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Conserved domains on  [gi|62161295|ref|YP_214861|]
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cytochrome c oxidase subunit II (mitochondrion) [Axinella corrugata]

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
 1-234 5.13e-172

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 472.34  E-value: 5.13e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    1 MDTPEPWQIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAF 80
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGAETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTA 160
Cdd:MTH00051  81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62161295  161 ADVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAMQSDEL 234
Cdd:MTH00051 161 ADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
 
Name Accession Description Interval E-value
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-234 5.13e-172

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 472.34  E-value: 5.13e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    1 MDTPEPWQIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAF 80
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGAETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTA 160
Cdd:MTH00051  81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62161295  161 ADVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAMQSDEL 234
Cdd:MTH00051 161 ADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-226 1.01e-95

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: 275.60  E-value: 1.01e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  95 PALTIKAIGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS*SV 174
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDF--NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 62161295 175 KIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 226
Cdd:cd13912  79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
97-218 1.15e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 239.62  E-value: 1.15e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    97 LTIKAIGHQWYWSYEYSDYGaeTIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS*SVKI 176
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFG--DLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 62161295   177 DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAV 218
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-230 2.84e-66

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 204.29  E-value: 2.84e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   7 WQIGFQDAASPVMEEIIFFHDQIM------FILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAF 80
Cdd:COG1622  17 GQLSLPDPAGPIAEEIDDLFWVSLiimlviFVLVFGLLLYFAIRYRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGAETiefdsymvptsdlnngdlrllevDNRLIVPIQTQVRVLVTA 160
Cdd:COG1622  97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-----------------------VNELVLPVGRPVRFLLTS 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295 161 ADVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAMQ 230
Cdd:COG1622 154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-228 2.21e-49

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: 160.24  E-value: 2.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    14 AASPVMEEIIFFHDQIMFILTIILTTVFWVIV------RALTTKHYHKYLFEGTLIEIIWTLIPAGILV-FIAFPSLKLL 86
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAyvvwkfRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    87 YLMDEVIDPALTIKAIGHQWYWSYEYSDYGAETiefdsymvptsdlnngdlrllevDNRLIVPIQTQVRVLVTAADVLHS 166
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPESGFTT-----------------------VNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62161295   167 FAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVA 228
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-234 5.13e-172

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 472.34  E-value: 5.13e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    1 MDTPEPWQIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAF 80
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGAETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTA 160
Cdd:MTH00051  81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62161295  161 ADVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAMQSDEL 234
Cdd:MTH00051 161 ADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-233 1.03e-156

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 434.18  E-value: 1.03e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    2 DTPEPWQIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFP 81
Cdd:MTH00023   9 DIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   82 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGAETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAA 161
Cdd:MTH00023  89 SLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGA 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62161295  162 DVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAMQSDE 233
Cdd:MTH00023 169 DVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSND 240
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 8-227 7.41e-139

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 388.42  E-value: 7.41e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    8 QIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFPSLKLLY 87
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDF--KNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  168 AVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWV 227
Cdd:MTH00154 164 TVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 4-231 4.84e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 366.16  E-value: 4.84e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    4 PEPWQIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFPSL 83
Cdd:MTH00117   2 ANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   84 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADV 163
Cdd:MTH00117  82 RILYLMDEINNPHLTIKAIGHQWYWSYEYTDY--KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62161295  164 LHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAMQS 231
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 8-232 1.84e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 354.63  E-value: 1.84e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    8 QIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFPSLKLLY 87
Cdd:MTH00140   6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYGaeTIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167
Cdd:MTH00140  86 LLDETNNPLLTVKAIGHQWYWSYEYSDFS--VIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62161295  168 AVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAMQSD 232
Cdd:MTH00140 164 TVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMSE 228
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 8-228 7.30e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 350.43  E-value: 7.30e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    8 QIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFPSLKLLY 87
Cdd:MTH00168   6 QLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYGaeTIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167
Cdd:MTH00168  86 LMDEIDKPDLTIKAVGHQWYWSYEYTDYN--DLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62161295  168 AVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVA 228
Cdd:MTH00168 164 TLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 6-233 1.26e-123

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 349.77  E-value: 1.26e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    6 PWQIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFPSLKL 85
Cdd:MTH00038   4 WLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165
Cdd:MTH00038  84 LYLMDEVNNPFLTIKAIGHQWYWSYEYTDY--NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62161295  166 SFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAMQSDE 233
Cdd:MTH00038 162 SWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 8-227 1.91e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 336.69  E-value: 1.91e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    8 QIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFPSLKLLY 87
Cdd:MTH00139   6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167
Cdd:MTH00139  86 LMDEVSDPYLTFKAVGHQWYWSYEYSDF--KNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  168 AVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWV 227
Cdd:MTH00139 164 TVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 6-229 2.15e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 333.99  E-value: 2.15e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    6 PWQIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFPSLKL 85
Cdd:MTH00129   4 PSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165
Cdd:MTH00129  84 LYLMDEINDPHLTIKAMGHQWYWSYEYTDY--EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62161295  166 SFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAM 229
Cdd:MTH00129 162 SWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSL 225
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-230 1.90e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 328.14  E-value: 1.90e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    2 DTPEPWQIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLF---EGTLIEIIWTLIPAGILVFI 78
Cdd:MTH00027  28 DANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYWnklDGSLIEVIWTLIPAFILILI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   79 AFPSLKLLYLMDE-VIDPALTIKAIGHQWYWSYEYSDYGAETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVL 157
Cdd:MTH00027 108 AFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVL 187

