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Conserved domains on  [gi|1938966205|gb|QPK42125|]
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cytochrome c oxidase subunit II (mitochondrion) [Scelimena melli]

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
 1-226 1.41e-135

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 379.56  E-value: 1.41e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  81 LHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMITET-TEMNSFRLLDVDNRTILPINTNIRILSSASDVL 159
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNeLENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966205 160 HAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKMI 226
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 1.41e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 379.56  E-value: 1.41e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  81 LHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMITET-TEMNSFRLLDVDNRTILPINTNIRILSSASDVL 159
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNeLENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966205 160 HAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKMI 226
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-221 5.37e-80

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: 235.16  E-value: 5.37e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  93 SSITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVLHAWTIPSLGIKI 171
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIpEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1938966205 172 DATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKW 221
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 2.91e-68

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 205.34  E-value: 2.91e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  95 ITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVLHAWTIPSLGIKIDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIpTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1938966205 174 TPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAV 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-225 4.70e-50

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 162.69  E-value: 4.70e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMI------NNKQSFIHMTSEHLIETTWTTMPAIVLI 74
Cdd:COG1622    13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  75 FIALPSLHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVefdsfmitettemnsfrlldVDNRTILPINTNIRILSS 154
Cdd:COG1622    93 VLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA--------------------TVNELVLPVGRPVRFLLT 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1938966205 155 ASDVLHAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKM 225
Cdd:COG1622   153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-223 1.16e-43

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: 145.60  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  13 TSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMI-----NNKQSFIHMTSEH-LIETTWTTMPA-IVLIFIALPSLHLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrKGDEEKPSQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  86 MMDDSSESSITVKTIGRQWYWSYEFSDFqkvefdsfmitettemnsfrLLDVDNRTILPINTNIRILSSASDVLHAWTIP 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPES--------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVP 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1938966205 166 SLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLS 223
Cdd:TIGR02866 142 ELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 1.41e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 379.56  E-value: 1.41e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  81 LHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMITET-TEMNSFRLLDVDNRTILPINTNIRILSSASDVL 159
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNeLENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966205 160 HAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKMI 226
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-225 1.68e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 311.10  E-value: 1.68e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  81 LHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVL 159
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVpENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1938966205 160 HAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKM 225
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-225 3.00e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 305.49  E-value: 3.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  81 LHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVL 159
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIpTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1938966205 160 HAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKM 225
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 9-225 5.34e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 302.22  E-value: 5.34e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   9 LQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPSLHLLYMMD 88
Cdd:MTH00117    9 FQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  89 DSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMITETTEMN-SFRLLDVDNRTILPINTNIRILSSASDVLHAWTIPSL 167
Cdd:MTH00117   89 EINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNgHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1938966205 168 GIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKM 225
Cdd:MTH00117  169 GVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 2.69e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 300.36  E-value: 2.69e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  81 LHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVL 159
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVpTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1938966205 160 HAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLS 223
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-226 4.37e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 297.38  E-value: 4.37e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  81 LHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVL 159
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVpTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966205 160 HAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKMI 226
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-224 4.64e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 287.52  E-value: 4.64e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  81 LHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVL 159
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLpTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1938966205 160 HAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSK 224
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 3.80e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 277.37  E-value: 3.80e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  81 LHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVL 159
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIpTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966205 160 HAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKMI 226
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 9-226 4.75e-94

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 275.09  E-value: 4.75e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   9 LQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPSLHLLYMMD 88
Cdd:MTH00023   18 FQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  89 DSSESSITVKTIGRQWYWSYEFSDFQK--VEFDSFMITeTTEMNS--FRLLDVDNRTILPINTNIRILSSASDVLHAWTI 164
Cdd:MTH00023   98 EVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVP-TSDLNSgdFRLLEVDNRLVVPINTHVRILVTGADVLHSFAV 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1938966205 165 PSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKMI 226
Cdd:MTH00023  177 PSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-226 1.44e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 265.81  E-value: 1.44e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  81 LHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVL 159
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIpTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966205 160 HAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKMI 226
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-226 1.97e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 262.90  E-value: 1.97e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  81 LHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVL 159
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTpTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966205 160 HAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKMI 226
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 10-223 1.91e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 260.48  E-value: 1.91e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  10 QDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPSLHLLYMMDD 89
Cdd:MTH00051   12 QDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  90 SSESSITVKTIGRQWYWSYEFSDF--QKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVLHAWTIPS 166
Cdd:MTH00051   92 VIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIpTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966205 167 LGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLS 223
Cdd:MTH00051  172 LSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVA 228
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-225 8.62e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 258.94  E-value: 8.62e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMINNKQSFIHMTSEHLIETTWTTMPAIVLIFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  81 LHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVL 159
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIpTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1938966205 160 HAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKM 225
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-221 5.37e-80

