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Conserved domains on  [gi|41406082|ref|NP_958799|]
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glutathione peroxidase 1 isoform 2 [Homo sapiens]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 16-84 6.31e-36

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member pfam00255:

Pssm-ID: 469754  Cd Length: 108  Bit Score: 117.84  E-value: 6.31e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41406082    16 VYAFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTVrDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQ 67
 
Name Accession Description Interval E-value
GSHPx pfam00255
Glutathione peroxidase;
16-84 6.31e-36

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 117.84  E-value: 6.31e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41406082    16 VYAFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTVrDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQ 67
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 15-84 3.13e-34

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: 114.92  E-value: 3.13e-34
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406082  15 SVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:cd00340   1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQ 68
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 15-84 4.62e-28

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 99.38  E-value: 4.62e-28
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406082  15 SVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:COG0386   3 SIYDFSVTTL-DGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQ 70
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 15-90 1.15e-18

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: 75.26  E-value: 1.15e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41406082    15 SVYAFSARPlAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQVRRAER 90
Cdd:TIGR02540   1 DFYSFEVKD-ARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSK 75
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 15-84 6.12e-18

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 74.50  E-value: 6.12e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406082   15 SVYAFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:PTZ00056  18 SIYDYTVKTLEG-TTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQ 86
 
Name Accession Description Interval E-value
GSHPx pfam00255
Glutathione peroxidase;
16-84 6.31e-36

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 117.84  E-value: 6.31e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41406082    16 VYAFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTVrDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQ 67
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 15-84 3.13e-34

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: 114.92  E-value: 3.13e-34
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406082  15 SVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:cd00340   1 SIYDFSVKDI-DGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQ 68
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 15-84 4.62e-28

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 99.38  E-value: 4.62e-28
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406082  15 SVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTvRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:COG0386   3 SIYDFSVTTL-DGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQ 70
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 15-90 1.15e-18

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: 75.26  E-value: 1.15e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41406082    15 SVYAFSARPlAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQVRRAER 90
Cdd:TIGR02540   1 DFYSFEVKD-ARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSK 75
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 15-84 6.12e-18

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 74.50  E-value: 6.12e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406082   15 SVYAFSARPLAGgEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:PTZ00056  18 SIYDYTVKTLEG-TTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQ 86
btuE PRK10606
putative glutathione peroxidase; Provisional
 27-84 2.81e-16

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 69.80  E-value: 2.81e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 41406082   27 GEPVSLGSLRGKVLLIENVASLUGTTvRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:PRK10606  15 GEVTTLEKYAGNVLLIVNVASKCGLT-PQYEQLENIQKAWADQGFVVLGFPCNQFLGQ 71
PLN02412 PLN02412
probable glutathione peroxidase
 14-84 4.18e-16

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 68.86  E-value: 4.18e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41406082   14 QSVYAFSARPLaGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:PLN02412   7 KSIYDFTVKDI-GGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQ 76
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 14-84 6.48e-16

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 69.54  E-value: 6.48e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41406082   14 QSVYAFSARPLAGGEpVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:PLN02399  77 KSVHDFTVKDIDGKD-VALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQ 146
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 15-84 4.67e-14

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 64.01  E-value: 4.67e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41406082   15 SVYAFSARPLAGGEpVSLGSLRG-KVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQ 84
Cdd:PTZ00256  19 SFFEFEAIDIDGQL-VQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQ 88
 
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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