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Conserved domains on  [gi|84871986|ref|NP_032186|]
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glutathione peroxidase 1 isoform 1 [Mus musculus]

Protein Classification

glutathione peroxidase( domain architecture ID 10085912)

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

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 ...
13-190 8.94e-74

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: 219.31  E-value: 8.94e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986  13 TVYAFSARPLtGGEPVSLGSLRGKVLLIENVASLUGTTiRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILN 92
Cdd:cd00340   1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986  93 SLKYVRPgggfePNFTLFEKCEVNGEKAHPLFTFLRNALPTPsddptalmtdpkyiiwspvCRNDIAWNFEKFLVGPDGV 172
Cdd:cd00340  79 FCETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGL-------------------LGKDIKWNFTKFLVDRDGE 134
                       170
                ....*....|....*...
gi 84871986 173 PVRRYSRRFRTIDIEPDI 190
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 ...
13-190 8.94e-74

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: 219.31  E-value: 8.94e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986  13 TVYAFSARPLtGGEPVSLGSLRGKVLLIENVASLUGTTiRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILN 92
Cdd:cd00340   1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986  93 SLKYVRPgggfePNFTLFEKCEVNGEKAHPLFTFLRNALPTPsddptalmtdpkyiiwspvCRNDIAWNFEKFLVGPDGV 172
Cdd:cd00340  79 FCETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGL-------------------LGKDIKWNFTKFLVDRDGE 134
                       170
                ....*....|....*...
gi 84871986 173 PVRRYSRRFRTIDIEPDI 190
Cdd:cd00340 135 VVKRFAPTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
14-128 1.24e-60

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 184.48  E-value: 1.24e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986    14 VYAFSARPLTGgEPVSLGSLRGKVLLIENVASLUGTTIrDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEIlns 93
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI--- 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 84871986    94 lKYVRPgGGFEPNFTLFEKCEVNGEKAHPLFTFLR 128
Cdd:pfam00255  76 -KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
12-194 4.23e-58

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 179.89  E-value: 4.23e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986  12 STVYAFSARPLTGgEPVSLGSLRGKVLLIENVASLUGTTiRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEIL 91
Cdd:COG0386   2 MSIYDFSVTTLDG-EPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986  92 N--SLKY-VrpgggfepNFTLFEKCEVNGEKAHPLFTFLRNALPTPSDDptalmtdpkyiiwspvcrNDIAWNFEKFLVG 168
Cdd:COG0386  80 EfcSLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG------------------GDIKWNFTKFLID 133
                       170       180
                ....*....|....*....|....*...
gi 84871986 169 PDGVPVRRYSRRFR--TIDIEPDIETLL 194
Cdd:COG0386 134 RDGNVVARFAPTTKpeDPELEAAIEKLL 161
PLN02412 PLN02412
probable glutathione peroxidase
6-196 1.97e-39

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 132.80  E-value: 1.97e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986    6 LSAAAQSTVYAFSARPLtGGEPVSLGSLRGKVLLIENVASLUGTTIRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENG 85
Cdd:PLN02412   1 MAEESPKSIYDFTVKDI-GGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986   86 KNEEILNSLKYVrpgggFEPNFTLFEKCEVNGEKAHPLFTFLRNalptpsdDPTALMTDPkyiiwspvcrndIAWNFEKF 165
Cdd:PLN02412  80 SNEEIQQTVCTR-----FKAEFPIFDKVDVNGKNTAPLYKYLKA-------EKGGLFGDA------------IKWNFTKF 135
                        170       180       190
                 ....*....|....*....|....*....|.
gi 84871986  166 LVGPDGVPVRRYSRRFRTIDIEPDIETLLSQ 196
Cdd:PLN02412 136 LVSKEGKVVQRYAPTTSPLKIEKDIQNLLGQ 166
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
15-194 9.40e-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: 109.93  E-value: 9.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986    15 YAFSARPLTGgEPVSLGSLRGKVLLIENVASLUGTTIRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILNsl 94
Cdd:TIGR02540   3 YSFEVKDARG-RTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIES-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986    95 kYVRPGGGFepNFTLFEKCEVNGEKAHPLFTFLrnaLPTPSDDPTalmtdpkyiiwspvcrndiaWNFEKFLVGPDGVPV 174
Cdd:TIGR02540  80 -FARRNYGV--TFPMFSKIKILGSEAEPAFRFL---VDSSKKEPR--------------------WNFWKYLVNPEGQVV 133
                         170       180
                  ....*....|....*....|
gi 84871986   175 RRYSRRFRTIDIEPDIETLL 194
Cdd:TIGR02540 134 KFWRPEEPVEEIRPEITALV 153
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
13-190 8.94e-74

