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Conserved domains on  [gi|90903249|ref|NP_058861|]
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phospholipid hydroperoxide glutathione peroxidase isoform A precursor [Rattus norvegicus]

Protein Classification

glutathione peroxidase( domain architecture ID 10085912)

glutathione peroxidase catalyzes the reduction of hydroperoxides using GSH as a specific electron donor

CATH:  3.40.30.10
EC:  1.11.1.-
Gene Ontology:  GO:0043295|GO:0004602|GO:0006979
SCOP:  4000042

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
40-193 6.11e-84

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


:

Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 244.73  E-value: 6.11e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249  40 SMHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGkTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEF 119
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCG-FTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90903249 120 AAG-YNVRFDMYSKICVNGDDAHPLWKWMKVQPKgrGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDL 193
Cdd:cd00340  80 CETnYGVTFPMFAKIDVNGENAHPLYKYLKEEAP--GLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
40-193 6.11e-84

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 244.73  E-value: 6.11e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249  40 SMHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGkTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEF 119
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCG-FTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90903249 120 AAG-YNVRFDMYSKICVNGDDAHPLWKWMKVQPKgrGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDL 193
Cdd:cd00340  80 CETnYGVTFPMFAKIDVNGENAHPLYKYLKEEAP--GLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
40-193 3.45e-70

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 210.32  E-value: 3.45e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249  40 SMHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGKTDvNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEF 119
Cdd:COG0386   3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90903249 120 -AAGYNVRFDMYSKICVNGDDAHPLWKWMKVQPKGrGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQ--VIEKDL 193
Cdd:COG0386  82 cSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPG-LLGGGDIKWNFTKFLIDRDGNVVARFAPTTKPEdpELEAAI 157
GSHPx pfam00255
Glutathione peroxidase;
41-148 7.08e-59

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 179.86  E-value: 7.08e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249    41 MHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGKTDvNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEFA 120
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
                          90       100
                  ....*....|....*....|....*....
gi 90903249   121 AG-YNVRFDMYSKICVNGDDAHPLWKWMK 148
Cdd:pfam00255  80 PGgYGVTFPLFSKIEVNGEKAHPVYKFLK 108
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
39-193 2.09e-57

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 180.87  E-value: 2.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249   39 RSMHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGKTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKE 118
Cdd:PLN02399  77 KSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQ 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90903249  119 FAAG-YNVRFDMYSKICVNGDDAHPLWKWMKvqPKGRGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDL 193
Cdd:PLN02399 157 FACTrFKAEFPIFDKVDVNGPSTAPVYQFLK--SNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDI 230
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
40-193 1.97e-44

putative glutathione peroxidase Gpx7; This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7.


Pssm-ID: 131592 [Multi-domain]  Cd Length: 153  Bit Score: 144.98  E-value: 1.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249    40 SMHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGKTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEF 119
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90903249   120 A-AGYNVRFDMYSKICVNGDDAHPLWKWMkVQPKGRgmlgnAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDL 193
Cdd:TIGR02540  81 ArRNYGVTFPMFSKIKILGSEAEPAFRFL-VDSSKK-----EPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEI 149
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
40-193 6.11e-84

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 244.73  E-value: 6.11e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249  40 SMHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGkTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEF 119
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCG-FTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90903249 120 AAG-YNVRFDMYSKICVNGDDAHPLWKWMKVQPKgrGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDL 193
Cdd:cd00340  80 CETnYGVTFPMFAKIDVNGENAHPLYKYLKEEAP--GLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
40-193 3.45e-70

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 210.32  E-value: 3.45e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249  40 SMHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGKTDvNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEF 119
Cdd:COG0386   3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90903249 120 -AAGYNVRFDMYSKICVNGDDAHPLWKWMKVQPKGrGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQ--VIEKDL 193
Cdd:COG0386  82 cSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPG-LLGGGDIKWNFTKFLIDRDGNVVARFAPTTKPEdpELEAAI 157
GSHPx pfam00255
Glutathione peroxidase;
41-148 7.08e-59

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 179.86  E-value: 7.08e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249    41 MHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGKTDvNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEFA 120
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
                          90       100
                  ....*....|....*....|....*....
gi 90903249   121 AG-YNVRFDMYSKICVNGDDAHPLWKWMK 148
Cdd:pfam00255  80 PGgYGVTFPLFSKIEVNGEKAHPVYKFLK 108
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
39-193 2.09e-57

