|
Name |
Accession |
Description |
Interval |
E-value |
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
46-198 |
3.01e-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: 312.15 E-value: 3.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVESF 125
Cdd:TIGR02540 1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157823095 126 ARKNYGVTFPIFHKIKILGPEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPLEAIRPHVSQMI 198
Cdd:TIGR02540 81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
46-194 |
3.26e-71 |
|
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: 213.15 E-value: 3.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTdKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVESF 125
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157823095 126 ARKNYGVTFPIFHKIKILGPEAEPAFRFLVDSSK----KEPRWNFWKYLVNPEGQVVKFWRPEEPLEAIRPHV 194
Cdd:cd00340 80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPgllgKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
46-201 |
1.18e-58 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 181.43 E-value: 1.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTdKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVESF 125
Cdd:COG0386 3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 126 ARKNYGVTFPIFHKIKILGPEAEPAFRFLVDSSK-----KEPRWNFWKYLVNPEGQVVKFWRPeepleAIRPHVSQMIGQ 200
Cdd:COG0386 82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPgllggGDIKWNFTKFLIDRDGNVVARFAP-----TTKPEDPELEAA 156
|
.
gi 157823095 201 I 201
Cdd:COG0386 157 I 157
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
42-200 |
1.34e-45 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 149.14 E-value: 1.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 42 PRINSFYSFEVKDAKGRMVSLEKFKG-KASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSK 120
Cdd:PTZ00256 15 PPTKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 121 EVESFARKNYGVTFPIFHKIKILGPEAEPAFRFL------VDSSKKEPR---WNFWKYLVNPEGQVVKFWRPEEPLEAIR 191
Cdd:PTZ00256 95 EIKEYVQKKFNVDFPLFQKIEVNGENTHEIYKYLrrnselFQNNTNEARqipWNFAKFLIDGQGKVVKYFSPKVNPNEMI 174
|
....*....
gi 157823095 192 PHVSQMIGQ 200
Cdd:PTZ00256 175 QDIEKLLNA 183
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
47-154 |
2.88e-40 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 133.25 E-value: 2.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 47 FYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKsYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVESFA 126
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQ-YTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
|
90 100
....*....|....*....|....*...
gi 157823095 127 RKNYGVTFPIFHKIKILGPEAEPAFRFL 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 |
3.01e-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: 312.15 E-value: 3.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVESF 125
Cdd:TIGR02540 1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157823095 126 ARKNYGVTFPIFHKIKILGPEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPLEAIRPHVSQMI 198
Cdd:TIGR02540 81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
46-194 |
3.26e-71 |
|
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: 213.15 E-value: 3.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTdKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVESF 125
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157823095 126 ARKNYGVTFPIFHKIKILGPEAEPAFRFLVDSSK----KEPRWNFWKYLVNPEGQVVKFWRPEEPLEAIRPHV 194
Cdd:cd00340 80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPgllgKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
46-201 |
1.18e-58 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 181.43 E-value: 1.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTdKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVESF 125
Cdd:COG0386 3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 126 ARKNYGVTFPIFHKIKILGPEAEPAFRFLVDSSK-----KEPRWNFWKYLVNPEGQVVKFWRPeepleAIRPHVSQMIGQ 200
Cdd:COG0386 82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPgllggGDIKWNFTKFLIDRDGNVVARFAP-----TTKPEDPELEAA 156
|
.
gi 157823095 201 I 201
Cdd:COG0386 157 I 157
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
42-200 |
1.34e-45 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 149.14 E-value: 1.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 42 PRINSFYSFEVKDAKGRMVSLEKFKG-KASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSK 120
Cdd:PTZ00256 15 PPTKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 121 EVESFARKNYGVTFPIFHKIKILGPEAEPAFRFL------VDSSKKEPR---WNFWKYLVNPEGQVVKFWRPEEPLEAIR 191
Cdd:PTZ00256 95 EIKEYVQKKFNVDFPLFQKIEVNGENTHEIYKYLrrnselFQNNTNEARqipWNFAKFLIDGQGKVVKYFSPKVNPNEMI 174
|
....*....
gi 157823095 192 PHVSQMIGQ 200
Cdd:PTZ00256 175 QDIEKLLNA 183
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
47-154 |
2.88e-40 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 133.25 E-value: 2.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 47 FYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKsYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVESFA 126
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQ-YTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
|
90 100
....*....|....*....|....*...
gi 157823095 127 RKNYGVTFPIFHKIKILGPEAEPAFRFL 154
Cdd:pfam00255 80 PGGYGVTFPLFSKIEVNGEKAHPVYKFL 107
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
46-200 |
2.92e-36 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 124.72 E-value: 2.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVESF 125
Cdd:PLN02412 8 SIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 126 ARKNYGVTFPIFHKIKILGPEAEPAFRFLvdssKKEP--------RWNFWKYLVNPEGQVVKFWRPEEPLEAIRPHVSQM 197
Cdd:PLN02412 88 VCTRFKAEFPIFDKVDVNGKNTAPLYKYL----KAEKgglfgdaiKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNL 163
|
...
