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Conserved domains on  [gi|939462969|gb|ALJ78849|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Phaulacridium marginale]

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
 1-222 1.15e-147

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 409.99  E-value: 1.15e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   1 NLSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLY 80
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  81 LLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAV 160
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939462969 161 PALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKMI 222
Cdd:MTH00154 166 PSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-222 1.15e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 409.99  E-value: 1.15e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   1 NLSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLY 80
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  81 LLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAV 160
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939462969 161 PALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKMI 222
Cdd:MTH00154 166 PSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 90-217 1.60e-86

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


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 251.72  E-value: 1.60e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  90 ITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 169
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 939462969 170 TPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKW 217
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
90-209 5.55e-77

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 227.29  E-value: 5.55e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   90 ITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 169
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 939462969  170 TPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIEST 209
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-221 2.71e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 158.07  E-value: 2.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   1 NLSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMV------ITYTNRNMLHGHLIETIWTALPAITLIFIALP 74
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIryrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  75 SLRLLYLLDDSVDAMITIKTIGRQWYWSYEYsdfidvefdtymtaetdLENNGfrllDVDNRTILPMNTEVRVLTSASDV 154
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-----------------PDQGI----ATVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939462969 155 LHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKM 221
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 8-219 2.84e-38

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: 131.35  E-value: 2.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969    8 ASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMM-----VITYTNRNMLHGH-LIETIWTALPAI--TLIFIALPSLRLL 79
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrKGDEEKPSQIHGNrRLEYVWTVIPLIivVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   80 YLLDDSVDAMiTIKTIGRQWYWSYEYsdfidvefdtymtaetdlENNGFRlldVDNRTILPMNTEVRVLTSASDVLHSWA 159
Cdd:TIGR02866  82 LERPIPKDAL-KVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  160 VPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLS 219
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-222 1.15e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 409.99  E-value: 1.15e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   1 NLSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLY 80
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  81 LLDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAV 160
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939462969 161 PALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKMI 222
Cdd:MTH00154 166 PSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 2-221 6.23e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 322.25  E-value: 6.23e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 81
Cdd:MTH00117   7 LGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  82 LDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVP 161
Cdd:MTH00117  87 MDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969 162 ALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKM 221
Cdd:MTH00117 167 SLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 2-221 3.02e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 312.81  E-value: 3.02e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 81
Cdd:MTH00139   7 LGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  82 LDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVP 161
Cdd:MTH00139  87 MDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969 162 ALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKM 221
Cdd:MTH00139 167 SLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 2-221 3.58e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 310.33  E-value: 3.58e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 81
Cdd:MTH00140   7 LGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  82 LDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVP 161
Cdd:MTH00140  87 LDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969 162 ALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKM 221
Cdd:MTH00140 167 SLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 2-222 9.12e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 306.63  E-value: 9.12e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 81
Cdd:MTH00038   7 LGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  82 LDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVP 161
Cdd:MTH00038  87 MDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939462969 162 ALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKMI 222
Cdd:MTH00038 167 SLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 2-219 1.63e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 295.74  E-value: 1.63e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 81
Cdd:MTH00168   7 LGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  82 LDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVP 161
Cdd:MTH00168  87 MDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 939462969 162 ALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLS 219
Cdd:MTH00168 167 SLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-220 1.98e-102

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 295.61  E-value: 1.98e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 81
Cdd:MTH00008   7 LMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  82 LDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVP 161
Cdd:MTH00008  87 MDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 939462969 162 ALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSK 220
Cdd:MTH00008 167 SLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-222 7.31e-97

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 281.61  E-value: 7.31e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 81
Cdd:MTH00098   7 LGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  82 LDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVP 161
Cdd:MTH00098  87 MDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939462969 162 ALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKMI 222
Cdd:MTH00098 167 SLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-222 1.51e-94

