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Conserved domains on  [gi|1063639065|gb|AOO35124|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Duronia chloronota]

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
 1-173 5.78e-107

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 304.83  E-value: 5.78e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00154   23 FHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00154  103 QWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQL 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00154  183 NFLINRPGLFFGQ 195
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-173 5.78e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 304.83  E-value: 5.78e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00154   23 FHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00154  103 QWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQL 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00154  183 NFLINRPGLFFGQ 195
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 73-173 6.10e-63

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: 190.09  E-value: 6.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  73 ITIKTIGRQWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDA 152
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|.
gi 1063639065 153 TPGRLNQGTFTINRPGLFFGQ 173
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQ 103
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
73-173 1.73e-59

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 181.07  E-value: 1.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  73 ITIKTIGRQWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDA 152
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|.
gi 1063639065 153 TPGRLNQGTFTINRPGLFFGQ 173
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQ 101
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-173 2.34e-31

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 112.61  E-value: 2.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVgysLSYML--MINYSNRN-------MLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADA 71
Cdd:COG1622    35 LFWVSLIIMLVIFVLV---FGLLLyfAIRYRRRKgdadpaqFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPED 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  72 MITIKTIGRQWYWSYEYsdfinvefdtymtPEKDLEyegfrlldVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKID 151
Cdd:COG1622   112 PLTVEVTGYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                         170       180
                  ....*....|....*....|..
gi 1063639065 152 ATPGRLNQGTFTINRPGLFFGQ 173
Cdd:COG1622   171 AIPGRVTELWFTADKPGTYRGQ 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 6-173 9.70e-25

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: 94.75  E-value: 9.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   6 MIVLLLITVIVGYSLSYMlMINYSNRN------MLHGH-LIETIWTTMPA-ITLIFIALPSLRLLYLLDDSADAMITIKT 77
Cdd:TIGR02866  17 LAVSTLISLLVAALLAYV-VWKFRRKGdeekpsQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  78 IGRQWYWSYEYSDFinvefdtymtpekdleyeGFRlldVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRL 157
Cdd:TIGR02866  96 TGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQT 154

                         170
                  ....*....|....*.
gi 1063639065 158 NQGTFTINRPGLFFGQ 173
Cdd:TIGR02866 155 NALWFNADEPGVYYGF 170
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-173 5.78e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 304.83  E-value: 5.78e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00154   23 FHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00154  103 QWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQL 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00154  183 NFLINRPGLFFGQ 195
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-173 2.11e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 232.50  E-value: 2.11e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00117   23 FHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00117  103 QWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQT 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00117  183 SFITTRPGVFYGQ 195
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-173 2.69e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 232.52  E-value: 2.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00140   23 FHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00140  103 QWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQL 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00140  183 SFEPKRPGVFYGQ 195
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-173 2.74e-76

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 227.43  E-value: 2.74e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00008   23 FHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00008  103 QWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQI 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00008  183 GFTITRPGVFYGQ 195
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-173 4.57e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 226.91  E-value: 4.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00139   23 FHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00139  103 QWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQV 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00139  183 GFFINRPGVFYGQ 195
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-173 3.31e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 222.27  E-value: 3.31e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00038   23 FHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00038  103 QWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQT 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00038  183 TFFISRTGLFYGQ 195
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-173 4.26e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 219.08  E-value: 4.26e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00168   23 FHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00168  103 QWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQL 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00168  183 AFLSSRPGSFYGQ 195
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-173 1.86e-68

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 207.26  E-value: 1.86e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00098   23 FHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00098  103 QWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQT 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00098  183 TLMSTRPGLYYGQ 195
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-173 5.42e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 206.17  E-value: 5.42e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00076   23 FHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00076  103 QWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQT 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00076  183 SFIASRPGVYYGQ 195
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-173 1.80e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 205.12  E-value: 1.80e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00185   23 FHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00185  103 QWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQA 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00185  183 TFIISRPGLYYGQ 195
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-173 4.21e-65

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 199.21  E-value: 4.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00023   32 FHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGH 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFI--NVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLN 158
Cdd:MTH00023  112 QWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLN 191

                         170
                  ....*....|....*
gi 1063639065 159 QGTFTINRPGLFFGQ 173
Cdd:MTH00023  192 QTGFFIKRPGVFYGQ 206
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-173 5.47e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 198.78  E-value: 5.47e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00129   23 FHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQG 160
Cdd:MTH00129  103 QWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQT 182

