|
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
|
|
|