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 276.25  E-value: 1.51e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 81
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  82 LDDSVDAMITIKTIGRQWYWSYEYSDFID--VEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWA 159
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939462969 160 VPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKMI 222
Cdd:MTH00023 176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-222 4.24e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 274.84  E-value: 4.24e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 81
Cdd:MTH00185   7 LGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  82 LDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVP 161
Cdd:MTH00185  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939462969 162 ALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKMI 222
Cdd:MTH00185 167 ALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 2-221 7.06e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 273.96  E-value: 7.06e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 81
Cdd:MTH00076   7 LGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  82 LDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVP 161
Cdd:MTH00076  87 MDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969 162 ALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKM 221
Cdd:MTH00076 167 SLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-222 9.99e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 271.20  E-value: 9.99e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 81
Cdd:MTH00129   7 LGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  82 LDDSVDAMITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVP 161
Cdd:MTH00129  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939462969 162 ALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKMI 222
Cdd:MTH00129 167 ALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-219 1.51e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 270.88  E-value: 1.51e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYL 81
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  82 LDDSVDAMITIKTIGRQWYWSYEYSDF--IDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWA 159
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969 160 VPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLS 219
Cdd:MTH00051 169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVA 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 90-217 1.60e-86

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


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 251.72  E-value: 1.60e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  90 ITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 169
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 939462969 170 TPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKW 217
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
90-209 5.55e-77

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 227.29  E-value: 5.55e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   90 ITIKTIGRQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 169
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 939462969  170 TPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIEST 209
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-220 3.36e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 217.59  E-value: 3.36e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   2 LSLQDGASPLMEQLSFFHDHtmvVLMLITVIVGYALSYMMVITYTNR------NMLHGHLIETIWTALPAITLIFIALPS 75
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQ---ILFILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  76 LRLLYLLDDSV-DAMITIKTIGRQWYWSYEYSDF--IDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSAS 152
Cdd:MTH00027 112 LRLLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939462969 153 DVLHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSK 220
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 18-218 3.19e-64

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 198.70  E-value: 3.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  18 FHDHTMVVLMLITVIVGYALSYMMVITYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLD-DSVDAMITIKTIG 96
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  97 RQWYWSYEYSDFIDVEFDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQ 176
Cdd:MTH00080 105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 939462969 177 GTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWL 218
Cdd:MTH00080 185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-221 2.71e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 158.07  E-value: 2.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   1 NLSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMMV------ITYTNRNMLHGHLIETIWTALPAITLIFIALP 74
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIryrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  75 SLRLLYLLDDSVDAMITIKTIGRQWYWSYEYsdfidvefdtymtaetdLENNGfrllDVDNRTILPMNTEVRVLTSASDV 154
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-----------------PDQGI----ATVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939462969 155 LHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLSKM 221
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 23-207 6.92e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 137.78  E-value: 6.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  23 MVVLMLITVIVgyalSYMMVITYTNRNmlhgHLIETIWTALPaiTLIFIALPSLRLLYLLDDSVDAMI-TIKTIGRQWYW 101
Cdd:MTH00047  24 WVYIMLCWQVV----SGNGSVNFGSEN----QVLELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWYW 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969 102 SYEYSDfiDVEFDTYMTAETDLENNGFRLLdvdnrtilpMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFSI 181
Cdd:MTH00047  94 SYEYSF--GGSYDSFMTDDIFGVDKPLRLV---------YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCP 162

                        170       180
                 ....*....|....*....|....*.
gi 939462969 182 NRPGLFFGQCSEICGANHSFMPIVIE 207
Cdd:MTH00047 163 DRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 8-219 2.84e-38

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: 131.35  E-value: 2.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969    8 ASPLMEQLSFFHDHTMVVLMLITVIVGYALSYMM-----VITYTNRNMLHGH-LIETIWTALPAI--TLIFIALPSLRLL 79
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrKGDEEKPSQIHGNrRLEYVWTVIPLIivVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969   80 YLLDDSVDAMiTIKTIGRQWYWSYEYsdfidvefdtymtaetdlENNGFRlldVDNRTILPMNTEVRVLTSASDVLHSWA 159
Cdd:TIGR02866  82 LERPIPKDAL-KVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  160 VPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWLS 219
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 113-210 1.65e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 128.40  E-value: 1.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969 113 FDTYMTAETDLENNGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQCS 192
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*...
gi 939462969 193 EICGANHSFMPIVIESTS 210
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVS 148
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 90-207 1.03e-25

