|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
1-233 |
3.82e-154 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 427.39 E-value: 3.82e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 1 MAFSYASFSTPFNGfaaNPSPITSAFLGPSLRFSTRTSKTRNPSNGVSVKSSNSHRFLVKSKNFSVYARAAAEKSVHDFT 80
Cdd:PLN02399 7 SSSSYASFKTVFNS---SPPPPSMAFLVPSLKSSTGISKSAFLSNGFSLKSPNSPGFLSKSRSFGVYARAATEKSVHDFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 81 VKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSSNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQFACTRFK 160
Cdd:PLN02399 84 VKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQFACTRFK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22329066 161 AEFPIFDKVDVNGPSTAPIYKFLKSNAGGFLGDIIKWNFEKFLVDKKGKVVERYPPTTSPFQIEKDIQKLLAA 233
Cdd:PLN02399 164 AEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLLAA 236
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
75-227 |
3.67e-93 |
|
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: 269.77 E-value: 3.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 75 SVHDFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSsNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQF 154
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22329066 155 ACTRFKAEFPIFDKVDVNGPSTAPIYKFLKSNAGGFLGDIIKWNFEKFLVDKKGKVVERYPPTTSPFQIEKDI 227
Cdd:cd00340 80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
75-231 |
9.72e-89 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 258.85 E-value: 9.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 75 SVHDFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSsNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQF 154
Cdd:COG0386 3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 155 ACTRFKAEFPIFDKVDVNGPSTAPIYKFLKSNAGGFLGD-IIKWNFEKFLVDKKGKVVERYPPTTSP--FQIEKDIQKLL 231
Cdd:COG0386 82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGgDIKWNFTKFLIDRDGNVVARFAPTTKPedPELEAAIEKLL 161
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
76-184 |
2.27e-48 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 154.43 E-value: 2.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 76 VHDFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSsNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQFA 155
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
|
90 100
....*....|....*....|....*....
gi 22329066 156 CTRFKAEFPIFDKVDVNGPSTAPIYKFLK 184
Cdd:pfam00255 80 PGGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
75-231 |
1.19e-45 |
|
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: 149.22 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 75 SVHDFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSSNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQF 154
Cdd:TIGR02540 1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329066 155 ACTRFKAEFPIFDKVDVNGPSTAPIYKFLKSNAggflGDIIKWNFEKFLVDKKGKVVERYPPTTSPFQIEKDIQKLL 231
Cdd:TIGR02540 81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
1-233 |
3.82e-154 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 427.39 E-value: 3.82e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 1 MAFSYASFSTPFNGfaaNPSPITSAFLGPSLRFSTRTSKTRNPSNGVSVKSSNSHRFLVKSKNFSVYARAAAEKSVHDFT 80
Cdd:PLN02399 7 SSSSYASFKTVFNS---SPPPPSMAFLVPSLKSSTGISKSAFLSNGFSLKSPNSPGFLSKSRSFGVYARAATEKSVHDFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 81 VKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSSNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQFACTRFK 160
Cdd:PLN02399 84 VKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQFACTRFK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22329066 161 AEFPIFDKVDVNGPSTAPIYKFLKSNAGGFLGDIIKWNFEKFLVDKKGKVVERYPPTTSPFQIEKDIQKLLAA 233
Cdd:PLN02399 164 AEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLLAA 236
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
71-233 |
4.48e-98 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 283.03 E-value: 4.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 71 AAEKSVHDFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSSNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPE 150
Cdd:PLN02412 4 ESPKSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 151 IKQFACTRFKAEFPIFDKVDVNGPSTAPIYKFLKSNAGGFLGDIIKWNFEKFLVDKKGKVVERYPPTTSPFQIEKDIQKL 230
Cdd:PLN02412 84 IQQTVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNL 163
|
...
gi 22329066 231 LAA 233
Cdd:PLN02412 164 LGQ 166
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
75-227 |
3.67e-93 |
|
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: 269.77 E-value: 3.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 75 SVHDFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSsNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQF 154
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22329066 155 ACTRFKAEFPIFDKVDVNGPSTAPIYKFLKSNAGGFLGDIIKWNFEKFLVDKKGKVVERYPPTTSPFQIEKDI 227
Cdd:cd00340 80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
75-231 |
9.72e-89 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 258.85 E-value: 9.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 75 SVHDFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSsNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQF 154
Cdd:COG0386 3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 155 ACTRFKAEFPIFDKVDVNGPSTAPIYKFLKSNAGGFLGD-IIKWNFEKFLVDKKGKVVERYPPTTSP--FQIEKDIQKLL 231
Cdd:COG0386 82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGgDIKWNFTKFLIDRDGNVVARFAPTTKPedPELEAAIEKLL 161
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
72-233 |
1.63e-69 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 211.16 E-value: 1.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 72 AEKSVHDFTVKDIDGNDVSLDKFKGKP-LLIVNVASRCGLTSSNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPE 150
Cdd:PTZ00256 16 PTKSFFEFEAIDIDGQLVQLSKFKGKKaIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 151 IKQFACTRFKAEFPIFDKVDVNGPSTAPIYKFLKSNAGGFLGDI-----IKWNFEKFLVDKKGKVVERYPPTTSPFQIEK 225
Cdd:PTZ00256 96 IKEYVQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNNTnearqIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQ 175
|
....*...
