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Conserved domains on  [gi|6715602|ref|NP_003987|]
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epididymal secretory glutathione peroxidase isoform 2 precursor [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 ...
 40-90 3.76e-15

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: 65.07  E-value: 3.76e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6715602     40 IYDYEAIALNKnEYVSFKQYVGKHILFVNVATYCGLTAQYPgmsvQGEDLY 90
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTPQYT----QLEELQ 46
 
Name Accession Description Interval E-value
GSHPx pfam00255
Glutathione peroxidase;
40-90 3.76e-15

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 65.07  E-value: 3.76e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6715602     40 IYDYEAIALNKnEYVSFKQYVGKHILFVNVATYCGLTAQYPgmsvQGEDLY 90
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTPQYT----QLEELQ 46
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 39-90 1.26e-12

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: 59.45  E-value: 1.26e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6715602   39 TIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLTAQYPGMsvqgEDLY 90
Cdd:cd00340   1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGL----EALY 47
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 39-90 9.32e-12

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 57.39  E-value: 9.32e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6715602   39 TIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLTAQYPGMsvqgEDLY 90
Cdd:COG0386   3 SIYDFSVTTLDGEP-VSLSDYKGKVLLIVNTASKCGFTPQYEGL----EALY 49
btuE PRK10606
putative glutathione peroxidase; Provisional
 39-90 4.32e-06

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 42.84  E-value: 4.32e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6715602    39 TIYDYEAIALNkNEYVSFKQYVGKHILFVNVATYCGLTAQYPGMsvqgEDLY 90
Cdd:PRK10606   4 SILTTVVTTID-GEVTTLEKYAGNVLLIVNVASKCGLTPQYEQL----ENIQ 50
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 41-78 1.61e-03

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: 35.58  E-value: 1.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6715602     41 YDYEAIALnKNEYVSFKQYVGKHILFVNVATYCGLTAQ 78
Cdd:TIGR02540   3 YSFEVKDA-RGRTVSLEKYRGKVSLVVNVASECGFTDQ 39
 
Name Accession Description Interval E-value
GSHPx pfam00255
Glutathione peroxidase;
40-90 3.76e-15

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 65.07  E-value: 3.76e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6715602     40 IYDYEAIALNKnEYVSFKQYVGKHILFVNVATYCGLTAQYPgmsvQGEDLY 90
Cdd:pfam00255   1 IYEFSAKDIDG-EPVPFDQYRGKVVLIVNVASKCGLTPQYT----QLEELQ 46
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 39-90 1.26e-12

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: 59.45  E-value: 1.26e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6715602   39 TIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLTAQYPGMsvqgEDLY 90
Cdd:cd00340   1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGL----EALY 47
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 39-90 9.32e-12

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 57.39  E-value: 9.32e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6715602   39 TIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLTAQYPGMsvqgEDLY 90
Cdd:COG0386   3 SIYDFSVTTLDGEP-VSLSDYKGKVLLIVNTASKCGFTPQYEGL----EALY 49
btuE PRK10606
putative glutathione peroxidase; Provisional
 39-90 4.32e-06

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 42.84  E-value: 4.32e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6715602    39 TIYDYEAIALNkNEYVSFKQYVGKHILFVNVATYCGLTAQYPGMsvqgEDLY 90
Cdd:PRK10606   4 SILTTVVTTID-GEVTTLEKYAGNVLLIVNVASKCGLTPQYEQL----ENIQ 50
PLN02412 PLN02412
probable glutathione peroxidase
 39-84 5.49e-05

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 39.59  E-value: 5.49e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 6715602    39 TIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLT-AQYPGMSV 84
Cdd:PLN02412   8 SIYDFTVKDIGGND-VSLNQYKGKVLLIVNVASKCGLTdSNYKELNV 53
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 36-77 3.98e-04

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 37.57  E-value: 3.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 6715602    36 EKgTIYDYEAIALNKNEyVSFKQYVGKHILFVNVATYCGLTA 77
Cdd:PLN02399  76 EK-SVHDFTVKDIDGKD-VALSKFKGKVLLIVNVASKCGLTS 115
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 34-78 4.63e-04

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 37.05  E-value: 4.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 6715602    34 KDEKGTIYDYEAIALNKNEyVSFKQYVGKH-ILFVNVATYCGLTAQ 78
Cdd:PTZ00256  14 QPPTKSFFEFEAIDIDGQL-VQLSKFKGKKaIIVVNVACKCGLTSD 58
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 41-78 1.61e-03

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: 35.58  E-value: 1.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6715602     41 YDYEAIALnKNEYVSFKQYVGKHILFVNVATYCGLTAQ 78
Cdd:TIGR02540   3 YSFEVKDA-RGRTVSLEKYRGKVSLVVNVASECGFTDQ 39
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 39-79 4.61e-03

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 34.44  E-value: 4.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 6715602    39 TIYDYEAIALNKNEYvSFKQYVGKHILFVNVATYCGLTAQY 79
Cdd:PTZ00056  18 SIYDYTVKTLEGTTV-PMSSLKNKVLMITNSASKCGLTKKH 57
 
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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