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Conserved domains on  [gi|540361620|gb|AGV08693|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Lirometopum coronatum]

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
 1-213 5.84e-150

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 415.38  E-value: 5.84e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00154 160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIE 212
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-213 5.84e-150

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 415.38  E-value: 5.84e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00154 160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIE 212
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-213 8.25e-86

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: 249.41  E-value: 8.25e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  93 PMITIKTVGHQWYWSYEYTDFNhPYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADVLHSWTVPALGVK 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFN-DLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 540361620 173 VDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:cd13912   80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVE 120
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 1.77e-75

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 223.06  E-value: 1.77e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   95 ITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADVLHSWTVPALGVKVD 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 540361620  175 ATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-213 2.77e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 157.68  E-value: 2.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   6 DLNLQNSASPLMEQLTFFHDHALMILLIITVLVayiMASLFFNQFTHR---------FLLEGQTIEVIWTILPAVTLIFI 76
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  77 ALPSLRLLYLLDEAMEPMITIKTVGHQWYWSYEYtdfnhpyefdsymipynemPNNGFrllDVDNRTILPMNTQIRVLVT 156
Cdd:COG1622   95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------------PDQGI---ATVNELVLPVGRPVRFLLT 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 540361620 157 AADVLHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:COG1622  153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-213 9.95e-37

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 127.11  E-value: 9.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   13 ASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFN-----------QFTHRFLLEgqtieVIWTILPAVTLIFIALPSL 81
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKfrrkgdeekpsQIHGNRRLE-----YVWTVIPLIIVVGLFAATA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   82 RLLYLLDEAMEP-MITIKTVGHQWYWSYEYtdfnhpyefdsymipynemPNNGFRlldVDNRTILPMNTQIRVLVTAADV 160
Cdd:TIGR02866  77 KGLLYLERPIPKdALKVKVTGYQWWWDFEY-------------------PESGFT---TVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 540361620  161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-213 5.84e-150

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 415.38  E-value: 5.84e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00154 160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIE 212
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-213 1.90e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 330.75  E-value: 1.90e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00140 160 IHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-213 5.76e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 327.06  E-value: 5.76e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00139 160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-213 8.94e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 326.49  E-value: 8.94e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKD-LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-213 1.60e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 323.58  E-value: 1.60e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDfNHPYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTD-YNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00038 160 LHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIE 212
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-213 7.66e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 318.85  E-value: 7.66e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00168 160 LHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-213 3.45e-108

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 309.86  E-value: 3.45e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00008 160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLE 212
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-213 6.49e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 296.63  E-value: 6.49e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYED-LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00129 160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-213 6.82e-102

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 294.35  E-value: 6.82e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   7 LNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPSLRLLYL 86
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  87 LDEAMEPMITIKTVGHQWYWSYEYTDFNHP-YEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADVLHSWT 165
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEGEtLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 540361620 166 VPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00023 176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIE 223
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-213 1.32e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 288.32  E-value: 1.32e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFnHPYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00185 160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVE 212
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-213 1.84e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 287.77  E-value: 1.84e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYED-LSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00098 160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLE 212
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-213 2.61e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 282.44  E-value: 2.61e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   7 LNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPSLRLLYL 86
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  87 LDEAMEPMITIKTVGHQWYWSYEYTDF-NHPYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADVLHSWT 165
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDYgTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 540361620 166 VPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00051 169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIE 216
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-213 3.18e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 279.74  E-value: 3.18e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  81 LRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADV 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361620 161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00076 160 LHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVE 212
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-213 8.25e-86

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: 249.41  E-value: 8.25e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  93 PMITIKTVGHQWYWSYEYTDFNhPYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADVLHSWTVPALGVK 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFN-DLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 540361620 173 VDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:cd13912   80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVE 120
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 1.77e-75

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 223.06  E-value: 1.77e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   95 ITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADVLHSWTVPALGVKVD 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 540361620  175 ATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-213 7.80e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 221.44  E-value: 7.80e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   7 LNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFL---LEGQTIEVIWTILPAVTLIFIALPSLRL 83
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  84 LYLLDE-AMEPMITIKTVGHQWYWSYEYTDFNHP-YEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADVL 161
Cdd:MTH00027 115 LYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKnIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 540361620 162 HSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00027 195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVE 246
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-213 1.33e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 184.06  E-value: 1.33e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   6 DLNLQNSA-SPLMEQLTFFHDHALMILLIITVLVAYIMASLFFNQFTHRFLLEGQTIEVIWTILPAVTLIFIALPSLRLL 84
Cdd:MTH00080   7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  85 YLLdEAM--EPMITIKTVGHQWYWSYEYTDFNHpYEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADVLH 162
Cdd:MTH00080  87 YYY-GLMnlDSNLTVKVTGHQWYWSYEFSDIPG-LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIH 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 540361620 163 SWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00080 165 SWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVE 215
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-213 2.77e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 157.68  E-value: 2.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   6 DLNLQNSASPLMEQLTFFHDHALMILLIITVLVayiMASLFFNQFTHR---------FLLEGQTIEVIWTILPAVTLIFI 76
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  77 ALPSLRLLYLLDEAMEPMITIKTVGHQWYWSYEYtdfnhpyefdsymipynemPNNGFrllDVDNRTILPMNTQIRVLVT 156
Cdd:COG1622   95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------------PDQGI---ATVNELVLPVGRPVRFLLT 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 540361620 157 AADVLHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:COG1622  153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-213 1.55e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 144.33  E-value: 1.55e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  57 EGQTIEVIWTILPAVtLIFIALPSLRLLYLLDEAMEPMITIKTVGHQWYWSYEYTDFNhpyEFDSYMIPYNEMPNNGFRL 136
Cdd:MTH00047  45 ENQVLELLWTVVPTL-LVLVLCFLNLNFITSDLDCFSSETIKVIGHQWYWSYEYSFGG---SYDSFMTDDIFGVDKPLRL 120