gi 157823095 198 IGQ 200
Cdd:PLN02412 164 LGQ 166
|
|
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
46-183 |
3.27e-36 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 126.94 E-value: 3.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVESF 125
Cdd:PLN02399 78 SVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQF 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823095 126 ARKNYGVTFPIFHKIKILGPEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRP 183
Cdd:PLN02399 158 ACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAggflGDLIKWNFEKFLVDKNGKVVERYPP 219
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
45-191 |
6.34e-36 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 124.50 E-value: 6.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 45 NSFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTdKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVES 124
Cdd:PRK10606 3 DSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLT-PQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 125 FARKNYGVTFPIFHKIKILGPEAEPAFRFLVD------------------SSKKEPR------WNFWKYLVNPEGQVVKF 180
Cdd:PRK10606 82 YCRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAaaptavapeesgfyarmvSKGRAPLypddilWNFEKFLVGRDGQVIQR 161
|
170
....*....|....*..
gi 157823095 181 WR----PEEP--LEAIR 191
Cdd:PRK10606 162 FSpdmtPEDPivMESIK 178
|
|
| PTZ00056 |
PTZ00056 |
glutathione peroxidase; Provisional |
46-199 |
3.15e-31 |
|
glutathione peroxidase; Provisional
Pssm-ID: 240248 [Multi-domain] Cd Length: 199 Bit Score: 113.02 E-value: 3.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 46 SFYSFEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVESF 125
Cdd:PTZ00056 18 SIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRKF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 126 ARKNyGVTFPIFHKIKILGPEAEPAFRFLV---------DSSKKEPRWNFWKYLVNPEGQVVKFWRPE-EPLEAIrPHVS 195
Cdd:PTZ00056 98 NDKN-KIKYNFFEPIEVNGENTHELFKFLKancdsmhdeNGTLKAIGWNFGKFLVNKSGNVVAYFSPRtEPLELE-KKIA 175
|
....
gi 157823095 196 QMIG 199
Cdd:PTZ00056 176 ELLG 179
|
|
| Bcp |
COG1225 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
50-206 |
2.56e-09 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 53.33 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 50 FEVKDAKGRMVSLEKFKGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFpcnqfgeSePKSSKEVESFARKn 129
Cdd:COG1225 4 FTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGV-------S-SDSDEAHKKFAEK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 130 YGVTFPIF----HKI-KILGPEAEPAFrflvdsskkeprwnfwkYLVNPEGQVVKFWRPEEPLeaiRPHVSQMIGQIILK 204
Cdd:COG1225 75 YGLPFPLLsdpdGEVaKAYGVRGTPTT-----------------FLIDPDGKIRYVWVGPVDP---RPHLEEVLEALLAE 134
|
..
gi 157823095 205 KK 206
Cdd:COG1225 135 LK 136
|
|
| TlpA_like_family |
cd02966 |
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
50-180 |
3.89e-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: 44.15 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 50 FEVKDAKGRMVSLEKFKGKAsLVVNV-ASDCRFTDKSYETLRELHKEFGPYHFNVLAFpcNqFGESEPkssKEVESFARK 128
Cdd:cd02966 2 FSLPDLDGKPVSLSDLKGKV-VLVNFwASWCPPCRAEMPELEALAKEYKDDGVEVVGV--N-VDDDDP---AAVKAFLKK 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 157823095 129 nYGVTFPIfhkikILGPEAEPAFRFLVDSSkkePRWnfwkYLVNPEGQVVKF 180
Cdd:cd02966 75 -YGITFPV-----LLDPDGELAKAYGVRGL---PTT----FLIDRDGRIRAR 113
|
|
| AhpC-TSA |
pfam00578 |
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
49-156 |
6.55e-06 |
|
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: 43.75 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 49 SFEVKDAKGRMVSLEKFKGKASLVVNVASD-CRFTDKSYETLRELHKEFGPYHFNVLAFPCNqfgesepkSSKEVESFAR 127
Cdd:pfam00578 7 DFELPDGDGGTVSLSDYRGKWVVLFFYPADwTPVCTTELPALADLYEEFKKLGVEVLGVSVD--------SPESHKAFAE 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 157823095 128 KnYGVTFPIFH--------KIKILGPEAEPAFR--FLVD 156
Cdd:pfam00578 79 K-YGLPFPLLSdpdgevarAYGVLNEEEGGALRatFVID 116
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
46-200 |
2.55e-05 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 42.37 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 46 SFYSFEVKDAKGRMVSLEKFKGKAsLVVNV-ASDCRFTDKSYETLRELHKEFGPYHFNVLAfpcnqFGESEPKsskeVES 124
Cdd:COG0526 7 PAPDFTLTDLDGKPLSLADLKGKP-VLVNFwATWCPPCRAEMPVLKELAEEYGGVVFVGVD-----VDENPEA----VKA 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823095 125 FARKnYGVTFPIfhkikILGPEAEPAFRFLVDSSkkePRWnfwkYLVNPEGQVVKFWRPEEPLEAIRPHVSQMIGQ 200
Cdd:COG0526 77 FLKE-LGLPYPV-----LLDPDGELAKAYGVRGI---PTT----VLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
|
|
| PRX_like1 |
cd02969 |
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ... |
49-135 |
2.45e-03 |
|
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: 37.22 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823095 49 SFEVKDAKGRMVSLEKF-KGKASLVVNVASDCRFTDKSYETLRELHKEFGPYHFNVLAFPCNQFGESEPKSSKEVESFAr 127
Cdd:cd02969 6 DFSLPDTDGKTYSLADFaDGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPENMKAKA- 84
|
....*...
gi 157823095 128 KNYGVTFP 135
Cdd:cd02969 85 KEHGYPFP 92
|
|
| |
