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Conserved domains on  [gi|145275168|ref|NP_109602|]
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glutathione peroxidase 2 [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 ...
7-182 9.76e-65

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: 195.81  E-value: 9.76e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   7 SFYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGTTtRDYNQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEILNS 85
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYkDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168  86 LKYVrpgggYQPTFSLTQKCDVNGQNEHPVFAYLKDKLPYPYddpfslmtdpkliiwspvrRSDVSWNFEKFLIGPEGEP 165
Cdd:cd00340   80 CETN-----YGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLL-------------------GKDIKWNFTKFLVDRDGEV 135
                        170
                 ....*....|....*..
gi 145275168 166 FRRYSRSFQTINIEPDI 182
Cdd:cd00340  136 VKRFAPTTDPEELEKDI 152
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
7-182 9.76e-65

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: 195.81  E-value: 9.76e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   7 SFYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGTTtRDYNQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEILNS 85
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYkDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168  86 LKYVrpgggYQPTFSLTQKCDVNGQNEHPVFAYLKDKLPYPYddpfslmtdpkliiwspvrRSDVSWNFEKFLIGPEGEP 165
Cdd:cd00340   80 CETN-----YGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLL-------------------GKDIKWNFTKFLVDRDGEV 135
                        170
                 ....*....|....*..
gi 145275168 166 FRRYSRSFQTINIEPDI 182
Cdd:cd00340  136 VKRFAPTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
8-120 1.19e-56

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 174.08  E-value: 1.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168    8 FYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGTTTrDYNQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEIlnsl 86
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYkDRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 145275168   87 KYVRPgGGYQPTFSLTQKCDVNGQNEHPVFAYLK 120
Cdd:pfam00255  76 KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
5-186 1.06e-48

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 155.62  E-value: 1.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   5 AKSFYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGtTTRDYNQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEIL 83
Cdd:COG0386    1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCG-FTPQYEGLEALYEKYkDRGLVVLGFPCNQFGGQEPGSNEEIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168  84 N--SLKY-VrpgggyqpTFSLTQKCDVNGQNEHPVFAYLKDKLPYPYDDpfslmtdpkliiwspvrrSDVSWNFEKFLIG 160
Cdd:COG0386   80 EfcSLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG------------------GDIKWNFTKFLID 133
                        170       180
                 ....*....|....*....|....*...
gi 145275168 161 PEGEPFRRYS--RSFQTINIEPDIKRLL 186
Cdd:COG0386  134 RDGNVVARFAptTKPEDPELEAAIEKLL 161
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
5-187 3.16e-36

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 124.49  E-value: 3.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   5 AKSFYDLSAVGLDGEKIDFNTFRGR-AVLIENVASLUGTTTRDYNQLNELQCRFPRR-LVVLGFPCNQFGHQENCQNEEI 82
Cdd:PTZ00256  17 TKSFFEFEAIDIDGQLVQLSKFKGKkAIIVVNVACKCGLTSDHYTQLVELYKQYKSQgLEILAFPCNQFMEQEPWDEPEI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168  83 LNslkYVRPGggYQPTFSLTQKCDVNGQNEHPVFAYLKdklpypyddpfslmTDPKLIIWSPVRRSDVSWNFEKFLIGPE 162
Cdd:PTZ00256  97 KE---YVQKK--FNVDFPLFQKIEVNGENTHEIYKYLR--------------RNSELFQNNTNEARQIPWNFAKFLIDGQ 157
                        170       180
                 ....*....|....*....|....*
gi 145275168 163 GEPFRRYSRSFQTINIEPDIKRLLK 187
Cdd:PTZ00256 158 GKVVKYFSPKVNPNEMIQDIEKLLN 182
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
7-186 1.74e-26