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: 235.16  E-value: 5.37e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  93 SSITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVLHAWTIPSLGIKI 171
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIpEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1938966205 172 DATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKW 221
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 9-224 6.18e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 219.90  E-value: 6.18e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   9 LQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMI--NNKQSFI-HMTSEHLIETTWTTMPAIVLIFIALPSLHLLY 85
Cdd:MTH00027   37 FQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILlgNNYYSYYwNKLDGSLIEVIWTLIPAFILILIAFPSLRLLY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  86 MMDDSSESS-ITVKTIGRQWYWSYEFSDF--QKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVLHA 161
Cdd:MTH00027  117 IMDECGFSAnITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIpTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHS 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1938966205 162 WTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSK 224
Cdd:MTH00027  197 WTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 2.91e-68

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 205.34  E-value: 2.91e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  95 ITVKTIGRQWYWSYEFSDFQKVEFDSFMI-TETTEMNSFRLLDVDNRTILPINTNIRILSSASDVLHAWTIPSLGIKIDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIpTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1938966205 174 TPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAV 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-222 4.80e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 196.00  E-value: 4.80e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  23 FHDHTMSIIMLITILVAHMMIYMINN---KQSFIHMtseHLIETTWTTMPAIVLIFIALPSLHLLYMMD-DSSESSITVK 98
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNfyfKSKKIEY---QFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  99 TIGRQWYWSYEFSDFQKVEFDSFM-ITETTEMNSFRLLDVDNRTILPINTNIRILSSASDVLHAWTIPSLGIKIDATPGR 177
Cdd:MTH00080  102 VTGHQWYWSYEFSDIPGLEFDSYMkSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGI 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1938966205 178 LNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWL 222
Cdd:MTH00080  182 LSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-225 4.70e-50

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 162.69  E-value: 4.70e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMI------NNKQSFIHMTSEHLIETTWTTMPAIVLI 74
Cdd:COG1622    13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  75 FIALPSLHLLYMMDDSSESSITVKTIGRQWYWSYEFSDFQKVefdsfmitettemnsfrlldVDNRTILPINTNIRILSS 154
Cdd:COG1622    93 VLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA--------------------TVNELVLPVGRPVRFLLT 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1938966205 155 ASDVLHAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLSKM 225
Cdd:COG1622   153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-223 1.16e-43

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: 145.60  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  13 TSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMI-----NNKQSFIHMTSEH-LIETTWTTMPA-IVLIFIALPSLHLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrKGDEEKPSQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  86 MMDDSSESSITVKTIGRQWYWSYEFSDFqkvefdsfmitettemnsfrLLDVDNRTILPINTNIRILSSASDVLHAWTIP 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPES--------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVP 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1938966205 166 SLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWLS 223
Cdd:TIGR02866 142 ELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-213 1.62e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 139.70  E-value: 1.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  17 MEQLMFFHDHTMSIIML---ITILVAHMMIYMINNKQSFIHMTSE-HLIETTWTTMPAIVLIFIALPSLHLLYMmDDSSE 92
Cdd:MTH00047    1 MNLSLLYYDIVCYILALcvfIPCWVYIMLCWQVVSGNGSVNFGSEnQVLELLWTVVPTLLVLVLCFLNLNFITS-DLDCF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  93 SSITVKTIGRQWYWSYEFSDfqKVEFDSFMiteTTEMNSfrlldVDNRTILPINTNIRILSSASDVLHAWTIPSLGIKID 172
Cdd:MTH00047   80 SSETIKVIGHQWYWSYEYSF--GGSYDSFM---TDDIFG-----VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMD 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1938966205 173 ATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAV 213
Cdd:MTH00047  150 AIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-218 4.83e-35

