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Conserved domains on  [gi|148728413|gb|ABR08681|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Hetrodes pupus]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 17-171 3.19e-79

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 234.72  E-value: 3.19e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  17 TLFFNKITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYM 96
Cdd:MTH00154  44 SLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYM 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148728413  97 LPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00154 123 IPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCS 197
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 17-171 3.19e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 234.72  E-value: 3.19e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  17 TLFFNKITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYM 96
Cdd:MTH00154  44 SLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYM 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148728413  97 LPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00154 123 IPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCS 197
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 68-171 5.68e-68

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: 202.80  E-value: 5.68e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  68 ITIKTIGHQWYWSYEYTDYSTpYEFDSYMLPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVD 81

                         90       100
                 ....*....|....*....|....
gi 148728413 148 AAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:cd13912   82 AVPGRLNQTSFFIERPGVYYGQCS 105
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
68-171 4.64e-61

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 184.92  E-value: 4.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413   68 ITIKTIGHQWYWSYEYTDYSTpYEFDSYMLPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100
                  ....*....|....*....|....
gi 148728413  148 AAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCS 103
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
68-171 8.18e-26

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 98.36  E-value: 8.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  68 ITIKTIGHQWYWSYEYTDYSTpyefdsymlpynemnmngfrllDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:COG1622  113 LTVEVTGYQWKWLFRYPDQGI----------------------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                         90       100
                 ....*....|....*....|....
gi 148728413 148 AAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:COG1622  171 AIPGRVTELWFTADKPGTYRGQCA 194
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 68-170 7.16e-23

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: 89.75  E-value: 7.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413   68 ITIKTIGHQWYWSYEYTDYstpyefdsymlpynemnmnGFRlldVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:TIGR02866  91 LKVKVTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKID 148

                          90       100
                  ....*....|....*....|...
gi 148728413  148 AAPGRLNQTGLFINRPGLFYGQC 170
Cdd:TIGR02866 149 AIPGQTNALWFNADEPGVYYGFC 171
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 17-171 3.19e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 234.72  E-value: 3.19e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  17 TLFFNKITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYM 96
Cdd:MTH00154  44 SLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYM 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148728413  97 LPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00154 123 IPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCS 197
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 68-171 5.68e-68

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: 202.80  E-value: 5.68e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  68 ITIKTIGHQWYWSYEYTDYSTpYEFDSYMLPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVD 81

                         90       100
                 ....*....|....*....|....
gi 148728413 148 AAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:cd13912   82 AVPGRLNQTSFFIERPGVYYGQCS 105
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 17-171 2.55e-67

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 204.70  E-value: 2.55e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  17 TLFFNKITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYM 96
Cdd:MTH00008  44 SLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-LEFDSYM 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148728413  97 LPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00008 123 LPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCS 197
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 18-171 2.51e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 199.39  E-value: 2.51e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  18 LFFNKITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYML 97
Cdd:MTH00140  45 LLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMV 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148728413  98 PYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00140 124 PENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCS 197
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 17-171 3.01e-64

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 196.48  E-value: 3.01e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  17 TLFFNKITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYM 96
Cdd:MTH00139  44 SLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-LSFDSYM 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148728413  97 LPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00139 123 IPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCS 197
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 61-171 2.69e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 191.67  E-value: 2.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  61 DETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYMLPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIP 140
Cdd:MTH00117  88 DEINNPHLTIKAIGHQWYWSYEYTDYKD-LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVP 166

                         90       100       110
                 ....*....|....*....|....*....|.
gi 148728413 141 SFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00117 167 SLGVKTDAVPGRLNQTSFITTRPGVFYGQCS 197
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
68-171 4.64e-61