                         170
                  ....*....|...
gi 1063639065 161 TFTINRPGLFFGQ 173
Cdd:MTH00129  183 AFIASRPGVFYGQ 195
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-173 4.96e-64

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 196.54  E-value: 4.96e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYSNRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADAMITIKTIGR 80
Cdd:MTH00051   25 FHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDF--INVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLN 158
Cdd:MTH00051  105 QWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLN 184

                         170
                  ....*....|....*
gi 1063639065 159 QGTFTINRPGLFFGQ 173
Cdd:MTH00051  185 QTSFFIKRPGVFYGQ 199
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 73-173 6.10e-63

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: 190.09  E-value: 6.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  73 ITIKTIGRQWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDA 152
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|.
gi 1063639065 153 TPGRLNQGTFTINRPGLFFGQ 173
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQ 103
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
73-173 1.73e-59

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 181.07  E-value: 1.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  73 ITIKTIGRQWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDA 152
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|.
gi 1063639065 153 TPGRLNQGTFTINRPGLFFGQ 173
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQ 101
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 8-173 6.70e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 159.04  E-value: 6.70e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   8 VLLLITVIVGYSLSYMLMINYSNR------NMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSA-DAMITIKTIGR 80
Cdd:MTH00027   55 ILFILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSANITIKVTGH 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  81 QWYWSYEYSDF--INVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLN 158
Cdd:MTH00027  135 QWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRIN 214

                         170
                  ....*....|....*
gi 1063639065 159 QGTFTINRPGLFFGQ 173
Cdd:MTH00027  215 ETGFLIKRPGIFYGQ 229
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-173 2.68e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 143.61  E-value: 2.68e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMINYS---NRNMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLD-DSADAMITIK 76
Cdd:MTH00080   22 FHNFNCSLLFGEFVLAFVVFLFLYLISNNfyfKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  77 TIGRQWYWSYEYSDFINVEFDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGR 156
Cdd:MTH00080  102 VTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGI 181

                         170
                  ....*....|....*..
gi 1063639065 157 LNQGTFTINRPGLFFGQ 173
Cdd:MTH00080  182 LSTLCYSFPMPGVFYGQ 198
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-173 2.34e-31

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 112.61  E-value: 2.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   1 FHDHTMIVLLLITVIVgysLSYML--MINYSNRN-------MLHGHLIETIWTTMPAITLIFIALPSLRLLYLLDDSADA 71
Cdd:COG1622    35 LFWVSLIIMLVIFVLV---FGLLLyfAIRYRRRKgdadpaqFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPED 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  72 MITIKTIGRQWYWSYEYsdfinvefdtymtPEKDLEyegfrlldVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKID 151
Cdd:COG1622   112 PLTVEVTGYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                         170       180
                  ....*....|....*....|..
gi 1063639065 152 ATPGRLNQGTFTINRPGLFFGQ 173
Cdd:COG1622   171 AIPGRVTELWFTADKPGTYRGQ 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 6-173 9.70e-25

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: 94.75  E-value: 9.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   6 MIVLLLITVIVGYSLSYMlMINYSNRN------MLHGH-LIETIWTTMPA-ITLIFIALPSLRLLYLLDDSADAMITIKT 77
Cdd:TIGR02866  17 LAVSTLISLLVAALLAYV-VWKFRRKGdeekpsQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  78 IGRQWYWSYEYSDFinvefdtymtpekdleyeGFRlldVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRL 157
Cdd:TIGR02866  96 TGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQT 154

                         170
                  ....*....|....*.
gi 1063639065 158 NQGTFTINRPGLFFGQ 173
Cdd:TIGR02866 155 NALWFNADEPGVYYGF 170
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 6-172 1.29e-24

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 94.25  E-value: 1.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   6 MIVLLLITVIVGYSLSymlmINYSNRNmlhgHLIETIWTTMPaiTLIFIALPSLRLLYLLDDSADAMI-TIKTIGRQWYW 84
Cdd:MTH00047   24 WVYIMLCWQVVSGNGS----VNFGSEN----QVLELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWYW 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  85 SYEYSDfiNVEFDTYMTPEKDLeyegfrlldVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTI 164
Cdd:MTH00047   94 SYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCP 162


