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Conserved domains on  [gi|148233237|ref|NP_001085022|]
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probable glutathione peroxidase 8-A [Xenopus laevis]

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 ...
 46-198 4.01e-110

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: 311.77  E-value: 4.01e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237   46 DFYSYEVTDAKGRAVALSKYRGKASLVVNVASGCPHAEANYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGAL 125
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148233237  126 AKRNYGVTFPMFSKIKILGSEAEPAYRFLVDSTKKEPRWNFWKYLVDPQGQVVKYWRPDETAESIRPEVASLV 198
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 ...
 46-198 4.01e-110

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: 311.77  E-value: 4.01e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237   46 DFYSYEVTDAKGRAVALSKYRGKASLVVNVASGCPHAEANYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGAL 125
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148233237  126 AKRNYGVTFPMFSKIKILGSEAEPAYRFLVDSTKKEPRWNFWKYLVDPQGQVVKYWRPDETAESIRPEVASLV 198
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 46-194 1.75e-73

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: 218.92  E-value: 1.75e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  46 DFYSYEVTDAKGRAVALSKYRGKASLVVNVASGCPhAEANYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGAL 125
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCG-FTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148233237 126 AKRNYGVTFPMFSKIKILGSEAEPAYRFLVDSTK----KEPRWNFWKYLVDPQGQVVKYWRPDETAESIRPEV 194
Cdd:cd00340   80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPgllgKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 46-201 1.18e-62

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 191.83  E-value: 1.18e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  46 DFYSYEVTDAKGRAVALSKYRGKASLVVNVASGC---PHaeanYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEI 122
Cdd:COG0386    3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCgftPQ----YEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237 123 GALAKRNYGVTFPMFSKIKILGSEAEPAYRFLVDSTK-----KEPRWNFWKYLVDPQGQVVKYWRPDETaesirPEVASL 197
Cdd:COG0386   79 AEFCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPgllggGDIKWNFTKFLIDRDGNVVARFAPTTK-----PEDPEL 153


                 ....
gi 148233237 198 VRQI 201
Cdd:COG0386  154 EAAI 157
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 47-200 3.22e-42

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 140.66  E-value: 3.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  47 FYSYEVTDAKGRAVALSKYRG-KASLVVNVASGCPHAEANYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGAL 125
Cdd:PTZ00256  20 FFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIKEY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237 126 AKRNYGVTFPMFSKIKILGSEAEPAYRFL----------VDSTKKEPrWNFWKYLVDPQGQVVKYWRPDETAESIRPEVA 195
Cdd:PTZ00256 100 VQKKFNVDFPLFQKIEVNGENTHEIYKYLrrnselfqnnTNEARQIP-WNFAKFLIDGQGKVVKYFSPKVNPNEMIQDIE 178


                 ....*
gi 148233237 196 SLVRQ 200
Cdd:PTZ00256 179 KLLNA 183
GSHPx pfam00255
Glutathione peroxidase;
47-154 2.42e-40

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 133.25  E-value: 2.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237   47 FYSYEVTDAKGRAVALSKYRGKASLVVNVASGCPhAEANYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGALA 126
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCG-LTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79

                          90       100
                  ....*....|....*....|....*...
gi 148233237  127 KRNYGVTFPMFSKIKILGSEAEPAYRFL 154
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 ...
 46-198 4.01e-110

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: 311.77  E-value: 4.01e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237   46 DFYSYEVTDAKGRAVALSKYRGKASLVVNVASGCPHAEANYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGAL 125
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148233237  126 AKRNYGVTFPMFSKIKILGSEAEPAYRFLVDSTKKEPRWNFWKYLVDPQGQVVKYWRPDETAESIRPEVASLV 198
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 46-194 1.75e-73

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: 218.92  E-value: 1.75e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  46 DFYSYEVTDAKGRAVALSKYRGKASLVVNVASGCPhAEANYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGAL 125
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCG-FTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148233237 126 AKRNYGVTFPMFSKIKILGSEAEPAYRFLVDSTK----KEPRWNFWKYLVDPQGQVVKYWRPDETAESIRPEV 194
Cdd:cd00340   80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPgllgKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 46-201 1.18e-62

