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Conserved domains on  [gi|41406084|ref|NP_000572|]
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glutathione peroxidase 1 isoform 1 [Homo sapiens]

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

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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 ...
15-192 3.30e-72

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: 215.46  E-value: 3.30e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084  15 SVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILN 94
Cdd:cd00340   1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084  95 SLKYVRPgggfePNFMLFEKCEVNGAGAHPLFAFLREALPAPsddatalmtdpklitwspvCRNDVAWNFEKFLVGPDGV 174
Cdd:cd00340  79 FCETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGL-------------------LGKDIKWNFTKFLVDRDGE 134
                       170
                ....*....|....*...
gi 41406084 175 PLRRYSRRFQTIDIEPDI 192
Cdd:cd00340 135 VVKRFAPTTDPEELEKDI 152
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
15-192 3.30e-72

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: 215.46  E-value: 3.30e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084  15 SVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILN 94
Cdd:cd00340   1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084  95 SLKYVRPgggfePNFMLFEKCEVNGAGAHPLFAFLREALPAPsddatalmtdpklitwspvCRNDVAWNFEKFLVGPDGV 174
Cdd:cd00340  79 FCETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGL-------------------LGKDIKWNFTKFLVDRDGE 134
                       170
                ....*....|....*...
gi 41406084 175 PLRRYSRRFQTIDIEPDI 192
Cdd:cd00340 135 VVKRFAPTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
16-130 2.05e-59

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 181.40  E-value: 2.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084    16 VYAFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTVrDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEIlns 95
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI--- 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 41406084    96 lKYVRPgGGFEPNFMLFEKCEVNGAGAHPLFAFLR 130
Cdd:pfam00255  76 -KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
15-196 3.98e-56

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 174.88  E-value: 3.98e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084  15 SVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILN 94
Cdd:COG0386   3 SIYDFSVTTL-DGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084  95 --SLKY-VrpgggfepNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDatalmtdpklitwspvcrNDVAWNFEKFLVGP 171
Cdd:COG0386  81 fcSLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG------------------GDIKWNFTKFLIDR 134
                       170       180
                ....*....|....*....|....*..
gi 41406084 172 DGVPLRRYSRRF--QTIDIEPDIEALL 196
Cdd:COG0386 135 DGNVVARFAPTTkpEDPELEAAIEKLL 161
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
15-198 6.45e-37

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 126.80  E-value: 6.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084   15 SVYAFSARPLAGGEpVSLGSLRG-KVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEIL 93
Cdd:PTZ00256  19 SFFEFEAIDIDGQL-VQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084   94 NslkYVRPggGFEPNFMLFEKCEVNGAGAHPLFAFLR---EALPAPSDDATalmtdpklitwspvcrnDVAWNFEKFLVG 170
Cdd:PTZ00256  98 E---YVQK--KFNVDFPLFQKIEVNGENTHEIYKYLRrnsELFQNNTNEAR-----------------QIPWNFAKFLID 155
                        170       180
                 ....*....|....*....|....*...
gi 41406084  171 PDGVPLRRYSRRFQTIDIEPDIEALLSQ 198
Cdd:PTZ00256 156 GQGKVVKYFSPKVNPNEMIQDIEKLLNA 183
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
15-196 2.80e-31

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: 111.47  E-value: 2.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084    15 SVYAFSARPlAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILN 94
Cdd:TIGR02540   1 DFYSFEVKD-ARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084    95 slkYVRPGGGFepNFMLFEKCEVNGAGAHPLFAFLREAlpapsddatalmtdpklitwspvCRNDVAWNFEKFLVGPDGV 174
Cdd:TIGR02540  80 ---FARRNYGV--TFPMFSKIKILGSEAEPAFRFLVDS-----------------------SKKEPRWNFWKYLVNPEGQ 131
                         170       180
                  ....*....|....*....|..
gi 41406084   175 PLRRYSRRFQTIDIEPDIEALL 196
Cdd:TIGR02540 132 VVKFWRPEEPVEEIRPEITALV 153
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
15-192 3.30e-72

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: 215.46  E-value: 3.30e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084  15 SVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILN 94
Cdd:cd00340   1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084  95 SLKYVRPgggfePNFMLFEKCEVNGAGAHPLFAFLREALPAPsddatalmtdpklitwspvCRNDVAWNFEKFLVGPDGV 174
Cdd:cd00340  79 FCETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGL-------------------LGKDIKWNFTKFLVDRDGE 134
                       170
                ....*....|....*...
gi 41406084 175 PLRRYSRRFQTIDIEPDI 192
Cdd:cd00340 135 VVKRFAPTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
16-130 2.05e-59

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 181.40  E-value: 2.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084    16 VYAFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTVrDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEIlns 95
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI--- 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 41406084    96 lKYVRPgGGFEPNFMLFEKCEVNGAGAHPLFAFLR 130
Cdd:pfam00255  76 -KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
15-196 3.98e-56