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: 219.31  E-value: 8.94e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986  13 TVYAFSARPLtGGEPVSLGSLRGKVLLIENVASLUGTTiRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILN 92
Cdd:cd00340   1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986  93 SLKYVRPgggfePNFTLFEKCEVNGEKAHPLFTFLRNALPTPsddptalmtdpkyiiwspvCRNDIAWNFEKFLVGPDGV 172
Cdd:cd00340  79 FCETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGL-------------------LGKDIKWNFTKFLVDRDGE 134
                       170
                ....*....|....*...
gi 84871986 173 PVRRYSRRFRTIDIEPDI 190
Cdd:cd00340 135 VVKRFAPTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
14-128 1.24e-60

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 184.48  E-value: 1.24e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986    14 VYAFSARPLTGgEPVSLGSLRGKVLLIENVASLUGTTIrDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEIlns 93
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI--- 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 84871986    94 lKYVRPgGGFEPNFTLFEKCEVNGEKAHPLFTFLR 128
Cdd:pfam00255  76 -KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
12-194 4.23e-58

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 179.89  E-value: 4.23e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986  12 STVYAFSARPLTGgEPVSLGSLRGKVLLIENVASLUGTTiRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEIL 91
Cdd:COG0386   2 MSIYDFSVTTLDG-EPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986  92 N--SLKY-VrpgggfepNFTLFEKCEVNGEKAHPLFTFLRNALPTPSDDptalmtdpkyiiwspvcrNDIAWNFEKFLVG 168
Cdd:COG0386  80 EfcSLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG------------------GDIKWNFTKFLID 133
                       170       180
                ....*....|....*....|....*...
gi 84871986 169 PDGVPVRRYSRRFR--TIDIEPDIETLL 194
Cdd:COG0386 134 RDGNVVARFAPTTKpeDPELEAAIEKLL 161
PLN02412 PLN02412
probable glutathione peroxidase
6-196 1.97e-39

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 132.80  E-value: 1.97e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986    6 LSAAAQSTVYAFSARPLtGGEPVSLGSLRGKVLLIENVASLUGTTIRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENG 85
Cdd:PLN02412   1 MAEESPKSIYDFTVKDI-GGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986   86 KNEEILNSLKYVrpgggFEPNFTLFEKCEVNGEKAHPLFTFLRNalptpsdDPTALMTDPkyiiwspvcrndIAWNFEKF 165
Cdd:PLN02412  80 SNEEIQQTVCTR-----FKAEFPIFDKVDVNGKNTAPLYKYLKA-------EKGGLFGDA------------IKWNFTKF 135
                        170       180       190
                 ....*....|....*....|....*....|.
gi 84871986  166 LVGPDGVPVRRYSRRFRTIDIEPDIETLLSQ 196
Cdd:PLN02412 136 LVSKEGKVVQRYAPTTSPLKIEKDIQNLLGQ 166
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
10-196 4.31e-39

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 132.19  E-value: 4.31e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986   10 AQSTVYAFSARPLTGGEpVSLGSLRG-KVLLIENVASLUGTTIRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNE 88
Cdd:PTZ00256  16 PTKSFFEFEAIDIDGQL-VQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986   89 EILNslkYVRPGggFEPNFTLFEKCEVNGEKAHPLFTFLRNAlptpSDDPTALMTDPKYIiwspvcrndiAWNFEKFLVG 168
Cdd:PTZ00256  95 EIKE---YVQKK--FNVDFPLFQKIEVNGENTHEIYKYLRRN----SELFQNNTNEARQI----------PWNFAKFLID 155
                        170       180
                 ....*....|....*....|....*...
gi 84871986  169 PDGVPVRRYSRRFRTIDIEPDIETLLSQ 196
Cdd:PTZ00256 156 GQGKVVKYFSPKVNPNEMIQDIEKLLNA 183
btuE PRK10606
putative glutathione peroxidase; Provisional
25-178 1.62e-37

