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Conserved domains on  [gi|1824669236|ref|YP_009740708|]
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cytochrome c oxidase subunit II (mitochondrion) [Euparatettix variabilis]

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
 1-225 2.23e-144

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 401.90  E-value: 2.23e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 2.23e-144

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 401.90  E-value: 2.23e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-222 8.46e-83

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 242.48  E-value: 8.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  94 SMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVLHSWAIPSLGVKID 173
Cdd:cd13912     2 SLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1824669236 174 ATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKW 222
Cdd:cd13912    82 AVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.37e-70

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 210.34  E-value: 3.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  95 MTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVLHSWAIPSLGVKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1824669236 175 TPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-225 2.16e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 171.16  E-value: 2.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIkIAM-------NNMSLRYMLSGHTIETIWTTLPAIVL 73
Cdd:COG1622    13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLL-YFAiryrrrkGDADPAQFHHNTKLEIVWTVIPIIIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  74 IFIAIPSLHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKmefdsfmlnydqanqdtfrllDVDNRTVLPINTNIRIL 153
Cdd:COG1622    92 IVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI---------------------ATVNELVLPVGRPVRFL 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824669236 154 TSASDVLHSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:COG1622   151 LTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-223 1.26e-40

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: 137.51  E-value: 1.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  14 SPLMEQLTFFHDHTMSIIMLITLMVS----YMMIKI-AMNNMSLRYMLSGHT-IETIWTTLPA-IVLIFIAIPSLHLLYM 86
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAallaYVVWKFrRKGDEEKPSQIHGNRrLEYVWTVIPLiIVVGLFAATAKGLLYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  87 MDDSTETSMTVKTIGRQWYWSYEYSDFkkmefdsfmlnydqanqdTFRlldVDNRTVLPINTNIRILTSASDVLHSWAIP 166
Cdd:TIGR02866  83 ERPIPKDALKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVP 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1824669236 167 SLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWL 223
Cdd:TIGR02866 142 ELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 2.23e-144

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 401.90  E-value: 2.23e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 5.56e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 335.37  E-value: 5.56e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKNT 226
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-225 3.06e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 325.90  E-value: 3.06e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-227 7.91e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 317.03  E-value: 7.91e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKNTI 227
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-225 3.10e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 308.00  E-value: 3.10e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 2.91e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 305.37  E-value: 2.91e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 3.03e-106

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 305.63  E-value: 3.03e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 5-225 2.50e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 288.57  E-value: 2.50e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   5 NNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPSLHLL 84
Cdd:MTH00023   14 WQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  85 YMMDDSTETSMTVKTIGRQWYWSYEYSDFKK--MEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVLHS 162
Cdd:MTH00023   94 YLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHS 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1824669236 163 WAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:MTH00023  174 FAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-222 2.02e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 278.14  E-value: 2.02e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKW 222
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-225 1.10e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 276.66  E-value: 1.10e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   7 MSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPSLHLLYM 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  87 MDDSTETSMTVKTIGRQWYWSYEYSDF--KKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVLHSWA 164
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1824669236 165 IPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVAT 229
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-222 6.04e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 274.67  E-value: 6.04e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKW 222
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-222 1.53e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 268.29  E-value: 1.53e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKW 222
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-225 1.74e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 265.49  E-value: 1.74e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  81 LHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-222 8.46e-83

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 242.48  E-value: 8.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  94 SMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVLHSWAIPSLGVKID 173
Cdd:cd13912     2 SLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1824669236 174 ATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKW 222
Cdd:cd13912    82 AVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-223 1.30e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 226.45  E-value: 1.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   7 MSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAMNNMSLRYM---LSGHTIETIWTTLPAIVLIFIAIPSLHL 83
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  84 LYMMDDST-ETSMTVKTIGRQWYWSYEYSDF--KKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVL 160
Cdd:MTH00027  115 LYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1824669236 161 HSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWL 223
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.37e-70

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 210.34  E-value: 3.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  95 MTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVLHSWAIPSLGVKIDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1824669236 175 TPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 4-225 3.14e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 204.09  E-value: 3.14e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   4 WNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIaMNNMSLRYMLSGH-TIETIWTTLPAIVLIFIAIPSLH 82
Cdd:MTH00080    6 YNLNFSNSLFSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLI-SNNFYFKSKKIEYqFGELLCSVFPVLILLMQMVPSLS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  83 LLYMMD-DSTETSMTVKTIGRQWYWSYEYSDFKKMEFDSFMLNYDQANQDTFRLLDVDNRTVLPINTNIRILTSASDVLH 161
Cdd:MTH00080   85 LLYYYGlMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIH 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1824669236 162 SWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:MTH00080  165 SWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKL 228
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-225 2.16e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 171.16  E-value: 2.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIkIAM-------NNMSLRYMLSGHTIETIWTTLPAIVL 73
Cdd:COG1622    13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLL-YFAiryrrrkGDADPAQFHHNTKLEIVWTVIPIIIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  74 IFIAIPSLHLLYMMDDSTETSMTVKTIGRQWYWSYEYSDFKKmefdsfmlnydqanqdtfrllDVDNRTVLPINTNIRIL 153
Cdd:COG1622    92 IVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI---------------------ATVNELVLPVGRPVRFL 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824669236 154 TSASDVLHSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWLKN 225
Cdd:COG1622   151 LTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 32-216 1.97e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 147.41  E-value: 1.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  32 MLITLMVSYMMI-KIAMNNMSLRYMLSGHTIETIWTTLPAIVLIFIAIPSLHLLYMmDDSTETSMTVKTIGRQWYWSYEY 110
Cdd:MTH00047   19 VFIPCWVYIMLCwQVVSGNGSVNFGSENQVLELLWTVVPTLLVLVLCFLNLNFITS-DLDCFSSETIKVIGHQWYWSYEY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236 111 SDfkKMEFDSFMlnydqaNQDTFrllDVDNRTVLPINTNIRILTSASDVLHSWAIPSLGVKIDATPGRLNQGIFLIKRPG 190
Cdd:MTH00047   98 SF--GGSYDSFM------TDDIF---GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHG 166

