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Conserved domains on  [gi|2473932268|ref|YP_010735796|]
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cytochrome c oxidase subunit II (mitochondrion) [China mantispoides]

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 3.05e-130

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 366.08  E-value: 3.05e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268   1 MATWSNLSLQDSSSSLMEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  81 IKMLYLMDDINEPNITIKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2473932268 161 HSWTIPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWVMMNN 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 3.05e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 366.08  E-value: 3.05e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268   1 MATWSNLSLQDSSSSLMEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  81 IKMLYLMDDINEPNITIKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2473932268 161 HSWTIPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWVMMNN 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 ...
 93-222 5.56e-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: 247.87  E-value: 5.56e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  93 PNITIKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKV 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473932268 173 DAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.21e-71

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 212.65  E-value: 3.21e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  95 ITIKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2473932268 175 VPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEAT 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
17-223 1.69e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 158.84  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  17 MEQLMFFHDHTMVILITISIIVAYFLMYM------SKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPSIKMLYLMDDI 90
Cdd:COG1622    29 AEEIDDLFWVSLIIMLVIFVLVFGLLLYFairyrrRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  91 NEPNITIKTIGRQWYWSYEYsdfsniefdsymtTEENnmnnsfrlIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGV 170
Cdd:COG1622   109 PEDPLTVEVTGYQWKWLFRY-------------PDQG--------IATVNELVLPVGRPVRFLLTSADVIHSFWVPALGG 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2473932268 171 KVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWV 223
Cdd:COG1622   168 KQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 17-223 7.41e-45

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: 148.68  E-value: 7.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  17 MEQLMFFHDHTMVILITISIIVAYFLMYMSknlmsYKY----------MIHGHM-IETLWTIMPA-MTLILIALPSIKML 84
Cdd:TIGR02866   6 AQQIAFLFLFVLAVSTLISLLVAALLAYVV-----WKFrrkgdeekpsQIHGNRrLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  85 YLMDDINEPNITIKTIGRQWYWSYEYSDFsniefdsymtteennmnnsfrLIEVDNNTVMPMNTSTRIMVSASDVIHSWT 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2473932268 165 IPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWV 223
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 3.05e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 366.08  E-value: 3.05e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268   1 MATWSNLSLQDSSSSLMEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  81 IKMLYLMDDINEPNITIKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2473932268 161 HSWTIPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWVMMNN 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 17-222 1.30e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 321.48  E-value: 1.30e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  17 MEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPSIKMLYLMDDINEPNIT 96
Cdd:MTH00117   17 MEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  97 IKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDAVP 176
Cdd:MTH00117   97 IKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVP 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2473932268 177 GRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKW 222
Cdd:MTH00117  177 GRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENW 222
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-225 9.88e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 301.86  E-value: 9.88e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268   1 MATWSNLSLQDSSSSLMEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  81 IKMLYLMDDINEPNITIKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVI 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473932268 161 HSWTIPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWVMM 225
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-223 1.75e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 296.23  E-value: 1.75e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268   1 MATWSNLSLQDSSSSLMEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  81 IKMLYLMDDINEPNITIKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVI 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2473932268 161 HSWTIPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWV 223
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWV 223
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-223 1.75e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 293.55  E-value: 1.75e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268   1 MATWSNLSLQDSSSSLMEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  81 IKMLYLMDDINEPNITIKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVI 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2473932268 161 HSWTIPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWV 223
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 2.67e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 293.04  E-value: 2.67e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268   1 MATWSNLSLQDSSSSLMEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  81 IKMLYLMDDINEPNITIKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVI 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2473932268 161 HSWTIPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWV 223
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-227 1.25e-100

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 291.37  E-value: 1.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268   1 MATWSNLSLQDSSSSLMEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  81 IKMLYLMDDINEPNITIKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVI 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2473932268 161 HSWTIPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWVMMNN 227
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 17-224 2.73e-94

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 275.86  E-value: 2.73e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  17 MEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPSIKMLYLMDDINEPNIT 96
Cdd:MTH00023   26 MEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  97 IKTIGRQWYWSYEYSDF--SNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDA 174
Cdd:MTH00023  106 IKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDA 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473932268 175 VPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWVM 224
Cdd:MTH00023  186 VPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 17-222 4.57e-94

