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Conserved domains on  [gi|145275165|ref|NP_110453|]
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glutathione peroxidase 1 [Rattus norvegicus]

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 ...
13-190 7.43e-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: 219.69  E-value: 7.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  13 TVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTtRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILN 92
Cdd:cd00340    1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  93 SLKYVRPgggfePNFTLFEKCEVNGEKAHPLFTFLRNALPAPsddptalmtdpkyiiwspvCRNDISWNFEKFLVGPDGV 172
Cdd:cd00340   79 FCETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGL-------------------LGKDIKWNFTKFLVDRDGE 134
                        170
                 ....*....|....*...
gi 145275165 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 7.43e-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: 219.69  E-value: 7.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  13 TVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTtRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILN 92
Cdd:cd00340    1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  93 SLKYVRPgggfePNFTLFEKCEVNGEKAHPLFTFLRNALPAPsddptalmtdpkyiiwspvCRNDISWNFEKFLVGPDGV 172
Cdd:cd00340   79 FCETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGL-------------------LGKDIKWNFTKFLVDRDGE 134
                        170
                 ....*....|....*...
gi 145275165 173 PVRRYSRRFRTIDIEPDI 190
Cdd:cd00340  135 VVKRFAPTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
14-128 1.91e-61

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 186.40  E-value: 1.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165   14 VYAFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTTrDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEIlns 93
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI--- 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 145275165   94 lKYVRPgGGFEPNFTLFEKCEVNGEKAHPLFTFLR 128
Cdd:pfam00255  76 -KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
12-194 4.14e-59

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 182.58  E-value: 4.14e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  12 STVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTtRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEIL 91
Cdd:COG0386    2 MSIYDFSVTTL-DGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  92 N--SLKY-VrpgggfepNFTLFEKCEVNGEKAHPLFTFLRNALPAPSDDptalmtdpkyiiwspvcrNDISWNFEKFLVG 168
Cdd:COG0386   80 EfcSLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG------------------GDIKWNFTKFLID 133
                        170       180
                 ....*....|....*....|....*...
gi 145275165 169 PDGVPVRRYSRRFR--TIDIEPDIEALL 194
Cdd:COG0386  134 RDGNVVARFAPTTKpeDPELEAAIEKLL 161
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
9-195 8.49e-40

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 134.12  E-value: 8.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165   9 VAQSTVYAFSARPLAGGEpVSLGSLRG-KVLLIENVASLUGTTTRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKN 87
Cdd:PTZ00256  15 PPTKSFFEFEAIDIDGQL-VQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  88 EEILNslkYVRPggGFEPNFTLFEKCEVNGEKAHPLFTFLRNAlpapSDDPTALMTDPKYiiwspvcrndISWNFEKFLV 167
Cdd:PTZ00256  94 PEIKE---YVQK--KFNVDFPLFQKIEVNGENTHEIYKYLRRN----SELFQNNTNEARQ----------IPWNFAKFLI 154
                        170       180
                 ....*....|....*....|....*...
gi 145275165 168 GPDGVPVRRYSRRFRTIDIEPDIEALLS 195
Cdd:PTZ00256 155 DGQGKVVKYFSPKVNPNEMIQDIEKLLN 182
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
15-194 1.06e-30

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: 1.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165   15 YAFSARPlAGGEPVSLGSLRGKVLLIENVASLUGTTTRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILNsl 94
Cdd:TIGR02540   3 YSFEVKD-ARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIES-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165   95 kYVRPGGGFepNFTLFEKCEVNGEKAHPLFTFLrnaLPAPSDDPTalmtdpkyiiwspvcrndisWNFEKFLVGPDGVPV 174
Cdd:TIGR02540  80 -FARRNYGV--TFPMFSKIKILGSEAEPAFRFL---VDSSKKEPR--------------------WNFWKYLVNPEGQVV 133
                         170       180
                  ....*....|....*....|
gi 145275165  175 RRYSRRFRTIDIEPDIEALL 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 7.43e-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: 219.69  E-value: 7.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  13 TVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTtRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILN 92
Cdd:cd00340    1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  93 SLKYVRPgggfePNFTLFEKCEVNGEKAHPLFTFLRNALPAPsddptalmtdpkyiiwspvCRNDISWNFEKFLVGPDGV 172
Cdd:cd00340   79 FCETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGL-------------------LGKDIKWNFTKFLVDRDGE 134
                        170
                 ....*....|....*...
gi 145275165 173 PVRRYSRRFRTIDIEPDI 190
Cdd:cd00340  135 VVKRFAPTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
14-128 1.91e-61

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 186.40  E-value: 1.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165   14 VYAFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTTrDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEIlns 93
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI--- 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 145275165   94 lKYVRPgGGFEPNFTLFEKCEVNGEKAHPLFTFLR 128
Cdd:pfam00255  76 -KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
12-194 4.14e-59

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 182.58  E-value: 4.14e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  12 STVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTtRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEIL 91
Cdd:COG0386    2 MSIYDFSVTTL-DGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  92 N--SLKY-VrpgggfepNFTLFEKCEVNGEKAHPLFTFLRNALPAPSDDptalmtdpkyiiwspvcrNDISWNFEKFLVG 168
Cdd:COG0386   80 EfcSLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG------------------GDIKWNFTKFLID 133
                        170       180
                 ....*....|....*....|....*...
gi 145275165 169 PDGVPVRRYSRRFR--TIDIEPDIEALL 194
Cdd:COG0386  134 RDGNVVARFAPTTKpeDPELEAAIEKLL 161
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
9-195 8.49e-40