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 191.83  E-value: 1.18e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  46 DFYSYEVTDAKGRAVALSKYRGKASLVVNVASGC---PHaeanYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEI 122
Cdd:COG0386    3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCgftPQ----YEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237 123 GALAKRNYGVTFPMFSKIKILGSEAEPAYRFLVDSTK-----KEPRWNFWKYLVDPQGQVVKYWRPDETaesirPEVASL 197
Cdd:COG0386   79 AEFCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPgllggGDIKWNFTKFLIDRDGNVVARFAPTTK-----PEDPEL 153


                 ....
gi 148233237 198 VRQI 201
Cdd:COG0386  154 EAAI 157
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 47-200 3.22e-42

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 140.66  E-value: 3.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  47 FYSYEVTDAKGRAVALSKYRG-KASLVVNVASGCPHAEANYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGAL 125
Cdd:PTZ00256  20 FFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIKEY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237 126 AKRNYGVTFPMFSKIKILGSEAEPAYRFL----------VDSTKKEPrWNFWKYLVDPQGQVVKYWRPDETAESIRPEVA 195
Cdd:PTZ00256 100 VQKKFNVDFPLFQKIEVNGENTHEIYKYLrrnselfqnnTNEARQIP-WNFAKFLIDGQGKVVKYFSPKVNPNEMIQDIE 178


                 ....*
gi 148233237 196 SLVRQ 200
Cdd:PTZ00256 179 KLLNA 183
GSHPx pfam00255
Glutathione peroxidase;
47-154 2.42e-40

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 133.25  E-value: 2.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237   47 FYSYEVTDAKGRAVALSKYRGKASLVVNVASGCPhAEANYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGALA 126
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCG-LTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79

                          90       100
                  ....*....|....*....|....*...
gi 148233237  127 KRNYGVTFPMFSKIKILGSEAEPAYRFL 154
Cdd:pfam00255  80 PGGYGVTFPLFSKIEVNGEKAHPVYKFL 107
btuE PRK10606
putative glutathione peroxidase; Provisional
 46-188 1.54e-37

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 128.74  E-value: 1.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  46 DFYSYEVTDAKGRAVALSKYRGKASLVVNVASGCPHAEaNYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGAL 125
Cdd:PRK10606   4 SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTP-QYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237 126 AKRNYGVTFPMFSKIKILGSEAEPAYRFLVD------------------STKKEPR------WNFWKYLVDPQGQVVKYW 181
Cdd:PRK10606  83 CRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAaaptavapeesgfyarmvSKGRAPLypddilWNFEKFLVGRDGQVIQRF 162


                 ....*..
gi 148233237 182 RPDETAE 188
Cdd:PRK10606 163 SPDMTPE 169
PLN02412 PLN02412
probable glutathione peroxidase
 48-200 4.96e-37

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 127.03  E-value: 4.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  48 YSYEVTDAKGRAVALSKYRGKASLVVNVASGCPHAEANYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGALAK 127
Cdd:PLN02412  10 YDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQTVC 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237 128 RNYGVTFPMFSKIKILGSEAEPAYRFL--------VDSTKkeprWNFWKYLVDPQGQVVKYWRPDETAESIRPEVASLVR 199
Cdd:PLN02412  90 TRFKAEFPIFDKVDVNGKNTAPLYKYLkaekgglfGDAIK----WNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLLG 165


                 .
gi 148233237 200 Q 200
Cdd:PLN02412 166 Q 166
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 48-197 1.04e-35

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 125.40  E-value: 1.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  48 YSYEVTDAKGRAVALSKYRGKASLVVNVASGCPHAEANYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGALAK 127
Cdd:PLN02399  80 HDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQFAC 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148233237 128 RNYGVTFPMFSKIKILGSEAEPAYRFLVDST----KKEPRWNFWKYLVDPQGQVVKYWRPDETAESIRPEVASL 197
Cdd:PLN02399 160 TRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAggflGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKL 233
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 47-209 2.51e-27