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 274.67  E-value: 4.57e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  17 MEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPSIKMLYLMDDINEPNIT 96
Cdd:MTH00098   17 MEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  97 IKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDAVP 176
Cdd:MTH00098   97 VKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIP 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2473932268 177 GRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKW 222
Cdd:MTH00098  177 GRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 17-225 5.18e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 274.67  E-value: 5.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  17 MEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPSIKMLYLMDDINEPNIT 96
Cdd:MTH00129   17 MEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  97 IKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDAVP 176
Cdd:MTH00129   97 IKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVP 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2473932268 177 GRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWVMM 225
Cdd:MTH00129  177 GRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSL 225
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 17-227 3.50e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 272.42  E-value: 3.50e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  17 MEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPSIKMLYLMDDINEPNIT 96
Cdd:MTH00076   17 MEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  97 IKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDAVP 176
Cdd:MTH00076   97 VKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIP 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2473932268 177 GRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWVMMNN 227
Cdd:MTH00076  177 GRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 17-222 1.90e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 268.29  E-value: 1.90e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  17 MEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPSIKMLYLMDDINEPNIT 96
Cdd:MTH00185   17 MEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  97 IKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDAVP 176
Cdd:MTH00185   97 IKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVP 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2473932268 177 GRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKW 222
Cdd:MTH00185  177 GRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 17-223 2.91e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 267.80  E-value: 2.91e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  17 MEQLMFFHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPSIKMLYLMDDINEPNIT 96
Cdd:MTH00051   19 MEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  97 IKTIGRQWYWSYEYSDF--SNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDA 174
Cdd:MTH00051   99 IKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDA 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2473932268 175 VPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWV 223
Cdd:MTH00051  179 VPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 5.56e-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: 247.87  E-value: 5.56e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  93 PNITIKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKV 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473932268 173 DAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.21e-71

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 212.65  E-value: 3.21e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  95 ITIKTIGRQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2473932268 175 VPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEAT 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 17-223 1.69e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 213.73  E-value: 1.69e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  17 MEQLMFFHDHTMVILITISIIVAYFLM--YMSKNLMSYKY-MIHGHMIETLWTIMPAMTLILIALPSIKMLYLMDD-INE 92
Cdd:MTH00027   45 MEEIIMLHDQILFILTIIVGVVLWLIIriLLGNNYYSYYWnKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEcGFS 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  93 PNITIKTIGRQWYWSYEYSDF--SNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGV 170
Cdd:MTH00027  125 ANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAV 204

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2473932268 171 KVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWV 223
Cdd:MTH00027  205 KMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-226 4.25e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 208.71  E-value: 4.25e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  23 FHDHTMVILITISIIVAYFLMYMSKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPSIKMLYLMDDIN-EPNITIKTIG 101
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268 102 RQWYWSYEYSDFSNIEFDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDAVPGRLNQ 181
Cdd:MTH00080  105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2473932268 182 TSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWVMMN 226
Cdd:MTH00080  185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
17-223 1.69e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 158.84  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  17 MEQLMFFHDHTMVILITISIIVAYFLMYM------SKNLMSYKYMIHGHMIETLWTIMPAMTLILIALPSIKMLYLMDDI 90
Cdd:COG1622    29 AEEIDDLFWVSLIIMLVIFVLVFGLLLYFairyrrRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  91 NEPNITIKTIGRQWYWSYEYsdfsniefdsymtTEENnmnnsfrlIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGV 170
Cdd:COG1622   109 PEDPLTVEVTGYQWKWLFRY-------------PDQG--------IATVNELVLPVGRPVRFLLTSADVIHSFWVPALGG 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2473932268 171 KVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWV 223
Cdd:COG1622   168 KQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 17-223 7.41e-45

