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Conserved domains on  [gi|1241822528|gb|ATA58332|]
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cytochrome c oxidase subunit II [Bolivaritettix yuanbaoshanensis]

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 1.65e-137

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 384.57  E-value: 1.65e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMVSEN--KNNFFRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNelENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKNQI 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 1.65e-137

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 384.57  E-value: 1.65e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMVSEN--KNNFFRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNelENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKNQI 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 1.65e-79

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: 234.00  E-value: 1.65e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  93 SNITIKTIGRQWYWSYEYSDFHKVEFDSFMVSEN--KNNFFRLLDVDNRTTLPINTYIRILTSASDVLHSWTIPSLGVKI 170
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDdlEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1241822528 171 DATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKW 220
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-212 5.73e-67

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 201.87  E-value: 5.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  95 ITIKTIGRQWYWSYEYSDFHKVEFDSFMVSENKNNF--FRLLDVDNRTTLPINTYIRILTSASDVLHSWTIPSLGVKIDA 172
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEgqLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1241822528 173 TPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAI 212
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-224 4.73e-46

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 152.29  E-value: 4.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMsqIFMnkmSFRYMLSE-----------HTIETIWTMIP 69
Cdd:COG1622    13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLL--LYF---AIRYRRRKgdadpaqfhhnTKLEIVWTVIP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  70 TMVLIFIAMPSLHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVefdsfmvsenknnffrlldVDNRTTLPINTYIR 149
Cdd:COG1622    88 IIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA-------------------TVNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241822528 150 ILTSASDVLHSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKNQ 224
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-221 1.64e-35

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: 124.42  E-value: 1.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  14 SPLMEQLSFFHDHSMSIIMMITSIV-SYMMSQIFmnkmSFRY--------MLSEHT-IETIWTMIP-TMVLIFIAMPSLH 82
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVW----KFRRkgdeekpsQIHGNRrLEYVWTVIPlIIVVGLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  83 LLYMMDDSTESNITIKTIGRQWYWSYEYSDFhkvefdsfmvsenknnffrLLDVDNRTTLPINTYIRILTSASDVLHSWT 162
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES-------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1241822528 163 IPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWL 221
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 1.65e-137

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 384.57  E-value: 1.65e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMVSEN--KNNFFRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNelENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKNQI 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-223 3.11e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 325.74  E-value: 3.11e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMVSENKNN--FFRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELElgDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKN 223
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-223 5.54e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 309.73  E-value: 5.54e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMVSENKNNF--FRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSgeFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKN 223
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-224 4.48e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 304.91  E-value: 4.48e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMVSEN--KNNFFRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQdlPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKNQ 224
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-223 4.22e-104

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 300.23  E-value: 4.22e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMV--SENKNNFFRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLptSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKN 223
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-225 4.30e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 297.38  E-value: 4.30e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMV--SENKNNFFRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVptSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKNQI 225
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 2.96e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 295.35  E-value: 2.96e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMV--SENKNNFFRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVptQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKN 223
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-224 6.67e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 274.35  E-value: 6.67e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   7 INLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPSLHLLYM 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  87 MDDSTESNITIKTIGRQWYWSYEYSDF--HKVEFDSFMV--SENKNNFFRLLDVDNRTTLPINTYIRILTSASDVLHSWT 162
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIptSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1241822528 163 IPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKNQ 224
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 5-223 1.18e-93

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 273.93  E-value: 1.18e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   5 NNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPSLHLL 84
Cdd:MTH00023   14 WQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  85 YMMDDSTESNITIKTIGRQWYWSYEYSDFHK--VEFDSFMV--SENKNNFFRLLDVDNRTTLPINTYIRILTSASDVLHS 160
Cdd:MTH00023   94 YLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVptSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHS 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1241822528 161 WTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKN 223
Cdd:MTH00023  174 FAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-220 1.83e-91

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 268.12  E-value: 1.83e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMV--SENKNNFFRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIptSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKW 220
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-220 5.72e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 261.96  E-value: 5.72e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMVSENK--NNFFRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDltPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKW 220
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-220 5.75e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 259.43  E-value: 5.75e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMVSENKNN--FFRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTpgQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKW 220
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 1.38e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 255.86  E-value: 1.38e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYMLSEHTIETIWTMIPTMVLIFIAMPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  81 LHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMVSENKNN--FFRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTpgQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKNQ 224
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-220 1.65e-79