gi 22329066 226 DIQKLLAA 233
Cdd:PTZ00256 176 DIEKLLNA 183
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
75-220 |
8.13e-54 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 171.11 E-value: 8.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 75 SVHDFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSsNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQF 154
Cdd:PRK10606 4 SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTP-QYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 155 ACTRFKAEFPIFDKVDVNGPSTAPIYKFL--------KSNAGGFL-------------GDIIkWNFEKFLVDKKGKVVER 213
Cdd:PRK10606 83 CRTTWGVTFPMFSKIEVNGEGRHPLYQKLiaaaptavAPEESGFYarmvskgraplypDDIL-WNFEKFLVGRDGQVIQR 161
|
....*..
gi 22329066 214 YPPTTSP 220
Cdd:PRK10606 162 FSPDMTP 168
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
76-184 |
2.27e-48 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 154.43 E-value: 2.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 76 VHDFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSsNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQFA 155
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
|
90 100
....*....|....*....|....*....
gi 22329066 156 CTRFKAEFPIFDKVDVNGPSTAPIYKFLK 184
Cdd:pfam00255 80 PGGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
|
|
| PTZ00056 |
PTZ00056 |
glutathione peroxidase; Provisional |
72-231 |
3.66e-47 |
|
glutathione peroxidase; Provisional
Pssm-ID: 240248 [Multi-domain] Cd Length: 199 Bit Score: 154.63 E-value: 3.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 72 AEKSVHDFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSSNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEI 151
Cdd:PTZ00056 15 LRKSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 152 KQFAcTRFKAEFPIFDKVDVNGPSTAPIYKFLKSNA------GGFLGDiIKWNFEKFLVDKKGKVVERYPPTTSPFQIEK 225
Cdd:PTZ00056 95 RKFN-DKNKIKYNFFEPIEVNGENTHELFKFLKANCdsmhdeNGTLKA-IGWNFGKFLVNKSGNVVAYFSPRTEPLELEK 172
|
....*.
gi 22329066 226 DIQKLL 231
Cdd:PTZ00056 173 KIAELL 178
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
75-231 |
1.19e-45 |
|
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: 149.22 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 75 SVHDFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSSNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQF 154
Cdd:TIGR02540 1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329066 155 ACTRFKAEFPIFDKVDVNGPSTAPIYKFLKSNAggflGDIIKWNFEKFLVDKKGKVVERYPPTTSPFQIEKDIQKLL 231
Cdd:TIGR02540 81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| Bcp |
COG1225 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
78-233 |
1.16e-11 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 60.26 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 78 DFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSSNYSELSQLYEKYKNQGFEILAFpcnqfggqEPGSNPEIKQFAcT 157
Cdd:COG1225 3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGV--------SSDSDEAHKKFA-E 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329066 158 RFKAEFPIFdkVDVNGpSTAPIYKflksnaggflgdiIKWNFEKFLVDKKGKVVERYpptTSPFQIEKDIQKLLAA 233
Cdd:COG1225 74 KYGLPFPLL--SDPDG-EVAKAYG-------------VRGTPTTFLIDPDGKIRYVW---VGPVDPRPHLEEVLEA 130
|
|
| TlpA_like_family |
cd02966 |
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
78-214 |
8.31e-10 |
|
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: 54.55 E-value: 8.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 78 DFTVKDIDGNDVSLDKFKGKPLLiVNV-ASRCGLTSSNYSELSQLYEKYKNQGFEILAFpcnqfgGQEPGSNPEIKQFAc 156
Cdd:cd02966 1 DFSLPDLDGKPVSLSDLKGKVVL-VNFwASWCPPCRAEMPELEALAKEYKDDGVEVVGV------NVDDDDPAAVKAFL- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329066 157 TRFKAEFPIFdkVDVNG-----------PSTapiykflksnaggflgdiikwnfekFLVDKKGKVVERY 214
Cdd:cd02966 73 KKYGITFPVL--LDPDGelakaygvrglPTT-------------------------FLIDRDGRIRARH 114
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
71-233 |
2.04e-09 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 54.31 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 71 AAEKSVHDFTVKDIDGNDVSLDKFKGKPLLiVNV-ASRCGLTSSNYSELSQLYEKYKnqGFEILAFPCNQfggqepgSNP 149
Cdd:COG0526 3 AVGKPAPDFTLTDLDGKPLSLADLKGKPVL-VNFwATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVDE-------NPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 150 EIKQFAcTRFKAEFPIF--------DKVDVNG-PSTapiykflksnaggflgdiikwnfekFLVDKKGKVVERYPPTTSP 220
Cdd:COG0526 73 AVKAFL-KELGLPYPVLldpdgelaKAYGVRGiPTT-------------------------VLIDKDGKIVARHVGPLSP 126
|
170
....*....|...