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 122.24  E-value: 4.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205 118 FDSFMIT-ETTEMNSFRLLDVDNRTILPINTNIRILSSASDVLHAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCS 196
Cdd:PTZ00047   51 FQSNLVTdEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 1938966205 197 EICGINHSFMPITIEAVNTTSF 218
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-211 2.26e-23

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: 90.05  E-value: 2.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  95 ITVKTIGRQWYWSYEFSDfqkvefdsfmitettemnsfrlLDVDNRTILPINTNIRILSSASDVLHAWTIPSLGIKIDAT 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAV 58

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1938966205 175 PGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIE 211
Cdd:cd13842    59 PGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-213 2.67e-19

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: 79.59  E-value: 2.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  94 SITVKTIGRQWYWSYEFSDFQKVEFdsfmitETTemnsfrlldvdNRTILPINTNIRILSSASDVLHAWTIPSLGIKIDA 173
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGI------VTA-----------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1938966205 174 TPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAV 213
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 8.41e-19

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: 77.76  E-value: 8.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205   1 MATWNNVYLQDSTSPMMEQLMFFHDHTMSIIMLITILVAHMMIYMI------NNKQSFIHMTSEHLIETTWTTMPAIVLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1938966205  75 FIALPSLHL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 71-222 4.35e-18

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 77.50  E-value: 4.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  71 IVLIFIALPSLHLLYMMD---DSSESSITVKTIGRQWYWSYEFSDfqkvefdsfmitETTEMNSFRLldvdnrtilPINT 147
Cdd:cd13918     6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPN------------GVTTGNTLRV---------PADT 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1938966205 148 NIRILSSASDVLHAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWL 222
Cdd:cd13918    65 PIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 2.25e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 74.60  E-value: 2.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  95 ITVKTIGRQWYWSYEFSDfQKVEFDSFMITETTEMNsfrlldvdnrtiLPINTNIRILSSASDVLHAWTIPSLGIKIDAT 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPG-GDGKLGTDDDVTSPELH------------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAV 68

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1938966205 175 PGRLNQSTFSIKRPGLMFGQCSEICGINHSFM 206
Cdd:cd13919    69 PGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-212 4.17e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 73.43  E-value: 4.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  94 SITVKTIGRQWYWSYEFSDFQKVefdsfmitettemnsfrlldvDNRTILPINTNIRILSSASDVLHAWTIPSLGIKIDA 173
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKRE---------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1938966205 174 TPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEA 212
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-222 7.13e-17

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 73.21  E-value: 7.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  95 ITVKTIGRQWYWSYEFSDFQkvefdsfmITETTEMnsfrlldvdnrtILPINTNIRILSSASDVLHAWTIPSLGIKIDAT 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEAN--------VTTSEQL------------VIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1938966205 175 PGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAVNTTSFIKWL 222
Cdd:cd13914    61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 143-213 1.34e-05

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: 42.56  E-value: 1.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1938966205 143 LPINTNIRILSSASDVLHAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAV 213
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-213 7.95e-04

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 37.36  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205  95 ITVKTIGRQWYWsyefsdfqkvefdsfmitettEMNsfrlldvdnRTILPINTNIRILSSASDVLHAWTI--PSLGI--K 170
Cdd:cd13916     1 QVVAVTGHQWYW---------------------ELS---------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQ 50

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1938966205 171 IDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAV 213
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTVV 93
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 137-211 5.78e-03

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 35.28  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966205 137 VDNRTILPINTNIR-ILSSASDVLHAWTIPSLGIKIDA---------------TPGRLNQSTFSIKRPGLMFGQCSEICG 200
Cdd:cd00920    21 GPPVLVVPVGDTVRvQFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGH 100

                          90
                  ....*....|.
gi 1938966205 201 iNHSFMPITIE 211
Cdd:cd00920   101 -NHAGMVGTIN 110
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 139-213 8.06e-03

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: 34.83  E-value: 8.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1938966205 139 NRTILPINTNIRILSSASDVLHAWTIPSLGIKIDATPGRLNQSTFSIKRPGLMFGQCSEICGINHSFMPITIEAV 213
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
 
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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