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Conserved domains on  [gi|2452628044|ref|YP_010698178|]
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cytochrome c oxidase subunit II (mitochondrion) [Thoradonta yunnana]

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
 1-225 3.51e-130

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 366.08  E-value: 3.51e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  81 LHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMI--NENNLSSFRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWIMNQI 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 3.51e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 366.08  E-value: 3.51e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  81 LHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMI--NENNLSSFRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWIMNQI 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-220 8.29e-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: 234.77  E-value: 8.29e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  93 STITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLS--SFRLLDVDNRAVMPIYTNIRILTSASDVLHSWTIPSLGIKI 170
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEkgQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2452628044 171 DATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKW 220
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-212 9.65e-68

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 203.80  E-value: 9.65e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  95 ITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLS--SFRLLDVDNRAVMPIYTNIRILTSASDVLHSWTIPSLGIKIDA 172
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEegQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2452628044 173 TPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAI 212
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-221 1.33e-44

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 148.82  E-value: 1.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMIsilmnLMSFRY-----------MLNDHFIETIWTMMP 69
Cdd:COG1622    13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLL-----YFAIRYrrrkgdadpaqFHHNTKLEIVWTVIP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  70 AMVLILIAIPSLHLLYMMDDSNESTITVKTIGRQWYWSYEYSDfQKIEfdsfminennlssfrlldVDNRAVMPIYTNIR 149
Cdd:COG1622    88 IIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA------------------TVNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2452628044 150 ILTSASDVLHSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWI 221
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-221 5.97e-37

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: 128.27  E-value: 5.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  14 SPLMEQLMFFHDHAMSIIMMITLMVSFFMIsilMNLMSFR---------YMLNDHFIETIWTMMPA-MVLILIAIPSLHL 83
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLA---YVVWKFRrkgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  84 LYMMDDSNESTITVKTIGRQWYWSYEYSDfqkiefdsfminennlSSFRlldVDNRAVMPIYTNIRILTSASDVLHSWTI 163
Cdd:TIGR02866  80 LYLERPIPKDALKVKVTGYQWWWDFEYPE----------------SGFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2452628044 164 PSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWI 221
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 3.51e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 366.08  E-value: 3.51e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  81 LHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMI--NENNLSSFRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWIMNQI 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-223 1.16e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 324.20  E-value: 1.16e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  81 LHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLSS--FRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELgdFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWIMN 223
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-221 3.58e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 310.31  E-value: 3.58e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  81 LHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLS--SFRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPngHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWI 221
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWS 223
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-223 1.20e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 306.26  E-value: 1.20e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  81 LHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLSS--FRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSgeFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWIMN 223
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-225 2.22e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 303.16  E-value: 2.22e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  81 LHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLSS--FRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTglPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWIMNQI 225
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-223 7.22e-104

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 299.46  E-value: 7.22e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  81 LHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLS--SFRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSpgQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWIMN 223
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 8.83e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 294.20  E-value: 8.83e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  81 LHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLS--SFRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSpgQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWIMN 223
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 5-223 2.06e-94

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 275.86  E-value: 2.06e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   5 NNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPSLHLL 84
Cdd:MTH00023   14 WQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  85 YMMDDSNESTITVKTIGRQWYWSYEYSDFQK--IEFDSFMINENNLSS--FRLLDVDNRAVMPIYTNIRILTSASDVLHS 160
Cdd:MTH00023   94 YLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSgdFRLLEVDNRLVVPINTHVRILVTGADVLHS 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2452628044 161 WTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWIMN 223
Cdd:MTH00023  174 FAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-220 7.89e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 271.59  E-value: 7.89e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  81 LHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLS--SFRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTpgQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKW 220
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-220 1.19e-92

