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Conserved domains on  [gi|1851937782|ref|XP_034841801|]
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glutathione peroxidase 6-like isoform X1 [Mirounga leonina]

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 ...
38-210 4.34e-61

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: 188.11  E-value: 4.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  38 TIYEYGALTLNEEEyIQFKRYAGKHVLFVNVATYUGLTAQYPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEILSG 117
Cdd:cd00340     1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782 118 LKHVRPgggfvPNFQLFEKGDVNGEKEQKVFTFLKNSCPPTSDllgsasqlfwepmkvHDIRWNFEKFLVGPDGVPVMRW 197
Cdd:cd00340    80 CETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG---------------KDIKWNFTKFLVDRDGEVVKRF 139
                         170
                  ....*....|...
gi 1851937782 198 FHKAPVSTVKSDI 210
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 ...
38-210 4.34e-61

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: 188.11  E-value: 4.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  38 TIYEYGALTLNEEEyIQFKRYAGKHVLFVNVATYUGLTAQYPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEILSG 117
Cdd:cd00340     1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782 118 LKHVRPgggfvPNFQLFEKGDVNGEKEQKVFTFLKNSCPPTSDllgsasqlfwepmkvHDIRWNFEKFLVGPDGVPVMRW 197
Cdd:cd00340    80 CETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG---------------KDIKWNFTKFLVDRDGEVVKRF 139
                         170
                  ....*....|...
gi 1851937782 198 FHKAPVSTVKSDI 210
Cdd:cd00340   140 APTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
39-152 7.34e-53

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 165.60  E-value: 7.34e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  39 IYEYGALTLNEEeYIQFKRYAGKHVLFVNVATYUGLTAQYPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEIlsgl 118
Cdd:pfam00255   1 IYEFSAKDIDGE-PVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1851937782 119 KHVRPgGGFVPNFQLFEKGDVNGEKEQKVFTFLK 152
Cdd:pfam00255  76 KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
38-197 9.80e-47

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 151.77  E-value: 9.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  38 TIYEYGALTLNEEEyIQFKRYAGKHVLFVNVATYUGLTAQYPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEILS- 116
Cdd:COG0386     3 SIYDFSVTTLDGEP-VSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEf 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782 117 -----GLKhvrpgggfvpnFQLFEKGDVNGEKEQKVFTFLKNSCPptsdllgsasqlfwEPMKVHDIRWNFEKFLVGPDG 191
Cdd:COG0386    82 cslnyGVT-----------FPMFAKIDVNGPNAHPLYKYLKEEAP--------------GLLGGGDIKWNFTKFLIDRDG 136

                  ....*.
gi 1851937782 192 VPVMRW 197
Cdd:COG0386   137 NVVARF 142
btuE PRK10606
putative glutathione peroxidase; Provisional
45-211 9.55e-34

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 119.11  E-value: 9.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  45 LTLNEEEYIQFKRYAGKHVLFVNVATYUGLTAQYPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEILSGLKhvrpg 124
Cdd:PRK10606   10 VTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYCR----- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782 125 GGFVPNFQLFEKGDVNGEKEQKVFTFL-----KNSCPPTSDLLGSASQLFWEPMKVHDIRWNFEKFLVGPDGVPVMRWfh 199
Cdd:PRK10606   85 TTWGVTFPMFSKIEVNGEGRHPLYQKLiaaapTAVAPEESGFYARMVSKGRAPLYPDDILWNFEKFLVGRDGQVIQRF-- 162
                         170
                  ....*....|..
gi 1851937782 200 kAPVSTVKSDIL 211
Cdd:PRK10606  163 -SPDMTPEDPIV 173
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
53-210 1.85e-25

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: 96.83  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  53 IQFKRYAGKHVLFVNVATYUGLTAQ-YPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEILSGLKHvrpggGFVPNF 131
Cdd:TIGR02540  15 VSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFARR-----NYGVTF 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1851937782 132 QLFEKGDVNGEKEQKVFTFLKNSCPPtsdllgsasqlfwEPmkvhdiRWNFEKFLVGPDGVPVMRWFHKAPVSTVKSDI 210
Cdd:TIGR02540  90 PMFSKIKILGSEAEPAFRFLVDSSKK-------------EP------RWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEI 149
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
38-210 4.34e-61

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: 188.11  E-value: 4.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  38 TIYEYGALTLNEEEyIQFKRYAGKHVLFVNVATYUGLTAQYPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEILSG 117
Cdd:cd00340     1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782 118 LKHVRPgggfvPNFQLFEKGDVNGEKEQKVFTFLKNSCPPTSDllgsasqlfwepmkvHDIRWNFEKFLVGPDGVPVMRW 197
Cdd:cd00340    80 CETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG---------------KDIKWNFTKFLVDRDGEVVKRF 139
                         170
                  ....*....|...
gi 1851937782 198 FHKAPVSTVKSDI 210
Cdd:cd00340   140 APTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
39-152 7.34e-53

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 165.60  E-value: 7.34e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  39 IYEYGALTLNEEeYIQFKRYAGKHVLFVNVATYUGLTAQYPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEIlsgl 118
Cdd:pfam00255   1 IYEFSAKDIDGE-PVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1851937782 119 KHVRPgGGFVPNFQLFEKGDVNGEKEQKVFTFLK 152
Cdd:pfam00255  76 KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
38-197 9.80e-47