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 102.62  E-value: 2.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  47 FYSYEVTDAKGRAVALSKYRGKASLVVNVASGCPHAEANYRSLQELHREFGPSHFTVLAFPCNQFGESEPGTNQEIGALA 126
Cdd:PTZ00056  19 IYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRKFN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237 127 KRNyGVTFPMFSKIKILGSEAEPAYRFLV---------DSTKKEPRWNFWKYLVDPQGQVVKYWRPDETAESIRPEVASL 197
Cdd:PTZ00056  99 DKN-KIKYNFFEPIEVNGENTHELFKFLKancdsmhdeNGTLKAIGWNFGKFLVNKSGNVVAYFSPRTEPLELEKKIAEL 177

                        170
                 ....*....|..
gi 148233237 198 VRQiimKKKEEL 209
Cdd:PTZ00056 178 LGV---KDYQEL 186
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
46-206 3.34e-09

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 53.33  E-value: 3.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  46 DFysyEVTDAKGRAVALSKYRGKASLVVNVASGCPHAEANYRSLQELHREFGPSHFTVLAFpcnqfgeSePGTNQEIGAL 125
Cdd:COG1225    3 DF---TLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGV-------S-SDSDEAHKKF 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237 126 AKRnYGVTFPMFS----KI-KILGSEAEPAYrflvdstkkeprwnfwkYLVDPQGQVVKYWRPDETAesiRPEVASLVRQ 200
Cdd:COG1225   72 AEK-YGLPFPLLSdpdgEVaKAYGVRGTPTT-----------------FLIDPDGKIRYVWVGPVDP---RPHLEEVLEA 130


                 ....*.
gi 148233237 201 IIMKKK 206
Cdd:COG1225  131 LLAELK 136
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 41-200 6.60e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 52.38  E-value: 6.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  41 RAKGGDFYSYEVTDAKGRAVALSKYRGKAsLVVNV-ASGCPHAEANYRSLQELHREFGPSHFTVLAFpcnqfgesepGTN 119
Cdd:COG0526    2 KAVGKPAPDFTLTDLDGKPLSLADLKGKP-VLVNFwATWCPPCRAEMPVLKELAEEYGGVVFVGVDV----------DEN 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237 120 QEIGALAKRNYGVTFPMfskikILGSEAEPAYRFLVDSTkkePRWnfwkYLVDPQGQVVKYWRPDETAESIRPEVASLVR 199
Cdd:COG0526   71 PEAVKAFLKELGLPYPV-----LLDPDGELAKAYGVRGI---PTT----VLIDKDGKIVARHVGPLSPEELEEALEKLLA 138


                 .
gi 148233237 200 Q 200
Cdd:COG0526  139 K 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 51-179 1.93e-06

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: 45.30  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237  51 EVTDAKGRAVALSKYRGKAsLVVNV-ASGCPHAEANYRSLQELHREFGPSHFTVLAFpcNQfgesEPGTNQEIGALAKRn 129
Cdd:cd02966    3 SLPDLDGKPVSLSDLKGKV-VLVNFwASWCPPCRAEMPELEALAKEYKDDGVEVVGV--NV----DDDDPAAVKAFLKK- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 148233237 130 YGVTFPMfskikILGSEAEPAYRFLVDSTkkePRWnfwkYLVDPQGQVVK 179
Cdd:cd02966   75 YGITFPV-----LLDPDGELAKAYGVRGL---PTT----FLIDRDGRIRA 112
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 46-160 3.17e-05

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: 41.83  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233237   46 DFysyEVTDAKGRAVALSKYRGKAsLVVNV--ASGCPHAEANYRSLQELHREFGPSHFTVLAFPCNqfgeSEPGTNQEIg 123
Cdd:pfam00578   7 DF---ELPDGDGGTVSLSDYRGKW-VVLFFypADWTPVCTTELPALADLYEEFKKLGVEVLGVSVD----SPESHKAFA- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 148233237  124 alakRNYGVTFPMFS--------KIKILGSEAEPAYR--FLVDSTKK 160
Cdd:pfam00578  78 ----EKYGLPFPLLSdpdgevarAYGVLNEEEGGALRatFVIDPDGK 120
 
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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