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Conserved domains on  [gi|193210707|ref|NP_001123171|]
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Glutathione peroxidase [Caenorhabditis elegans]

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 ...
32-188 9.44e-76

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: 224.32  E-value: 9.44e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  32 TIYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTnSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEADINKF 111
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193210707 112 VNEKFSFEPDLYGKVTVNGGpligEEEPLWTFLKKEQGGTLFDAIKWNFTKFLVNRQGKVVARFGPSTNPKSFEEEI 188
Cdd:cd00340   80 CETNYGVTFPMFAKIDVNGE----NAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
32-188 9.44e-76

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: 224.32  E-value: 9.44e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  32 TIYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTnSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEADINKF 111
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193210707 112 VNEKFSFEPDLYGKVTVNGGpligEEEPLWTFLKKEQGGTLFDAIKWNFTKFLVNRQGKVVARFGPSTNPKSFEEEI 188
Cdd:cd00340   80 CETNYGVTFPMFAKIDVNGE----NAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
32-192 9.28e-63

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 191.44  E-value: 9.28e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  32 TIYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTnSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEADINKF 111
Cdd:COG0386    3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707 112 VNEKF--SFepDLYGKVTVNGGpligEEEPLWTFLKKEQGGTLFD-AIKWNFTKFLVNRQGKVVARFGPSTNPKS--FEE 186
Cdd:COG0386   82 CSLNYgvTF--PMFAKIDVNGP----NAHPLYKYLKEEAPGLLGGgDIKWNFTKFLIDRDGNVVARFAPTTKPEDpeLEA 155

                 ....*.
gi 193210707 187 EIVKLL 192
Cdd:COG0386  156 AIEKLL 161
PLN02412 PLN02412
probable glutathione peroxidase
27-192 2.27e-57

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 178.26  E-value: 2.27e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  27 DMSTGTIYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTNSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEA 106
Cdd:PLN02412   3 EESPKSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707 107 DINKFVNEKFSFEPDLYGKVTVNGgpliGEEEPLWTFLKKEQGGTLFDAIKWNFTKFLVNRQGKVVARFGPSTNPKSFEE 186
Cdd:PLN02412  83 EIQQTVCTRFKAEFPIFDKVDVNG----KNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEK 158

                 ....*.
gi 193210707 187 EIVKLL 192
Cdd:PLN02412 159 DIQNLL 164
GSHPx pfam00255
Glutathione peroxidase;
33-145 2.43e-35

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 120.15  E-value: 2.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707   33 IYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTnSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEADINKFV 112
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLT-PQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 193210707  113 NEKFSFEPDLYGKVTVNGgpliGEEEPLWTFLK 145
Cdd:pfam00255  80 PGGYGVTFPLFSKIEVNG----EKAHPVYKFLK 108
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
34-192 7.02e-34

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: 118.01  E-value: 7.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707   34 YDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTNSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEADINKFVN 113
Cdd:TIGR02540   3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  114 EKFSFEPDLYGKVTVNGgpliGEEEPLWTFL----KKEQggtlfdaiKWNFTKFLVNRQGKVVARFGPSTNPKSFEEEIV 189
Cdd:TIGR02540  83 RNYGVTFPMFSKIKILG----SEAEPAFRFLvdssKKEP--------RWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEIT 150

                  ...
gi 193210707  190 KLL 192
Cdd:TIGR02540 151 ALV 153
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
32-188 9.44e-76

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: 224.32  E-value: 9.44e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  32 TIYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTnSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEADINKF 111
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193210707 112 VNEKFSFEPDLYGKVTVNGGpligEEEPLWTFLKKEQGGTLFDAIKWNFTKFLVNRQGKVVARFGPSTNPKSFEEEI 188
Cdd:cd00340   80 CETNYGVTFPMFAKIDVNGE----NAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
32-192 9.28e-63

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 191.44  E-value: 9.28e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  32 TIYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTnSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEADINKF 111
Cdd:COG0386    3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707 112 VNEKF--SFepDLYGKVTVNGGpligEEEPLWTFLKKEQGGTLFD-AIKWNFTKFLVNRQGKVVARFGPSTNPKS--FEE 186
Cdd:COG0386   82 CSLNYgvTF--PMFAKIDVNGP----NAHPLYKYLKEEAPGLLGGgDIKWNFTKFLIDRDGNVVARFAPTTKPEDpeLEA 155

                 ....*.
gi 193210707 187 EIVKLL 192
Cdd:COG0386  156 AIEKLL 161
PLN02412 PLN02412
probable glutathione peroxidase
27-192 2.27e-57

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 178.26  E-value: 2.27e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  27 DMSTGTIYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTNSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEA 106
Cdd:PLN02412   3 EESPKSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707 107 DINKFVNEKFSFEPDLYGKVTVNGgpliGEEEPLWTFLKKEQGGTLFDAIKWNFTKFLVNRQGKVVARFGPSTNPKSFEE 186
Cdd:PLN02412  83 EIQQTVCTRFKAEFPIFDKVDVNG----KNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEK 158

