|
Name |
Accession |
Description |
Interval |
E-value |
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
1-159 |
8.36e-107 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 301.23 E-value: 8.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 1 MTSAYDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFTPQYTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQ 80
Cdd:COG0386 1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 81 FCSLDYPVSFPLSEKIEVNGEGADPLWAWMTHEKRGLLGSARIKWNFSKFLVDRQGQVVSRHAPTTRPE--QLRSAIEAL 158
Cdd:COG0386 81 FCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGDIKWNFTKFLIDRDGNVVARFAPTTKPEdpELEAAIEKL 160
|
.
gi 924465472 159 L 159
Cdd:COG0386 161 L 161
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
3-155 |
2.06e-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: 267.07 E-value: 2.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 3 SAYDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFTPQYTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQFC 82
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 924465472 83 SLDYPVSFPLSEKIEVNGEGADPLWAWMTHEKRGLLGSArIKWNFSKFLVDRQGQVVSRHAPTTRPEQLRSAI 155
Cdd:cd00340 81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKD-IKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
3-159 |
1.46e-53 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 169.31 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 3 SAYDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFTP-QYTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQF 81
Cdd:PLN02399 78 SVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQF 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 924465472 82 CSLDYPVSFPLSEKIEVNGEGADPLWAWMTHEKRGLLGSArIKWNFSKFLVDRQGQVVSRHAPTTRPEQLRSAIEALL 159
Cdd:PLN02399 158 ACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDL-IKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLL 234
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
5-110 |
5.88e-52 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 160.98 E-value: 5.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 5 YDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFTPQYTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQFCSL 84
Cdd:pfam00255 2 YEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCPG 81
|
90 100
....*....|....*....|....*.
gi 924465472 85 DYPVSFPLSEKIEVNGEGADPLWAWM 110
Cdd:pfam00255 82 GYGVTFPLFSKIEVNGEKAHPVYKFL 107
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
5-159 |
2.04e-37 |
|
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: 125.33 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 5 YDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFTPQ-YTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQFCS 83
Cdd:TIGR02540 3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 924465472 84 LDYPVSFPLSEKIEVNGEGADPLWAWMTHEkrgllgSARI-KWNFSKFLVDRQGQVVSRHAPTTRPEQLRSAIEALL 159
Cdd:TIGR02540 83 RNYGVTFPMFSKIKILGSEAEPAFRFLVDS------SKKEpRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
1-159 |
8.36e-107 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 301.23 E-value: 8.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 1 MTSAYDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFTPQYTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQ 80
Cdd:COG0386 1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 81 FCSLDYPVSFPLSEKIEVNGEGADPLWAWMTHEKRGLLGSARIKWNFSKFLVDRQGQVVSRHAPTTRPE--QLRSAIEAL 158
Cdd:COG0386 81 FCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGDIKWNFTKFLIDRDGNVVARFAPTTKPEdpELEAAIEKL 160
|
.
gi 924465472 159 L 159
Cdd:COG0386 161 L 161
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
3-155 |
2.06e-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: 267.07 E-value: 2.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 3 SAYDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFTPQYTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQFC 82
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 924465472 83 SLDYPVSFPLSEKIEVNGEGADPLWAWMTHEKRGLLGSArIKWNFSKFLVDRQGQVVSRHAPTTRPEQLRSAI 155
Cdd:cd00340 81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKD-IKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
3-159 |
1.46e-53 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 169.31 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 3 SAYDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFTP-QYTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQF 81
Cdd:PLN02399 78 SVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQF 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 924465472 82 CSLDYPVSFPLSEKIEVNGEGADPLWAWMTHEKRGLLGSArIKWNFSKFLVDRQGQVVSRHAPTTRPEQLRSAIEALL 159
Cdd:PLN02399 158 ACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDL-IKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLL 234
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
2-159 |
4.94e-53 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 166.10 E-value: 4.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 2 TSAYDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFTPQYTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQF 81
Cdd:PRK10606 3 DSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 82 CSLDYPVSFPLSEKIEVNGEGADPLW-------------------AWMTHEKRGLLGSARIKWNFSKFLVDRQGQVVSRH 142
Cdd:PRK10606 83 CRTTWGVTFPMFSKIEVNGEGRHPLYqkliaaaptavapeesgfyARMVSKGRAPLYPDDILWNFEKFLVGRDGQVIQRF 162
|
170
....*....|....*....
