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Conserved domains on  [gi|124484821|ref|YP_001031203|]
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cytochrome c oxidase subunit II (mitochondrion) [Amphimedon queenslandica]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475883)

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 MTH00051
cytochrome c oxidase subunit II; Provisional
 20-251 2.87e-145

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 405.70  E-value: 2.87e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  20 DAPEPWQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALP 99
Cdd:MTH00051   2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 100 SLKLLYLMDEIGEPALTIKAVGHQWYWSYEYSDYGNSTVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGA 179
Cdd:MTH00051  82 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124484821 180 DVLHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIGALLSE 251
Cdd:MTH00051 162 DVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
 
Name Accession Description Interval E-value
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 20-251 2.87e-145

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 405.70  E-value: 2.87e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  20 DAPEPWQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALP 99
Cdd:MTH00051   2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 100 SLKLLYLMDEIGEPALTIKAVGHQWYWSYEYSDYGNSTVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGA 179
Cdd:MTH00051  82 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124484821 180 DVLHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIGALLSE 251
Cdd:MTH00051 162 DVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 113-244 2.62e-93

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: 270.21  E-value: 2.62e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 113 PALTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLHSFAVPSLAV 192
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFND--LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 124484821 193 KIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNW 244
Cdd:cd13912   79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
115-236 6.45e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 238.46  E-value: 6.45e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  115 LTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLHSFAVPSLAVKI 194
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD--LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 124484821  195 DAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGV 236
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
25-247 8.45e-65

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 201.21  E-value: 8.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  25 WQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIV------RALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIAL 98
Cdd:COG1622   17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLyfairyRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  99 PSLKLLYLMDEIGEPALTIKAVGHQWYWSYEYSDYGNSTvefdsymiptsdlnsgdlrllevDNRLVVPIHTQVRVLVTG 178
Cdd:COG1622   97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-----------------------VNELVLPVGRPVRFLLTS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124484821 179 ADVLHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIGA 247
Cdd:COG1622  154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 32-245 1.19e-46

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: 154.08  E-value: 1.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821   32 PGCYLMEDIVQFHDWIMYILVLILSFVLWLIV------RALTTNSTNMYLVDAPVIEIIWTLIPAGVLM-FIALPSLKLL 104
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAyvvwkfRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  105 YLMDEIGEPALTIKAVGHQWYWSYEYSDYGNSTVefdsymiptsdlnsgdlrllevdNRLVVPIHTQVRVLVTGADVLHS 184
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPESGFTTV-----------------------NELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124484821  185 FAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWI 245
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 20-251 2.87e-145

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 405.70  E-value: 2.87e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  20 DAPEPWQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALP 99
Cdd:MTH00051   2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 100 SLKLLYLMDEIGEPALTIKAVGHQWYWSYEYSDYGNSTVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGA 179
Cdd:MTH00051  82 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124484821 180 DVLHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIGALLSE 251
Cdd:MTH00051 162 DVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 13-251 1.12e-142

