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Conserved domains on  [gi|15618997|ref|NP_056511|]
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glutathione peroxidase 7 precursor [Homo sapiens]

Protein Classification

glutathione peroxidase( domain architecture ID 10798236)

glutathione peroxidase catalyzes the reduction of hydroperoxides using GSH as a specific electron donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 24-176 2.00e-114

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: 321.78  E-value: 2.00e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997    24 DFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESF 103
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15618997   104 ARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQTSGKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITALV 176
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
 
Name Accession Description Interval E-value
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 24-176 2.00e-114

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: 321.78  E-value: 2.00e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997    24 DFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESF 103
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15618997   104 ARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQTSGKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITALV 176
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 24-172 3.70e-82

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: 240.11  E-value: 3.70e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997  24 DFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQhYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESF 103
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQ-YEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15618997 104 ARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQ----TSGKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQI 172
Cdd:cd00340  80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEeapgLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 24-180 2.59e-73

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 218.02  E-value: 2.59e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997  24 DFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQhYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESF 103
Cdd:COG0386   3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQ-YEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997 104 ARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQTS-----GKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEvrPQITALVRK 178
Cdd:COG0386  82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEApgllgGGDIKWNFTKFLIDRDGNVVARFAPTTKPED--PELEAAIEK 159


                ..
gi 15618997 179 LI 180
Cdd:COG0386 160 LL 161
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 25-175 3.26e-51

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 162.62  E-value: 3.26e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997   25 FYDFKAVNIRGKLVSLEKYRG-SVSLVVNVASECGFTDQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESF 103
Cdd:PTZ00256  20 FFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIKEY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997  104 ARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQTS---------GKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITA 174
Cdd:PTZ00256 100 VQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSelfqnntneARQIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQDIEK 179


                 .
gi 15618997  175 L 175
Cdd:PTZ00256 180 L 180
GSHPx pfam00255
Glutathione peroxidase;
25-132 2.56e-47

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 150.20  E-value: 2.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997    25 FYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQhYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESFA 104
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQ-YTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79

                          90       100
                  ....*....|....*....|....*...
gi 15618997   105 RRTYSVSFPMFSKIAVTGTGAHPAFKYL 132
Cdd:pfam00255  80 PGGYGVTFPLFSKIEVNGEKAHPVYKFL 107
 
Name Accession Description Interval E-value
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 24-176 2.00e-114

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: 321.78  E-value: 2.00e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997    24 DFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESF 103
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15618997   104 ARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQTSGKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITALV 176
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 24-172 3.70e-82

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: 240.11  E-value: 3.70e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997  24 DFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQhYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESF 103
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQ-YEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15618997 104 ARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQ----TSGKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQI 172
Cdd:cd00340  80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEeapgLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 24-180 2.59e-73

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 218.02  E-value: 2.59e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997  24 DFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQhYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESF 103
Cdd:COG0386   3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQ-YEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997 104 ARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQTS-----GKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEvrPQITALVRK 178
Cdd:COG0386  82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEApgllgGGDIKWNFTKFLIDRDGNVVARFAPTTKPED--PELEAAIEK 159


                ..
gi 15618997 179 LI 180
Cdd:COG0386 160 LL 161
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 25-175 3.26e-51

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 162.62  E-value: 3.26e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997   25 FYDFKAVNIRGKLVSLEKYRG-SVSLVVNVASECGFTDQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESF 103
Cdd:PTZ00256  20 FFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIKEY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997  104 ARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQTS---------GKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITA 174
Cdd:PTZ00256 100 VQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSelfqnntneARQIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQDIEK 179


                 .
gi 15618997  175 L 175
Cdd:PTZ00256 180 L 180
GSHPx pfam00255
Glutathione peroxidase;
25-132 2.56e-47

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 150.20  E-value: 2.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997    25 FYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQhYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESFA 104
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQ-YTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79

                          90       100
                  ....*....|....*....|....*...
gi 15618997   105 RRTYSVSFPMFSKIAVTGTGAHPAFKYL 132
Cdd:pfam00255  80 PGGYGVTFPLFSKIEVNGEKAHPVYKFL 107
btuE PRK10606
putative glutathione peroxidase; Provisional
 22-183 1.73e-43

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 142.99  E-value: 1.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997   22 EQDFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQhYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIE 101
Cdd:PRK10606   2 QDSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQ-YEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997  102 SFARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQ------------------TSGKEPT------WNFWKYLVAPDGKVVG 157
Cdd:PRK10606  81 TYCRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAaaptavapeesgfyarmvSKGRAPLypddilWNFEKFLVGRDGQVIQ 160