                         170       180
                  ....*....|....*....|....*.
gi 1824669236 191 LLFGQCSEICGVNHSFMPITIEAVNN 216
Cdd:MTH00047  167 VFVGYCSELCGVGHSYMPIVIEVVDV 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-223 1.26e-40

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: 137.51  E-value: 1.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  14 SPLMEQLTFFHDHTMSIIMLITLMVS----YMMIKI-AMNNMSLRYMLSGHT-IETIWTTLPA-IVLIFIAIPSLHLLYM 86
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAallaYVVWKFrRKGDEEKPSQIHGNRrLEYVWTVIPLiIVVGLFAATAKGLLYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  87 MDDSTETSMTVKTIGRQWYWSYEYSDFkkmefdsfmlnydqanqdTFRlldVDNRTVLPINTNIRILTSASDVLHSWAIP 166
Cdd:TIGR02866  83 ERPIPKDALKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVP 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1824669236 167 SLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWL 223
Cdd:TIGR02866 142 ELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 134-225 4.77e-35

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 122.24  E-value: 4.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236 134 RLLDVDNRTVLPINTNIRILTSASDVLHSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEA 213
Cdd:PTZ00047   67 RQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEA 146

                          90
                  ....*....|....*.
gi 1824669236 214 VNNKSFI----KWLKN 225
Cdd:PTZ00047  147 VSPEAYAahakKYYKD 162
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.85e-24

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: 92.74  E-value: 1.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  95 MTVKTIGRQWYWSYEYSDfkkmefdsfmlnydqanqdtfrlLDVDNRTVLPINTNIRILTSASDVLHSWAIPSLGVKIDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1824669236 175 TPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 5.11e-23

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 88.93  E-value: 5.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236   1 MATWNNMSLQNSSSPLMEQLTFFHDHTMSIIMLITLMVSYMMIKIAM------NNMSLRYMLSGHTIETIWTTLPAIVLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1824669236  75 FIAIPSLHL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-214 2.29e-21

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: 84.98  E-value: 2.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  94 SMTVKTIGRQWYWSYEYSDFKKMEFDSfmlnydqANQdtfrlldvdnrTVLPINTNIRILTSASDVLHSWAIPSLGVKID 173
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGIVT-------ANE-----------LHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1824669236 174 ATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAV 214
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-223 3.64e-20

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: 82.07  E-value: 3.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  96 TVKTIGRQWYWSYEYSDfkkmefdsfmlnydqANQDTFrlldvdNRTVLPINTNIRILTSASDVLHSWAIPSLGVKIDAT 175
Cdd:cd13914     2 EIEVEAYQWGWEFSYPE---------------ANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1824669236 176 PGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWL 223
Cdd:cd13914    61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 6.43e-20

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: 81.15  E-value: 6.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  95 MTVKTIGRQWYWSYEYsdfkkmefdsfmLNYDQanQDTFRLLDVDNRTVLPINTNIRILTSASDVLHSWAIPSLGVKIDA 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRY------------PGGDG--KLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1824669236 175 TPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFM 207
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-213 1.00e-19

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 80.37  E-value: 1.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  94 SMTVKTIGRQWYWSYEYSDFKKmefdsfmlnydqanqdtfrlldVDNRTVLPINTNIRILTSASDVLHSWAIPSLGVKID 173
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKR----------------------EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1824669236 174 ATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEA 213
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 71-223 1.51e-19

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 81.35  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  71 IVLIFIAIPSLHLLYMMD---DSTETSMTVKTIGRQWYWSYEYSDfkkmefdsfmlNYDQANQdtfrlldvdnrTVLPIN 147
Cdd:cd13918     6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPN-----------GVTTGNT-----------LRVPAD 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824669236 148 TNIRILTSASDVLHSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAVNNKSFIKWL 223
Cdd:cd13918    64 TPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-214 8.27e-05

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: 40.25  E-value: 8.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824669236 140 NRTVLPINTNIRILTSASDVLHSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAV 214
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-214 7.18e-04

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 37.75  E-value: 7.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236  96 TVKTIGRQWYWSYeysdfkkmefdsfmlnydqanqdtfrlldvdNRTVLPINTNIRILTSASDVLHSWAIPS----LGVK 171
Cdd:cd13916     2 VVAVTGHQWYWEL-------------------------------SRTEIPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1824669236 172 IDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAV 214
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTVV 93
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-214 3.70e-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: 35.60  E-value: 3.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824669236 140 NRTVLPINTNIRILTSASDVLHSWAIPSLGVKIDATPGRLNQGIFLIKRPGLLFGQCSEICGVNHSFMPITIEAV 214
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 138-212 4.98e-03

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 35.67  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824669236 138 VDNRTVLPINTNIR-ILTSASDVLHSWAIPSLGVKIDATPGRLNQGI---------------FLIKRPGLLFGQCSEICG 201
Cdd:cd00920    21 GPPVLVVPVGDTVRvQFVNKLGENHSVTIAGFGVPVVAMAGGANPGLvntlvigpgesaevtFTTDQAGVYWFYCTIPGH 100

                          90
                  ....*....|.
gi 1824669236 202 vNHSFMPITIE 212
Cdd:cd00920   101 -NHAGMVGTIN 110
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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