|
Name |
Accession |
Description |
Interval |
E-value |
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
1-158 |
1.11e-101 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 288.51 E-value: 1.11e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 1 METIYDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFTSQFEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQ 80
Cdd:COG0386 1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 81 NCKLNYGVTFPMHQKIDVKGEHQLPLFRYLTAAQHGFF-NKKIKWNFTKFLVDREGNVVKRFAPQKKP--VQIEREIEKL 157
Cdd:COG0386 81 FCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLgGGDIKWNFTKFLIDRDGNVVARFAPTTKPedPELEAAIEKL 160
|
.
gi 613163074 158 L 158
Cdd:COG0386 161 L 161
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
3-154 |
2.02e-92 |
|
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: 264.76 E-value: 2.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 3 TIYDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFTSQFEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQNC 82
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613163074 83 KLNYGVTFPMHQKIDVKGEHQLPLFRYLTAAQHGFFNKKIKWNFTKFLVDREGNVVKRFAPQKKPVQIEREI 154
Cdd:cd00340 81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
3-147 |
1.87e-60 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 184.98 E-value: 1.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 3 TIYDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFTSQFEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQNC 82
Cdd:PRK10606 4 SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 83 KLNYGVTFPMHQKIDVKGEHQLPLFRYLTAA--------QHGFFNK------------KIKWNFTKFLVDREGNVVKRFA 142
Cdd:PRK10606 84 RTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAaptavapeESGFYARmvskgraplypdDILWNFEKFLVGRDGQVIQRFS 163
|
....*
gi 613163074 143 PQKKP 147
Cdd:PRK10606 164 PDMTP 168
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
4-110 |
2.31e-44 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 141.72 E-value: 2.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 4 IYDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFTSQFEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQNCK 83
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80
|
90 100
....*....|....*....|....*..
gi 613163074 84 LNYGVTFPMHQKIDVKGEHQLPLFRYL 110
Cdd:pfam00255 81 GGYGVTFPLFSKIEVNGEKAHPVYKFL 107
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
5-158 |
5.45e-43 |
|
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: 139.59 E-value: 5.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 5 YDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFTSQ-FEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQNCK 83
Cdd:TIGR02540 3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613163074 84 LNYGVTFPMHQKIDVKGEHQLPLFRYLTAAQhgffNKKIKWNFTKFLVDREGNVVKRFAPQKKPVQIEREIEKLL 158
Cdd:TIGR02540 83 RNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
1-158 |
1.11e-101 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 288.51 E-value: 1.11e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 1 METIYDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFTSQFEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQ 80
Cdd:COG0386 1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 81 NCKLNYGVTFPMHQKIDVKGEHQLPLFRYLTAAQHGFF-NKKIKWNFTKFLVDREGNVVKRFAPQKKP--VQIEREIEKL 157
Cdd:COG0386 81 FCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLgGGDIKWNFTKFLIDRDGNVVARFAPTTKPedPELEAAIEKL 160
|
.
