218 2.48e-72

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 215.74  E-value: 2.48e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   99 ITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDA 178
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 338164010  179 SPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESI 218
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
32-229 1.73e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 161.53  E-value: 1.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  32 LLILTLVTCTVSYILIS--LIFN--KFNHR-------YLLEGQTIEMIWTILPAITLIFIALPSLKLIYLIDEIRNPLIT 100
Cdd:COG1622   35 LFWVSLIIMLVIFVLVFglLLYFaiRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLT 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010 101 IKIIGHQWYWSYEYSDfEKIEfdsymvpysnlnnfnfrlleVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDASP 180
Cdd:COG1622  115 VEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIP 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 338164010 181 GRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKS 229
Cdd:COG1622  174 GRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 22-227 3.26e-39

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 134.05  E-value: 3.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   22 EQLSFFHDHALLILTLVTCTVSYILISLIFnKFNHR-------YLLEGQTIEMIWTILPA-ITLIFIALPSLKLIYLIDE 93
Cdd:TIGR02866   7 QQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLLYLERP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   94 IRNPLITIKIIGHQWYWSYEYSDFekiefdsymvpysnlnnfnfrLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTG 173
Cdd:TIGR02866  86 IPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELG 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 338164010  174 IKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWL 227
Cdd:TIGR02866 145 GKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 6-230 4.59e-144

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 401.13  E-value: 4.59e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   6 ATWKTSLFLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSL 85
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  86 KLIYLIDEIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIH 165
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338164010 166 SWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKSF 230
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 6-229 1.29e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 336.91  E-value: 1.29e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   6 ATWKTSLFLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSL 85
Cdd:MTH00140   2 SYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  86 KLIYLIDEIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIH 165
Cdd:MTH00140  82 RLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338164010 166 SWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKS 229
Cdd:MTH00140 162 SWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 5-230 1.92e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 328.97  E-value: 1.92e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   5 IATWKTSLFLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPS 84
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  85 LKLIYLIDEIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVI 164
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338164010 165 HSWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKSF 230
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNF 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 5-230 4.95e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 327.83  E-value: 4.95e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   5 IATWKTSLFLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPS 84
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  85 LKLIYLIDEIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVI 164
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338164010 165 HSWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKSF 230
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 13-230 7.77e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 327.26  E-value: 7.77e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  13 FLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSLKLIYLID 92
Cdd:MTH00117   9 FQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  93 EIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPST 172
Cdd:MTH00117  89 EINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 338164010 173 GIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKSF 230
Cdd:MTH00117 169 GVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 5-230 2.40e-112

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 321.04  E-value: 2.40e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   5 IATWKTSLFLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPS 84
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  85 LKLIYLIDEIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVI 164
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338164010 165 HSWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKSF 230
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSF 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 6-227 2.83e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 320.77  E-value: 2.83e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   6 ATWKTSLFLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSL 85
Cdd:MTH00168   2 ATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  86 KLIYLIDEIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIH 165
Cdd:MTH00168  82 RLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338164010 166 SWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWL 227
Cdd:MTH00168 162 SWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 13-229 5.20e-102

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 295.51  E-value: 5.20e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  13 FLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSLKLIYLID 92
Cdd:MTH00023  18 FQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  93 EIRNPLITIKIIGHQWYWSYEYSDF--EKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIP 170
Cdd:MTH00023  98 EVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVP 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 338164010 171 STGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKS 229
Cdd:MTH00023 178 SLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 13-229 4.35e-100

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 290.08  E-value: 4.35e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  13 FLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSLKLIYLID 92
Cdd:MTH00098   9 FQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  93 EIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPST 172
Cdd:MTH00098  89 EINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 338164010 173 GIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKS 229
Cdd:MTH00098 169 GLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSAS 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 13-226 3.54e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 287.77  E-value: 3.54e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  13 FLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSLKLIYLID 92
Cdd:MTH00129   9 FQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  93 EIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPST 172
Cdd:MTH00129  89 EINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPAL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 338164010 173 GIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKW 226
Cdd:MTH00129 169 GVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 13-229 1.39e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 286.68  E-value: 1.39e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  13 FLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSLKLIYLID 92
Cdd:MTH00051  11 FQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  93 EIRNPLITIKIIGHQWYWSYEYSDF--EKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIP 170
Cdd:MTH00051  91 EVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVP 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 338164010 171 STGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKS 229
Cdd:MTH00051 171 SLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVAT 229
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 13-229 8.05e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 279.36  E-value: 8.05e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  13 FLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSLKLIYLID 92
Cdd:MTH00076   9 FQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  93 EIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPST 172
Cdd:MTH00076  89 EINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 338164010 173 GIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKS 229
Cdd:MTH00076 169 GIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 13-226 1.88e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 278.31  E-value: 1.88e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  13 FLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSLKLIYLID 92
Cdd:MTH00185   9 LQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  93 EIRNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPST 172
Cdd:MTH00185  89 EINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPAL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 338164010 173 GIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKW 226
Cdd:MTH00185 169 GVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 97-226 1.62e-85

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: 249.41  E-value: 1.62e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  97 PLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKI 176
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 338164010 177 DASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKW 226
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 13-227 2.22e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 223.75  E-value: 2.22e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  13 FLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYL---LEGQTIEMIWTILPAITLIFIALPSLKLIY 89
Cdd:MTH00027  37 FQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRLLY 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  90 LIDE-IRNPLITIKIIGHQWYWSYEYSDF--EKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHS 166
Cdd:MTH00027 117 IMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHS 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338164010 167 WTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWL 227
Cdd:MTH00027 197 WTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
99-218 2.48e-72