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62161295  158 VTAADVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAMQ 230
Cdd:MTH00027 188 ITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGRE 260
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 4-229 1.89e-113

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 323.98  E-value: 1.89e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    4 PEPWQIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFPSL 83
Cdd:MTH00098   2 AYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   84 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADV 163
Cdd:MTH00098  82 RILYMMDEINNPSLTVKTMGHQWYWSYEYTDY--EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62161295  164 LHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAM 229
Cdd:MTH00098 160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSAS 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 8-227 1.92e-111

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 319.11  E-value: 1.92e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    8 QIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFPSLKLLY 87
Cdd:MTH00008   6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167
Cdd:MTH00008  86 LMDEVSNPSITLKTIGHQWYWSYEYSDF--SNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  168 AVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWV 227
Cdd:MTH00008 164 TVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 5-226 7.69e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 317.60  E-value: 7.69e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    5 EPWQIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFPSLK 84
Cdd:MTH00185   3 HPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   85 LLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVL 164
Cdd:MTH00185  83 ILYLMDEINDPHLTIKAMGHQWYWSYEYTDY--EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62161295  165 HSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 226
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 6-232 3.30e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 313.25  E-value: 3.30e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    6 PWQIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFPSLKL 85
Cdd:MTH00076   4 PSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165
Cdd:MTH00076  84 LYLMDEINDPHLTVKAIGHQWYWSYEYTDY--EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62161295  166 SFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAMQSD 232
Cdd:MTH00076 162 SWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 95-226 1.01e-95

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: 275.60  E-value: 1.01e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  95 PALTIKAIGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS*SV 174
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDF--NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 62161295 175 KIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 226
Cdd:cd13912  79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
97-218 1.15e-81

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 239.62  E-value: 1.15e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    97 LTIKAIGHQWYWSYEYSDYGaeTIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS*SVKI 176
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFG--DLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 62161295   177 DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAV 218
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 25-226 6.74e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 229.13  E-value: 6.74e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   25 FHDQIMFILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAFPSLKLLYLMDEV-IDPALTIKAIG 103
Cdd:MTH00080  25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  104 HQWYWSYEYSDYGAetIEFDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS*SVKIDAVPGRL 183
Cdd:MTH00080 105 HQWYWSYEFSDIPG--LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGIL 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 62161295  184 NQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 226
Cdd:MTH00080 183 STLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW 225
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-230 2.84e-66

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 204.29  E-value: 2.84e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   7 WQIGFQDAASPVMEEIIFFHDQIM------FILTIILTTVFWVIVRALTTKHYHKYLFEGTLIEIIWTLIPAGILVFIAF 80
Cdd:COG1622  17 GQLSLPDPAGPIAEEIDDLFWVSLiimlviFVLVFGLLLYFAIRYRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGAETiefdsymvptsdlnngdlrllevDNRLIVPIQTQVRVLVTA 160
Cdd:COG1622  97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-----------------------VNELVLPVGRPVRFLLTS 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295 161 ADVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVAMQ 230
Cdd:COG1622 154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-228 2.21e-49

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: 160.24  E-value: 2.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    14 AASPVMEEIIFFHDQIMFILTIILTTVFWVIV------RALTTKHYHKYLFEGTLIEIIWTLIPAGILV-FIAFPSLKLL 86
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAyvvwkfRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295    87 YLMDEVIDPALTIKAIGHQWYWSYEYSDYGAETiefdsymvptsdlnngdlrllevDNRLIVPIQTQVRVLVTAADVLHS 166
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPESGFTT-----------------------VNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62161295   167 FAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWVA 228
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 59-218 3.52e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 159.73  E-value: 3.52e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295   59 EGTLIEIIWTLIPAGILVFIAFpsLKLLYLM-DEVIDPALTIKAIGHQWYWSYEYSDYGaetiEFDSYMvptSDLNNGdl 137
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVLCF--LNLNFITsDLDCFSSETIKVIGHQWYWSYEYSFGG----SYDSFM---TDDIFG-- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  138 rlleVDNRLIVPIQTQVRVLVTAADVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEA 217
Cdd:MTH00047 114 ----VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEV 189


