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Conserved domains on  [gi|33186887|ref|NP_874360|]
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glutathione peroxidase 6 precursor [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

 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 ...
39-211 5.81e-56

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: 175.01  E-value: 5.81e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887  39 TIYEYGALTLNGEEyIQFKQFAGKHVLFVNVAAYUGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEILLG 118
Cdd:cd00340   1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887 119 LKYVcpgsgFVPSFQLFEKGDVNGEKEQKVFTFLKNSCPPTSDllgsssqlfwepmkvHDIRWNFEKFLVGPDGVPVMHW 198
Cdd:cd00340  80 CETN-----YGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG---------------KDIKWNFTKFLVDRDGEVVKRF 139
                       170
                ....*....|...
gi 33186887 199 FHQAPVSTVKSDI 211
Cdd:cd00340 140 APTTDPEELEKDI 152
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
39-211 5.81e-56

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: 175.01  E-value: 5.81e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887  39 TIYEYGALTLNGEEyIQFKQFAGKHVLFVNVAAYUGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEILLG 118
Cdd:cd00340   1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887 119 LKYVcpgsgFVPSFQLFEKGDVNGEKEQKVFTFLKNSCPPTSDllgsssqlfwepmkvHDIRWNFEKFLVGPDGVPVMHW 198
Cdd:cd00340  80 CETN-----YGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG---------------KDIKWNFTKFLVDRDGEVVKRF 139
                       170
                ....*....|...
gi 33186887 199 FHQAPVSTVKSDI 211
Cdd:cd00340 140 APTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
40-153 4.74e-51

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 160.98  E-value: 4.74e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887    40 IYEYGALTLNGEeYIQFKQFAGKHVLFVNVAAYUGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEIllgl 119
Cdd:pfam00255   1 IYEFSAKDIDGE-PVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 33186887   120 KYVCPGsGFVPSFQLFEKGDVNGEKEQKVFTFLK 153
Cdd:pfam00255  76 KYFCPG-GYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
39-198 1.92e-43

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 143.29  E-value: 1.92e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887  39 TIYEYGALTLNGEEyIQFKQFAGKHVLFVNVAAYUGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEI--L 116
Cdd:COG0386   3 SIYDFSVTTLDGEP-VSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIaeF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887 117 LGLKY-VcpgsgfvpSFQLFEKGDVNGEKEQKVFTFLKNScppTSDLLGSSsqlfwepmkvhDIRWNFEKFLVGPDGVPV 195
Cdd:COG0386  82 CSLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEE---APGLLGGG-----------DIKWNFTKFLIDRDGNVV 139

                ...
gi 33186887 196 MHW 198
Cdd:COG0386 140 ARF 142
btuE PRK10606
putative glutathione peroxidase; Provisional
39-192 2.77e-31

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 112.94  E-value: 2.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887   39 TIYEYGALTLNGEEyIQFKQFAGKHVLFVNVAAYUGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEIllg 118
Cdd:PRK10606   4 SILTTVVTTIDGEV-TTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI--- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33186887  119 lKYVCPGSgFVPSFQLFEKGDVNGEKEQKVFTFL-----KNSCPPTSDLLGSSSQLFWEPMKVHDIRWNFEKFLVGPDG 192
Cdd:PRK10606  80 -KTYCRTT-WGVTFPMFSKIEVNGEGRHPLYQKLiaaapTAVAPEESGFYARMVSKGRAPLYPDDILWNFEKFLVGRDG 156
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
41-211 1.48e-24

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: 94.52  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887    41 YEYGALTLNGEeYIQFKQFAGKHVLFVNVAAYUGLAAQ-YPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEILLGL 119
Cdd:TIGR02540   3 YSFEVKDARGR-TVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887   120 KyvcpgSGFVPSFQLFEKGDVNGEKEQKVFTFLKNSCPPtsdllgsssqlfwEPmkvhdiRWNFEKFLVGPDGVPVMHWF 199
Cdd:TIGR02540  82 R-----RNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKK-------------EP------RWNFWKYLVNPEGQVVKFWR 137
                         170
                  ....*....|..
gi 33186887   200 HQAPVSTVKSDI 211
Cdd:TIGR02540 138 PEEPVEEIRPEI 149
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
39-211 5.81e-56

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: 175.01  E-value: 5.81e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887  39 TIYEYGALTLNGEEyIQFKQFAGKHVLFVNVAAYUGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEILLG 118
Cdd:cd00340   1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887 119 LKYVcpgsgFVPSFQLFEKGDVNGEKEQKVFTFLKNSCPPTSDllgsssqlfwepmkvHDIRWNFEKFLVGPDGVPVMHW 198
Cdd:cd00340  80 CETN-----YGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG---------------KDIKWNFTKFLVDRDGEVVKRF 139
                       170
                ....*....|...
gi 33186887 199 FHQAPVSTVKSDI 211
Cdd:cd00340 140 APTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
40-153 4.74e-51

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 160.98  E-value: 4.74e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887    40 IYEYGALTLNGEeYIQFKQFAGKHVLFVNVAAYUGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEIllgl 119
Cdd:pfam00255   1 IYEFSAKDIDGE-PVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 33186887   120 KYVCPGsGFVPSFQLFEKGDVNGEKEQKVFTFLK 153
Cdd:pfam00255  76 KYFCPG-GYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
39-198 1.92e-43