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: 98.75  E-value: 1.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168    7 SFYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGTTTRDYNQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEILNS 85
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELgPSHFNVLAFPCNQFGESEPDSSKEIESF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   86 LKyvrpgGGYQPTFSLTQKCDVNGQNEHPVFAYLKDklpypyddpfSLMTDPKliiwspvrrsdvsWNFEKFLIGPEGEP 165
Cdd:TIGR02540  81 AR-----RNYGVTFPMFSKIKILGSEAEPAFRFLVD----------SSKKEPR-------------WNFWKYLVNPEGQV 132
                         170       180
                  ....*....|....*....|.
gi 145275168  166 FRRYSRSFQTINIEPDIKRLL 186
Cdd:TIGR02540 133 VKFWRPEEPVEEIRPEITALV 153
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
7-182 9.76e-65

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: 195.81  E-value: 9.76e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   7 SFYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGTTtRDYNQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEILNS 85
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYkDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168  86 LKYVrpgggYQPTFSLTQKCDVNGQNEHPVFAYLKDKLPYPYddpfslmtdpkliiwspvrRSDVSWNFEKFLIGPEGEP 165
Cdd:cd00340   80 CETN-----YGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLL-------------------GKDIKWNFTKFLVDRDGEV 135
                        170
                 ....*....|....*..
gi 145275168 166 FRRYSRSFQTINIEPDI 182
Cdd:cd00340  136 VKRFAPTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
8-120 1.19e-56

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 174.08  E-value: 1.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168    8 FYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGTTTrDYNQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEIlnsl 86
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYkDRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 145275168   87 KYVRPgGGYQPTFSLTQKCDVNGQNEHPVFAYLK 120
Cdd:pfam00255  76 KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
5-186 1.06e-48

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 155.62  E-value: 1.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   5 AKSFYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGtTTRDYNQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEIL 83
Cdd:COG0386    1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCG-FTPQYEGLEALYEKYkDRGLVVLGFPCNQFGGQEPGSNEEIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168  84 N--SLKY-VrpgggyqpTFSLTQKCDVNGQNEHPVFAYLKDKLPYPYDDpfslmtdpkliiwspvrrSDVSWNFEKFLIG 160
Cdd:COG0386   80 EfcSLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG------------------GDIKWNFTKFLID 133
                        170       180
                 ....*....|....*....|....*...
gi 145275168 161 PEGEPFRRYS--RSFQTINIEPDIKRLL 186
Cdd:COG0386  134 RDGNVVARFAptTKPEDPELEAAIEKLL 161
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
5-187 3.16e-36

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 124.49  E-value: 3.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   5 AKSFYDLSAVGLDGEKIDFNTFRGR-AVLIENVASLUGTTTRDYNQLNELQCRFPRR-LVVLGFPCNQFGHQENCQNEEI 82
Cdd:PTZ00256  17 TKSFFEFEAIDIDGQLVQLSKFKGKkAIIVVNVACKCGLTSDHYTQLVELYKQYKSQgLEILAFPCNQFMEQEPWDEPEI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168  83 LNslkYVRPGggYQPTFSLTQKCDVNGQNEHPVFAYLKdklpypyddpfslmTDPKLIIWSPVRRSDVSWNFEKFLIGPE 162
Cdd:PTZ00256  97 KE---YVQKK--FNVDFPLFQKIEVNGENTHEIYKYLR--------------RNSELFQNNTNEARQIPWNFAKFLIDGQ 157
                        170       180
                 ....*....|....*....|....*
gi 145275168 163 GEPFRRYSRSFQTINIEPDIKRLLK 187
Cdd:PTZ00256 158 GKVVKYFSPKVNPNEMIQDIEKLLN 182
PLN02412 PLN02412
probable glutathione peroxidase
6-186 2.68e-31