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 174.88  E-value: 3.98e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084  15 SVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILN 94
Cdd:COG0386   3 SIYDFSVTTL-DGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084  95 --SLKY-VrpgggfepNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDatalmtdpklitwspvcrNDVAWNFEKFLVGP 171
Cdd:COG0386  81 fcSLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG------------------GDIKWNFTKFLIDR 134
                       170       180
                ....*....|....*....|....*..
gi 41406084 172 DGVPLRRYSRRF--QTIDIEPDIEALL 196
Cdd:COG0386 135 DGNVVARFAPTTkpEDPELEAAIEKLL 161
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
15-198 6.45e-37

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 126.80  E-value: 6.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084   15 SVYAFSARPLAGGEpVSLGSLRG-KVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEIL 93
Cdd:PTZ00256  19 SFFEFEAIDIDGQL-VQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084   94 NslkYVRPggGFEPNFMLFEKCEVNGAGAHPLFAFLR---EALPAPSDDATalmtdpklitwspvcrnDVAWNFEKFLVG 170
Cdd:PTZ00256  98 E---YVQK--KFNVDFPLFQKIEVNGENTHEIYKYLRrnsELFQNNTNEAR-----------------QIPWNFAKFLID 155
                        170       180
                 ....*....|....*....|....*...
gi 41406084  171 PDGVPLRRYSRRFQTIDIEPDIEALLSQ 198
Cdd:PTZ00256 156 GQGKVVKYFSPKVNPNEMIQDIEKLLNA 183
PLN02412 PLN02412
probable glutathione peroxidase
14-198 1.71e-36

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 125.10  E-value: 1.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084   14 QSVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEIL 93
Cdd:PLN02412   7 KSIYDFTVKDI-GGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084   94 NSLKYVrpgggFEPNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDAtalmtdpklitwspvcrndVAWNFEKFLVGPDG 173
Cdd:PLN02412  86 QTVCTR-----FKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDA-------------------IKWNFTKFLVSKEG 141
                        170       180
                 ....*....|....*....|....*
gi 41406084  174 VPLRRYSRRFQTIDIEPDIEALLSQ 198
Cdd:PLN02412 142 KVVQRYAPTTSPLKIEKDIQNLLGQ 166
btuE PRK10606
putative glutathione peroxidase; Provisional
27-180 3.68e-34

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 119.88  E-value: 3.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084   27 GEPVSLGSLRGKVLLIENVASLUGTTvRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEIlnsLKYVRpgGGFE 106
Cdd:PRK10606  15 GEVTTLEKYAGNVLLIVNVASKCGLT-PQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI---KTYCR--TTWG 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41406084  107 PNFMLFEKCEVNGAGAHPLFAFLREALP---AP--SDDATALMTDPKlitwSPVCRNDVAWNFEKFLVGPDGVPLRRYS 180
Cdd:PRK10606  89 VTFPMFSKIEVNGEGRHPLYQKLIAAAPtavAPeeSGFYARMVSKGR----APLYPDDILWNFEKFLVGRDGQVIQRFS 163
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
15-196 2.61e-32

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 115.34  E-value: 2.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084   15 SVYAFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILN 94
Cdd:PTZ00056  18 SIYDYTVKTLEG-TTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084   95 SLKyvrpggGFEPNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDATALmtdpklitwspvcrNDVAWNFEKFLVGPDGV 174
Cdd:PTZ00056  97 FND------KNKIKYNFFEPIEVNGENTHELFKFLKANCDSMHDENGTL--------------KAIGWNFGKFLVNKSGN 156
                        170       180
                 ....*....|....*....|..
gi 41406084  175 PLRRYSRRFQTIDIEPDIEALL 196
Cdd:PTZ00056 157 VVAYFSPRTEPLELEKKIAELL 178
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
15-196 2.80e-31

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: 111.47  E-value: 2.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084    15 SVYAFSARPlAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILN 94
Cdd:TIGR02540   1 DFYSFEVKD-ARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084    95 slkYVRPGGGFepNFMLFEKCEVNGAGAHPLFAFLREAlpapsddatalmtdpklitwspvCRNDVAWNFEKFLVGPDGV 174
Cdd:TIGR02540  80 ---FARRNYGV--TFPMFSKIKILGSEAEPAFRFLVDS-----------------------SKKEPRWNFWKYLVNPEGQ 131
                         170       180
                  ....*....|....*....|..
gi 41406084   175 PLRRYSRRFQTIDIEPDIEALL 196
Cdd:TIGR02540 132 VVKFWRPEEPVEEIRPEITALV 153
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
14-197 4.52e-30

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 110.76  E-value: 4.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084   14 QSVYAFSARPLAGGEpVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEIL 93
Cdd:PLN02399  77 KSVHDFTVKDIDGKD-VALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIK 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406084   94 NsLKYVRpgggFEPNFMLFEKCEVNGAGAHPLFAFLREalpapsdDATALMTDpkLITwspvcrndvaWNFEKFLVGPDG 173
Cdd:PLN02399 156 Q-FACTR----FKAEFPIFDKVDVNGPSTAPVYQFLKS-------NAGGFLGD--LIK----------WNFEKFLVDKNG 211
                        170       180
                 ....*....|....*....|....
gi 41406084  174 VPLRRYSRRFQTIDIEPDIEALLS 197
Cdd:PLN02399 212 KVVERYPPTTSPFQIEKDIQKLLA 235
 
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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