gi 613163074 158 L 158
Cdd:COG0386 161 L 161
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
3-154 |
2.02e-92 |
|
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: 264.76 E-value: 2.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 3 TIYDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFTSQFEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQNC 82
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613163074 83 KLNYGVTFPMHQKIDVKGEHQLPLFRYLTAAQHGFFNKKIKWNFTKFLVDREGNVVKRFAPQKKPVQIEREI 154
Cdd:cd00340 81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
3-147 |
1.87e-60 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 184.98 E-value: 1.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 3 TIYDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFTSQFEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQNC 82
Cdd:PRK10606 4 SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 83 KLNYGVTFPMHQKIDVKGEHQLPLFRYLTAA--------QHGFFNK------------KIKWNFTKFLVDREGNVVKRFA 142
Cdd:PRK10606 84 RTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAaptavapeESGFYARmvskgraplypdDILWNFEKFLVGRDGQVIQRFS 163
|
....*
gi 613163074 143 PQKKP 147
Cdd:PRK10606 164 PDMTP 168
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
2-158 |
8.04e-59 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 180.18 E-value: 8.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 2 ETIYDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFT-SQFEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQ 80
Cdd:PLN02412 7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613163074 81 NCKLNYGVTFPMHQKIDVKGEHQLPLFRYLTAAQHGFFNKKIKWNFTKFLVDREGNVVKRFAPQKKPVQIEREIEKLL 158
Cdd:PLN02412 87 TVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLL 164
|
|
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
2-158 |
2.25e-55 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 173.93 E-value: 2.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 2 ETIYDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFT-SQFEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQ 80
Cdd:PLN02399 77 KSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTsSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQ 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613163074 81 NCKLNYGVTFPMHQKIDVKGEHQLPLFRYLTAAQHGFFNKKIKWNFTKFLVDREGNVVKRFAPQKKPVQIEREIEKLL 158
Cdd:PLN02399 157 FACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLL 234
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
3-158 |
1.15e-46 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 149.91 E-value: 1.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 3 TIYDFVVETNKGVTYKLDAYKG-DVMLIVNTASECGFTSQ-FEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQ 80
Cdd:PTZ00256 19 SFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIKE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 81 NCKLNYGVTFPMHQKIDVKGEHQLPLFRYLTAAQHGFFN-----KKIKWNFTKFLVDREGNVVKRFAPQKKPVQIEREIE 155
Cdd:PTZ00256 99 YVQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNntneaRQIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQDIE 178
|
...
gi 613163074 156 KLL 158
Cdd:PTZ00256 179 KLL 181
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
4-110 |
2.31e-44 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 141.72 E-value: 2.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 4 IYDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFTSQFEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQNCK 83
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80
|
90 100
....*....|....*....|....*..
gi 613163074 84 LNYGVTFPMHQKIDVKGEHQLPLFRYL 110
Cdd:pfam00255 81 GGYGVTFPLFSKIEVNGEKAHPVYKFL 107
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
5-158 |
5.45e-43 |
|
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: 139.59 E-value: 5.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 5 YDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFTSQ-FEGLQSLYEKYKDQGFVILGFPCNQFGGQEPGSGEEAAQNCK 83
Cdd:TIGR02540 3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613163074 84 LNYGVTFPMHQKIDVKGEHQLPLFRYLTAAQhgffNKKIKWNFTKFLVDREGNVVKRFAPQKKPVQIEREIEKLL 158
Cdd:TIGR02540 83 RNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| PTZ00056 |
PTZ00056 |
glutathione peroxidase; Provisional |
3-158 |
4.15e-35 |
|
glutathione peroxidase; Provisional
Pssm-ID: 240248 [Multi-domain] Cd Length: 199 Bit Score: 121.11 E-value: 4.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 3 TIYDFVVETNKGVTYKLDAYKGDVMLIVNTASECGFT-SQFEGLQSLYEKYKDQGFVILGFPCNQFGGQEpgsGEEAAQN 81
Cdd:PTZ00056 18 SIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTkKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQE---FPNTKDI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 82 CKLN--YGVTFPMHQKIDVKGEHQLPLFRYLTAAQHGFFNKK-----IKWNFTKFLVDREGNVVKRFAPQKKPVQIEREI 154
Cdd:PTZ00056 95 RKFNdkNKIKYNFFEPIEVNGENTHELFKFLKANCDSMHDENgtlkaIGWNFGKFLVNKSGNVVAYFSPRTEPLELEKKI 174
|
....