                 ....*.
gi 193210707 187 EIVKLL 192
Cdd:PLN02412 159 DIQNLL 164
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
32-192 1.81e-53

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 170.47  E-value: 1.81e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  32 TIYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTNSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEADINKF 111
Cdd:PLN02399  78 SVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQF 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707 112 VNEKFSFEPDLYGKVTVNGgpliGEEEPLWTFLKKEQGGTLFDAIKWNFTKFLVNRQGKVVARFGPSTNPKSFEEEIVKL 191
Cdd:PLN02399 158 ACTRFKAEFPIFDKVDVNG----PSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKL 233

                 .
gi 193210707 192 L 192
Cdd:PLN02399 234 L 234
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
25-193 5.17e-41

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 137.20  E-value: 5.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  25 KIDMSTGTIYDFSVRDNSGDLVSLDKYSGL-VVIIVNVASYCGLTNSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPH 103
Cdd:PTZ00256  12 QIQPPTKSFFEFEAIDIDGQLVQLSKFKGKkAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPW 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707 104 CEADINKFVNEKFSFEPDLYGKVTVNGgpliGEEEPLWTFLKKEQggTLFDA-------IKWNFTKFLVNRQGKVVARFG 176
Cdd:PTZ00256  92 DEPEIKEYVQKKFNVDFPLFQKIEVNG----ENTHEIYKYLRRNS--ELFQNntnearqIPWNFAKFLIDGQGKVVKYFS 165
                        170
                 ....*....|....*..
gi 193210707 177 PSTNPKSFEEEIVKLLD 193
Cdd:PTZ00256 166 PKVNPNEMIQDIEKLLN 182
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
32-192 1.82e-36

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 126.12  E-value: 1.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  32 TIYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTNSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEADINKF 111
Cdd:PTZ00056  18 SIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRKF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707 112 vNEKFSFEPDLYGKVTVNGgpliGEEEPLWTFLKKE------QGGTLfDAIKWNFTKFLVNRQGKVVARFGPSTNPKSFE 185
Cdd:PTZ00056  98 -NDKNKIKYNFFEPIEVNG----ENTHELFKFLKANcdsmhdENGTL-KAIGWNFGKFLVNKSGNVVAYFSPRTEPLELE 171

                 ....*..
gi 193210707 186 EEIVKLL 192
Cdd:PTZ00056 172 KKIAELL 178
GSHPx pfam00255
Glutathione peroxidase;
33-145 2.43e-35

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 120.15  E-value: 2.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707   33 IYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTnSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEADINKFV 112
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLT-PQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 193210707  113 NEKFSFEPDLYGKVTVNGgpliGEEEPLWTFLK 145
Cdd:pfam00255  80 PGGYGVTFPLFSKIEVNG----EKAHPVYKFLK 108
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
34-192 7.02e-34

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: 118.01  E-value: 7.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707   34 YDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTNSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEADINKFVN 113
Cdd:TIGR02540   3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  114 EKFSFEPDLYGKVTVNGgpliGEEEPLWTFL----KKEQggtlfdaiKWNFTKFLVNRQGKVVARFGPSTNPKSFEEEIV 189
Cdd:TIGR02540  83 RNYGVTFPMFSKIKILG----SEAEPAFRFLvdssKKEP--------RWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEIT 150

                  ...
gi 193210707  190 KLL 192
Cdd:TIGR02540 151 ALV 153
btuE PRK10606
putative glutathione peroxidase; Provisional
28-181 1.26e-32

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 115.64  E-value: 1.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  28 MSTgTIYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTnSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEAD 107
Cdd:PRK10606   1 MQD-SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLT-PQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707 108 INKFVNEKFSFEPDLYGKVTVNGgpliGEEEPLWTFL--------KKEQGGTL------------FDAIKWNFTKFLVNR 167
Cdd:PRK10606  79 IKTYCRTTWGVTFPMFSKIEVNG----EGRHPLYQKLiaaaptavAPEESGFYarmvskgraplyPDDILWNFEKFLVGR 154
                        170
                 ....*....|....
gi 193210707 168 QGKVVARFGPSTNP 181
Cdd:PRK10606 155 DGQVIQRFSPDMTP 168
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
32-194 2.42e-04

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 39.67  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707  32 TIYDFSVRDNSGDLVSLDKYSGLVVIiVNV-ASYCGltnsnykelkslndkyhlrglrvaafPCNQfgfQEPHceadINK 110
Cdd:COG0526    7 PAPDFTLTDLDGKPLSLADLKGKPVL-VNFwATWCP--------------------------PCRA---EMPV----LKE 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210707 111 FVNE--KFSFepdlygkVTVNggplIGEEEPLWT-FLKKEQGG--TLFD-----AIKWNF----TKFLVNRQGKVVARFG 176
Cdd:COG0526   53 LAEEygGVVF-------VGVD----VDENPEAVKaFLKELGLPypVLLDpdgelAKAYGVrgipTTVLIDKDGKIVARHV 121
                        170
                 ....*....|....*...
gi 193210707 177 PSTNPKSFEEEIVKLLDE 194
Cdd:COG0526  122 GPLSPEELEEALEKLLAK 139
 
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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