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Conserved domains on  [gi|1509167427|gb|AYQ22814|]
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cytochrome c oxidase subunit 2 (mitochondrion) [Coscineuta sp. OR249]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 9.95e-153

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 423.09  E-value: 9.95e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKMI 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 9.95e-153

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 423.09  E-value: 9.95e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKMI 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-222 9.15e-87

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: 252.49  E-value: 9.15e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  95 ITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGVKIDA 174
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1509167427 175 TPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKW 222
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.22e-76

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 226.52  E-value: 1.22e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  95 ITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGVKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1509167427 175 TPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIEST 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 2.12e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 161.15  E-value: 2.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   6 NLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYmFIIKFSNRN-------MLHGHLIETIWTALPAITLIFIAL 78
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLY-FAIRYRRRKgdadpaqFHHNTKLEIVWTVIPIIIVIVLAV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  79 PSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYsdfvnvefdtymkPESDLEidefrlldVDNRTILPMNTEVRVLTSASD 158
Cdd:COG1622    97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRFLLTSAD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1509167427 159 VLHSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKM 226
Cdd:COG1622   156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-224 5.14e-39

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: 133.66  E-value: 5.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  13 ASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYmFIIKFSNRN------MLHGH-LIETIWTALPAI--TLIFIALPSLRL 83
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAY-VVWKFRRKGdeekpsQIHGNrRLEYVWTVIPLIivVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  84 LYLLDDSVDAMiTIKTIGRQWYWSYEYSDFvnvefdtymkpesdleidefrLLDVDNRTILPMNTEVRVLTSASDVLHSW 163
Cdd:TIGR02866  81 YLERPIPKDAL-KVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1509167427 164 AVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLS 224
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 9.95e-153

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 423.09  E-value: 9.95e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKMI 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 3.80e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 322.82  E-value: 3.80e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKM 226
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 2.93e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 320.73  E-value: 2.93e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKM 226
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 5.10e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 319.94  E-value: 5.10e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKM 226
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-227 1.44e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 313.95  E-value: 1.44e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKMI 227
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 5.83e-105

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 302.16  E-value: 5.83e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSK 225
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 9.37e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 296.51  E-value: 9.37e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLS 224
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 4.14e-98

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 285.07  E-value: 4.14e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKMI 227
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-227 8.31e-97

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 282.02  E-value: 8.31e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   7 LSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 86
Cdd:MTH00023   16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  87 LDDSVDAMITIKTIGRQWYWSYEYSDFV--NVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWA 164
Cdd:MTH00023   96 MDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1509167427 165 VPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKMI 227
Cdd:MTH00023  176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 3.87e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 277.43  E-value: 3.87e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKM 226
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 4.16e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 275.05  E-value: 4.16e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKMI 227
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 1.39e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 273.68  E-value: 1.39e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVL 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1509167427 161 HSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKMI 227
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-224 9.44e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 268.96  E-value: 9.44e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   7 LSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  87 LDDSVDAMITIKTIGRQWYWSYEYSDF--VNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWA 164
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427 165 VPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLS 224
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVA 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-222 9.15e-87

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: 252.49  E-value: 9.15e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  95 ITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGVKIDA 174
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1509167427 175 TPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKW 222
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.22e-76

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 226.52  E-value: 1.22e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  95 ITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGVKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1509167427 175 TPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIEST 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-225 7.22e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 224.90  E-value: 7.22e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   7 LSLQDSASPLMEQLSFFHDHtmvVLLMITIIVGYSLSYMFIIKFSNR------NMLHGHLIETIWTALPAITLIFIALPS 80
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQ---ILFILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  81 LRLLYLLDDSV-DAMITIKTIGRQWYWSYEYSDF--VNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSAS 157
Cdd:MTH00027  112 LRLLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1509167427 158 DVLHSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSK 225
Cdd:MTH00027  192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-223 4.57e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 206.40  E-value: 4.57e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   6 NLSLQDSA-SPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFIIKFSNRNMLHGHLIETIWTALPAITLIFIALPSLRLL 84
Cdd:MTH00080    7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  85 YLLD-DSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVLHSW 163
Cdd:MTH00080   87 YYYGlMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSW 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427 164 AVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWL 223
Cdd:MTH00080  167 ALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 2.12e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 161.15  E-value: 2.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   6 NLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYmFIIKFSNRN-------MLHGHLIETIWTALPAITLIFIAL 78
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLY-FAIRYRRRKgdadpaqFHHNTKLEIVWTVIPIIIVIVLAV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  79 PSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYsdfvnvefdtymkPESDLEidefrlldVDNRTILPMNTEVRVLTSASD 158
Cdd:COG1622    97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRFLLTSAD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1509167427 159 VLHSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLSKM 226
Cdd:COG1622   156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-224 5.14e-39