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 143.29  E-value: 1.92e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887  39 TIYEYGALTLNGEEyIQFKQFAGKHVLFVNVAAYUGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEI--L 116
Cdd:COG0386   3 SIYDFSVTTLDGEP-VSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIaeF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887 117 LGLKY-VcpgsgfvpSFQLFEKGDVNGEKEQKVFTFLKNScppTSDLLGSSsqlfwepmkvhDIRWNFEKFLVGPDGVPV 195
Cdd:COG0386  82 CSLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEE---APGLLGGG-----------DIKWNFTKFLIDRDGNVV 139

                ...
gi 33186887 196 MHW 198
Cdd:COG0386 140 ARF 142
btuE PRK10606
putative glutathione peroxidase; Provisional
39-192 2.77e-31

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 112.94  E-value: 2.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887   39 TIYEYGALTLNGEEyIQFKQFAGKHVLFVNVAAYUGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEIllg 118
Cdd:PRK10606   4 SILTTVVTTIDGEV-TTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI--- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33186887  119 lKYVCPGSgFVPSFQLFEKGDVNGEKEQKVFTFL-----KNSCPPTSDLLGSSSQLFWEPMKVHDIRWNFEKFLVGPDG 192
Cdd:PRK10606  80 -KTYCRTT-WGVTFPMFSKIEVNGEGRHPLYQKLiaaapTAVAPEESGFYARMVSKGRAPLYPDDILWNFEKFLVGRDG 156
PLN02412 PLN02412
probable glutathione peroxidase
39-192 7.22e-30

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 108.92  E-value: 7.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887   39 TIYEYGALTLNGEEyIQFKQFAGKHVLFVNVAAYUGLA-AQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEIll 117
Cdd:PLN02412   8 SIYDFTVKDIGGND-VSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEI-- 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33186887  118 gLKYVCpgSGFVPSFQLFEKGDVNGEKEQKVFTFLKNScppTSDLLGSSsqlfwepmkvhdIRWNFEKFLVGPDG 192
Cdd:PLN02412  85 -QQTVC--TRFKAEFPIFDKVDVNGKNTAPLYKYLKAE---KGGLFGDA------------IKWNFTKFLVSKEG 141
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
37-217 3.19e-29

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 107.54  E-value: 3.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887   37 TGTIYEYGALTLNGEEyIQFKQFAGKHV-LFVNVAAYUGLAAQ-YPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSE 114
Cdd:PTZ00256  17 TKSFFEFEAIDIDGQL-VQLSKFKGKKAiIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887  115 IllgLKYVCpgSGFVPSFQLFEKGDVNGEKEQKVFTFLKNScpptSDLLGSSSQlfwepmKVHDIRWNFEKFLVGPDGVP 194
Cdd:PTZ00256  96 I---KEYVQ--KKFNVDFPLFQKIEVNGENTHEIYKYLRRN----SELFQNNTN------EARQIPWNFAKFLIDGQGKV 160
                        170       180
                 ....*....|....*....|...
gi 33186887  195 VMHWFHQAPVSTVKSDILEYLKQ 217
Cdd:PTZ00256 161 VKYFSPKVNPNEMIQDIEKLLNA 183
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
39-192 8.92e-29

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 108.06  E-value: 8.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887   39 TIYEYGALTLNGEEyIQFKQFAGKHVLFVNVAAYUGL-AAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEIll 117
Cdd:PLN02399  78 SVHDFTVKDIDGKD-VALSKFKGKVLLIVNVASKCGLtSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEI-- 154
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33186887  118 gLKYVCpgSGFVPSFQLFEKGDVNGEKEQKVFTFLKNScppTSDLLGSSsqlfwepmkvhdIRWNFEKFLVGPDG 192
Cdd:PLN02399 155 -KQFAC--TRFKAEFPIFDKVDVNGPSTAPVYQFLKSN---AGGFLGDL------------IKWNFEKFLVDKNG 211
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
41-211 1.48e-24

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: 94.52  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887    41 YEYGALTLNGEeYIQFKQFAGKHVLFVNVAAYUGLAAQ-YPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEILLGL 119
Cdd:TIGR02540   3 YSFEVKDARGR-TVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887   120 KyvcpgSGFVPSFQLFEKGDVNGEKEQKVFTFLKNSCPPtsdllgsssqlfwEPmkvhdiRWNFEKFLVGPDGVPVMHWF 199
Cdd:TIGR02540  82 R-----RNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKK-------------EP------RWNFWKYLVNPEGQVVKFWR 137
                         170
                  ....*....|..
gi 33186887   200 HQAPVSTVKSDI 211
Cdd:TIGR02540 138 PEEPVEEIRPEI 149
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
39-192 1.50e-16

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 74.89  E-value: 1.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186887   39 TIYEYGALTLNGEEYiQFKQFAGKHVLFVNVAAYUGLAAQY-PELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEIll 117
Cdd:PTZ00056  18 SIYDYTVKTLEGTTV-PMSSLKNKVLMITNSASKCGLTKKHvDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDI-- 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33186887  118 glkyvcpgSGFVPS----FQLFEKGDVNGEKEQKVFTFLKNSCPPTSDllgsssqlfwEPMKVHDIRWNFEKFLVGPDG 192
Cdd:PTZ00056  95 --------RKFNDKnkikYNFFEPIEVNGENTHELFKFLKANCDSMHD----------ENGTLKAIGWNFGKFLVNKSG 155
 
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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