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 128.35  E-value: 1.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986   25 GEPVSLGSLRGKVLLIENVASLUGTTiRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEIlnsLKYVRpgGGFE 104
Cdd:PRK10606  15 GEVTTLEKYAGNVLLIVNVASKCGLT-PQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI---KTYCR--TTWG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986  105 PNFTLFEKCEVNGEKAHPLFTFLRNALPTP----SDDPTALMTD----PKYIiwspvcrNDIAWNFEKFLVGPDGVPVRR 176
Cdd:PRK10606  89 VTFPMFSKIEVNGEGRHPLYQKLIAAAPTAvapeESGFYARMVSkgraPLYP-------DDILWNFEKFLVGRDGQVIQR 161

                 ..
gi 84871986  177 YS 178
Cdd:PRK10606 162 FS 163
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
8-195 2.94e-33

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 118.85  E-value: 2.94e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986    8 AAAQSTVYAFSARPLTGGEpVSLGSLRGKVLLIENVASLUGTTIRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKN 87
Cdd:PLN02399  73 AATEKSVHDFTVKDIDGKD-VALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSN 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986   88 EEILNsLKYVRpgggFEPNFTLFEKCEVNGEKAHPLFTFLRNalptpsdDPTALMTDPkyiiwspvcrndIAWNFEKFLV 167
Cdd:PLN02399 152 PEIKQ-FACTR----FKAEFPIFDKVDVNGPSTAPVYQFLKS-------NAGGFLGDL------------IKWNFEKFLV 207
                        170       180
                 ....*....|....*....|....*...
gi 84871986  168 GPDGVPVRRYSRRFRTIDIEPDIETLLS 195
Cdd:PLN02399 208 DKNGKVVERYPPTTSPFQIEKDIQKLLA 235
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
10-194 1.02e-32

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 116.49  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986   10 AQSTVYAFSARPLTGgEPVSLGSLRGKVLLIENVASLUGTTIRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEE 89
Cdd:PTZ00056  15 LRKSIYDYTVKTLEG-TTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986   90 ILNSLKyvrpggGFEPNFTLFEKCEVNGEKAHPLFTFLRNALPTPSDDPTALmtdpkyiiwspvcrNDIAWNFEKFLVGP 169
Cdd:PTZ00056  94 IRKFND------KNKIKYNFFEPIEVNGENTHELFKFLKANCDSMHDENGTL--------------KAIGWNFGKFLVNK 153
                        170       180
                 ....*....|....*....|....*
gi 84871986  170 DGVPVRRYSRRFRTIDIEPDIETLL 194
Cdd:PTZ00056 154 SGNVVAYFSPRTEPLELEKKIAELL 178
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
15-194 9.40e-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: 109.93  E-value: 9.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986    15 YAFSARPLTGgEPVSLGSLRGKVLLIENVASLUGTTIRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILNsl 94
Cdd:TIGR02540   3 YSFEVKDARG-RTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIES-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84871986    95 kYVRPGGGFepNFTLFEKCEVNGEKAHPLFTFLrnaLPTPSDDPTalmtdpkyiiwspvcrndiaWNFEKFLVGPDGVPV 174
Cdd:TIGR02540  80 -FARRNYGV--TFPMFSKIKILGSEAEPAFRFL---VDSSKKEPR--------------------WNFWKYLVNPEGQVV 133
                         170       180
                  ....*....|....*....|
gi 84871986   175 RRYSRRFRTIDIEPDIETLL 194
Cdd:TIGR02540 134 KFWRPEEPVEEIRPEITALV 153
 
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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