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 184.92  E-value: 4.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413   68 ITIKTIGHQWYWSYEYTDYSTpYEFDSYMLPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100
                  ....*....|....*....|....
gi 148728413  148 AAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCS 103
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 17-171 8.87e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 187.99  E-value: 8.87e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  17 TLFFNKITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYM 96
Cdd:MTH00038  44 SLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYND-LEFDSYM 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148728413  97 LPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00038 123 VPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCS 197
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 18-171 9.83e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 187.50  E-value: 9.83e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  18 LFFNKITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYML 97
Cdd:MTH00168  45 LVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-LEFDSYMV 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148728413  98 PYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00168 124 PTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCS 197
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 21-171 2.80e-60

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 186.88  E-value: 2.80e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  21 NKITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTP-YEFDSYMLPY 99
Cdd:MTH00023  57 GKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGEtLEFDSYMVPT 136

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148728413 100 NEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00023 137 SDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCS 208
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 21-171 5.63e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 178.44  E-value: 5.63e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  21 NKITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTP-YEFDSYMLPY 99
Cdd:MTH00051  50 TKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDtIEFDSYMIPT 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148728413 100 NEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00051 130 SDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCS 201
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 22-171 6.87e-56

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 175.29  E-value: 6.87e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  22 KITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYMLPYNE 101
Cdd:MTH00098  49 KLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYED-LSFDSYMIPTSD 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413 102 MNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00098 128 LKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCS 197
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 22-171 4.35e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 173.53  E-value: 4.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  22 KITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYMLPYNE 101
Cdd:MTH00185  49 KLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQ-LEFDSYMTPTQD 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413 102 MNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00185 128 LTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCS 197
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 22-171 2.65e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 171.44  E-value: 2.65e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  22 KITHRYFLVEQTIETLWTILPIITLILIMLFSLRLLYLLDETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYMLPYNE 101
Cdd:MTH00129  49 KLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYED-LGFDSYMIPTQD 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413 102 MNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00129 128 LTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCS 197
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 61-171 5.07e-53

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 168.03  E-value: 5.07e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  61 DETMNYKITIKTIGHQWYWSYEYTDYSTpYEFDSYMLPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIP 140
Cdd:MTH00076  88 DEINDPHLTVKAIGHQWYWSYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVP 166

                         90       100       110
                 ....*....|....*....|....*....|.
gi 148728413 141 SFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00076 167 SLGIKTDAIPGRLNQTSFIASRPGVYYGQCS 197
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 68-171 1.01e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 148.25  E-value: 1.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  68 ITIKTIGHQWYWSYEYTDYSTP-YEFDSYMLPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKI 146
Cdd:MTH00027 127 ITIKVTGHQWYWSYSYEDYGEKnIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKM 206

                         90       100
                 ....*....|....*....|....*
gi 148728413 147 DAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00027 207 DAVPGRINETGFLIKRPGIFYGQCS 231
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 62-171 5.70e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 137.45  E-value: 5.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  62 ETMNYK--ITIKTIGHQWYWSYEYTDYSTpYEFDSYMLPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTI 139
Cdd:MTH00080  90 GLMNLDsnLTVKVTGHQWYWSYEFSDIPG-LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWAL 168

                         90       100       110
                 ....*....|....*....|....*....|..
gi 148728413 140 PSFGVKIDAAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00080 169 PSLSIKMDAMSGILSTLCYSFPMPGVFYGQCS 200
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 90-171 1.26e-27

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 101.05  E-value: 1.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  90 YEFDSYMLPYNEMNMNGFRLLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQ 169
Cdd:PTZ00047  49 YSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128


                 ..
gi 148728413 170 CS 171
Cdd:PTZ00047 129 CS 130
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 69-171 1.20e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 99.64  E-value: 1.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  69 TIKTIGHQWYWSYEYTDYStpyEFDSYMLPYNEMnmngfrlldVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDA 148
Cdd:MTH00047  83 TIKVIGHQWYWSYEYSFGG---SYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDA 150