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: 234.00  E-value: 1.65e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  93 SNITIKTIGRQWYWSYEYSDFHKVEFDSFMVSEN--KNNFFRLLDVDNRTTLPINTYIRILTSASDVLHSWTIPSLGVKI 170
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDdlEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1241822528 171 DATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKW 220
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-221 1.26e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 221.44  E-value: 1.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   7 INLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKMSFRYM---LSEHTIETIWTMIPTMVLIFIAMPSLHL 83
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  84 LYMMDDST-ESNITIKTIGRQWYWSYEYSDF--HKVEFDSFMVSENKNNF--FRLLDVDNRTTLPINTYIRILTSASDVL 158
Cdd:MTH00027  115 LYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFgdLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1241822528 159 HSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWL 221
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-212 5.73e-67

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 201.87  E-value: 5.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  95 ITIKTIGRQWYWSYEYSDFHKVEFDSFMVSENKNNF--FRLLDVDNRTTLPINTYIRILTSASDVLHSWTIPSLGVKIDA 172
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEgqLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1241822528 173 TPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAI 212
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 5-223 1.13e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 197.54  E-value: 1.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   5 NNINLQDSL-SPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFMNKmSFRYMLSEH-TIETIWTMIPTMVLIFIAMPSLH 82
Cdd:MTH00080    6 YNLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNF-YFKSKKIEYqFGELLCSVFPVLILLMQMVPSLS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  83 LLYMMD-DSTESNITIKTIGRQWYWSYEYSDFHKVEFDSFMVSENKNNF--FRLLDVDNRTTLPINTYIRILTSASDVLH 159
Cdd:MTH00080   85 LLYYYGlMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLgePRLLEVDNRCVLPCDTNIRFCITSSDVIH 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1241822528 160 SWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKN 223
Cdd:MTH00080  165 SWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKL 228
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-224 4.73e-46

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 152.29  E-value: 4.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMsqIFMnkmSFRYMLSE-----------HTIETIWTMIP 69
Cdd:COG1622    13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLL--LYF---AIRYRRRKgdadpaqfhhnTKLEIVWTVIP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  70 TMVLIFIAMPSLHLLYMMDDSTESNITIKTIGRQWYWSYEYSDFHKVefdsfmvsenknnffrlldVDNRTTLPINTYIR 149
Cdd:COG1622    88 IIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA-------------------TVNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241822528 150 ILTSASDVLHSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWLKNQ 224
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 30-212 1.08e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 150.49  E-value: 1.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  30 IIMMITSIVSYMMSQIFMNKmsfrymlsEHTIETIWTMIPTMVLIFIAMPSLHLLYMmDDSTESNITIKTIGRQWYWSYE 109
Cdd:MTH00047   26 YIMLCWQVVSGNGSVNFGSE--------NQVLELLWTVVPTLLVLVLCFLNLNFITS-DLDCFSSETIKVIGHQWYWSYE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528 110 YSDfhKVEFDSFMVSENKNnffrlldVDNRTTLPINTYIRILTSASDVLHSWTIPSLGVKIDATPGRLNQSMFLIKRPGI 189
Cdd:MTH00047   97 YSF--GGSYDSFMTDDIFG-------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGV 167

                         170       180
                  ....*....|....*....|...
gi 1241822528 190 MFGQCSEICGINHSFMPIAIEAI 212
Cdd:MTH00047  168 FVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-212 5.37e-36

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 124.55  E-value: 5.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528 118 FDSFMVSEN--KNNFFRLLDVDNRTTLPINTYIRILTSASDVLHSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCS 195
Cdd:PTZ00047   51 FQSNLVTDEdlKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*..
gi 1241822528 196 EICGINHSFMPIAIEAI 212
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAV 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-221 1.64e-35

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: 124.42  E-value: 1.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  14 SPLMEQLSFFHDHSMSIIMMITSIV-SYMMSQIFmnkmSFRY--------MLSEHT-IETIWTMIP-TMVLIFIAMPSLH 82
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVW----KFRRkgdeekpsQIHGNRrLEYVWTVIPlIIVVGLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  83 LLYMMDDSTESNITIKTIGRQWYWSYEYSDFhkvefdsfmvsenknnffrLLDVDNRTTLPINTYIRILTSASDVLHSWT 162
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES-------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1241822528 163 IPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWL 221
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-210 9.83e-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: 88.12  E-value: 9.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  95 ITIKTIGRQWYWSYEYSDfhkvefdsfmvsenknnffrlLDVDNRTTLPINTYIRILTSASDVLHSWTIPSLGVKIDATP 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN---------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVP 59

