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Conserved domains on  [gi|497382044|ref|WP_009696257|]
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MULTISPECIES: glutathione peroxidase [Vibrio]

Protein Classification

glutathione peroxidase( domain architecture ID 10785352)

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
PubMed:  11215509
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 25-181 5.21e-73

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


:

Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 216.87  E-value: 5.21e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  25 CPDILQGKQRLLNStEEIALCDaFKGKTLLVVNTASQCGFTPQFEQLEQLHQTYKDQNFSVVGFPSNDF-RQDRGSEEKT 103
Cdd:COG0386    1 MMSIYDFSVTTLDG-EPVSLSD-YKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044 104 AKICYLDYGVTFPMMAKTSVLGEDANPVFTQISTQAGIT-----PKWNFYKFLINKEGKVVATFPSSTSPTSTTLTNMIE 178
Cdd:COG0386   79 AEFCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLlgggdIKWNFTKFLIDRDGNVVARFAPTTKPEDPELEAAIE 158


                 ...
gi 497382044 179 QQL 181
Cdd:COG0386  159 KLL 161
 
Name Accession Description Interval E-value
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 25-181 5.21e-73

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 216.87  E-value: 5.21e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  25 CPDILQGKQRLLNStEEIALCDaFKGKTLLVVNTASQCGFTPQFEQLEQLHQTYKDQNFSVVGFPSNDF-RQDRGSEEKT 103
Cdd:COG0386    1 MMSIYDFSVTTLDG-EPVSLSD-YKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044 104 AKICYLDYGVTFPMMAKTSVLGEDANPVFTQISTQAGIT-----PKWNFYKFLINKEGKVVATFPSSTSPTSTTLTNMIE 178
Cdd:COG0386   79 AEFCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLlgggdIKWNFTKFLIDRDGNVVARFAPTTKPEDPELEAAIE 158


                 ...
gi 497382044 179 QQL 181
Cdd:COG0386  159 KLL 161
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 40-162 1.92e-60

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: 184.64  E-value: 1.92e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  40 EEIALCDaFKGKTLLVVNTASQCGFTPQFEQLEQLHQTYKDQNFSVVGFPSNDF-RQDRGSEEKTAKICYLDYGVTFPMM 118
Cdd:cd00340   13 EPVSLSK-YKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEIKEFCETNYGVTFPMF 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 497382044 119 AKTSVLGEDANPVFTQISTQAG----ITPKWNFYKFLINKEGKVVATF 162
Cdd:cd00340   92 AKIDVNGENAHPLYKYLKEEAPgllgKDIKWNFTKFLVDRDGEVVKRF 139
btuE PRK10606
putative glutathione peroxidase; Provisional
 46-181 1.41e-39

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 132.98  E-value: 1.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  46 DAFKGKTLLVVNTASQCGFTPQFEQLEQLHQTYKDQNFSVVGFPSNDFR-QDRGSEEKTAKICYLDYGVTFPMMAKTSVL 124
Cdd:PRK10606  21 EKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLgQEPGSDEEIKTYCRTTWGVTFPMFSKIEVN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044 125 GEDANPVFTQISTQA------------------GITPK------WNFYKFLINKEGKVVATFPSSTSPTSTTLTNMIEQQ 180
Cdd:PRK10606 101 GEGRHPLYQKLIAAAptavapeesgfyarmvskGRAPLypddilWNFEKFLVGRDGQVIQRFSPDMTPEDPIVMESIKLA 180


                 .
gi 497382044 181 L 181
Cdd:PRK10606 181 L 181
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 48-159 3.12e-32

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: 113.01  E-value: 3.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044   48 FKGKTLLVVNTASQCGFTPQ-FEQLEQLHQTYKDQNFSVVGFPSNDF-RQDRGSEEKTAKICYLDYGVTFPMMAKTSVLG 125
Cdd:TIGR02540  20 YRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFgESEPDSSKEIESFARRNYGVTFPMFSKIKILG 99

                          90       100       110
                  ....*....|....*....|....*....|....
gi 497382044  126 EDANPVFTQISTQAGITPKWNFYKFLINKEGKVV 159
Cdd:TIGR02540 100 SEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVV 133
GSHPx pfam00255
Glutathione peroxidase;
46-133 1.73e-31

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 109.75  E-value: 1.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044   46 DAFKGKTLLVVNTASQCGFTPQFEQLEQLHQTYKDQNFSVVGFPSNDF-RQDRGSEEKTAKICYLDYGVTFPMMAKTSVL 124
Cdd:pfam00255  17 DQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFgKQEPGSNEEIKYFCPGGYGVTFPLFSKIEVN 96