gi 924465472 143 APTTRPE--QLRSAIEALL 159
Cdd:PRK10606 163 SPDMTPEdpIVMESIKLAL 181
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
3-159 |
1.50e-52 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 164.39 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 3 SAYDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFT-PQYTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQF 81
Cdd:PLN02412 8 SIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 924465472 82 CSLDYPVSFPLSEKIEVNGEGADPLWAWMTHEKRGLLGSArIKWNFSKFLVDRQGQVVSRHAPTTRPEQLRSAIEALL 159
Cdd:PLN02412 88 VCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDA-IKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLL 164
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
5-110 |
5.88e-52 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 160.98 E-value: 5.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 5 YDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFTPQYTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQFCSL 84
Cdd:pfam00255 2 YEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCPG 81
|
90 100
....*....|....*....|....*.
gi 924465472 85 DYPVSFPLSEKIEVNGEGADPLWAWM 110
Cdd:pfam00255 82 GYGVTFPLFSKIEVNGEKAHPVYKFL 107
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
2-159 |
2.53e-49 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 156.84 E-value: 2.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 2 TSAYDFSFRDLDGQPQALARYQGHP-LLLVNVASRCGFTPQ-YTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIR 79
Cdd:PTZ00256 18 KSFFEFEAIDIDGQLVQLSKFKGKKaIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 80 QFCSLDYPVSFPLSEKIEVNGEGADPLWAWM---THEKRGLLGSAR-IKWNFSKFLVDRQGQVVSRHAPTTRPEQLRSAI 155
Cdd:PTZ00256 98 EYVQKKFNVDFPLFQKIEVNGENTHEIYKYLrrnSELFQNNTNEARqIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQDI 177
|
....
gi 924465472 156 EALL 159
Cdd:PTZ00256 178 EKLL 181
|
|
| PTZ00056 |
PTZ00056 |
glutathione peroxidase; Provisional |
3-159 |
3.93e-38 |
|
glutathione peroxidase; Provisional
Pssm-ID: 240248 [Multi-domain] Cd Length: 199 Bit Score: 128.82 E-value: 3.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 3 SAYDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFTPQYTG-LEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQF 81
Cdd:PTZ00056 18 SIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDqMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRKF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 82 CSlDYPVSFPLSEKIEVNGEGADPLWAWMT------HEKRGLLGSarIKWNFSKFLVDRQGQVVSRHAPTTRPEQLRSAI 155
Cdd:PTZ00056 98 ND-KNKIKYNFFEPIEVNGENTHELFKFLKancdsmHDENGTLKA--IGWNFGKFLVNKSGNVVAYFSPRTEPLELEKKI 174
|
....
gi 924465472 156 EALL 159
Cdd:PTZ00056 175 AELL 178
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
5-159 |
2.04e-37 |
|
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: 125.33 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 5 YDFSFRDLDGQPQALARYQGHPLLLVNVASRCGFTPQ-YTGLEQLWQDYRERGLVVIGFPCNQFGAQEPGDAAQIRQFCS 83
Cdd:TIGR02540 3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 924465472 84 LDYPVSFPLSEKIEVNGEGADPLWAWMTHEkrgllgSARI-KWNFSKFLVDRQGQVVSRHAPTTRPEQLRSAIEALL 159
Cdd:TIGR02540 83 RNYGVTFPMFSKIKILGSEAEPAFRFLVDS------SKKEpRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
2-159 |
1.31e-11 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 58.55 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 2 TSAYDFSFRDLDGQPQALARYQGHPlLLVNV-ASRCG----FTPQytgLEQLWQDYreRGLVVIGFPCNQfgaqepgDAA 76
Cdd:COG0526 6 KPAPDFTLTDLDGKPLSLADLKGKP-VLVNFwATWCPpcraEMPV---LKELAEEY--GGVVFVGVDVDE-------NPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 77 QIRQFCSlDYPVSFPLsekievngeGADPlwawmthekrglLGSARIKWNFSK----FLVDRQGQVVSRHAPTTRPEQLR 152
Cdd:COG0526 73 AVKAFLK-ELGLPYPV---------LLDP------------DGELAKAYGVRGipttVLIDKDGKIVARHVGPLSPEELE 130
|
....*..