                         90       100
                 ....*....|....*....|...
gi 148728413 149 APGRLNQTGLFINRPGLFYGQCS 171
Cdd:MTH00047 151 IPGRINHLFFCPDRHGVFVGYCS 173
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
68-171 8.18e-26

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 98.36  E-value: 8.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  68 ITIKTIGHQWYWSYEYTDYSTpyefdsymlpynemnmngfrllDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:COG1622  113 LTVEVTGYQWKWLFRYPDQGI----------------------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                         90       100
                 ....*....|....*....|....
gi 148728413 148 AAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:COG1622  171 AIPGRVTELWFTADKPGTYRGQCA 194
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 68-170 7.16e-23

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: 89.75  E-value: 7.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413   68 ITIKTIGHQWYWSYEYTDYstpyefdsymlpynemnmnGFRlldVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:TIGR02866  91 LKVKVTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKID 148

                          90       100
                  ....*....|....*....|...
gi 148728413  148 AAPGRLNQTGLFINRPGLFYGQC 170
Cdd:TIGR02866 149 AIPGQTNALWFNADEPGVYYGFC 171
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 68-171 3.25e-18

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: 75.03  E-value: 3.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  68 ITIKTIGHQWYWSYEYTDYSTPyefdsymlpynemnmngfrlldvdNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNVRTP------------------------NEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                         90       100
                 ....*....|....*....|....
gi 148728413 148 AAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:cd13842   57 AVPGYTSELWFVADKPGTYTIICA 80
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 68-171 1.61e-15

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: 68.03  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  68 ITIKTIGHQWYWSYEYTDYStPYEFDSYmlpyNEMnmngfrlldvdnrtILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEP-GRGIVTA----NEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                         90       100
                 ....*....|....*....|....
gi 148728413 148 AAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:cd04213   63 MIPGRTNRLWLQADEPGVYRGQCA 86
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 68-171 1.95e-14

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 65.35  E-value: 1.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  68 ITIKTIGHQWYWSYEYTDYSTPYEFDSyMLPYNEMNmngfrlldvdnrtiLPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDGKLGTDD-DVTSPELH--------------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                         90       100
                 ....*....|....*....|....
gi 148728413 148 AAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:cd13919   67 AVPGRTTRLWFTPTREGEYEVRCA 90
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 68-171 4.54e-11

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: 56.48  E-value: 4.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  68 ITIKTIGHQWYWSYEYTdystpyefdsymlpynemnmNGFRlldVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:cd13915    2 LEIQVTGRQWMWEFTYP--------------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                         90       100
                 ....*....|....*....|....
gi 148728413 148 AAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:cd13915   59 VVPGRYTYLWFEATKPGEYDLFCT 82
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 68-170 1.15e-09

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: 53.61  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  68 ITIKTIGHQWYWSYEYtdySTPYEFDSYMlpynemnmngfrlldvdnrtILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:cd13918   33 LEVEVEGFQFGWQFEY---PNGVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPELRVKAD 89

                         90       100
                 ....*....|....*....|...
gi 148728413 148 AAPGRLNQTGLFINRPGLFYGQC 170
Cdd:cd13918   90 AIPGEYTSTWFEADEPGTYEAKC 112
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 68-171 3.85e-08

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: 48.94  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728413  68 ITIKTIGHQWYWSYEYTDYStpyefdsymlpynemnmngfrlLDVDNRTILPFNTQIRMLVTAADVLHSWTIPSFGVKID 147
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEAN----------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                         90       100
                 ....*....|....*....|....
gi 148728413 148 AAPGRLNQTGLFINRPGLFYGQCS 171
Cdd:cd13914   59 AFPGQYNTIKTEATEEGEYQLYCA 82
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 114-169 5.80e-05

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: 40.22  E-value: 5.80e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148728413 114 NRTILPFNTQIRMLVTAADVLHSWTIPSFGVKIDAAPGRLNQTGLFINRPGLFYGQ 169
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80
 
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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