|
Name |
Accession |
Description |
Interval |
E-value |
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
1-177 |
4.52e-92 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 265.02 E-value: 4.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 1 MGIYDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLTPQYEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQV 80
Cdd:COG0386 2 MSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 81 CMMKFGTKFKIFDKIEVNGANTAPLYAYLKSVKPQDKGNhlfkdfvlklaalgekrdeGDIKWNFTKFLVNRDGEVVERF 160
Cdd:COG0386 82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG-------------------GDIKWNFTKFLIDRDGNVVARF 142
|
170
....*....|....*....
gi 488147744 161 APSVTPE--EIEADIRALL 177
Cdd:COG0386 143 APTTKPEdpELEAAIEKLL 161
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
3-173 |
2.44e-85 |
|
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: 247.43 E-value: 2.44e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 3 IYDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLTPQYEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQVCM 82
Cdd:cd00340 2 IYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFCE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 83 MKFGTKFKIFDKIEVNGANTAPLYAYLKSVKPQDKGNhlfkdfvlklaalgekrdegDIKWNFTKFLVNRDGEVVERFAP 162
Cdd:cd00340 82 TNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGK--------------------DIKWNFTKFLVDRDGEVVKRFAP 141
|
170
....*....|.
gi 488147744 163 SVTPEEIEADI 173
Cdd:cd00340 142 TTDPEELEKDI 152
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
3-177 |
1.64e-60 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 185.58 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 3 IYDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLT-PQYEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQVC 81
Cdd:PLN02412 9 IYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 82 MMKFGTKFKIFDKIEVNGANTAPLYAYLKSvkpqDKGNHLfkdfvlklaalgekrdeGD-IKWNFTKFLVNRDGEVVERF 160
Cdd:PLN02412 89 CTRFKAEFPIFDKVDVNGKNTAPLYKYLKA----EKGGLF-----------------GDaIKWNFTKFLVSKEGKVVQRY 147
|
170
....*....|....*..
gi 488147744 161 APSVTPEEIEADIRALL 177
Cdd:PLN02412 148 APTTSPLKIEKDIQNLL 164
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
3-110 |
7.30e-44 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 140.95 E-value: 7.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 3 IYDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLTPQYEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQVCM 82
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80
|
90 100
....*....|....*....|....*...
gi 488147744 83 MKFGTKFKIFDKIEVNGANTAPLYAYLK 110
Cdd:pfam00255 81 GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
4-177 |
4.06e-38 |
|
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: 128.03 E-value: 4.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 4 YDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLTPQ-YEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQVCM 82
Cdd:TIGR02540 3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 83 MKFGTKFKIFDKIEVNGANTAPLYAYL-KSVKPQDkgnhlfkdfvlklaalgekrdegdiKWNFTKFLVNRDGEVVERFA 161
Cdd:TIGR02540 83 RNYGVTFPMFSKIKILGSEAEPAFRFLvDSSKKEP-------------------------RWNFWKYLVNPEGQVVKFWR 137
|
170
....*....|....*.
gi 488147744 162 PSVTPEEIEADIRALL 177
Cdd:TIGR02540 138 PEEPVEEIRPEITALV 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
1-177 |
4.52e-92 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 265.02 E-value: 4.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 1 MGIYDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLTPQYEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQV 80
Cdd:COG0386 2 MSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 81 CMMKFGTKFKIFDKIEVNGANTAPLYAYLKSVKPQDKGNhlfkdfvlklaalgekrdeGDIKWNFTKFLVNRDGEVVERF 160
Cdd:COG0386 82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGG-------------------GDIKWNFTKFLIDRDGNVVARF 142
|
170
....*....|....*....
gi 488147744 161 APSVTPE--EIEADIRALL 177
Cdd:COG0386 143 APTTKPEdpELEAAIEKLL 161
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
3-173 |
2.44e-85 |
|
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: 247.43 E-value: 2.44e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 3 IYDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLTPQYEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQVCM 82
Cdd:cd00340 2 IYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFCE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 83 MKFGTKFKIFDKIEVNGANTAPLYAYLKSVKPQDKGNhlfkdfvlklaalgekrdegDIKWNFTKFLVNRDGEVVERFAP 162
Cdd:cd00340 82 TNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGK--------------------DIKWNFTKFLVDRDGEVVKRFAP 141
|
170
....*....|.
