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Conserved domains on  [gi|1958749621|ref|XP_038957865|]
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probable glutathione peroxidase 8 isoform X1 [Rattus norvegicus]

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 ...
 46-132 1.16e-52

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 TIGR02540:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 153  Bit Score: 163.47  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749621  46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEI--L 123
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIesF 80


                  ....*....
gi 1958749621 124 PRRNQGGTF 132
Cdd:TIGR02540  81 ARRNYGVTF 89
 
Name Accession Description Interval E-value
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 46-132 1.16e-52

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: 163.47  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749621  46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEI--L 123
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIesF 80


                  ....*....
gi 1958749621 124 PRRNQGGTF 132
Cdd:TIGR02540  81 ARRNYGVTF 89
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 46-132 2.96e-37

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: 124.16  E-value: 2.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749621  46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTdKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEILP- 124
Cdd:cd00340     1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEf 79


                  ....*....
gi 1958749621 125 -RRNQGGTF 132
Cdd:cd00340    80 cETNYGVTF 88
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 46-122 1.04e-29

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 105.16  E-value: 1.04e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749621  46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTdKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEI 122
Cdd:COG0386     3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEI 78
GSHPx pfam00255
Glutathione peroxidase;
47-122 2.60e-29

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 102.82  E-value: 2.60e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749621  47 FYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKsYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEI 122
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQ-YTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI 75
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 42-123 6.39e-24

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 91.36  E-value: 6.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749621  42 PRINSFYSFEVKDAKGRMVSLEKFKG-KASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSK 120
Cdd:PTZ00256   15 PPTKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEP 94


                  ...
gi 1958749621 121 EIL 123
Cdd:PTZ00256   95 EIK 97
 
Name Accession Description Interval E-value
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 46-132 1.16e-52

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: 163.47  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749621  46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEI--L 123
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIesF 80


                  ....*....
gi 1958749621 124 PRRNQGGTF 132
Cdd:TIGR02540  81 ARRNYGVTF 89
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 46-132 2.96e-37

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: 124.16  E-value: 2.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749621  46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTdKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEILP- 124
Cdd:cd00340     1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEf 79


                  ....*....
gi 1958749621 125 -RRNQGGTF 132
Cdd:cd00340    80 cETNYGVTF 88
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 46-122 1.04e-29

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 105.16  E-value: 1.04e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749621  46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTdKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEI 122
Cdd:COG0386     3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEI 78
GSHPx pfam00255
Glutathione peroxidase;
47-122 2.60e-29

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 102.82  E-value: 2.60e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749621  47 FYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKsYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEI 122
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQ-YTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI 75
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 42-123 6.39e-24

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 91.36  E-value: 6.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749621  42 PRINSFYSFEVKDAKGRMVSLEKFKG-KASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSK 120
Cdd:PTZ00256   15 PPTKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEP 94


                  ...
gi 1958749621 121 EIL 123
Cdd:PTZ00256   95 EIK 97
PLN02412 PLN02412
probable glutathione peroxidase
 46-123 1.06e-21

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 85.04  E-value: 1.06e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749621  46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEIL 123
Cdd:PLN02412    8 SIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQ 85
btuE PRK10606
putative glutathione peroxidase; Provisional
 45-122 1.50e-21

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 85.21  E-value: 1.50e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749621  45 NSFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTdKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEI 122
Cdd:PRK10606    3 DSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLT-PQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI 79
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 46-122 1.93e-21

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 86.11  E-value: 1.93e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749621  46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEI 122
Cdd:PLN02399   78 SVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEI 154
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 46-122 6.36e-17

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 73.35  E-value: 6.36e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749621  46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEI 122
Cdd:PTZ00056   18 SIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDI 94
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
50-105 1.86e-05

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 41.77  E-value: 1.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749621  50 FEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLA 105
Cdd:COG1225     4 FTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLG 59
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 50-105 7.16e-04

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 36.83  E-value: 7.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749621  50 FEVKDAKGRMVSLEKFKGKAsLVVNV-ASDCRFTDKSYETLRELHKEFGPYHFNVLA 105
Cdd:cd02966     2 FSLPDLDGKPVSLSDLKGKV-VLVNFwASWCPPCRAEMPELEALAKEYKDDGVEVVG 57
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 46-101 1.84e-03

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 36.21  E-value: 1.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749621  46 SFYSFEVKDAKGRMVSLEKFKGKAsLVVNV-ASDCRFTDKSYETLRELHKEFGPYHF 101
Cdd:COG0526     7 PAPDFTLTDLDGKPLSLADLKGKP-VLVNFwATWCPPCRAEMPVLKELAEEYGGVVF 62
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 49-105 2.93e-03

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 35.28  E-value: 2.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749621  49 SFEVKDAKGRMVSLEKFKGKASLVVNVASD-CRFTDKSYETLRELHKEFGPYHFNVLA 105
Cdd:pfam00578   7 DFELPDGDGGTVSLSDYRGKWVVLFFYPADwTPVCTTELPALADLYEEFKKLGVEVLG 64
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 49-105 6.59e-03

Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF.


Pssm-ID: 239267 [Multi-domain]  Cd Length: 171  Bit Score: 34.91  E-value: 6.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749621  49 SFEVKDAKGRMVSLEKF-KGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLA 105
Cdd:cd02969     6 DFSLPDTDGKTYSLADFaDGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVA 63
 
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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