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Conserved domains on  [gi|807201056|ref|NP_001293130|]
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probable glutathione peroxidase 8 isoform d [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 ...
 14-105 7.90e-60

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: 180.42  E-value: 7.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056   14 PRAKFGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWKPEEP 93
Cdd:TIGR02540  62 PCNQFGESEPDSSKEIESFARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEP 141

                          90
                  ....*....|..
gi 807201056   94 IEVIRPDIAALV 105
Cdd:TIGR02540 142 VEEIRPEITALV 153
 
Name Accession Description Interval E-value
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 14-105 7.90e-60

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: 180.42  E-value: 7.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056   14 PRAKFGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWKPEEP 93
Cdd:TIGR02540  62 PCNQFGESEPDSSKEIESFARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEP 141

                          90
                  ....*....|..
gi 807201056   94 IEVIRPDIAALV 105
Cdd:TIGR02540 142 VEEIRPEITALV 153
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 18-101 1.42e-32

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: 111.45  E-value: 1.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056  18 FGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSK----KEPRWNFWKYLVNPEGQVVKFWKPEEP 93
Cdd:cd00340   65 FGGQEPGSNEEIKEFCETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPgllgKDIKWNFTKFLVDRDGEVVKRFAPTTD 144


                 ....*...
gi 807201056  94 IEVIRPDI 101
Cdd:cd00340  145 PEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 18-104 1.23e-24

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 91.29  E-value: 1.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056  18 FGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSK-----KEPRWNFWKYLVNPEGQVVKFW---- 88
Cdd:COG0386   67 FGGQEPGSNEEIAEFCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPgllggGDIKWNFTKFLIDRDGNVVARFaptt 146

                         90
                 ....*....|....*.
gi 807201056  89 KPEEPIevIRPDIAAL 104
Cdd:COG0386  147 KPEDPE--LEAAIEKL 160
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 14-107 1.20e-21

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 84.43  E-value: 1.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056  14 PRAKFGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFL------VDSSKKEPR---WNFWKYLVNPEGQV 84
Cdd:PTZ00256  81 PCNQFMEQEPWDEPEIKEYVQKKFNVDFPLFQKIEVNGENTHEIYKYLrrnselFQNNTNEARqipWNFAKFLIDGQGKV 160

                         90       100
                 ....*....|....*....|...
gi 807201056  85 VKFWKPEEPIEVIRPDIAALVRQ 107
Cdd:PTZ00256 161 VKYFSPKVNPNEMIQDIEKLLNA 183
GSHPx pfam00255
Glutathione peroxidase;
14-61 1.97e-09

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 50.81  E-value: 1.97e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 807201056   14 PRAKFGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFL 61
Cdd:pfam00255  60 PCNQFGKQEPGSNEEIKYFCPGGYGVTFPLFSKIEVNGEKAHPVYKFL 107
 
Name Accession Description Interval E-value
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 14-105 7.90e-60

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: 180.42  E-value: 7.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056   14 PRAKFGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWKPEEP 93
Cdd:TIGR02540  62 PCNQFGESEPDSSKEIESFARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEP 141

                          90
                  ....*....|..
gi 807201056   94 IEVIRPDIAALV 105
Cdd:TIGR02540 142 VEEIRPEITALV 153
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 18-101 1.42e-32

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: 111.45  E-value: 1.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056  18 FGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSK----KEPRWNFWKYLVNPEGQVVKFWKPEEP 93
Cdd:cd00340   65 FGGQEPGSNEEIKEFCETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPgllgKDIKWNFTKFLVDRDGEVVKRFAPTTD 144


                 ....*...
gi 807201056  94 IEVIRPDI 101
Cdd:cd00340  145 PEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 18-104 1.23e-24

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 91.29  E-value: 1.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056  18 FGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSK-----KEPRWNFWKYLVNPEGQVVKFW---- 88
Cdd:COG0386   67 FGGQEPGSNEEIAEFCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPgllggGDIKWNFTKFLIDRDGNVVARFaptt 146