                 .
gi 62161295  218 V 218
Cdd:MTH00047 190 V 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 122-223 3.53e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 148.43  E-value: 3.53e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  122 FDSYMVPTSDLNNGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCS 201
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|..
gi 62161295  202 EICGANHSFMPIVIEAVSLDKY 223
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVSPEAY 152
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 4-85 6.01e-31

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: 109.34  E-value: 6.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295     4 PEPWQIGFQDAASPVMEEIIFFHDQIMFILTIILTTVFWVIVRALTTKHY------HKYLFEGTLIEIIWTLIPAGILVF 77
Cdd:pfam02790   2 PTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILIL 81


                  ....*...
gi 62161295    78 IAFPSLKL 85
Cdd:pfam02790  82 IALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 96-211 6.21e-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: 107.32  E-value: 6.21e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  96 ALTIKAIGHQWYWSYEYSDYGAETIEfdsymvpTSdlnngdlrllevdNRLIVPIQTQVRVLVTAADVLHSFAVPS*SVK 175
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPDEPGRGIV-------TA-------------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGK 60

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 62161295 176 IDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 211
Cdd:cd04213  61 MDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 97-216 5.72e-28

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: 101.99  E-value: 5.72e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  97 LTIKAIGHQWYWSYEYSDygaetiefdsymvptsdlnngdlrlLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS*SVKI 176
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKV 55

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 62161295 177 DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIE 216
Cdd:cd13842  56 DAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-211 1.78e-24

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: 93.08  E-value: 1.78e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  96 ALTIKAIGHQWYWSYEYSdygaetiefdsymvptsdlnNGDlrllEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS*SVK 175
Cdd:cd13915   1 ALEIQVTGRQWMWEFTYP--------------------NGK----REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIK 56

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 62161295 176 IDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 211
Cdd:cd13915  57 QDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-211 6.00e-24

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: 91.93  E-value: 6.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  96 ALTIKAIGHQWYWSYEYSDYGAETIEFDsymvptsDLNNGDLRLlevdnrlivPIQTQVRVLVTAADVLHSFAVPS*SVK 175
Cdd:cd13919   1 ALVVEVTAQQWAWTFRYPGGDGKLGTDD-------DVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVK 64

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 62161295 176 IDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 211
Cdd:cd13919  65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 85-227 9.00e-24

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: 92.52  E-value: 9.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  85 LLYLMD---EVIDPALTIKAIGHQWYWSYEYSDYGAETiefdsymvptsdlnngdlrllevdNRLIVPIQTQVRVLVTAA 161
Cdd:cd13918  18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTG------------------------NTLRVPADTPIALRVTST 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62161295 162 DVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWV 227
Cdd:cd13918  74 DVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-227 5.72e-20

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 81.69  E-value: 5.72e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  98 TIKAIGHQWYWSYEYSDYGAETiefdsymvptsdlnngdlrllevDNRLIVPIQTQVRVLVTAADVLHSFAVPS*SVKID 177
Cdd:cd13914   2 EIEVEAYQWGWEFSYPEANVTT-----------------------SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 62161295 178 AVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWV 227
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 ...
 144-211 4.56e-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: 57.58  E-value: 4.56e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62161295 144 NRLIVPIQTQVRVLVTAADVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 211
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 97-218 5.51e-08

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: 49.47  E-value: 5.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  97 LTIKAIGHQWYWSYEYSDYGAETIefdsymvptsdlnngdlrllevdNRLIVPIQTQVRVLVTAADVLHSFAVPS*SVKI 176
Cdd:cd04212   1 LEIQVVSLDWKWLFIYPEQGIATV-----------------------NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQI 57

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 62161295 177 DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAV 218
Cdd:cd04212  58 YAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-211 6.16e-06

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 43.52  E-value: 6.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295  98 TIKAIGHQWYWSYEYSDYGA-ETIEFDsymvptsdlnngdlrllevdnrlivpiqtqvrvlVTAADVLHSFAVPS*SVKI 176
Cdd:cd13916   2 VVAVTGHQWYWELSRTEIPAgKPVEFR----------------------------------VTSADVNHGFGIYDPDMRL 47

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 62161295 177 ----DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 211
Cdd:cd13916  48 laqtQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 133-216 2.45e-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: 39.52  E-value: 2.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161295 133 NNGDLRLLEVDNRLIVPIQTQVRV-LVTAADVLHSFAVPS*SVKIDA---------------VPGRLNQTSFFIKRPGVF 196
Cdd:cd00920  12 FTYNGVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVY 91

                        90       100
                ....*....|....*....|
gi 62161295 197 YGQCSEICGaNHSFMPIVIE 216
Cdd:cd00920  92 WFYCTIPGH-NHAGMVGTIN 110
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 154-211 5.23e-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: 37.98  E-value: 5.23e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62161295 154 VRVLVT----AADVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 211
Cdd:cd04223  26 VTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 155-211 6.48e-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: 35.04  E-value: 6.48e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62161295 155 RVLVTAADVLHSFAVPS*SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 211
Cdd:cd13917  25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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