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 399.12  E-value: 1.12e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  13 LGNWGYGDAPEPWQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGV 92
Cdd:MTH00023   2 FNNFFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  93 LMFIALPSLKLLYLMDEIGEPALTIKAVGHQWYWSYEYSDYGNSTVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQV 172
Cdd:MTH00023  82 LVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124484821 173 RVLVTGADVLHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIGALLSE 251
Cdd:MTH00023 162 RILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSND 240
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 26-245 1.21e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 362.99  E-value: 1.21e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  26 QLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALPSLKLLY 105
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 106 LMDEIGEPALTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLHSF 185
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDFKN--IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 186 AVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWI 245
Cdd:MTH00154 164 TVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 22-245 6.95e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 351.14  E-value: 6.95e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  22 PEPWQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALPSL 101
Cdd:MTH00117   2 ANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 102 KLLYLMDEIGEPALTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADV 181
Cdd:MTH00117  82 RILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKD--LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124484821 182 LHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWI 245
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWS 223
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 26-248 2.84e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 339.61  E-value: 2.84e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  26 QLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALPSLKLLY 105
Cdd:MTH00140   6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 106 LMDEIGEPALTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLHSF 185
Cdd:MTH00140  86 LLDETNNPLLTVKAIGHQWYWSYEYSDFSV--IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124484821 186 AVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIGAL 248
Cdd:MTH00140 164 TVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 24-251 2.04e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 337.44  E-value: 2.04e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  24 PWQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALPSLKL 103
Cdd:MTH00038   4 WLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 104 LYLMDEIGEPALTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLH 183
Cdd:MTH00038  84 LYLMDEVNNPFLTIKAIGHQWYWSYEYTDYND--LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124484821 184 SFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIGALLSE 251
Cdd:MTH00038 162 SWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 26-245 5.83e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 336.18  E-value: 5.83e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  26 QLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALPSLKLLY 105
Cdd:MTH00168   6 QLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 106 LMDEIGEPALTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLHSF 185
Cdd:MTH00168  86 LMDEIDKPDLTIKAVGHQWYWSYEYTDYND--LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 186 AVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWI 245
Cdd:MTH00168 164 TLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 24-251 5.39e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 331.29  E-value: 5.39e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  24 PWQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALPSLKL 103
Cdd:MTH00129   4 PSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 104 LYLMDEIGEPALTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLH 183
Cdd:MTH00129  84 LYLMDEINDPHLTIKAMGHQWYWSYEYTDYED--LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124484821 184 SFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIGALLSE 251
Cdd:MTH00129 162 SWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLED 229
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 26-245 1.79e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 324.75  E-value: 1.79e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  26 QLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALPSLKLLY 105
Cdd:MTH00139   6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 106 LMDEIGEPALTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLHSF 185
Cdd:MTH00139  86 LMDEVSDPYLTFKAVGHQWYWSYEYSDFKN--LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 186 AVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWI 245
Cdd:MTH00139 164 TVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 22-244 6.14e-112

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 320.90  E-value: 6.14e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  22 PEPWQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALPSL 101
Cdd:MTH00098   2 AYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 102 KLLYLMDEIGEPALTIKAVGHQWYWSYEYSDYGNSTveFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADV 181
Cdd:MTH00098  82 RILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLS--FDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124484821 182 LHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNW 244
Cdd:MTH00098 160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 23-251 2.36e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 314.52  E-value: 2.36e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  23 EPWQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALPSLK 102
Cdd:MTH00185   3 HPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 103 LLYLMDEIGEPALTIKAVGHQWYWSYEYSDYgnSTVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVL 182
Cdd:MTH00185  83 ILYLMDEINDPHLTIKAMGHQWYWSYEYTDY--EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124484821 183 HSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIGALLSE 251
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEE 229
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 24-250 4.36e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 311.33  E-value: 4.36e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  24 PWQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALPSLKL 103
Cdd:MTH00076   4 PSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 104 LYLMDEIGEPALTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLH 183
Cdd:MTH00076  84 LYLMDEINDPHLTVKAIGHQWYWSYEYTDYED--LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124484821 184 SFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIGALLS 250
Cdd:MTH00076 162 SWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 20-246 4.21e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 307.72  E-value: 4.21e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  20 DAPEPWQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYL---VDAPVIEIIWTLIPAGVLMFI 96
Cdd:MTH00027  28 DANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  97 ALPSLKLLYLMDEIGEPA-LTIKAVGHQWYWSYEYSDYGNSTVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVL 175
Cdd:MTH00027 108 AFPSLRLLYIMDECGFSAnITIKVTGHQWYWSYSYEDYGEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVL 187

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124484821 176 VTGADVLHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIG 246
Cdd:MTH00027 188 ITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIG 258
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 26-245 5.94e-104

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 300.62  E-value: 5.94e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  26 QLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIALPSLKLLY 105
Cdd:MTH00008   6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 106 LMDEIGEPALTIKAVGHQWYWSYEYSDYgnSTVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLHSF 185
Cdd:MTH00008  86 LMDEVSNPSITLKTIGHQWYWSYEYSDF--SNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 186 AVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWI 245
Cdd:MTH00008 164 TVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 113-244 2.62e-93

