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Conserved domains on  [gi|69880139|gb|AAZ04254|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Sinopodisma qinlingensis]

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
 1-195 3.92e-127

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 356.83  E-value: 3.92e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQ 195
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-195 3.92e-127

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 356.83  E-value: 3.92e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQ 195
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-195 5.16e-64

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: 193.56  E-value: 5.16e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139  95 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWTVPALGIKIDA 174
Cdd:cd13912   3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                        90       100
                ....*....|....*....|.
gi 69880139 175 TPGRLNQGTFTMNRPGLFFGQ 195
Cdd:cd13912  83 VPGRLNQTSFFIERPGVYYGQ 103
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-195 1.18e-58

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 179.53  E-value: 1.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    95 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWTVPALGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|.
gi 69880139   175 TPGRLNQGTFTMNRPGLFFGQ 195
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQ 101
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-195 1.70e-34

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 121.47  E-value: 1.70e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   6 NLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVgytLSYMLIISF---------TSRNMLHGHLIETIWTALPAITLIFI 76
Cdd:COG1622  18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIryrrrkgdaDPAQFHHNTKLEIVWTVIPIIIVIVL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139  77 ALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDfvdvefdtymtpENDLKINEFRLldvdnrtilPMNTEVRVLTSA 156
Cdd:COG1622  95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD------------QGIATVNELVL---------PVGRPVRFLLTS 153

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 69880139 157 SDVLHSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:COG1622 154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-195 2.07e-26

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: 99.76  E-value: 2.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    13 ASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLiisFTSRN--------MLHGH-LIETIWTALPAI--TLIFIALPSL 81
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVV---WKFRRkgdeekpsQIHGNrRLEYVWTVIPLIivVGLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    82 RLLYLLDDSVDAMiTIKTIGRQWYWSYEYSDFvdvefdtymtpendlkinefrLLDVDNRTILPMNTEVRVLTSASDVLH 161
Cdd:TIGR02866  79 LLYLERPIPKDAL-KVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIH 136

                         170       180       190
                  ....*....|....*....|....*....|....
gi 69880139   162 SWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:TIGR02866 137 SFWVPELGGKIDAIPGQTNALWFNADEPGVYYGF 170
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-195 3.92e-127

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 356.83  E-value: 3.92e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQ 195
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-195 1.05e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 269.66  E-value: 1.05e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQ 195
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-195 8.82e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 264.88  E-value: 8.82e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQ 195
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-195 3.17e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 261.00  E-value: 3.17e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQ 195
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-195 8.06e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 260.02  E-value: 8.06e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQ 195
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-195 1.22e-84

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 249.39  E-value: 1.22e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQ 195
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-195 8.76e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 242.19  E-value: 8.76e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQ 195
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-195 2.08e-78

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 233.46  E-value: 2.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQ 195
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-195 7.53e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 227.46  E-value: 7.53e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQ 195
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-195 9.80e-75

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 224.63  E-value: 9.80e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    7 LSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 86
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   87 LDDSVDAMITIKTIGRQWYWSYEYSDFVD--VEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWT 164
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                        170       180       190
                 ....*....|....*....|....*....|.
gi 69880139  165 VPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00023 176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQ 206
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-195 1.29e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 223.89  E-value: 1.29e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQ 195
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-195 1.62e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 223.82  E-value: 1.62e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 69880139  161 HSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQ 195
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-195 1.17e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 214.26  E-value: 1.17e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    7 LSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLIISFTSRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 86
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   87 LDDSVDAMITIKTIGRQWYWSYEYSDF--VDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWT 164
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                        170       180       190
                 ....*....|....*....|....*....|.
gi 69880139  165 VPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00051 169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQ 199
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-195 5.16e-64

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: 193.56  E-value: 5.16e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139  95 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWTVPALGIKIDA 174
Cdd:cd13912   3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                        90       100
                ....*....|....*....|.
gi 69880139 175 TPGRLNQGTFTMNRPGLFFGQ 195
Cdd:cd13912  83 VPGRLNQTSFFIERPGVYYGQ 103
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-195 1.18e-58

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 179.53  E-value: 1.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    95 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWTVPALGIKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|.
gi 69880139   175 TPGRLNQGTFTMNRPGLFFGQ 195
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQ 101
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-195 1.04e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 177.14  E-value: 1.04e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    7 LSLQDSASPLMEQLSFFHDHtmvVLLMITIIVGYTLSYMLIISFTSR------NMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQ---ILFILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   81 LRLLYLLDDSV-DAMITIKTIGRQWYWSYEYSDF--VDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSAS 157
Cdd:MTH00027 112 LRLLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 69880139  158 DVLHSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQ 229
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 20-195 1.79e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 147.46  E-value: 1.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   20 LSFFHDHTMVVLLMITIIVGYTLSYMLIISFT---SRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLD-DSVDAMI 95
Cdd:MTH00080  19 MDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNfyfKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   96 TIKTIGRQWYWSYEYSDFVDVEFDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWTVPALGIKIDAT 175
Cdd:MTH00080  99 TVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                        170       180
                 ....*....|....*....|
gi 69880139  176 PGRLNQGTFTMNRPGLFFGQ 195
Cdd:MTH00080 179 SGILSTLCYSFPMPGVFYGQ 198
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-195 1.70e-34

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 121.47  E-value: 1.70e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   6 NLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVgytLSYMLIISF---------TSRNMLHGHLIETIWTALPAITLIFI 76
Cdd:COG1622  18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIryrrrkgdaDPAQFHHNTKLEIVWTVIPIIIVIVL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139  77 ALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDfvdvefdtymtpENDLKINEFRLldvdnrtilPMNTEVRVLTSA 156
Cdd:COG1622  95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD------------QGIATVNELVL---------PVGRPVRFLLTS 153