                  ....*....
gi 497382044  125 GEDANPVFT 133
Cdd:pfam00255  97 GEKAHPVYK 105
 
Name Accession Description Interval E-value
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 25-181 5.21e-73

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 216.87  E-value: 5.21e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  25 CPDILQGKQRLLNStEEIALCDaFKGKTLLVVNTASQCGFTPQFEQLEQLHQTYKDQNFSVVGFPSNDF-RQDRGSEEKT 103
Cdd:COG0386    1 MMSIYDFSVTTLDG-EPVSLSD-YKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044 104 AKICYLDYGVTFPMMAKTSVLGEDANPVFTQISTQAGIT-----PKWNFYKFLINKEGKVVATFPSSTSPTSTTLTNMIE 178
Cdd:COG0386   79 AEFCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLlgggdIKWNFTKFLIDRDGNVVARFAPTTKPEDPELEAAIE 158


                 ...
gi 497382044 179 QQL 181
Cdd:COG0386  159 KLL 161
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 40-162 1.92e-60

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: 184.64  E-value: 1.92e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  40 EEIALCDaFKGKTLLVVNTASQCGFTPQFEQLEQLHQTYKDQNFSVVGFPSNDF-RQDRGSEEKTAKICYLDYGVTFPMM 118
Cdd:cd00340   13 EPVSLSK-YKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEIKEFCETNYGVTFPMF 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 497382044 119 AKTSVLGEDANPVFTQISTQAG----ITPKWNFYKFLINKEGKVVATF 162
Cdd:cd00340   92 AKIDVNGENAHPLYKYLKEEAPgllgKDIKWNFTKFLVDRDGEVVKRF 139
btuE PRK10606
putative glutathione peroxidase; Provisional
 46-181 1.41e-39

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 132.98  E-value: 1.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  46 DAFKGKTLLVVNTASQCGFTPQFEQLEQLHQTYKDQNFSVVGFPSNDFR-QDRGSEEKTAKICYLDYGVTFPMMAKTSVL 124
Cdd:PRK10606  21 EKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLgQEPGSDEEIKTYCRTTWGVTFPMFSKIEVN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044 125 GEDANPVFTQISTQA------------------GITPK------WNFYKFLINKEGKVVATFPSSTSPTSTTLTNMIEQQ 180
Cdd:PRK10606 101 GEGRHPLYQKLIAAAptavapeesgfyarmvskGRAPLypddilWNFEKFLVGRDGQVIQRFSPDMTPEDPIVMESIKLA 180


                 .
gi 497382044 181 L 181
Cdd:PRK10606 181 L 181
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 48-159 3.12e-32

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: 113.01  E-value: 3.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044   48 FKGKTLLVVNTASQCGFTPQ-FEQLEQLHQTYKDQNFSVVGFPSNDF-RQDRGSEEKTAKICYLDYGVTFPMMAKTSVLG 125
Cdd:TIGR02540  20 YRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFgESEPDSSKEIESFARRNYGVTFPMFSKIKILG 99

                          90       100       110
                  ....*....|....*....|....*....|....
gi 497382044  126 EDANPVFTQISTQAGITPKWNFYKFLINKEGKVV 159
Cdd:TIGR02540 100 SEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVV 133
GSHPx pfam00255
Glutathione peroxidase;
46-133 1.73e-31

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 109.75  E-value: 1.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044   46 DAFKGKTLLVVNTASQCGFTPQFEQLEQLHQTYKDQNFSVVGFPSNDF-RQDRGSEEKTAKICYLDYGVTFPMMAKTSVL 124
Cdd:pfam00255  17 DQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFgKQEPGSNEEIKYFCPGGYGVTFPLFSKIEVN 96


                  ....*....
gi 497382044  125 GEDANPVFT 133
Cdd:pfam00255  97 GEKAHPVYK 105
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 48-162 2.30e-25

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 96.37  E-value: 2.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  48 FKG-KTLLVVNTASQCGFTPQ-FEQLEQLHQTYKDQNFSVVGFPSNDFR-QDRGSEEKTAKICYLDYGVTFPMMAKTSVL 124
Cdd:PTZ00256  38 FKGkKAIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMeQEPWDEPEIKEYVQKKFNVDFPLFQKIEVN 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 497382044 125 GEDANPVFT---------QISTQAGITPKWNFYKFLINKEGKVVATF 162
Cdd:PTZ00256 118 GENTHEIYKylrrnselfQNNTNEARQIPWNFAKFLIDGQGKVVKYF 164
PLN02412 PLN02412
probable glutathione peroxidase
 46-162 4.28e-25