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 111.62  E-value: 2.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   6 KSFYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGTTTRDYNQLNELQCRFPRR-LVVLGFPCNQFGHQENCQNEEILN 84
Cdd:PLN02412   7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQgFEILAFPCNQFLGQEPGSNEEIQQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168  85 SLKYVrpgggYQPTFSLTQKCDVNGQNEHPVFAYLKDKLPYPYDDPfslmtdpkliiwspvrrsdVSWNFEKFLIGPEGE 164
Cdd:PLN02412  87 TVCTR-----FKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDA-------------------IKWNFTKFLVSKEGK 142
                        170       180
                 ....*....|....*....|..
gi 145275168 165 PFRRYSRSFQTINIEPDIKRLL 186
Cdd:PLN02412 143 VVQRYAPTTSPLKIEKDIQNLL 164
btuE PRK10606
putative glutathione peroxidase; Provisional
7-170 1.11e-29

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 107.94  E-value: 1.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   7 SFYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGTTTRdYNQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEIlns 85
Cdd:PRK10606   4 SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQ-YEQLENIQKAWaDQGFVVLGFPCNQFLGQEPGSDEEI--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168  86 LKYVRpgGGYQPTFSLTQKCDVNGQNEHPVFAYLKDKLPY---PYDDPFSLMTDPKLiiWSPVRRSDVSWNFEKFLIGPE 162
Cdd:PRK10606  80 KTYCR--TTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTavaPEESGFYARMVSKG--RAPLYPDDILWNFEKFLVGRD 155

                 ....*...
gi 145275168 163 GEPFRRYS 170
Cdd:PRK10606 156 GQVIQRFS 163
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
6-186 8.69e-28

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 104.21  E-value: 8.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   6 KSFYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGTTTRDYNQLNELQCRFPRR-LVVLGFPCNQFGHQENCQNEEILN 84
Cdd:PLN02399  77 KSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQgFEILAFPCNQFGGQEPGSNPEIKQ 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168  85 sLKYVRpgggYQPTFSLTQKCDVNGQNEHPVFAYLKDKLPYPYDDpfslmtdpkLIiwspvrrsdvSWNFEKFLIGPEGE 164
Cdd:PLN02399 157 -FACTR----FKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGD---------LI----------KWNFEKFLVDKNGK 212
                        170       180
                 ....*....|....*....|..
gi 145275168 165 PFRRYSRSFQTINIEPDIKRLL 186
Cdd:PLN02399 213 VVERYPPTTSPFQIEKDIQKLL 234
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
6-188 2.48e-27

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 102.24  E-value: 2.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   6 KSFYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGTTTRDYNQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEIL- 83
Cdd:PTZ00056  17 KSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFnPLGLEILAFPTSQFLNQEFPNTKDIRk 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168  84 ----NSLKYvrpgggyqPTFSLtqkCDVNGQNEHPVFAYLKDKLPYPYDDPFSLmtdpkliiwspvrrSDVSWNFEKFLI 159
Cdd:PTZ00056  97 fndkNKIKY--------NFFEP---IEVNGENTHELFKFLKANCDSMHDENGTL--------------KAIGWNFGKFLV 151
                        170       180
                 ....*....|....*....|....*....
gi 145275168 160 GPEGEPFRRYSRSFQTINIEPDIKRLLKV 188
Cdd:PTZ00056 152 NKSGNVVAYFSPRTEPLELEKKIAELLGV 180
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
7-186 1.74e-26

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: 98.75  E-value: 1.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168    7 SFYDLSAVGLDGEKIDFNTFRGRAVLIENVASLUGTTTRDYNQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEILNS 85
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELgPSHFNVLAFPCNQFGESEPDSSKEIESF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275168   86 LKyvrpgGGYQPTFSLTQKCDVNGQNEHPVFAYLKDklpypyddpfSLMTDPKliiwspvrrsdvsWNFEKFLIGPEGEP 165
Cdd:TIGR02540  81 AR-----RNYGVTFPMFSKIKILGSEAEPAFRFLVD----------SSKKEPR-------------WNFWKYLVNPEGQV 132
                         170       180
                  ....*....|....*....|.
gi 145275168  166 FRRYSRSFQTINIEPDIKRLL 186
Cdd:TIGR02540 133 VKFWRPEEPVEEIRPEITALV 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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