                        170       180
                 ....*....|....*....|....*.
gi 15618997  158 AWDPTVSVEEvrPQITALVrKLILLK 183
Cdd:PRK10606 161 RFSPDMTPED--PIVMESI-KLALAK 183
PLN02412 PLN02412
probable glutathione peroxidase
 23-176 1.17e-42

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 140.51  E-value: 1.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997   23 QDFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIES 102
Cdd:PLN02412   7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15618997  103 FARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQTSG----KEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITALV 176
Cdd:PLN02412  87 TVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGglfgDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLL 164
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 22-175 2.04e-40

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 136.95  E-value: 2.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997   22 EQDFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIE 101
Cdd:PLN02399  76 EKSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIK 155

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15618997  102 SFARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQTS----GKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITAL 175
Cdd:PLN02399 156 QFACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAggflGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKL 233
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 25-178 2.07e-34

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 120.34  E-value: 2.07e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997   25 FYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESFA 104
Cdd:PTZ00056  19 IYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRKFN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997  105 RRtYSVSFPMFSKIAVTGTGAHPAFKYLAQTSG---------KEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITAL 175
Cdd:PTZ00056  99 DK-NKIKYNFFEPIEVNGENTHELFKFLKANCDsmhdengtlKAIGWNFGKFLVNKSGNVVAYFSPRTEPLELEKKIAEL 177


                 ...
gi 15618997  176 VRK 178
Cdd:PTZ00056 178 LGV 180
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
27-179 3.05e-08

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 50.25  E-value: 3.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997  27 DFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQHYRALQQLQRDLGPHHFNVLAFpcnqfgqqEPDSNKEIESFARR 106
Cdd:COG1225   3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGV--------SSDSDEAHKKFAEK 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15618997 107 tYSVSFPMFS----KIAVT-GTGAHPAFkylaqtsgkeptwnfwkYLVAPDGKVVGAWDPTVSV-EEVRPQITALVRKL 179
Cdd:COG1225  75 -YGLPFPLLSdpdgEVAKAyGVRGTPTT-----------------FLIDPDGKIRYVWVGPVDPrPHLEEVLEALLAEL 135
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 27-176 6.01e-04

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: 38.76  E-value: 6.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997  27 DFKAVNIRGKLVSLEKYRGSVSLVVNVAS-ECGFTDQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESFAR 105
Cdd:cd02969   6 DFSLPDTDGKTYSLADFADGKALVVMFICnHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPENMKAKAK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997 106 RtYSVSFPMFskiaVTGTGAhpafkyLAQTSGKEPTWNFwkYLVAPDGKVV---------GAWDPTVSVEEVRPQITALV 176
Cdd:cd02969  86 E-HGYPFPYL----LDETQE------VAKAYGAACTPDF--FLFDPDGKLVyrgriddsrPGNDPPVTGRDLRAALDALL 152
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 27-116 6.55e-04

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: 37.97  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997    27 DFKAVNIRGKLVSLEKYRGSVsLVVNV--ASECGFTDQHYRALQQLQRDLGPHHFNVLAFpcnqfgqqEPDSNKEIESFA 104
Cdd:pfam00578   7 DFELPDGDGGTVSLSDYRGKW-VVLFFypADWTPVCTTELPALADLYEEFKKLGVEVLGV--------SVDSPESHKAFA 77

                          90
                  ....*....|..
gi 15618997   105 RRtYSVSFPMFS 116
Cdd:pfam00578  78 EK-YGLPFPLLS 88
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 20-178 7.45e-03

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 35.05  E-value: 7.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997  20 QQEQDFYDFKAVNIRGKLVSLEKYRGSVsLVVNV-ASECGFTDQHYRALQQLQRDLGPhhFNVLAFPCNqfgqqepDSNK 98
Cdd:COG0526   3 AVGKPAPDFTLTDLDGKPLSLADLKGKP-VLVNFwATWCPPCRAEMPVLKELAEEYGG--VVFVGVDVD-------ENPE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15618997  99 EIESFARRtYSVSFP--------MFSKIAVTGTgahpafkylaqtsgkePTWnfwkYLVAPDGKVVGAWDPTVSVEEVRP 170
Cdd:COG0526  73 AVKAFLKE-LGLPYPvlldpdgeLAKAYGVRGI----------------PTT----VLIDKDGKIVARHVGPLSPEELEE 131


                ....*...
gi 15618997 171 QITALVRK 178
Cdd:COG0526 132 ALEKLLAK 139
 
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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