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 540361620 137 LdvdnrtilpMNTQIRVLVTAADVLHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00047 121 V---------YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-213 3.59e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 134.95  E-value: 3.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620 117 YEFDSYMIPYNEMPNNGFRLLDVDNRTILPMNTQIRVLVTAADVLHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQ 196
Cdd:PTZ00047  49 YSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128

                         90
                 ....*....|....*..
gi 540361620 197 CSEICGANHSFMPIVIE 213
Cdd:PTZ00047 129 CSEMCGTLHGFMPIVVE 145
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-213 9.95e-37

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 127.11  E-value: 9.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   13 ASPLMEQLTFFHDHALMILLIITVLVAYIMASLFFN-----------QFTHRFLLEgqtieVIWTILPAVTLIFIALPSL 81
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKfrrkgdeekpsQIHGNRRLE-----YVWTVIPLIIVVGLFAATA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620   82 RLLYLLDEAMEP-MITIKTVGHQWYWSYEYtdfnhpyefdsymipynemPNNGFRlldVDNRTILPMNTQIRVLVTAADV 160
Cdd:TIGR02866  77 KGLLYLERPIPKdALKVKVTGYQWWWDFEY-------------------PESGFT---TVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 540361620  161 LHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-213 7.22e-27

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: 98.52  E-value: 7.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  95 ITIKTVGHQWYWSYEYTDFNHPyefdsymipynempnngfrlldvdNRTILPMNTQIRVLVTAADVLHSWTVPALGVKVD 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNVRTP------------------------NEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 540361620 175 ATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFMPIVIE 213
Cdd:cd13842   57 AVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 2.66e-24

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: 91.62  E-value: 2.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620    1 MATWSDLNLQNSASPLMEQLTFFHDHALMILLIITVLVAYIMASLFF------NQFTHRFLLEGQTIEVIWTILPAVTLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 540361620   75 FIA 77
Cdd:pfam02790  81 LIA 83
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-208 4.15e-24

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: 91.53  E-value: 4.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  95 ITIKTVGHQWYWSYEYtdfnhpyefdsymipynemPNNGFRLLDVDNRTILPMNTQIRVLVTAADVLHSWTVPALGVKVD 174
Cdd:cd04213    2 LTIEVTGHQWWWEFRY-------------------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 540361620 175 ATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFM 208
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-208 4.45e-19

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: 78.44  E-value: 4.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  95 ITIKTVGHQWYWSyeytdFNHPyefdsymipynempnNGFRlldVDNRTILPMNTQIRVLVTAADVLHSWTVPALGVKVD 174
Cdd:cd13915    2 LEIQVTGRQWMWE-----FTYP---------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100       110
                 ....*....|....*....|....*....|....
gi 540361620 175 ATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFM 208
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-208 7.64e-19

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: 78.07  E-value: 7.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  95 ITIKTVGHQWYWSYEYtdfnhpyefdsymipynemPNNGFRLLDVDNRTI----LPMNTQIRVLVTAADVLHSWTVPALG 170
Cdd:cd13919    2 LVVEVTAQQWAWTFRY-------------------PGGDGKLGTDDDVTSpelhLPVGRPVLFNLRSKDVIHSFWVPEFR 62

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 540361620 171 VKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFM 208
Cdd:cd13919   63 VKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-208 2.26e-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: 2.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  88 DEAMEPMITIKTVGHQWYWSYEYtdfnhpyefdsymipynemPNNGFRLldvdNRTILPMNTQIRVLVTAADVLHSWTVP 167
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEY-------------------PNGVTTG----NTLRVPADTPIALRVTSTDVFHTFGIP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 540361620 168 ALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFM 208
Cdd:cd13918   83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-208 1.55e-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: 74.75  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  95 ITIKTVGHQWYWSYEYTDFNhpyefdsymipynempnngfrlLDVDNRTILPMNTQIRVLVTAADVLHSWTVPALGVKVD 174
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEAN----------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                         90       100       110
                 ....*....|....*....|....*....|....
gi 540361620 175 ATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFM 208
Cdd:cd13914   59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 145-208 1.24e-06

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: 45.25  E-value: 1.24e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 540361620 145 LPMNTQIRVLVTAADVLHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFM 208
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 141-208 1.18e-04

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: 39.84  E-value: 1.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 540361620 141 NRTILPMNTQIRVLVTAADVLHSWTVPALGVKVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFM 208
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-208 4.23e-04

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 38.13  E-value: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620  95 ITIKTVGHQWYWsyeytdfnhpyefdsymipynEMpnngfrlldvdNRTILPMNTQIRVLVTAADVLHSWTV--PALGV- 171
Cdd:cd13916    1 QVVAVTGHQWYW---------------------EL-----------SRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLl 48

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 540361620 172 -KVDATPGRLNQTNFFTSRPGIFYGQCSEICGANHSFM 208
Cdd:cd13916   49 aQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 121-213 1.32e-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: 37.21  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361620 121 SYMIPYNEMPNNGFrlldVDNRTILPMNTQIRV-LVTAADVLHSWTVPALGVKVDA---------------TPGRLNQTN 184
Cdd:cd00920    7 DWGWSFTYNGVLLF----GPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVT 82

                         90       100
                 ....*....|....*....|....*....
gi 540361620 185 FFTSRPGIFYGQCSEICGaNHSFMPIVIE 213
Cdd:cd00920   83 FTTDQAGVYWFYCTIPGH-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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