gi 924465472 153 SAIEALL 159
Cdd:COG0526 131 EALEKLL 137
|
|
| Bcp |
COG1225 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
4-159 |
1.97e-10 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 55.26 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 4 AYDFSFRDLDGQPQALARYQGHPLLLVNVASRCGF-TPQYTGLEQLWQDYRERGLVVIGFpcnqfgaqEPGDAAQIRQFC 82
Cdd:COG1225 1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGcTAELPELRDLYEEFKDKGVEVLGV--------SSDSDEAHKKFA 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 924465472 83 SlDYPVSFPLsekievngeGADPlwawmthekRGLLGSA-RIKWNFSKFLVDRQGQVVSRHA-PTTRPEQLRSAIEALL 159
Cdd:COG1225 73 E-KYGLPFPL---------LSDP---------DGEVAKAyGVRGTPTTFLIDPDGKIRYVWVgPVDPRPHLEEVLEALL 132
|
|
| TlpA_like_family |
cd02966 |
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
6-143 |
2.63e-09 |
|
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: 51.85 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 6 DFSFRDLDGQPQALARYQGHPlLLVNV-ASRCGF----TPQytgLEQLWQDYRERGLVVIGFpcnqfgAQEPGDAAQIRQ 80
Cdd:cd02966 1 DFSLPDLDGKPVSLSDLKGKV-VLVNFwASWCPPcraeMPE---LEALAKEYKDDGVEVVGV------NVDDDDPAAVKA 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 924465472 81 FcSLDYPVSFPLsekievngeGADPlwawmthekrglLGSARIKWN----FSKFLVDRQGQVVSRHA 143
Cdd:cd02966 71 F-LKKYGITFPV---------LLDP------------DGELAKAYGvrglPTTFLIDRDGRIRARHV 115
|
|
| AhpC-TSA |
pfam00578 |
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
6-139 |
6.75e-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: 42.98 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 6 DFSFRDLDGQPQALARYQGHPLLLVNVASrcGFTP----QYTGLEQLWQDYRERGLVVIGFPCNqfgaqepgDAAQIRQF 81
Cdd:pfam00578 7 DFELPDGDGGTVSLSDYRGKWVVLFFYPA--DWTPvcttELPALADLYEEFKKLGVEVLGVSVD--------SPESHKAF 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 924465472 82 CSlDYPVSFPLsekievngeGADPlwawmTHEKRGLLGSARIKWNFSK---FLVDRQGQVV 139
Cdd:pfam00578 77 AE-KYGLPFPL---------LSDP-----DGEVARAYGVLNEEEGGALratFVIDPDGKVR 122
|
|
| PRX_BCP |
cd03017 |
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ... |
2-139 |
1.62e-04 |
|
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: 39.45 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 2 TSAYDFSFRDLDGQPQALARYQGHPLLLVnvasrcgF---------TPQYTGLEQLWQDYRERGLVVIGFpcnqfgaqEP 72
Cdd:cd03017 1 DKAPDFTLPDQDGETVSLSDLRGKPVVLY-------FypkddtpgcTKEACDFRDLYEEFKALGAVVIGV--------SP 65
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924465472 73 GDAAQIRQF---CSLDYPVsfpLSEKievNGEGADPLWAWMtHEKRGLLGSARikwnfSKFLVDRQGQVV 139
Cdd:cd03017 66 DSVESHAKFaekYGLPFPL---LSDP---DGKLAKAYGVWG-EKKKKYMGIER-----STFLIDPDGKIV 123
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| PRX_like1 |
cd02969 |
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ... |
2-61 |
3.98e-03 |
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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: 36.06 E-value: 3.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 924465472 2 TSAYDFSFRDLDGQPQALARYQGHPLLLvnVASRCGFTP----QYTGLEQLWQDYRERGLVVIG 61
Cdd:cd02969 2 SPAPDFSLPDTDGKTYSLADFADGKALV--VMFICNHCPyvkaIEDRLNRLAKEYGAKGVAVVA 63
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