                         90
                 ....*....|....*.
gi 807201056  89 KPEEPIevIRPDIAAL 104
Cdd:COG0386  147 KPEDPE--LEAAIEKL 160
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 14-107 1.20e-21

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 84.43  E-value: 1.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056  14 PRAKFGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFL------VDSSKKEPR---WNFWKYLVNPEGQV 84
Cdd:PTZ00256  81 PCNQFMEQEPWDEPEIKEYVQKKFNVDFPLFQKIEVNGENTHEIYKYLrrnselFQNNTNEARqipWNFAKFLIDGQGKV 160

                         90       100
                 ....*....|....*....|...
gi 807201056  85 VKFWKPEEPIEVIRPDIAALVRQ 107
Cdd:PTZ00256 161 VKYFSPKVNPNEMIQDIEKLLNA 183
PLN02412 PLN02412
probable glutathione peroxidase
 14-107 1.40e-10

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 54.99  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056  14 PRAKFGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFLvdssKKEP--------RWNFWKYLVNPEGQVV 85
Cdd:PLN02412  69 PCNQFLGQEPGSNEEIQQTVCTRFKAEFPIFDKVDVNGKNTAPLYKYL----KAEKgglfgdaiKWNFTKFLVSKEGKVV 144

                         90       100
                 ....*....|....*....|..
gi 807201056  86 KFWKPEEPIEVIRPDIAALVRQ 107
Cdd:PLN02412 145 QRYAPTTSPLKIEKDIQNLLGQ 166
btuE PRK10606
putative glutathione peroxidase; Provisional
 14-96 6.91e-10

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 53.62  E-value: 6.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056  14 PRAKFGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFLVD------------------SSKKEPR----- 70
Cdd:PRK10606  64 PCNQFLGQEPGSDEEIKTYCRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAaaptavapeesgfyarmvSKGRAPLypddi 143

                         90       100       110
                 ....*....|....*....|....*....|.
gi 807201056  71 -WNFWKYLVNPEGQVVKFWK----PEEPIEV 96
Cdd:PRK10606 144 lWNFEKFLVGRDGQVIQRFSpdmtPEDPIVM 174
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 14-104 9.38e-10

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 53.75  E-value: 9.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056  14 PRAKFGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWK 89
Cdd:PLN02399 139 PCNQFGGQEPGSNPEIKQFACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAggflGDLIKWNFEKFLVDKNGKVVERYP 218

                         90
                 ....*....|....*
gi 807201056  90 PEEPIEVIRPDIAAL 104
Cdd:PLN02399 219 PTTSPFQIEKDIQKL 233
GSHPx pfam00255
Glutathione peroxidase;
14-61 1.97e-09

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 50.81  E-value: 1.97e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 807201056   14 PRAKFGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFL 61
Cdd:pfam00255  60 PCNQFGKQEPGSNEEIKYFCPGGYGVTFPLFSKIEVNGEKAHPVYKFL 107
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 14-105 3.23e-08

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 49.47  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201056  14 PRAKFGESEPRPSKEVESFARKNyGVTFPIFHKIKILGSEGEPAFRFLV---------DSSKKEPRWNFWKYLVNPEGQV 84
Cdd:PTZ00056  79 PTSQFLNQEFPNTKDIRKFNDKN-KIKYNFFEPIEVNGENTHELFKFLKancdsmhdeNGTLKAIGWNFGKFLVNKSGNV 157

                         90       100
                 ....*....|....*....|..
gi 807201056  85 VKFWKPE-EPIEVIrPDIAALV 105
Cdd:PTZ00056 158 VAYFSPRtEPLELE-KKIAELL 178
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 76-106 3.74e-03

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 34.88  E-value: 3.74e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 807201056  76 YLVNPEGQVVKFWKPEEPIEVIRPDIAALVR 106
Cdd:COG1999  125 YLVDPDGRLRGYYPAGEDPEELAADLKALLE 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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