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: 133.66  E-value: 5.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  13 ASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYmFIIKFSNRN------MLHGH-LIETIWTALPAI--TLIFIALPSLRL 83
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAY-VVWKFRRKGdeekpsQIHGNrRLEYVWTVIPLIivVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  84 LYLLDDSVDAMiTIKTIGRQWYWSYEYSDFvnvefdtymkpesdleidefrLLDVDNRTILPMNTEVRVLTSASDVLHSW 163
Cdd:TIGR02866  81 YLERPIPKDAL-KVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1509167427 164 AVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWLS 224
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 28-212 3.24e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 131.23  E-value: 3.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  28 MVVLLMITIIVGYSLSymfiIKFSNRNmlhgHLIETIWTALPaiTLIFIALPSLRLLYLLDDSVDAMI-TIKTIGRQWYW 106
Cdd:MTH00047   24 WVYIMLCWQVVSGNGS----VNFGSEN----QVLELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWYW 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427 107 SYEYSDfvNVEFDTYMkpeSDLeidefrLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGVKIDATPGRLNQGTFMM 186
Cdd:MTH00047   94 SYEYSF--GGSYDSFM---TDD------IFGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCP 162

                         170       180
                  ....*....|....*....|....*.
gi 1509167427 187 NRPGLFFGQCSEICGANHSFMPIVIE 212
Cdd:MTH00047  163 DRHGVFVGYCSELCGVGHSYMPIVIE 188
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-215 1.19e-35

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 123.78  E-value: 1.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427 118 FDTYMKPESDLEIDEFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*...
gi 1509167427 198 EICGANHSFMPIVIESTS 215
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVS 148
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 5.38e-26

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 96.60  E-value: 5.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  95 ITIKTIGRQWYWSYEYSDfvnvefdtymkpesdleidefrlLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGVKIDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1509167427 175 TPGRLNQGTFMMNRPGLFFGQCSEICGANHSFMPIVIE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 6.29e-23

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 88.83  E-value: 6.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  95 ITIKTIGRQWYWSYEYSDFVNVEFDTymkpesdleidefrlldvDNRTILPMNTEVRVLTSASDVLHSWAVPALGVKIDA 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509167427 175 TPGRLNQGTFMMNRPGLFFGQCSEICGANHSFM 207
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 1.04e-22

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: 88.16  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427   1 MATWSNLSLQDSASPLMEQLSFFHDHTMVVLLMITIIVGYSLSYMFI------IKFSNRNMLHGHLIETIWTALPAITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 1509167427  75 FIA 77
Cdd:pfam02790  81 LIA 83
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 3.46e-21

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 84.61  E-value: 3.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  95 ITIKTIGRQWYWSYEYSDFvnvefDTYMKPESDLEIDEFRLldvdnrtilPMNTEVRVLTSASDVLHSWAVPALGVKIDA 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509167427 175 TPGRLNQGTFMMNRPGLFFGQCSEICGANHSFM 207
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 6.46e-21

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 83.45  E-value: 6.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  95 ITIKTIGRQWYWSYEYsdfvnvefdtymkPESDLEIDEfrlLDVdnrtilPMNTEVRVLTSASDVLHSWAVPALGVKIDA 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTY-------------PNGKREINE---LHV------PVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509167427 175 TPGRLNQGTFMMNRPGLFFGQCSEICGANHSFM 207
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-223 4.17e-17

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 73.98  E-value: 4.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  95 ITIKTIGRQWYWSYEYsdfvnvefdtymkPESDLeidefrllDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGVKIDA 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSY-------------PEANV--------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1509167427 175 TPGRLNqgTFMMN--RPGLFFGQCSEICGANHSFMPIVIESTSANLFIKWL 223
Cdd:cd13914    60 FPGQYN--TIKTEatEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-207 5.68e-16

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 71.72  E-value: 5.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427  88 DDSVDAMITIKTIGRQWYWSYEYSDFVNvefdtymkpesdlEIDEFRLldvdnrtilPMNTEVRVLTSASDVLHSWAVPA 167
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPNGVT-------------TGNTLRV---------PADTPIALRVTSTDVFHTFGIPE 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1509167427 168 LGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFM 207
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 144-207 4.40e-07

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 46.79  E-value: 4.40e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1509167427 144 LPMNTEVRVLTSASDVLHSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFM 207
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 138-212 1.79e-05

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 42.60  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509167427 138 VDNRTILPMNTEVRV-LTSASDVLHSWAVPALGVKIDA---------------TPGRLNQGTFMMNRPGLFFGQCSEICG 201
Cdd:cd00920    21 GPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGH 100

                          90
                  ....*....|.
gi 1509167427 202 aNHSFMPIVIE 212
Cdd:cd00920   101 -NHAGMVGTIN 110
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-207 2.08e-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: 36.37  E-value: 2.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1509167427 140 NRTILPMNTEVR-VLTSASdVLHSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFM 207
Cdd:cd04212    25 NELVIPVGRPVNfRLTSDS-VMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 149-207 4.66e-03

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


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 35.29  E-value: 4.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1509167427 149 EVRV-LTS---ASDVLHSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFM 207
Cdd:cd04223    25 EVTVhLTNleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 147-207 7.74e-03

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 34.65  E-value: 7.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1509167427 147 NTEVRVLTSASDVLHSWAVPALGVKIDATPGRLNQGTFMMNRPGLFFGQCSEICGANHSFM 207
Cdd:cd13917    21 GKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
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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