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Conserved domains on  [gi|938339314|ref|YP_009171515|]
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cytochrome c oxidase subunit 2 (mitochondrion) [Pseudothericles compressifrons]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 3.98e-155

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 429.25  E-value: 3.98e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKMI 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 3.98e-155

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 429.25  E-value: 3.98e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKMI 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-222 2.88e-83

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: 243.63  E-value: 2.88e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  95 LTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVLHSWAVPALGVKVDA 174
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 938339314 175 TPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKW 222
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 2.65e-75

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 223.06  E-value: 2.65e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   95 LTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVLHSWAVPALGVKVDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 938339314  175 TPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIEST 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 2.67e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 173.48  E-value: 2.67e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   6 NLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTL----KSNLSYR--YMLHGHTIESIWTVLPAMTLVFIAFP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrRRKGDADpaQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  80 SIRMLYLIDDTSDALLTIKTIGRQWYWSYEYsdfmdvefdvymtPENKMseesfrllDVDNRTILPMNSSIRVLTSASDV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGI--------ATVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938339314 160 LHSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKM 226
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-224 3.26e-41

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: 139.05  E-value: 3.26e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   13 ASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLksnLSYRY--------MLHGHT-IESIWTVLPAMTLV-FIAFPSIR 82
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVV---WKFRRkgdeekpsQIHGNRrLEYVWTVIPLIIVVgLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   83 MLYLIDDTSDALLTIKTIGRQWYWSYEYSDFmdvefdvymtpenkmseesfrLLDVDNRTILPMNSSIRVLTSASDVLHS 162
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 938339314  163 WAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMS 224
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 3.98e-155

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 429.25  E-value: 3.98e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKMI 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 2.25e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 343.82  E-value: 2.25e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKM 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 2.46e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 333.83  E-value: 2.46e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKM 226
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-228 1.63e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 328.97  E-value: 1.63e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKMIS 228
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLE 228
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 7.25e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 327.44  E-value: 7.25e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKM 226
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 1.14e-112

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 321.81  E-value: 1.14e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSK 225
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 1.52e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 316.54  E-value: 1.52e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMS 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 6.49e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 302.40  E-value: 6.49e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKMI 227
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 4.89e-102

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 295.09  E-value: 4.89e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKMI 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-228 2.11e-101

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 293.97  E-value: 2.11e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   7 LSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPSIRMLYL 86
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  87 IDDTSDALLTIKTIGRQWYWSYEYSDFMD--VEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVLHSWA 164
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 938339314 165 VPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKMIS 228
Cdd:MTH00023 176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 2.86e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 290.63  E-value: 2.86e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKMI 227
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 1.93e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 288.22  E-value: 1.93e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  81 IRMLYLIDDTSDALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKM 226
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-224 1.22e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 281.67  E-value: 1.22e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   7 LSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPSIRMLYL 86
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  87 IDDTSDALLTIKTIGRQWYWSYEYSDF--MDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVLHSWA 164
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314 165 VPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMS 224
Cdd:MTH00051 169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVA 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-222 2.88e-83

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: 243.63  E-value: 2.88e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  95 LTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVLHSWAVPALGVKVDA 174
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 938339314 175 TPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKW 222
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-225 2.51e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 231.07  E-value: 2.51e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   7 LSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYM---LHGHTIESIWTVLPAMTLVFIAFPSIRM 83
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  84 LYLIDDTS-DALLTIKTIGRQWYWSYEYSDF--MDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVL 160
Cdd:MTH00027 115 LYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 938339314 161 HSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSK 225
Cdd:MTH00027 195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 2.65e-75

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 223.06  E-value: 2.65e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   95 LTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVLHSWAVPALGVKVDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 938339314  175 TPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIEST 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-223 5.85e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 208.71  E-value: 5.85e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   6 NLSFQDSA-SPLMEQLSFFHDHALIILIVITLVVGYFLMYTLKSNLSYRYMLHGHTIESIWTVLPAMTLVFIAFPSIRML 84
Cdd:MTH00080   7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  85 YLIDDTS-DALLTIKTIGRQWYWSYEYSDFMDVEFDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRVLTSASDVLHSW 163
Cdd:MTH00080  87 YYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSW 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314 164 AVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWM 223
Cdd:MTH00080 167 ALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 2.67e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 173.48  E-value: 2.67e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   6 NLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTL----KSNLSYR--YMLHGHTIESIWTVLPAMTLVFIAFP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrRRKGDADpaQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  80 SIRMLYLIDDTSDALLTIKTIGRQWYWSYEYsdfmdvefdvymtPENKMseesfrllDVDNRTILPMNSSIRVLTSASDV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGI--------ATVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938339314 160 LHSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMSKM 226
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-224 3.26e-41

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: 139.05  E-value: 3.26e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   13 ASPLMEQLSFFHDHALIILIVITLVVGYFLMYTLksnLSYRY--------MLHGHT-IESIWTVLPAMTLV-FIAFPSIR 82
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVV---WKFRRkgdeekpsQIHGNRrLEYVWTVIPLIIVVgLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314   83 MLYLIDDTSDALLTIKTIGRQWYWSYEYSDFmdvefdvymtpenkmseesfrLLDVDNRTILPMNSSIRVLTSASDVLHS 162
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 938339314  163 WAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWMS 224
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 60-212 4.92e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 135.85  E-value: 4.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  60 TIESIWTVLPAMTLVFIAFPSIRML-YLIDDTSDAllTIKTIGRQWYWSYEYSDfmDVEFDVYMTPENKMseesfrlldV 138
Cdd:MTH00047  48 VLELLWTVVPTLLVLVLCFLNLNFItSDLDCFSSE--TIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------V 114