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 134.12  E-value: 8.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165   9 VAQSTVYAFSARPLAGGEpVSLGSLRG-KVLLIENVASLUGTTTRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKN 87
Cdd:PTZ00256  15 PPTKSFFEFEAIDIDGQL-VQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  88 EEILNslkYVRPggGFEPNFTLFEKCEVNGEKAHPLFTFLRNAlpapSDDPTALMTDPKYiiwspvcrndISWNFEKFLV 167
Cdd:PTZ00256  94 PEIKE---YVQK--KFNVDFPLFQKIEVNGENTHEIYKYLRRN----SELFQNNTNEARQ----------IPWNFAKFLI 154
                        170       180
                 ....*....|....*....|....*...
gi 145275165 168 GPDGVPVRRYSRRFRTIDIEPDIEALLS 195
Cdd:PTZ00256 155 DGQGKVVKYFSPKVNPNEMIQDIEKLLN 182
PLN02412 PLN02412
probable glutathione peroxidase
10-194 2.28e-38

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 130.11  E-value: 2.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  10 AQSTVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTTRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEE 89
Cdd:PLN02412   5 SPKSIYDFTVKDI-GGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  90 ILNSLKYVrpgggFEPNFTLFEKCEVNGEKAHPLFTFLRNalpapsdDPTALMTDPkyiiwspvcrndISWNFEKFLVGP 169
Cdd:PLN02412  84 IQQTVCTR-----FKAEFPIFDKVDVNGKNTAPLYKYLKA-------EKGGLFGDA------------IKWNFTKFLVSK 139
                        170       180
                 ....*....|....*....|....*
gi 145275165 170 DGVPVRRYSRRFRTIDIEPDIEALL 194
Cdd:PLN02412 140 EGKVVQRYAPTTSPLKIEKDIQNLL 164
btuE PRK10606
putative glutathione peroxidase; Provisional
25-178 4.62e-37

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 127.20  E-value: 4.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  25 GEPVSLGSLRGKVLLIENVASLUGTTTRdYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEIlnsLKYVRpgGGFE 104
Cdd:PRK10606  15 GEVTTLEKYAGNVLLIVNVASKCGLTPQ-YEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI---KTYCR--TTWG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165 105 PNFTLFEKCEVNGEKAHPLFTFLRNALP---APSD-DPTALMTD----PKYIiwspvcrNDISWNFEKFLVGPDGVPVRR 176
Cdd:PRK10606  89 VTFPMFSKIEVNGEGRHPLYQKLIAAAPtavAPEEsGFYARMVSkgraPLYP-------DDILWNFEKFLVGRDGQVIQR 161

                 ..
gi 145275165 177 YS 178
Cdd:PRK10606 162 FS 163
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
10-197 1.69e-33

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 118.42  E-value: 1.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  10 AQSTVYAFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTTRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEE 89
Cdd:PTZ00056  15 LRKSIYDYTVKTLEG-TTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  90 ILNSLKyvrpggGFEPNFTLFEKCEVNGEKAHPLFTFLRNALPAPSDDPTALmtdpkyiiwspvcrNDISWNFEKFLVGP 169
Cdd:PTZ00056  94 IRKFND------KNKIKYNFFEPIEVNGENTHELFKFLKANCDSMHDENGTL--------------KAIGWNFGKFLVNK 153
                        170       180
                 ....*....|....*....|....*...
gi 145275165 170 DGVPVRRYSRRFRTIDIEPDIEALLSKQ 197
Cdd:PTZ00056 154 SGNVVAYFSPRTEPLELEKKIAELLGVK 181
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
8-195 2.64e-32

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 116.54  E-value: 2.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165   8 AVAQSTVYAFSARPLAGGEpVSLGSLRGKVLLIENVASLUGTTTRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKN 87
Cdd:PLN02399  73 AATEKSVHDFTVKDIDGKD-VALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSN 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165  88 EEILNsLKYVRpgggFEPNFTLFEKCEVNGEKAHPLFTFLRNalpapsdDPTALMTDPkyiiwspvcrndISWNFEKFLV 167
Cdd:PLN02399 152 PEIKQ-FACTR----FKAEFPIFDKVDVNGPSTAPVYQFLKS-------NAGGFLGDL------------IKWNFEKFLV 207
                        170       180
                 ....*....|....*....|....*...
gi 145275165 168 GPDGVPVRRYSRRFRTIDIEPDIEALLS 195
Cdd:PLN02399 208 DKNGKVVERYPPTTSPFQIEKDIQKLLA 235
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
15-194 1.06e-30

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: 1.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165   15 YAFSARPlAGGEPVSLGSLRGKVLLIENVASLUGTTTRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILNsl 94
Cdd:TIGR02540   3 YSFEVKD-ARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIES-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275165   95 kYVRPGGGFepNFTLFEKCEVNGEKAHPLFTFLrnaLPAPSDDPTalmtdpkyiiwspvcrndisWNFEKFLVGPDGVPV 174
Cdd:TIGR02540  80 -FARRNYGV--TFPMFSKIKILGSEAEPAFRFL---VDSSKKEPR--------------------WNFWKYLVNPEGQVV 133
                         170       180
                  ....*....|....*....|
gi 145275165  175 RRYSRRFRTIDIEPDIEALL 194
Cdd:TIGR02540 134 KFWRPEEPVEEIRPEITALV 153
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
16-73 4.61e-06

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 44.47  E-value: 4.61e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145275165  16 AFSArPLAGGEPVSLGSLRGKVLLIENVASLUGTTTRDYTEMNDLQKRLGPRGLVVLG 73
Cdd:COG1225    3 DFTL-PDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLG 59
 
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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