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 215.74  E-value: 2.48e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   99 ITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDA 178
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 338164010  179 SPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESI 218
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 16-230 4.92e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 211.41  E-value: 4.92e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  16 SSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIFNKFNHRYLLEGQTIEMIWTILPAITLIFIALPSLKLIYLIDEI- 94
Cdd:MTH00080  14 LFSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMn 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  95 RNPLITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTGI 174
Cdd:MTH00080  94 LDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSI 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 338164010 175 KIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKSF 230
Cdd:MTH00080 174 KMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
32-229 1.73e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 161.53  E-value: 1.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  32 LLILTLVTCTVSYILIS--LIFN--KFNHR-------YLLEGQTIEMIWTILPAITLIFIALPSLKLIYLIDEIRNPLIT 100
Cdd:COG1622   35 LFWVSLIIMLVIFVLVFglLLYFaiRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLT 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010 101 IKIIGHQWYWSYEYSDfEKIEfdsymvpysnlnnfnfrlleVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDASP 180
Cdd:COG1622  115 VEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIP 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 338164010 181 GRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWLKS 229
Cdd:COG1622  174 GRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 61-218 1.89e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 152.42  E-value: 1.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  61 EGQTIEMIWTILPaiTLIFIALPSLKLIYLIDEIR-NPLITIKIIGHQWYWSYEYSDfeKIEFDSYMVPYSNLnnfnfrl 139
Cdd:MTH00047  45 ENQVLELLWTVVP--TLLVLVLCFLNLNFITSDLDcFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG------- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338164010 140 leVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESI 218
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 22-227 3.26e-39

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


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 134.05  E-value: 3.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   22 EQLSFFHDHALLILTLVTCTVSYILISLIFnKFNHR-------YLLEGQTIEMIWTILPA-ITLIFIALPSLKLIYLIDE 93
Cdd:TIGR02866   7 QQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLLYLERP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010   94 IRNPLITIKIIGHQWYWSYEYSDFekiefdsymvpysnlnnfnfrLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTG 173
Cdd:TIGR02866  86 IPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELG 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 338164010  174 IKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWL 227
Cdd:TIGR02866 145 GKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 122-228 1.77e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 128.40  E-value: 1.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010 122 FDSYMVPYSNLNNFNFRLLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCS 201
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100       110
                 ....*....|....*....|....*....|.
gi 338164010 202 EICGINHSFMPISIESISQMSFI----KWLK 228
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVSPEAYAahakKYYK 161
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 99-216 1.64e-26

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 98.14  E-value: 1.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  99 ITIKIIGHQWYWSYEYSDfekiefdsymvpysnlnnfnfrlLEVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDA 178
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 338164010 179 SPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIE 216
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), ...
 99-211 7.58e-24

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


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 91.53  E-value: 7.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  99 ITIKIIGHQWYWSYEYSDFEKIEFdsymvpysnlnnfnfrllEVDNRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDA 178
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPGRGI------------------VTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90       100       110
                 ....*....|....*....|....*....|...
gi 338164010 179 SPGRINQMNLILNRTGLFYGQCSEICGINHSFM 211
Cdd:cd04213   64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-227 5.02e-20

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 81.69  E-value: 5.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  99 ITIKIIGHQWYWSYEYSDfekiefdsymvpySNLNNFNfrllevdnRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDA 178
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPE-------------ANVTTSE--------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 338164010 179 SPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWL 227
Cdd:cd13914   60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 5-87 5.39e-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: 80.84  E-value: 5.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010    5 IATWKTSLFLDSSSFLLEQLSFFHDHALLILTLVTCTVSYILISLIF------NKFNHRYLLEGQTIEMIWTILPAITLI 78
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 338164010   79 FIALPSLKL 87
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-211 7.32e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 81.15  E-value: 7.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  99 ITIKIIGHQWYWSYEYSDFEKIEFDSYMVPYSNLnnfnfrllevdnrtVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDA 178
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 338164010 179 SPGRINQMNLILNRTGLFYGQCSEICGINHSFM 211
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-227 7.93e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 74.03  E-value: 7.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  99 ITIKIIGHQWYWSYEYSdfekiefdsymVPYSNLNNFnfrllevdnrtVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDA 178
Cdd:cd13918   33 LEVEVEGFQFGWQFEYP-----------NGVTTGNTL-----------RVPADTPIALRVTSTDVFHTFGIPELRVKADA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 338164010 179 SPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIESISQMSFIKWL 227
Cdd:cd13918   91 IPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-211 2.76e-16

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 71.51  E-value: 2.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338164010  99 ITIKIIGHQWYWSYEYSDFEKIefdsymvpysnlnnfnfrllevDNRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDA 178
Cdd:cd13915    2 LEIQVTGRQWMWEFTYPNGKRE----------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90       100       110
                 ....*....|....*....|....*....|...
gi 338164010 179 SPGRINQMNLILNRTGLFYGQCSEICGINHSFM 211
Cdd:cd13915   60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 144-216 5.10e-10

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 54.88  E-value: 5.10e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338164010 144 NRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFMPISIE 216
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKII 97
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 144-211 2.80e-06

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: 44.46  E-value: 2.80e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338164010 144 NRTVLPYQTQIRILTTSSDVIHSWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFM 211
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 147-211 1.80e-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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 36.58  E-value: 1.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338164010 147 VLPYQTQIRILTTSSDVIHSWTIPSTGIKIDASPGRINQMNLILNRTGLFYGQCSEICGINHSFM 211
Cdd:cd13917   17 VLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
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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