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: 270.21  E-value: 2.62e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 113 PALTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLHSFAVPSLAV 192
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFND--LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 124484821 193 KIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNW 244
Cdd:cd13912   79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
115-236 6.45e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 238.46  E-value: 6.45e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  115 LTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLHSFAVPSLAVKI 194
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD--LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 124484821  195 DAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGV 236
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 37-249 1.92e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 218.34  E-value: 1.92e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  37 MEDIVQFHDWIMYIlVLILSFVLWLIVRALTTN-STNMYLVDAPVIEIIWTLIPAGVLMFIALPSLKLLYLMDEIG-EPA 114
Cdd:MTH00080  19 MDWFHNFNCSLLFG-EFVLAFVVFLFLYLISNNfYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSN 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 115 LTIKAVGHQWYWSYEYSDYGNstVEFDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLHSFAVPSLAVKI 194
Cdd:MTH00080  98 LTVKVTGHQWYWSYEFSDIPG--LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKM 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 124484821 195 DAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIGALL 249
Cdd:MTH00080 176 DAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLL 230
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
25-247 8.45e-65

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 201.21  E-value: 8.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  25 WQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIV------RALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFIAL 98
Cdd:COG1622   17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLyfairyRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  99 PSLKLLYLMDEIGEPALTIKAVGHQWYWSYEYSDYGNSTvefdsymiptsdlnsgdlrllevDNRLVVPIHTQVRVLVTG 178
Cdd:COG1622   97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-----------------------VNELVLPVGRPVRFLLTS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124484821 179 ADVLHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWIGA 247
Cdd:COG1622  154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 43-236 8.73e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 159.35  E-value: 8.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  43 FHDWIMYILVLILSFVLWLIV----RALTTNSTNMYLVDAPVIEIIWTLIPAGVLMFiaLPSLKLLYLMDEI-GEPALTI 117
Cdd:MTH00047   7 YYDIVCYILALCVFIPCWVYImlcwQVVSGNGSVNFGSENQVLELLWTVVPTLLVLV--LCFLNLNFITSDLdCFSSETI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 118 KAVGHQWYWSYEYSDYGnstvEFDSYMipTSDLNSgdlrlleVDNRLVVPIHTQVRVLVTGADVLHSFAVPSLAVKIDAV 197
Cdd:MTH00047  85 KVIGHQWYWSYEYSFGG----SYDSFM--TDDIFG-------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAI 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 124484821 198 PGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGV 236
Cdd:MTH00047 152 PGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 32-245 1.19e-46

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: 154.08  E-value: 1.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821   32 PGCYLMEDIVQFHDWIMYILVLILSFVLWLIV------RALTTNSTNMYLVDAPVIEIIWTLIPAGVLM-FIALPSLKLL 104
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAyvvwkfRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  105 YLMDEIGEPALTIKAVGHQWYWSYEYSDYGNSTVefdsymiptsdlnsgdlrllevdNRLVVPIHTQVRVLVTGADVLHS 184
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPESGFTTV-----------------------NELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124484821  185 FAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWI 245
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 140-241 4.31e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 148.81  E-value: 4.31e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 140 FDSYMIPTSDLNSGDLRLLEVDNRLVVPIHTQVRVLVTGADVLHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCS 219
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|..
gi 124484821 220 EICGANHSFMPIVIEGVAMEKY 241
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVSPEAY 152
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 114-229 1.10e-30

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: 109.63  E-value: 1.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 114 ALTIKAVGHQWYWSYEYSDYGNSTVEfdsymipTSdlnsgdlrllevdNRLVVPIHTQVRVLVTGADVLHSFAVPSLAVK 193
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPGRGIV-------TA-------------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGK 60

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 124484821 194 IDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFM 229
Cdd:cd04213   61 MDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 115-234 8.69e-30

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: 107.00  E-value: 8.69e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 115 LTIKAVGHQWYWSYEYSDygnstvefdsymiptsdlnsgdlrlLEVDNRLVVPIHTQVRVLVTGADVLHSFAVPSLAVKI 194
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKV 55

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 124484821 195 DAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIE 234
Cdd:cd13842   56 DAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-244 1.40e-26

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: 100.22  E-value: 1.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  83 IIWTLipaGVLMFIALPSlkllylmDEIGEPALTIKAVGHQWYWSYEYSDYGNSTvefdsymiptsdlnsgdlrllevdN 162
Cdd:cd13918   11 IVWTY---GMLLYVEDPP-------DEADEDALEVEVEGFQFGWQFEYPNGVTTG------------------------N 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 163 RLVVPIHTQVRVLVTGADVLHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYT 242
Cdd:cd13918   57 TLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFE 136