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 180.87  E-value: 2.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249   39 RSMHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGKTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKE 118
Cdd:PLN02399  77 KSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQ 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90903249  119 FAAG-YNVRFDMYSKICVNGDDAHPLWKWMKvqPKGRGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDL 193
Cdd:PLN02399 157 FACTrFKAEFPIFDKVDVNGPSTAPVYQFLK--SNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDI 230
PLN02412 PLN02412
probable glutathione peroxidase
39-193 5.73e-56

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 174.79  E-value: 5.73e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249   39 RSMHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGKTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKE 118
Cdd:PLN02412   7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90903249  119 FAAG-YNVRFDMYSKICVNGDDAHPLWKWMKVQpKGrGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDL 193
Cdd:PLN02412  87 TVCTrFKAEFPIFDKVDVNGKNTAPLYKYLKAE-KG-GLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDI 160
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
38-193 8.84e-51

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 161.85  E-value: 8.84e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249   38 ARSMHEFAAKDIDGHMVCLDKYRGCVC-IVTNVASQUGKTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEI 116
Cdd:PTZ00256  17 TKSFFEFEAIDIDGQLVQLSKFKGKKAiIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249  117 KEFA-AGYNVRFDMYSKICVNGDDAHPLWKWMKVQPKG-RGMLGNA--IKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKD 192
Cdd:PTZ00256  97 KEYVqKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELfQNNTNEArqIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQD 176

                 .
gi 90903249  193 L 193
Cdd:PTZ00256 177 I 177
btuE PRK10606
putative glutathione peroxidase; Provisional
47-190 1.55e-45

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 148.77  E-value: 1.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249   47 KDIDGHMVCLDKYRGCVCIVTNVASQUGKTDvNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEFAAG-YNV 125
Cdd:PRK10606  11 TTIDGEVTTLEKYAGNVLLIVNVASKCGLTP-QYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYCRTtWGV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249  126 RFDMYSKICVNGDDAHPLWKWM------KVQPKGRGML------GNA------IKWNFTKFLIDKNGCVVKRYGP-M--E 184
Cdd:PRK10606  90 TFPMFSKIEVNGEGRHPLYQKLiaaaptAVAPEESGFYarmvskGRAplypddILWNFEKFLVGRDGQVIQRFSPdMtpE 169

                 ....*.
gi 90903249  185 EPQVIE 190
Cdd:PRK10606 170 DPIVME 175
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
40-193 1.97e-44

putative glutathione peroxidase Gpx7; This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7.


Pssm-ID: 131592 [Multi-domain]  Cd Length: 153  Bit Score: 144.98  E-value: 1.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249    40 SMHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGKTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEF 119
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90903249   120 A-AGYNVRFDMYSKICVNGDDAHPLWKWMkVQPKGRgmlgnAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDL 193
Cdd:TIGR02540  81 ArRNYGVTFPMFSKIKILGSEAEPAFRFL-VDSSKK-----EPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEI 149
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
39-193 2.31e-43

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 143.45  E-value: 2.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249   39 RSMHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGKTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKE 118
Cdd:PTZ00056  17 KSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRK 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90903249  119 FAAGYNVRFDMYSKICVNGDDAHPLWKWMKVQPKG----RGMLgNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDL 193
Cdd:PTZ00056  97 FNDKNKIKYNFFEPIEVNGENTHELFKFLKANCDSmhdeNGTL-KAIGWNFGKFLVNKSGNVVAYFSPRTEPLELEKKI 174
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
43-193 4.29e-07

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 47.17  E-value: 4.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903249  43 EFAAKDIDGHMVCLDKYRGCVCIVTNVASQUG--KTDVNytQLVDLHARYAECGLRILAFpcnqfgrqEPGSNQEIKEFA 120
Cdd:COG1225   3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPgcTAELP--ELRDLYEEFKDKGVEVLGV--------SSDSDEAHKKFA 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90903249 121 AGYNVRFDMYSkicvngDDAHPLWKWMKVqPKGRGMlgnaikwnftkFLIDKNGCVVKRY-GPMEEPQVIEKDL 193
Cdd:COG1225  73 EKYGLPFPLLS------DPDGEVAKAYGV-RGTPTT-----------FLIDPDGKIRYVWvGPVDPRPHLEEVL 128
 
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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