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 95.06  E-value: 4.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  46 DAFKGKTLLVVNTASQCGFT-PQFEQLEQLHQTYKDQNFSVVGFPSNDFR-QDRGSEEKTAKICYLDYGVTFPMMAKTSV 123
Cdd:PLN02412  25 NQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLgQEPGSNEEIQQTVCTRFKAEFPIFDKVDV 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 497382044 124 LGEDANPVFTQISTQAG----ITPKWNFYKFLINKEGKVVATF 162
Cdd:PLN02412 105 NGKNTAPLYKYLKAEKGglfgDAIKWNFTKFLVSKEGKVVQRY 147
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 46-159 1.23e-22

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 90.34  E-value: 1.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  46 DAFKGKTLLVVNTASQCGFTP-QFEQLEQLHQTYKDQNFSVVGFPSNDFR-QDRGSEEKTAKICYLDYGVTFPMMAKTSV 123
Cdd:PLN02399  95 SKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGgQEPGSNPEIKQFACTRFKAEFPIFDKVDV 174

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 497382044 124 LGEDANPVFTQISTQAG----ITPKWNFYKFLINKEGKVV 159
Cdd:PLN02399 175 NGPSTAPVYQFLKSNAGgflgDLIKWNFEKFLVDKNGKVV 214
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 48-162 3.61e-19

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 80.67  E-value: 3.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  48 FKGKTLLVVNTASQCGFTPQ-FEQLEQLHQTYKDQNFSVVGFPSNDF-RQDRgseEKTAKICYLD--YGVTFPMMAKTSV 123
Cdd:PTZ00056  37 LKNKVLMITNSASKCGLTKKhVDQMNRLHSVFNPLGLEILAFPTSQFlNQEF---PNTKDIRKFNdkNKIKYNFFEPIEV 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497382044 124 LGEDANPVFTQISTQagiTP------------KWNFYKFLINKEGKVVATF 162
Cdd:PTZ00056 114 NGENTHELFKFLKAN---CDsmhdengtlkaiGWNFGKFLVNKSGNVVAYF 161
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
40-162 7.74e-06

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 43.32  E-value: 7.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  40 EEIALCDaFKGKTLLVVNTASQCGF-TPQFEQLEQLHQTYKDQNFSVVG-FPSNDFRQdrgseEKTAKicylDYGVTFPM 117
Cdd:COG1225   12 KTVSLSD-LRGKPVVLYFYATWCPGcTAELPELRDLYEEFKDKGVEVLGvSSDSDEAH-----KKFAE----KYGLPFPL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 497382044 118 maktsVLGEDAnpvftQISTQAGI--TPkwnfYKFLINKEGKVVATF 162
Cdd:COG1225   82 -----LSDPDG-----EVAKAYGVrgTP----TTFLIDPDGKIRYVW 114
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 46-162 6.22e-05

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 41.21  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044  46 DAFKGKTLLVVNTASQCGftP---QFEQLEQLHQTYKDqnFSVVGFpsndfrqDRGSEEKTAKICYLDYGVTFPmmakts 122
Cdd:COG0526   24 ADLKGKPVLVNFWATWCP--PcraEMPVLKELAEEYGG--VVFVGV-------DVDENPEAVKAFLKELGLPYP------ 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 497382044 123 VLGEDANPVFTQISTQAgiTPkwnfYKFLINKEGKVVATF 162
Cdd:COG0526   87 VLLDPDGELAKAYGVRG--IP----TTVLIDKDGKIVARH 120
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 47-162 4.02e-04

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 38.89  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497382044   47 AFKGKTLLVVNTASQcgFTP----QFEQLEQLHQTYKDQNFSVVGF--PSNDFRQDRGSEEktakicyldYGVTFPMMAK 120
Cdd:pfam08534  25 DFKGKKVVLNFWPGA--FCPtcsaEHPYLEKLNELYKEKGVDVVAVnsDNDAFFVKRFWGK---------EGLPFPFLSD 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 497382044  121 TSV-LGEDANPVFTQISTQAGITPKWnfykFLINKEGKVVATF 162
Cdd:pfam08534  94 GNAaFTKALGLPIEEDASAGLRSPRY----AVIDEDGKVVYLF 132
 
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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