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 938339314 139 DNRTILPMNSSIRVLTSASDVLHSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIE 212
Cdd:MTH00047 115 DKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 134-219 5.67e-34

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 119.54  E-value: 5.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314 134 RLLDVDNRTILPMNSSIRVLTSASDVLHSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIES 213
Cdd:PTZ00047  67 RQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEA 146


                 ....*.
gi 938339314 214 TSTNMF 219
Cdd:PTZ00047 147 VSPEAY 152
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 2.75e-26

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 97.37  E-value: 2.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  95 LTIKTIGRQWYWSYEYSDfmdvefdvymtpenkmseesfrlLDVDNRTILPMNSSIRVLTSASDVLHSWAVPALGVKVDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 938339314 175 TPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIE 212
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 3.57e-25

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: 94.32  E-value: 3.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314    1 MATWSNLSFQDSASPLMEQLSFFHDHALIILIVITLVVGYFLMYTL------KSNLSYRYMLHGHTIESIWTVLPAMTLV 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 938339314   75 FIAFPSIRM 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 3.94e-23

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: 89.60  E-value: 3.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  95 LTIKTIGRQWYWSYEYSDfmdvefdvymtpenkmseESFRLLDVDNRTILPMNSSIRVLTSASDVLHSWAVPALGVKVDA 174
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPD------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90       100       110
                 ....*....|....*....|....*....|...
gi 938339314 175 TPGRLNQAIFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd04213   64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 7.22e-22

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: 86.14  E-value: 7.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  95 LTIKTIGRQWYWSYEYsdfmdvefdvymtPENKMSeesfrlldvDNRTILPMNSSIRVLTSASDVLHSWAVPALGVKVDA 174
Cdd:cd13915    2 LEIQVTGRQWMWEFTY-------------PNGKRE---------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90       100       110
                 ....*....|....*....|....*....|...
gi 938339314 175 TPGRLNQAIFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd13915   60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 1.33e-21

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: 85.77  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  95 LTIKTIGRQWYWSYEY--SDFMDVEFDVYMTPEnkmseesfrlldvdnrTILPMNSSIRVLTSASDVLHSWAVPALGVKV 172
Cdd:cd13919    2 LVVEVTAQQWAWTFRYpgGDGKLGTDDDVTSPE----------------LHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQ 65

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 938339314 173 DATPGRLNQAIFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd13919   66 DAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-223 8.34e-17

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 73.21  E-value: 8.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  96 TIKTIGRQWYWSYEYsdfmdvefdvymtPENKMSEEsfrlldvdNRTILPMNSSIRVLTSASDVLHSWAVPALGVKVDAT 175
Cdd:cd13914    2 EIEVEAYQWGWEFSY-------------PEANVTTS--------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 938339314 176 PGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWM 223
Cdd:cd13914   61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-223 1.26e-14

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: 68.25  E-value: 1.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  88 DDTSDALLTIKTIGRQWYWSYEYSdfmdvefdvymtpeNKMSEEsfrlldvdNRTILPMNSSIRVLTSASDVLHSWAVPA 167
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYP--------------NGVTTG--------NTLRVPADTPIALRVTSTDVFHTFGIPE 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 938339314 168 LGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFMPIVIESTSTNMFIKWM 223
Cdd:cd13918   84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 144-207 5.01e-07

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: 46.41  E-value: 5.01e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 938339314 144 LPMNSSIRVLTSASDVLHSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 118-212 1.04e-05

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: 43.37  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314 118 FDVYMTPENKMSEESFRLLDVDNRTILPMNSSIRV-LTSASDVLHSWAVPALGVKVDA---------------TPGRLNQ 181
Cdd:cd00920    1 ITVTASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAE 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 938339314 182 AIFTINRPGLFFGQCSEICGaNHSFMPIVIE 212
Cdd:cd00920   81 VTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 8.49e-05

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: 40.06  E-value: 8.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314  96 TIKTIGRQWYWSyeysdfmdvefdvymtpenkMSeesfrlldvdnRTILPMNSSIRVLTSASDVLHSWAV--PALGV--K 171
Cdd:cd13916    2 VVAVTGHQWYWE--------------------LS-----------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQ 50

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 938339314 172 VDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd13916   51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 156-207 5.37e-03

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 35.29  E-value: 5.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 938339314 156 ASDVLHSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQCSEICGANHSFM 207
Cdd:cd04223   36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 120-207 7.20e-03

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 37.26  E-value: 7.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339314 120 VYMT---PENKMSEesFRLLDVDNRTILPMNssirvLTSASDVLHSWAVPALGVKVDATPGRLNQAIFTINRPGLFFGQC 196
Cdd:PRK02888 543 VYMTsqaPAFGLRE--FTVKQGDEVTVIVTN-----LDKVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYC 615

                         90
                 ....*....|.
gi 938339314 197 SEICGANHSFM 207
Cdd:PRK02888 616 TWFCHALHMEM 626
 
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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