gi 488147744 163 SVTPEEIEADI 173
Cdd:cd00340 142 TTDPEELEKDI 152
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
3-177 |
1.64e-60 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 185.58 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 3 IYDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLT-PQYEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQVC 81
Cdd:PLN02412 9 IYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 82 MMKFGTKFKIFDKIEVNGANTAPLYAYLKSvkpqDKGNHLfkdfvlklaalgekrdeGD-IKWNFTKFLVNRDGEVVERF 160
Cdd:PLN02412 89 CTRFKAEFPIFDKVDVNGKNTAPLYKYLKA----EKGGLF-----------------GDaIKWNFTKFLVSKEGKVVQRY 147
|
170
....*....|....*..
gi 488147744 161 APSVTPEEIEADIRALL 177
Cdd:PLN02412 148 APTTSPLKIEKDIQNLL 164
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
3-176 |
6.58e-60 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 184.21 E-value: 6.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 3 IYDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLTPQYEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQVCM 82
Cdd:PRK10606 5 ILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYCR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 83 MKFGTKFKIFDKIEVNGANTAPLYAYL-----KSVKPQDKGnhlfkdFVLKLAALGEK-RDEGDIKWNFTKFLVNRDGEV 156
Cdd:PRK10606 85 TTWGVTFPMFSKIEVNGEGRHPLYQKLiaaapTAVAPEESG------FYARMVSKGRApLYPDDILWNFEKFLVGRDGQV 158
|
170 180
....*....|....*....|...
gi 488147744 157 VERFAPSVTPEE---IEADIRAL 176
Cdd:PRK10606 159 IQRFSPDMTPEDpivMESIKLAL 181
|
|
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
3-177 |
7.22e-56 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 175.86 E-value: 7.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 3 IYDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLTP-QYEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQVC 81
Cdd:PLN02399 79 VHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQFA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 82 MMKFGTKFKIFDKIEVNGANTAPLYAYLKSvkpqDKGNHLfkdfvlklaalgekrdeGD-IKWNFTKFLVNRDGEVVERF 160
Cdd:PLN02399 159 CTRFKAEFPIFDKVDVNGPSTAPVYQFLKS----NAGGFL-----------------GDlIKWNFEKFLVDKNGKVVERY 217
|
170
....*....|....*..
gi 488147744 161 APSVTPEEIEADIRALL 177
Cdd:PLN02399 218 PPTTSPFQIEKDIQKLL 234
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
3-177 |
1.15e-50 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 161.08 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 3 IYDFQMKDAEGNAVDLSGYRG-KVLLIVNTATRCGLTPQ-YEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQV 80
Cdd:PTZ00256 20 FFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIKEY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 81 CMMKFGTKFKIFDKIEVNGANTAPLYAYLKSVKPQDKGNHlfkdfvlklaalGEKRdegDIKWNFTKFLVNRDGEVVERF 160
Cdd:PTZ00256 100 VQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNNT------------NEAR---QIPWNFAKFLIDGQGKVVKYF 164
|
170
....*....|....*..
gi 488147744 161 APSVTPEEIEADIRALL 177
Cdd:PTZ00256 165 SPKVNPNEMIQDIEKLL 181
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
3-110 |
7.30e-44 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 140.95 E-value: 7.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 3 IYDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLTPQYEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQVCM 82
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80
|
90 100
....*....|....*....|....*...
gi 488147744 83 MKFGTKFKIFDKIEVNGANTAPLYAYLK 110
Cdd:pfam00255 81 GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
|
|
| PTZ00056 |
PTZ00056 |
glutathione peroxidase; Provisional |
3-177 |
3.24e-40 |
|
glutathione peroxidase; Provisional
Pssm-ID: 240248 [Multi-domain] Cd Length: 199 Bit Score: 134.98 E-value: 3.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 3 IYDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLTPQY-EALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQVc 81
Cdd:PTZ00056 19 IYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHvDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRKF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 82 MMKFGTKFKIFDKIEVNGANTAPLYAYLKSVKPQ--DKGNHLfkdfvlklaalgekrdeGDIKWNFTKFLVNRDGEVVER 159
Cdd:PTZ00056 98 NDKNKIKYNFFEPIEVNGENTHELFKFLKANCDSmhDENGTL-----------------KAIGWNFGKFLVNKSGNVVAY 160
|
170
....*....|....*...