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 151.77  E-value: 9.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  38 TIYEYGALTLNEEEyIQFKRYAGKHVLFVNVATYUGLTAQYPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEILS- 116
Cdd:COG0386     3 SIYDFSVTTLDGEP-VSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEf 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782 117 -----GLKhvrpgggfvpnFQLFEKGDVNGEKEQKVFTFLKNSCPptsdllgsasqlfwEPMKVHDIRWNFEKFLVGPDG 191
Cdd:COG0386    82 cslnyGVT-----------FPMFAKIDVNGPNAHPLYKYLKEEAP--------------GLLGGGDIKWNFTKFLIDRDG 136

                  ....*.
gi 1851937782 192 VPVMRW 197
Cdd:COG0386   137 NVVARF 142
btuE PRK10606
putative glutathione peroxidase; Provisional
45-211 9.55e-34

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 119.11  E-value: 9.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  45 LTLNEEEYIQFKRYAGKHVLFVNVATYUGLTAQYPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEILSGLKhvrpg 124
Cdd:PRK10606   10 VTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYCR----- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782 125 GGFVPNFQLFEKGDVNGEKEQKVFTFL-----KNSCPPTSDLLGSASQLFWEPMKVHDIRWNFEKFLVGPDGVPVMRWfh 199
Cdd:PRK10606   85 TTWGVTFPMFSKIEVNGEGRHPLYQKLiaaapTAVAPEESGFYARMVSKGRAPLYPDDILWNFEKFLVGRDGQVIQRF-- 162
                         170
                  ....*....|..
gi 1851937782 200 kAPVSTVKSDIL 211
Cdd:PRK10606  163 -SPDMTPEDPIV 173
PLN02412 PLN02412
probable glutathione peroxidase
53-216 4.83e-29

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 106.61  E-value: 4.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  53 IQFKRYAGKHVLFVNVATYUGLT-AQYPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEILSGLKHVrpgggFVPNF 131
Cdd:PLN02412   22 VSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQTVCTR-----FKAEF 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782 132 QLFEKGDVNGEKEQKVFTFLKNScppTSDLLGSAsqlfwepmkvhdIRWNFEKFLVGPDGVPVMRWFHKAPVSTVKSDIL 211
Cdd:PLN02412   97 PIFDKVDVNGKNTAPLYKYLKAE---KGGLFGDA------------IKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQ 161

                  ....*
gi 1851937782 212 EYLKQ 216
Cdd:PLN02412  162 NLLGQ 166
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
36-216 1.43e-28

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 106.00  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  36 TGTIYEYGALTLNEEEyIQFKRYAGKHV-LFVNVATYUGLTAQ-YPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSE 113
Cdd:PTZ00256   17 TKSFFEFEAIDIDGQL-VQLSKFKGKKAiIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782 114 ILSGLKHvrpggGFVPNFQLFEKGDVNGEKEQKVFTFLKNScpptSDLLGSASQlfwepmKVHDIRWNFEKFLVGPDGVP 193
Cdd:PTZ00256   96 IKEYVQK-----KFNVDFPLFQKIEVNGENTHEIYKYLRRN----SELFQNNTN------EARQIPWNFAKFLIDGQGKV 160
                         170       180
                  ....*....|....*....|...
gi 1851937782 194 VMRWFHKAPVSTVKSDILEYLKQ 216
Cdd:PTZ00256  161 VKYFSPKVNPNEMIQDIEKLLNA 183
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
38-197 1.29e-26

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 102.29  E-value: 1.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  38 TIYEYGALTLNEEEyIQFKRYAGKHVLFVNVATYUGLTA-QYPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEIlS 116
Cdd:PLN02399   78 SVHDFTVKDIDGKD-VALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEI-K 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782 117 GLKHVRpgggFVPNFQLFEKGDVNGEKEQKVFTFLKNScppTSDLLGSAsqlfwepmkvhdIRWNFEKFLVGPDGVPVMR 196
Cdd:PLN02399  156 QFACTR----FKAEFPIFDKVDVNGPSTAPVYQFLKSN---AGGFLGDL------------IKWNFEKFLVDKNGKVVER 216

                  .
gi 1851937782 197 W 197
Cdd:PLN02399  217 Y 217
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
53-210 1.85e-25

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: 96.83  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  53 IQFKRYAGKHVLFVNVATYUGLTAQ-YPELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEILSGLKHvrpggGFVPNF 131
Cdd:TIGR02540  15 VSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFARR-----NYGVTF 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1851937782 132 QLFEKGDVNGEKEQKVFTFLKNSCPPtsdllgsasqlfwEPmkvhdiRWNFEKFLVGPDGVPVMRWFHKAPVSTVKSDI 210
Cdd:TIGR02540  90 PMFSKIKILGSEAEPAFRFLVDSSKK-------------EP------RWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEI 149
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
38-191 1.26e-17

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 77.59  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851937782  38 TIYEYGALTLnEEEYIQFKRYAGKHVLFVNVATYUGLTAQY-PELNALQDELKPSGVVVLGFPCNQFGKQEPGKNSEILS 116
Cdd:PTZ00056   18 SIYDYTVKTL-EGTTVPMSSLKNKVLMITNSASKCGLTKKHvDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRK 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1851937782 117 GLKHvrpgggFVPNFQLFEKGDVNGEKEQKVFTFLKNSCPPTSDLLGSASqlfwepmkvhDIRWNFEKFLVGPDG 191
Cdd:PTZ00056   97 FNDK------NKIKYNFFEPIEVNGENTHELFKFLKANCDSMHDENGTLK----------AIGWNFGKFLVNKSG 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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