|
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
|
|
|