gi 613163074 155 EKLL 158
Cdd:PTZ00056 175 AELL 178
|
|
| Bcp |
COG1225 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
6-158 |
3.42e-10 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 54.87 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 6 DFVVETNKGVTYKLDAYKGDVMLIVNTASECGF-TSQFEGLQSLYEKYKDQGFVILGFpcnqfggqepgSGEEAAQnckl 84
Cdd:COG1225 3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGcTAELPELRDLYEEFKDKGVEVLGV-----------SSDSDEA---- 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613163074 85 nygvtfpmHQKidVKGEHQLPlFRYLTAAQHGFFNK-KIKWNFTKFLVDREGNVVKRFAPQKKPV-QIEREIEKLL 158
Cdd:COG1225 68 --------HKK--FAEKYGLP-FPLLSDPDGEVAKAyGVRGTPTTFLIDPDGKIRYVWVGPVDPRpHLEEVLEALL 132
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
2-158 |
3.06e-08 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 49.69 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 2 ETIYDFVVETNKGVTYKLDAYKGDVMLIVNTASECGF-TSQFEGLQSLYEKYKdqGFVILGFPCNQfggqepgsGEEAAQ 80
Cdd:COG0526 6 KPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPcRAEMPVLKELAEEYG--GVVFVGVDVDE--------NPEAVK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 81 NCKLNYGVTFPMH--------QKIDVKGehqLPlfryltaaqhgffnkkikwnfTKFLVDREGNVVKRFAPQKKPVQIER 152
Cdd:COG0526 76 AFLKELGLPYPVLldpdgelaKAYGVRG---IP---------------------TTVLIDKDGKIVARHVGPLSPEELEE 131
|
....*.
gi 613163074 153 EIEKLL 158
Cdd:COG0526 132 ALEKLL 137
|
|
| TlpA_like_family |
cd02966 |
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
6-142 |
6.87e-05 |
|
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: 39.91 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 6 DFVVETNKGVTYKLDAYKGDVMLIVNTASECGfTSQFE--GLQSLYEKYKDQGFVILGFpcNQfggqePGSGEEAAQNCK 83
Cdd:cd02966 1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCP-PCRAEmpELEALAKEYKDDGVEVVGV--NV-----DDDDPAAVKAFL 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 613163074 84 LNYGVTFPMHqkIDVKGEhqlplfrylTAAQHGffnkKIKWNFTkFLVDREGNVVKRFA 142
Cdd:cd02966 73 KKYGITFPVL--LDPDGE---------LAKAYG----VRGLPTT-FLIDRDGRIRARHV 115
|
|
| AhpC-TSA |
pfam00578 |
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
6-140 |
1.44e-04 |
|
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: 39.51 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 6 DFVVETNKGVTYKLDAYKGD-VMLIVNTASEC-GFTSQFEGLQSLYEKYKDQGFVILGFPCNqfggqepgsGEEAAQNCK 83
Cdd:pfam00578 7 DFELPDGDGGTVSLSDYRGKwVVLFFYPADWTpVCTTELPALADLYEEFKKLGVEVLGVSVD---------SPESHKAFA 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 84 LNYGVTFPMhqKIDVKGEhqlplfrylTAAQHGFFNKkiKWNFTK---FLVDREGNVVKR 140
Cdd:pfam00578 78 EKYGLPFPL--LSDPDGE---------VARAYGVLNE--EEGGALratFVIDPDGKVRYI 124
|
|
| PRK03147 |
PRK03147 |
thiol-disulfide oxidoreductase ResA; |
6-139 |
2.69e-03 |
|
thiol-disulfide oxidoreductase ResA;
Pssm-ID: 179545 [Multi-domain] Cd Length: 173 Bit Score: 36.52 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 6 DFVVETNKGVTYKLDAYKGDVMLIVNTASECGFTSQ-FEGLQSLYEKYKDQGFVILGFPCNqfggqEPgsgEEAAQNCKL 84
Cdd:PRK03147 43 NFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKeMPYMNELYPKYKEKGVEIIAVNVD-----ET---ELAVKNFVN 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613163074 85 NYGVTFPM-----HQKIDVKGEHQLPlfryltaaqhgffnkkikwnfTKFLVDREGNVVK 139
Cdd:PRK03147 115 RYGLTFPVaidkgRQVIDAYGVGPLP---------------------TTFLIDKDGKVVK 153
|
|
| |