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: 148.68  E-value: 7.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  17 MEQLMFFHDHTMVILITISIIVAYFLMYMSknlmsYKY----------MIHGHM-IETLWTIMPA-MTLILIALPSIKML 84
Cdd:TIGR02866   6 AQQIAFLFLFVLAVSTLISLLVAALLAYVV-----WKFrrkgdeekpsQIHGNRrLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  85 YLMDDINEPNITIKTIGRQWYWSYEYSDFsniefdsymtteennmnnsfrLIEVDNNTVMPMNTSTRIMVSASDVIHSWT 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2473932268 165 IPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWV 223
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 61-214 1.25e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 147.79  E-value: 1.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  61 IETLWTIMPamTLILIALPSIKMLYLMDDIN-EPNITIKTIGRQWYWSYEYSDfsNIEFDSYMTTEENNMNNSFRLIevd 139
Cdd:MTH00047   49 LELLWTVVP--TLLVLVLCFLNLNFITSDLDcFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFGVDKPLRLV--- 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473932268 140 nntvmpMNTSTRIMVSASDVIHSWTIPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEAT 214
Cdd:MTH00047  122 ------YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-219 3.11e-36

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 125.32  E-value: 3.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268 118 FDSYMTTEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDAVPGRLNQTSININRPGLLYGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 2473932268 198 EICGANHSFMPIVIEATSMKNF 219
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.34e-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: 93.13  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  95 ITIKTIGRQWYWSYEYSDfsniefdsymtteennmnnsfrlIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2473932268 175 VPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIE 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 1.29e-22

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: 88.06  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  95 ITIKTIGRQWYWSYEYSDfsniefdsymtteennmnNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDA 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPD------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2473932268 175 VPGRLNQTSININRPGLLYGQCSEICGANHSFM 207
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 3.82e-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: 81.92  E-value: 3.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  95 ITIKTIGRQWYWSYEYsdfsniefdsymttEENNMNNSFRLIEVDNNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDA 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRY--------------PGGDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2473932268 175 VPGRLNQTSININRPGLLYGQCSEICGANHSFM 207
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 1.85e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 77.28  E-value: 1.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  95 ITIKTIGRQWYWSYEYSDfsniefdsyMTTEENNMnnsfrlievdnntVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDA 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPN---------GKREINEL-------------HVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2473932268 175 VPGRLNQTSININRPGLLYGQCSEICGANHSFM 207
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-223 7.40e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 75.91  E-value: 7.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  95 ITIKTIGRQWYWSYEYSDFSNIEFDSymtteennmnnsfrlievdnnTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDA 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEANVTTSEQ---------------------LVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2473932268 175 VPGRLNQTSININRPGLLYGQCSEICGANHSFMPIVIEATSMKNFMKWV 223
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-207 4.71e-16

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 72.10  E-value: 4.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  83 MLYLMD---DINEPNITIKTIGRQWYWSYEYSDfsniefdsyMTTEENNMnnsfrlievdnntVMPMNTSTRIMVSASDV 159
Cdd:cd13918    18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYPN---------GVTTGNTL-------------RVPADTPIALRVTSTDV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2473932268 160 IHSWTIPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFM 207
Cdd:cd13918    76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.10e-15

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


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 69.67  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268   1 MATWSNLSLQDSSSSLMEQLMFFHDHTMVILITISIIVAYFLMYM------SKNLMSYKYMIHGHMIETLWTIMPAMTLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTClirfnrRKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 2473932268  75 LIALPSIKM 83
Cdd:pfam02790  81 LIALPSFKL 89
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 7.64e-08

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: 48.72  E-value: 7.64e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2473932268 140 NNTVMPMNTSTRIMVSASDVIHSWTIPSMGVKVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFM 207
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 8.53e-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: 34.66  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932268  95 ITIKTIGRQWYWSyeysdfsniefdsyMTTEEnnmnnsfrlievdnntvMPMNTSTRIMVSASDVIHSWTI--PSMGV-- 170
Cdd:cd13916     1 QVVAVTGHQWYWE--------------LSRTE-----------------IPAGKPVEFRVTSADVNHGFGIydPDMRLla 49

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2473932268 171 KVDAVPGRLNQTSININRPGLLYGQCSEICGANHSFM 207
Cdd:cd13916    50 QTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 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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