                 ..
gi 124484821 243 NW 244
Cdd:cd13918  137 AW 138
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 114-229 6.58e-26

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: 97.31  E-value: 6.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 114 ALTIKAVGHQWYWSYEYSDyGNSTvefdsymiptsdlnsgdlrllevDNRLVVPIHTQVRVLVTGADVLHSFAVPSLAVK 193
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYPN-GKRE-----------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIK 56

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 124484821 194 IDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFM 229
Cdd:cd13915   57 QDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 114-229 4.39e-25

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: 95.40  E-value: 4.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 114 ALTIKAVGHQWYWSYEYSDYgnstvefDSYMIPTSDLNSGDLRLlevdnrlvvPIHTQVRVLVTGADVLHSFAVPSLAVK 193
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPGG-------DGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVK 64

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 124484821 194 IDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFM 229
Cdd:cd13919   65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 21-103 1.37e-24

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: 93.55  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821   21 APEPWQLGLQDPGCYLMEDIVQFHDWIMYILVLILSFVLWLIVRALTTNS------TNMYLVDAPVIEIIWTLIPAGVLM 94
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNrrknpiTARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 124484821   95 FIALPSLKL 103
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 116-245 4.96e-22

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: 87.46  E-value: 4.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 116 TIKAVGHQWYWSYEYSDYGNSTvefdsymiptsdlnsgdlrllevDNRLVVPIHTQVRVLVTGADVLHSFAVPSLAVKID 195
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEANVTT-----------------------SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 124484821 196 AVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFMPIVIEGVAMEKYTNWI 245
Cdd:cd13914   59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 162-229 4.11e-11

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: 57.96  E-value: 4.11e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124484821 162 NRLVVPIHTQVRVLVTGADVLHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFM 229
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 115-229 5.27e-11

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: 57.94  E-value: 5.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 115 LTIKAVGHQWYWSYEYSDYGNSTVefdsymiptsdlnsgdlrllevdNRLVVPIHTQVRVLVTGADVLHSFAVPSLAVKI 194
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQGIATV-----------------------NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQI 57

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 124484821 195 DAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFM 229
Cdd:cd04212   58 YAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 116-229 2.67e-07

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 47.38  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 116 TIKAVGHQWYWSyeysdygnstvefdsymIPTSDLNSGDLrllevdnrlvvpihtqVRVLVTGADVLHSFAVPS----LA 191
Cdd:cd13916    2 VVAVTGHQWYWE-----------------LSRTEIPAGKP----------------VEFRVTSADVNHGFGIYDpdmrLL 48

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 124484821 192 VKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFM 229
Cdd:cd13916   49 AQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 151-234 4.73e-05

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 41.45  E-value: 4.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821 151 NSGDLRLLEVDNRLVVPIHTQVRV-LVTGADVLHSFAVPSLAVKIDA---------------VPGRLNQTNFLIKRPGVY 214
Cdd:cd00920   12 FTYNGVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVY 91

                         90       100
                 ....*....|....*....|
gi 124484821 215 YGQCSEICGaNHSFMPIVIE 234
Cdd:cd00920   92 WFYCTIPGH-NHAGMVGTIN 110
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 83-229 8.26e-05

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 42.86  E-value: 8.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124484821  83 IIWTlIPAGVLMFIALPSLKLLYLMDEI-----GEPALTIKAVGHQWYWSYEYSDYGNSTVefdsymiptsdlnsgdlrl 157
Cdd:PRK10525  91 VVWT-VPILIIIFLAVLTWKTTHALEPSkplahDEKPITIEVVSMDWKWFFIYPEQGIATV------------------- 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124484821 158 levdNRLVVPIHTQVRVLVTGADVLHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFM 229
Cdd:PRK10525 151 ----NEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGM 218
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 180-229 8.02e-04

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: 37.60  E-value: 8.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 124484821 180 DVLHSFAVPSLAVKIDAVPGRLNQTNFLIKRPGVYYGQCSEICGANHSFM 229
Cdd:cd04223   38 DITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 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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