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: 95.83  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  90 ITIKTIGRQWYWSYEYSDfidvefdtymtaetdlenngfrlLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 169
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 939462969 170 TPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIE 207
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), ...
 90-202 1.63e-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: 90.37  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  90 ITIKTIGRQWYWSYEYSDFIDVEFDTymtaetdlenngfrlldvDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 169
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90       100       110
                 ....*....|....*....|....*....|...
gi 939462969 170 TPGRLNQGTFSINRPGLFFGQCSEICGANHSFM 202
Cdd:cd04213   64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 90-202 1.55e-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: 84.99  E-value: 1.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  90 ITIKTIGRQWYWSYEYSdfidvefdtymtaetdlenNGFRlldVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 169
Cdd:cd13915    2 LEIQVTGRQWMWEFTYP-------------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90       100       110
                 ....*....|....*....|....*....|...
gi 939462969 170 TPGRLNQGTFSINRPGLFFGQCSEICGANHSFM 202
Cdd:cd13915   60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 90-202 3.97e-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: 84.23  E-value: 3.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  90 ITIKTIGRQWYWSYEYSDFidvefDTYMTAETDLENNGFRLldvdnrtilPMNTEVRVLTSASDVLHSWAVPALGIKIDA 169
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 939462969 170 TPGRLNQGTFSINRPGLFFGQCSEICGANHSFM 202
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-72 3.48e-19

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: 78.53  E-value: 3.48e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939462969    1 NLSLQDGASPLMEQLSFFHDHTMVVLMLITVIVGYALsYMMVITY-------TNRNMLHGHLIETIWTALPAITLIFIA 72
Cdd:pfam02790   6 GLGFQDAASPLMEGLLELHDYIMFILTLILILVLYIL-VTCLIRFnrrknpiTARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 90-218 3.76e-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: 3.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  90 ITIKTIGRQWYWSYEYSDfidvefdtymtaetdlENNgfrllDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 169
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPE----------------ANV-----TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 939462969 170 TPGRLNQGTFSINRPGLFFGQCSEICGANHSFMPIVIESTSVNLFIKWL 218
Cdd:cd13914   60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-202 7.62e-14

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 65.94  E-value: 7.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  83 DDSVDAMITIKTIGRQWYWSYEYSdfidvefdtymtaetdlenNGFRLLdvdNRTILPMNTEVRVLTSASDVLHSWAVPA 162
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYP-------------------NGVTTG---NTLRVPADTPIALRVTSTDVFHTFGIPE 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 939462969 163 LGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFM 202
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 ...
 139-202 2.82e-06

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 44.48  E-value: 2.82e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939462969 139 LPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFM 202
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 109-207 9.73e-04

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 37.60  E-value: 9.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969 109 IDVEFDTYMTAETDLENNGFrlldVDNRTILPMNTEVRV-LTSASDVLHSWAVPALGIKIDA---------------TPG 172
Cdd:cd00920    1 ITVTASDWGWSFTYNGVLLF----GPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPG 76

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 939462969 173 RLNQGTFSINRPGLFFGQCSEICGaNHSFMPIVIE 207
Cdd:cd00920   77 ESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 142-202 1.68e-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: 36.58  E-value: 1.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939462969 142 NTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFM 202
Cdd:cd13917   21 GKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 90-202 2.18e-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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 36.21  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939462969  90 ITIKTIGRQWYWSYeysdfidvefdtymtaetdlenngfrlldvdNRTILPMNTEVRVLTSASDVLHSWAV--PALGI-- 165
Cdd:cd13916    1 QVVAVTGHQWYWEL-------------------------------SRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLla 49

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 939462969 166 KIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFM 202
Cdd:cd13916   50 QTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 135-202 3.32e-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: 35.99  E-value: 3.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939462969 135 NRTILPMNTEVR-VLTSASdVLHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFM 202
Cdd:cd04212   25 NELVIPVGRPVNfRLTSDS-VMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 144-202 6.43e-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: 34.90  E-value: 6.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939462969 144 EVRV-LTS---ASDVLHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEICGANHSFM 202
Cdd:cd04223   25 EVTVhLTNleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
 
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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