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 69880139 157 SDVLHSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:COG1622 154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-195 2.07e-26

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: 99.76  E-value: 2.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    13 ASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLiisFTSRN--------MLHGH-LIETIWTALPAI--TLIFIALPSL 81
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVV---WKFRRkgdeekpsQIHGNrRLEYVWTVIPLIivVGLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139    82 RLLYLLDDSVDAMiTIKTIGRQWYWSYEYSDFvdvefdtymtpendlkinefrLLDVDNRTILPMNTEVRVLTSASDVLH 161
Cdd:TIGR02866  79 LLYLERPIPKDAL-KVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIH 136

                         170       180       190
                  ....*....|....*....|....*....|....
gi 69880139   162 SWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:TIGR02866 137 SFWVPELGGKIDAIPGQTNALWFNADEPGVYYGF 170
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 30-194 5.81e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 98.49  E-value: 5.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139   30 VLLMITIIVGYTL-SYMLIISFTSRNmlhgHLIETIWTALPaiTLIFIALPSLRLLYLLDDSVDAMI-TIKTIGRQWYWS 107
Cdd:MTH00047  21 IPCWVYIMLCWQVvSGNGSVNFGSEN----QVLELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWYWS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139  108 YEYSDfvDVEFDTYMTPENDLkinefrlldVDNRTILPMNTEVRVLTSASDVLHSWTVPALGIKIDATPGRLNQGTFTMN 187
Cdd:MTH00047  95 YEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPD 163


                 ....*..
gi 69880139  188 RPGLFFG 194
Cdd:MTH00047 164 RHGVFVG 170
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 7.32e-23

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: 87.39  E-value: 7.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139     1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYTLSYMLI------ISFTSRNMLHGHLIETIWTALPAITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 69880139    75 FIA 77
Cdd:pfam02790  81 LIA 83
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-195 1.55e-22

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 88.72  E-value: 1.55e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69880139  118 FDTYMTPENDLKINEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWTVPALGIKIDATPGRLNQGTFTMNRPGLFFGQ 195
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-195 3.11e-16

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: 70.73  E-value: 3.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139  95 ITIKTIGRQWYWSYEYSDFVDVEFDTymtpendlkINEFRLldvdnrtilPMNTEVRVLTSASDVLHSWTVPALGIKIDA 174
Cdd:cd04213   2 LTIEVTGHQWWWEFRYPDEPGRGIVT---------ANELHI---------PVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                        90       100
                ....*....|....*....|.
gi 69880139 175 TPGRLNQGTFTMNRPGLFFGQ 195
Cdd:cd04213  64 IPGRTNRLWLQADEPGVYRGQ 84
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-195 7.55e-16

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: 69.63  E-value: 7.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139  95 ITIKTIGRQWYWSYEYSDfvdvefdtymtpendlkinefrlLDVDNRTILPMNTEVRVLTSASDVLHSWTVPALGIKIDA 174
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100
                ....*....|....*....|.
gi 69880139 175 TPGRLNQGTFTMNRPGLFFGQ 195
Cdd:cd13842  58 VPGYTSELWFVADKPGTYTII 78
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-192 6.69e-15

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 66.88  E-value: 6.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139  95 ITIKTIGRQWYWSYEYsdfvdvefdtymtPENDLKINEfrlLDVdnrtilPMNTEVRVLTSASDVLHSWTVPALGIKIDA 174
Cdd:cd13915   2 LEIQVTGRQWMWEFTY-------------PNGKREINE---LHV------PVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                        90
                ....*....|....*...
gi 69880139 175 TPGRLNQGTFTMNRPGLF 192
Cdd:cd13915  60 VPGRYTYLWFEATKPGEY 77
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-195 1.80e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 66.12  E-value: 1.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139  95 ITIKTIGRQWYWSYEYSDFvdvefDTYMTPENDLKINEFRLldvdnrtilPMNTEVRVLTSASDVLHSWTVPALGIKIDA 174
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                        90       100
                ....*....|....*....|.
gi 69880139 175 TPGRLNQGTFTMNRPGLFFGQ 195
Cdd:cd13919  68 VPGRTTRLWFTPTREGEYEVR 88
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-180 5.30e-10

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: 54.34  E-value: 5.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139  95 ITIKTIGRQWYWSYEYSDfvdvefdtymtpENdlkinefrlLDVDNRTILPMNTEVRVLTSASDVLHSWTVPALGIKIDA 174
Cdd:cd13914   1 VEIEVEAYQWGWEFSYPE------------AN---------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                ....*.
gi 69880139 175 TPGRLN 180
Cdd:cd13914  60 FPGQYN 65
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-190 6.15e-07

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: 46.68  E-value: 6.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69880139  88 DDSVDAMITIKTIGRQWYWSYEYSDFVdvefdtymTPENDLKInefrlldvdnrtilPMNTEVRVLTSASDVLHSWTVPA 167
Cdd:cd13918  26 DEADEDALEVEVEGFQFGWQFEYPNGV--------TTGNTLRV--------------PADTPIALRVTSTDVFHTFGIPE 83

                        90       100
                ....*....|....*....|...
gi 69880139 168 LGIKIDATPGRLNQGTFTMNRPG 190
Cdd:cd13918  84 LRVKADAIPGEYTSTWFEADEPG 106
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 144-192 1.75e-03

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 36.39  E-value: 1.75e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 69880139 144 LPMNTEVRVLTSASDVLHSWTVPALGIKIDATPGRLNQGTFTMNRPGLF 192
Cdd:cd13913  29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEY 77
 
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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