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1241822528 175 GRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIE 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), ...
 95-205 4.05e-21

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: 84.21  E-value: 4.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  95 ITIKTIGRQWYWSYEYSDFHKVEFDSfmvsenknnffrlldvDNRTTLPINTYIRILTSASDVLHSWTIPSLGVKIDATP 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT----------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIP 65

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1241822528 175 GRLNQSMFLIKRPGIMFGQCSEICGINHSFM 205
Cdd:cd04213    66 GRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.03e-20

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


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 82.76  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528   1 MATWNNINLQDSLSPLMEQLSFFHDHSMSIIMMITSIVSYMMSQIFM------NKMSFRYMLSEHTIETIWTMIPTMVLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1241822528  75 FIAMPSLHL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-221 3.14e-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: 77.88  E-value: 3.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  83 LLYMMDDSTESN---ITIKTIGRQWYWSYEYSDfhKVEFDSFMVsenknnffrlldvdnrttLPINTYIRILTSASDVLH 159
Cdd:cd13918    18 LLYVEDPPDEADedaLEVEVEGFQFGWQFEYPN--GVTTGNTLR------------------VPADTPIALRVTSTDVFH 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1241822528 160 SWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWL 221
Cdd:cd13918    78 TFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-205 1.39e-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: 74.97  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  95 ITIKTIGRQWYWSYEYSDfHKVEFDSFMVsenknnffrlldvdnrttlPINTYIRILTSASDVLHSWTIPSLGVKIDATP 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPN-GKREINELHV-------------------PVGKPVRLILTSKDVIHSFYVPAFRIKQDVVP 61

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1241822528 175 GRLNQSMFLIKRPGIMFGQCSEICGINHSFM 205
Cdd:cd13915    62 GRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-205 2.12e-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: 2.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  95 ITIKTIGRQWYWSYEYsdfhkvefdsfmvsENKNNFFRLLDVDNRTTL--PINTYIRILTSASDVLHSWTIPSLGVKIDA 172
Cdd:cd13919     2 LVVEVTAQQWAWTFRY--------------PGGDGKLGTDDDVTSPELhlPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1241822528 173 TPGRLNQSMFLIKRPGIMFGQCSEICGINHSFM 205
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-221 2.52e-16

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 71.67  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  95 ITIKTIGRQWYWSYEYSDfhkvefdsfmvsENKNNFfrlldvdNRTTLPINTYIRILTSASDVLHSWTIPSLGVKIDATP 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPE------------ANVTTS-------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFP 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1241822528 175 GRLNQSMFLIKRPGIMFGQCSEICGINHSFMPIAIEAINLKLFIKWL 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 ...
 138-205 2.19e-04

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: 39.09  E-value: 2.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1241822528 138 NRTTLPINTYIRILTSASDVLHSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFM 205
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-205 1.37e-03

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 36.98  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528  95 ITIKTIGRQWYWSYeysdfhkvefdsfmvsenknnffrlldvdNRTTLPINTYIRILTSASDVLHSWTIPS----LGVKI 170
Cdd:cd13916     1 QVVAVTGHQWYWEL-----------------------------SRTEIPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQT 51

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1241822528 171 DATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFM 205
Cdd:cd13916    52 QAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 138-205 3.92e-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: 35.60  E-value: 3.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1241822528 138 NRTTLPINTYIRILTSASDVLHSWTIPSLGVKIDATPGRLNQSMFLIKRPGIMFGQCSEICGINHSFM 205
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 103-210 7.77e-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: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822528 103 QWYWSYEYSDFHKVEFDSFMVSENKnnffrlldvdnrttlpinTYIRILTSASDVLHSWTIPSLGVKIDA---------- 172
Cdd:cd00920     7 DWGWSFTYNGVLLFGPPVLVVPVGD------------------TVRVQFVNKLGENHSVTIAGFGVPVVAmagganpglv 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1241822528 173 -----TPGRLNQSMFLIKRPGIMFGQCSEICGiNHSFMPIAIE 210
Cdd:cd00920    69 ntlviGPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
 
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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