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Conserved domains on  [gi|90903238|ref|NP_001034936|]
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phospholipid hydroperoxide glutathione peroxidase GPX4 isoform B 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

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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 ...
40-168 6.36e-72

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: 215.84  E-value: 6.36e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238  40 SMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGkTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEF 119
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCG-FTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 90903238 120 AAG-YNVKFDMFSKICVNGDDAHPLWKWMKIQPkgKGILGNAIKWNFTKF 168
Cdd:cd00340  80 CETnYGVTFPMFAKIDVNGENAHPLYKYLKEEA--PGLLGKDIKWNFTKF 127
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
40-168 6.36e-72

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: 215.84  E-value: 6.36e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238  40 SMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGkTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEF 119
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCG-FTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 90903238 120 AAG-YNVKFDMFSKICVNGDDAHPLWKWMKIQPkgKGILGNAIKWNFTKF 168
Cdd:cd00340  80 CETnYGVTFPMFAKIDVNGENAHPLYKYLKEEA--PGLLGKDIKWNFTKF 127
GSHPx pfam00255
Glutathione peroxidase;
41-148 1.09e-63

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 193.34  E-value: 1.09e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238    41 MHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGKTEvNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFA 120
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
                          90       100
                  ....*....|....*....|....*....
gi 90903238   121 AG-YNVKFDMFSKICVNGDDAHPLWKWMK 148
Cdd:pfam00255  80 PGgYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
40-168 1.53e-61

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 189.52  E-value: 1.53e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238  40 SMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGKTEvNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEF 119
Cdd:COG0386   3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 90903238 120 -AAGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGIlGNAIKWNFTKF 168
Cdd:COG0386  82 cSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLG-GGDIKWNFTKF 130
PLN02412 PLN02412
probable glutathione peroxidase
39-168 6.38e-46

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 150.14  E-value: 6.38e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238   39 RSMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKE 118
Cdd:PLN02412   7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 90903238  119 FAAG-YNVKFDMFSKICVNGDDAHPLWKWMKIQpKGkGILGNAIKWNFTKF 168
Cdd:PLN02412  87 TVCTrFKAEFPIFDKVDVNGKNTAPLYKYLKAE-KG-GLFGDAIKWNFTKF 135
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
40-168 3.82e-38

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: 129.96  E-value: 3.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238    40 SMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEF 119
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 90903238   120 A-AGYNVKFDMFSKICVNGDDAHPLWKWMkIQPKGKgilgnAIKWNFTKF 168
Cdd:TIGR02540  81 ArRNYGVTFPMFSKIKILGSEAEPAFRFL-VDSSKK-----EPRWNFWKY 124
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
40-168 6.36e-72

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: 215.84  E-value: 6.36e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238  40 SMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGkTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEF 119
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCG-FTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 90903238 120 AAG-YNVKFDMFSKICVNGDDAHPLWKWMKIQPkgKGILGNAIKWNFTKF 168
Cdd:cd00340  80 CETnYGVTFPMFAKIDVNGENAHPLYKYLKEEA--PGLLGKDIKWNFTKF 127
GSHPx pfam00255
Glutathione peroxidase;
41-148 1.09e-63

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 193.34  E-value: 1.09e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238    41 MHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGKTEvNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFA 120
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
                          90       100
                  ....*....|....*....|....*....
gi 90903238   121 AG-YNVKFDMFSKICVNGDDAHPLWKWMK 148
Cdd:pfam00255  80 PGgYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
40-168 1.53e-61

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 189.52  E-value: 1.53e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238  40 SMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGKTEvNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEF 119
Cdd:COG0386   3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 90903238 120 -AAGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGIlGNAIKWNFTKF 168
Cdd:COG0386  82 cSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLG-GGDIKWNFTKF 130
PLN02412 PLN02412
probable glutathione peroxidase
39-168 6.38e-46

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 150.14  E-value: 6.38e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238   39 RSMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKE 118
Cdd:PLN02412   7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 90903238  119 FAAG-YNVKFDMFSKICVNGDDAHPLWKWMKIQpKGkGILGNAIKWNFTKF 168
Cdd:PLN02412  87 TVCTrFKAEFPIFDKVDVNGKNTAPLYKYLKAE-KG-GLFGDAIKWNFTKF 135
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
39-168 9.44e-46

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 151.98  E-value: 9.44e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238   39 RSMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKE 118
Cdd:PLN02399  77 KSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQ 156
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 90903238  119 FAAG-YNVKFDMFSKICVNGDDAHPLWKWMKiqPKGKGILGNAIKWNFTKF 168
Cdd:PLN02399 157 FACTrFKAEFPIFDKVDVNGPSTAPVYQFLK--SNAGGFLGDLIKWNFEKF 205
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
38-168 3.20e-44

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 146.44  E-value: 3.20e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238   38 ARSMHEFSAKDIDGHMVNLDKYRGFVC-IVTNVASQUGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEI 116
Cdd:PTZ00256  17 TKSFFEFEAIDIDGQLVQLSKFKGKKAiIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEI 96
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 90903238  117 KEFA-AGYNVKFDMFSKICVNGDDAHPLWKWMKIQP---KGKGILGNAIKWNFTKF 168
Cdd:PTZ00256  97 KEYVqKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSelfQNNTNEARQIPWNFAKF 152
btuE PRK10606
putative glutathione peroxidase; Provisional
47-168 9.16e-39

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 132.20  E-value: 9.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238   47 KDIDGHMVNLDKYRGFVCIVTNVASQUGKTEvNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFAAG-YNV 125
Cdd:PRK10606  11 TTIDGEVTTLEKYAGNVLLIVNVASKCGLTP-QYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYCRTtWGV 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90903238  126 KFDMFSKICVNGDDAHPLWKWM------KIQPKGKGIL------GNA------IKWNFTKF 168
Cdd:PRK10606  90 TFPMFSKIEVNGEGRHPLYQKLiaaaptAVAPEESGFYarmvskGRAplypddILWNFEKF 150
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
40-168 3.82e-38

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: 129.96  E-value: 3.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238    40 SMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEF 119
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 90903238   120 A-AGYNVKFDMFSKICVNGDDAHPLWKWMkIQPKGKgilgnAIKWNFTKF 168
Cdd:TIGR02540  81 ArRNYGVTFPMFSKIKILGSEAEPAFRFL-VDSSKK-----EPRWNFWKY 124
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
39-168 2.12e-35

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 124.19  E-value: 2.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90903238   39 RSMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKE 118
Cdd:PTZ00056  17 KSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRK 96
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 90903238  119 FAAGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKG----KGILgNAIKWNFTKF 168
Cdd:PTZ00056  97 FNDKNKIKYNFFEPIEVNGENTHELFKFLKANCDSmhdeNGTL-KAIGWNFGKF 149
 
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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