                  ....*...
gi 1063639065 165 NRPGLFFG 172
Cdd:MTH00047  163 DRHGVFVG 170
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 96-173 3.45e-22

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 87.18  E-value: 3.45e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063639065  96 FDTYMTPEKDLEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTINRPGLFFGQ 173
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 73-173 7.44e-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: 68.86  E-value: 7.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  73 ITIKTIGRQWYWSYEYSDfinvefdtymtpekdleyegfrlLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDA 152
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100
                  ....*....|....*....|.
gi 1063639065 153 TPGRLNQGTFTINRPGLFFGQ 173
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTII 78
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 73-173 2.51e-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: 65.35  E-value: 2.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  73 ITIKTIGRQWYWSYEYsdfinvefdtymtPEKDlEYEGFRLLDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDA 152
Cdd:cd13919     2 LVVEVTAQQWAWTFRY-------------PGGD-GKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100
                  ....*....|....*....|.
gi 1063639065 153 TPGRLNQGTFTINRPGLFFGQ 173
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVR 88
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 73-173 2.85e-14

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: 64.95  E-value: 2.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  73 ITIKTIGRQWYWSYEYsdfinvefdtymtpeKDLEYEGFRLLdvdNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDA 152
Cdd:cd04213     2 LTIEVTGHQWWWEFRY---------------PDEPGRGIVTA---NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100
                  ....*....|....*....|.
gi 1063639065 153 TPGRLNQGTFTINRPGLFFGQ 173
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQ 84
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 73-170 8.16e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 63.80  E-value: 8.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  73 ITIKTIGRQWYWSYEYSDfinvefdtymtpekdleyeGFRlldVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDA 152
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90
                  ....*....|....*...
gi 1063639065 153 TPGRLNQGTFTINRPGLF 170
Cdd:cd13915    60 VPGRYTYLWFEATKPGEY 77
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-55 1.87e-11

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: 57.34  E-value: 1.87e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063639065   1 FHDHTMIVLLLITVIVGYSLSYMLMiNY-------SNRNMLHGHLIETIWTTMPAITLIFIA 55
Cdd:pfam02790  23 LHDYIMFILTLILILVLYILVTCLI-RFnrrknpiTARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 73-158 1.28e-09

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: 52.80  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  73 ITIKTIGRQWYWSYEYSDfINVefdtymtpekdleyegfrllDVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKIDA 152
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPE-ANV--------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                  ....*.
gi 1063639065 153 TPGRLN 158
Cdd:cd13914    60 FPGQYN 65
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 66-168 7.23e-06

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: 43.60  E-value: 7.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  66 DDSADAMiTIKTIGRQWYWSYEYSDfiNVEFDTYMtpekdleyegfrlldvdnrtILPMNTEVQMLTSASDVLHSWAVPA 145
Cdd:cd13918    27 EADEDAL-EVEVEGFQFGWQFEYPN--GVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPE 83

                          90       100
                  ....*....|....*....|...
gi 1063639065 146 LGIKIDATPGRLNQGTFTINRPG 168
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPG 106
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 118-173 1.14e-03

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 36.76  E-value: 1.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063639065 118 NRTILPMNTEVQM-LTSASdVLHSWAVPALGIKIDATPGRLNQGTFTINRPGLFFGQ 173
Cdd:cd04212    25 NELVIPVGRPVNFrLTSDS-VMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 5-172 8.14e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 35.93  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065   5 TMIVLLLITVIVGYSLSYMLMINY--SNR------NMLHGHLIETIWTTMPAITLIFIALPSLRLLYLLD-----DSADA 71
Cdd:PRK10525   46 TAFGLMLIVVIPAILMAVGFAWKYraSNKdakyspNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEpskplAHDEK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639065  72 MITIKTIGRQWYWSYEYsdfinvefdtymtPEKDLEyegfrlldVDNRTILPMNTEVQMLTSASDVLHSWAVPALGIKID 151
Cdd:PRK10525  126 PITIEVVSMDWKWFFIY-------------PEQGIA--------TVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIY 184

                         170       180
                  ....*....|....*....|.
gi 1063639065 152 ATPGRLNQGTFTINRPGLFFG 172
Cdd:PRK10525  185 AMAGMQTRLHLIANEPGTYDG 205
 
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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