gi 488147744 160 FAPSVTPEEIEADIRALL 177
Cdd:PTZ00056 161 FSPRTEPLELEKKIAELL 178
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
4-177 |
4.06e-38 |
|
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: 128.03 E-value: 4.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 4 YDFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGLTPQ-YEALQKLYAQYTAEGLEILDFPCNQFREQAPESSGEIAQVCM 82
Cdd:TIGR02540 3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 83 MKFGTKFKIFDKIEVNGANTAPLYAYL-KSVKPQDkgnhlfkdfvlklaalgekrdegdiKWNFTKFLVNRDGEVVERFA 161
Cdd:TIGR02540 83 RNYGVTFPMFSKIKILGSEAEPAFRFLvDSSKKEP-------------------------RWNFWKYLVNPEGQVVKFWR 137
|
170
....*....|....*.
gi 488147744 162 PSVTPEEIEADIRALL 177
Cdd:TIGR02540 138 PEEPVEEIRPEITALV 153
|
|
| Bcp |
COG1225 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
5-59 |
7.25e-09 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 51.79 E-value: 7.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 488147744 5 DFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGL-TPQYEALQKLYAQYTAEGLEIL 59
Cdd:COG1225 3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGcTAELPELRDLYEEFKDKGVEVL 58
|
|
| TlpA_like_family |
cd02966 |
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
5-59 |
2.13e-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: 44.53 E-value: 2.13e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488147744 5 DFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGltP-QYE--ALQKLYAQYTAEGLEIL 59
Cdd:cd02966 1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCP--PcRAEmpELEALAKEYKDDGVEVV 56
|
|
| AhpC-TSA |
pfam00578 |
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
5-59 |
6.77e-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: 43.37 E-value: 6.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488147744 5 DFQMKDAEGNAVDLSGYRGKVLLIVNTATR----CglTPQYEALQKLYAQYTAEGLEIL 59
Cdd:pfam00578 7 DFELPDGDGGTVSLSDYRGKWVVLFFYPADwtpvC--TTELPALADLYEEFKKLGVEVL 63
|
|
| Sco1 |
COG1999 |
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ... |
148-177 |
3.40e-03 |
|
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441602 Cd Length: 156 Bit Score: 36.42 E-value: 3.40e-03
10 20 30
....*....|....*....|....*....|
gi 488147744 148 FLVNRDGEVVERFAPSVTPEEIEADIRALL 177
Cdd:COG1999 125 YLVDPDGRLRGYYPAGEDPEELAADLKALL 154
|
|
| PRK03147 |
PRK03147 |
thiol-disulfide oxidoreductase ResA; |
5-59 |
5.37e-03 |
|
thiol-disulfide oxidoreductase ResA;
Pssm-ID: 179545 [Multi-domain] Cd Length: 173 Bit Score: 35.75 E-value: 5.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488147744 5 DFQMKDAEGNAVDLSGYRGKVLLIVNTATRCGltP---QYEALQKLYAQYTAEGLEIL 59
Cdd:PRK03147 43 NFVLTDLEGKKIELKDLKGKGVFLNFWGTWCK--PcekEMPYMNELYPKYKEKGVEII 98
|
|
| PRX_BCP |
cd03017 |
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ... |
5-59 |
5.73e-03 |
|
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.
Pssm-ID: 239315 Cd Length: 140 Bit Score: 35.60 E-value: 5.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488147744 5 DFQMKDAEGNAVDLSGYRGKVLLIV-----NTAtrcGLTPQYEALQKLYAQYTAEGLEIL 59
Cdd:cd03017 5 DFTLPDQDGETVSLSDLRGKPVVLYfypkdDTP---GCTKEACDFRDLYEEFKALGAVVI 61
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| Redoxin |
pfam08534 |
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
5-59 |
9.73e-03 |
|
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 35.04 E-value: 9.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488147744 5 DFQMKDA--EGNAVDLSGYRGKVLLIVNTATR-CGL-TPQYEALQKLYAQYTAEGLEIL 59
Cdd:pfam08534 8 DFTLPDAatDGNTVSLSDFKGKKVVLNFWPGAfCPTcSAEHPYLEKLNELYKEKGVDVV 66
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