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 270.82  E-value: 1.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  81 LHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLS--SFRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKpgELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKW 220
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-224 5.84e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 269.34  E-value: 5.84e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   7 LSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPSLHLLYM 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  87 MDDSNESTITVKTIGRQWYWSYEYSDF--QKIEFDSFMINENNLSS--FRLLDVDNRAVMPIYTNIRILTSASDVLHSWT 162
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSgdLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2452628044 163 IPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWIMNQ 224
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-220 6.65e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 264.05  E-value: 6.65e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  81 LHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLSS--FRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPgqFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKW 220
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 9.53e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 261.25  E-value: 9.53e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVsFFMISILMNL-MSFRYMLNDHFIETIWTMMPAMVLILIAIP 79
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLV-LYIITIMMTTkLTNTNTMDAQEIEMVWTIMPAIILIVIALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  80 SLHLLYMMDDSNESTITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLS--SFRLLDVDNRAVMPIYTNIRILTSASDV 157
Cdd:MTH00076   80 SLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTpgQFRLLEVDNRMVVPMESPIRMLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2452628044 158 LHSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWIMNQ 224
Cdd:MTH00076  160 LHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-220 8.29e-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: 234.77  E-value: 8.29e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  93 STITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLS--SFRLLDVDNRAVMPIYTNIRILTSASDVLHSWTIPSLGIKI 170
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEkgQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2452628044 171 DATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKW 220
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-221 1.29e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 224.13  E-value: 1.29e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   7 LSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYM---LNDHFIETIWTMMPAMVLILIAIPSLHL 83
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  84 LYMMDDSN-ESTITVKTIGRQWYWSYEYSDF--QKIEFDSFMINENNLS--SFRLLDVDNRAVMPIYTNIRILTSASDVL 158
Cdd:MTH00027  115 LYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEfgDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2452628044 159 HSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWI 221
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-212 9.65e-68

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 203.80  E-value: 9.65e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  95 ITVKTIGRQWYWSYEYSDFQKIEFDSFMINENNLS--SFRLLDVDNRAVMPIYTNIRILTSASDVLHSWTIPSLGIKIDA 172
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEegQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2452628044 173 TPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAI 212
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 5-223 1.18e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 194.84  E-value: 1.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   5 NNLSLQDSI-SPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLNDHFIETIWTMMPAMVLILIAIPSLHL 83
Cdd:MTH00080    6 YNLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  84 LYMMDDSN-ESTITVKTIGRQWYWSYEYSDFQKIEFDSFM--INENNLSSFRLLDVDNRAVMPIYTNIRILTSASDVLHS 160
Cdd:MTH00080   86 LYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMksLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHS 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2452628044 161 WTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWIMN 223
Cdd:MTH00080  166 WALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKL 228
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-221 1.33e-44

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 148.82  E-value: 1.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMIsilmnLMSFRY-----------MLNDHFIETIWTMMP 69
Cdd:COG1622    13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLL-----YFAIRYrrrkgdadpaqFHHNTKLEIVWTVIP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  70 AMVLILIAIPSLHLLYMMDDSNESTITVKTIGRQWYWSYEYSDfQKIEfdsfminennlssfrlldVDNRAVMPIYTNIR 149
Cdd:COG1622    88 IIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA------------------TVNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2452628044 150 ILTSASDVLHSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWI 221
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-212 3.14e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 143.94  E-value: 3.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  17 MEQLMFFHDHAMSIIMMITLMVSFFMISILMNLMSFRYMLN----DHFIETIWTMMPAM-VLILIAipsLHLLYMMDDSN 91
Cdd:MTH00047    1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSGNGSVNfgseNQVLELLWTVVPTLlVLVLCF---LNLNFITSDLD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  92 -ESTITVKTIGRQWYWSYEYSDfqKIEFDSFMINENNLssfrlldVDNRAVMPIYTNIRILTSASDVLHSWTIPSLGIKI 170
Cdd:MTH00047   78 cFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG-------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKM 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2452628044 171 DATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAI 212
Cdd:MTH00047  149 DAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-221 5.97e-37