gi 22329066 221 FQIEKDIQKLLAA 233
Cdd:COG0526 127 EELEEALEKLLAK 139
|
|
| AhpC-TSA |
pfam00578 |
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
78-213 |
4.65e-08 |
|
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: 50.30 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 78 DFTVKDIDGNDVSLDKFKGKPLLIVNVASR-CGLTSSNYSELSQLYEKYKNQGFEILAFPCNqfggqepgSNPEIKQFAc 156
Cdd:pfam00578 7 DFELPDGDGGTVSLSDYRGKWVVLFFYPADwTPVCTTELPALADLYEEFKKLGVEVLGVSVD--------SPESHKAFA- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 22329066 157 TRFKAEFPIFdkVDVNGpSTAPIYKFLKSNAGGFLGDIikwnfekFLVDKKGKVVER 213
Cdd:pfam00578 78 EKYGLPFPLL--SDPDG-EVARAYGVLNEEEGGALRAT-------FVIDPDGKVRYI 124
|
|
| Sco1 |
COG1999 |
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ... |
80-233 |
7.31e-07 |
|
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441602 Cd Length: 156 Bit Score: 47.59 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 80 TVKDIDGNDVSLDKFKGKPLLIVNVASRCG----LTSSNyseLSQLYEKYKNQG---FEILAF---PCN----------- 138
Cdd:COG1999 4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPdvcpTTLAN---LAQVQEALGEDGgddVQVLFIsvdPERdtpevlkayae 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 139 QFGGQE----PGSNPEIKQFAcTRFKAefpIFDKVDVNGpstapiYKFLKSNaggflgdiikwNFekFLVDKKGKVVERY 214
Cdd:COG1999 81 AFGAPRwiglTGDPEEIAALA-KAFGV---YYEKVPDGD------YTFDHSA-----------AV--YLVDPDGRLRGYY 137
|
170
....*....|....*....
gi 22329066 215 PPTTSPFQIEKDIQKLLAA 233
Cdd:COG1999 138 PAGEDPEELAADLKALLEE 156
|
|
| PRK03147 |
PRK03147 |
thiol-disulfide oxidoreductase ResA; |
64-212 |
1.07e-06 |
|
thiol-disulfide oxidoreductase ResA;
Pssm-ID: 179545 [Multi-domain] Cd Length: 173 Bit Score: 47.31 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 64 FSVYARAAAEKSVH-------DFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSSNYSELSQLYEKYKNQGFEILAFP 136
Cdd:PRK03147 22 YTIYSNFFADKEKVqvgkeapNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 137 CNqfggqepGSNPEIKQFAcTRFKAEFPI-FDK----VDVNGPSTAPIykflksnaggflgdiikwnfeKFLVDKKGKVV 211
Cdd:PRK03147 102 VD-------ETELAVKNFV-NRYGLTFPVaIDKgrqvIDAYGVGPLPT---------------------TFLIDKDGKVV 152
|
.
gi 22329066 212 E 212
Cdd:PRK03147 153 K 153
|
|
| Redoxin |
pfam08534 |
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
71-214 |
4.89e-06 |
|
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 45.05 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 71 AAEKSVHDFTVKDI--DGNDVSLDKFKGKPLLIVNVASR-CGLTSSNYSELSQLYEKYKNQGFEILAFPCNQfggqepgS 147
Cdd:pfam08534 1 KAGDKAPDFTLPDAatDGNTVSLSDFKGKKVVLNFWPGAfCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDN-------D 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22329066 148 NPEIKQFaCTRFKAEFPIFdkVDVNGpstapiyKFLKSnaggfLGDIIKWNFEK-------FLVDKKGKVVERY 214
Cdd:pfam08534 74 AFFVKRF-WGKEGLPFPFL--SDGNA-------AFTKA-----LGLPIEEDASAglrspryAVIDEDGKVVYLF 132
|
|
| PRX_like1 |
cd02969 |
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ... |
78-164 |
1.81e-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: 40.69 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329066 78 DFTVKDIDGNDVSLDKF-KGKPLLIVNVASRCGLTSSNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQFAc 156
Cdd:cd02969 6 DFSLPDTDGKTYSLADFaDGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPENMKAKA- 84
|
....*...
gi 22329066 157 TRFKAEFP 164
Cdd:cd02969 85 KEHGYPFP 92
|
|
| Tpx |
COG2077 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
77-101 |
4.94e-03 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441680 Cd Length: 168 Bit Score: 36.61 E-value: 4.94e-03
10 20
....*....|....*....|....*
gi 22329066 77 HDFTVKDIDGNDVSLDKFKGKPLLI 101
Cdd:COG2077 25 PDFTLVDTDLSDVTLSDFAGKRKVL 49
|
|
| |