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: 128.27  E-value: 5.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  14 SPLMEQLMFFHDHAMSIIMMITLMVSFFMIsilMNLMSFR---------YMLNDHFIETIWTMMPA-MVLILIAIPSLHL 83
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLA---YVVWKFRrkgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  84 LYMMDDSNESTITVKTIGRQWYWSYEYSDfqkiefdsfminennlSSFRlldVDNRAVMPIYTNIRILTSASDVLHSWTI 163
Cdd:TIGR02866  80 LYLERPIPKDALKVKVTGYQWWWDFEYPE----------------SGFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2452628044 164 PSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWI 221
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-217 2.87e-36

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 125.32  E-value: 2.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044 118 FDSFMINENNLSS--FRLLDVDNRAVMPIYTNIRILTSASDVLHSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCS 195
Cdd:PTZ00047   51 FQSNLVTDEDLKPgmLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 2452628044 196 EICGMNHSFMPIAIEAINTKSF 217
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-210 3.25e-22

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: 86.97  E-value: 3.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  95 ITVKTIGRQWYWSYEYSDfqkiefdsfminennlssfrlLDVDNRAVMPIYTNIRILTSASDVLHSWTIPSLGIKIDATP 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN---------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVP 59

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2452628044 175 GRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIE 210
Cdd:cd13842    60 GYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-205 1.17e-20

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: 83.05  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  94 TITVKTIGRQWYWSYEYSDFQKIEFdsfmINENNLssfrlldvdnraVMPIYTNIRILTSASDVLHSWTIPSLGIKIDAT 173
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGI----VTANEL------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMI 64

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2452628044 174 PGRLNQSIFFIKRPGLMFGQCSEICGMNHSFM 205
Cdd:cd04213    65 PGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 2.50e-18

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: 76.60  E-value: 2.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044   1 MATWNNLSLQDSISPLMEQLMFFHDHAMSIIMMITLMVSFFMISILMNL------MSFRYMLNDHFIETIWTMMPAMVLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFnrrknpITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 2452628044  75 LIAIPSLHL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-205 8.39e-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: 75.36  E-value: 8.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  94 TITVKTIGRQWYWSYEYSDFQKIefdsfminennlssfrlldvDNRAVMPIYTNIRILTSASDVLHSWTIPSLGIKIDAT 173
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKRE--------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2452628044 174 PGRLNQSIFFIKRPGLMFGQCSEICGMNHSFM 205
Cdd:cd13915    61 PGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 71-220 9.03e-17

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 74.03  E-value: 9.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  71 MVLILIAIPSLHLLYMMD---DSNESTITVKTIGRQWYWSYEYSdfqkiefdsfmineNNLSSFrlldvdNRAVMPIYTN 147
Cdd:cd13918     6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYP--------------NGVTTG------NTLRVPADTP 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2452628044 148 IRILTSASDVLHSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKW 220
Cdd:cd13918    66 IALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-205 1.15e-15

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: 69.98  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  94 TITVKTIGRQWYWSYEY--SDFQKIEFDSFMINEnnlssfrlldvdnrAVMPIYTNIRILTSASDVLHSWTIPSLGIKID 171
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYpgGDGKLGTDDDVTSPE--------------LHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2452628044 172 ATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFM 205
Cdd:cd13919    67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-221 2.85e-15

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: 68.97  E-value: 2.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452628044  95 ITVKTIGRQWYWSYEYsdfqkiefdsfmiNENNLSSFrlldvdNRAVMPIYTNIRILTSASDVLHSWTIPSLGIKIDATP 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSY-------------PEANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFP 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2452628044 175 GRLNQSIFFIKRPGLMFGQCSEICGMNHSFMPIAIEAINTKSFIKWI 221
Cdd:cd13914    62 GQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 143-205 6.95e-03

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: 34.85  E-value: 6.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2452628044 143 PIYTNIRILTSASDVLHSWTIPSLGIKIDATPGRLNQSIFFIKRPGLMFGQCSEICGMNHSFM 205
Cdd:cd13913    30 PAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
 
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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