|
Name |
Accession |
Description |
Interval |
E-value |
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
1-159 |
1.07e-116 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 326.26 E-value: 1.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 1 MSTLYSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFTPQYAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIGA 80
Cdd:COG0386 1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 81 FCERNYGVTFPMFAKIDVKGDHAHPLYRYLTDEAPGILGLKAIKWNFTKFLIDREGRIVKRYAPSTKPD--EIAADIDKL 158
Cdd:COG0386 81 FCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGDIKWNFTKFLIDRDGNVVARFAPTTKPEdpELEAAIEKL 160
|
.
gi 499868794 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 |
3.55e-104 |
|
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: 294.42 E-value: 3.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 3 TLYSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFTPQYAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIGAFC 82
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499868794 83 ERNYGVTFPMFAKIDVKGDHAHPLYRYLTDEAPGILGlKAIKWNFTKFLIDREGRIVKRYAPSTKPDEIAADI 155
Cdd:cd00340 81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG-KDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
2-150 |
5.83e-62 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 188.83 E-value: 5.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 2 STLYSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFTPQYAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIGAF 81
Cdd:PRK10606 3 DSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 82 CERNYGVTFPMFAKIDVKGDHAHPLYRYLTDEAPGILGLKA-------------------IKWNFTKFLIDREGRIVKRY 142
Cdd:PRK10606 83 CRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTAVAPEEsgfyarmvskgraplypddILWNFEKFLVGRDGQVIQRF 162
|
....*...
gi 499868794 143 APSTKPDE 150
Cdd:PRK10606 163 SPDMTPED 170
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
5-159 |
1.29e-54 |
|
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: 169.25 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 5 YSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFTPQ-YAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIGAFCE 83
Cdd:TIGR02540 3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499868794 84 RNYGVTFPMFAKIDVKGDHAHPLYRYLTDEAPgilglKAIKWNFTKFLIDREGRIVKRYAPSTKPDEIAADIDKLL 159
Cdd:TIGR02540 83 RNYGVTFPMFSKIKILGSEAEPAFRFLVDSSK-----KEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
4-110 |
2.30e-53 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 164.45 E-value: 2.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 4 LYSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFTPQYAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIGAFCE 83
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80
|
90 100
....*....|....*....|....*..
gi 499868794 84 RNYGVTFPMFAKIDVKGDHAHPLYRYL 110
Cdd:pfam00255 81 GGYGVTFPLFSKIEVNGEKAHPVYKFL 107
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
1-159 |
1.07e-116 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 326.26 E-value: 1.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 1 MSTLYSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFTPQYAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIGA 80
Cdd:COG0386 1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 81 FCERNYGVTFPMFAKIDVKGDHAHPLYRYLTDEAPGILGLKAIKWNFTKFLIDREGRIVKRYAPSTKPD--EIAADIDKL 158
Cdd:COG0386 81 FCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGDIKWNFTKFLIDRDGNVVARFAPTTKPEdpELEAAIEKL 160
|
.
gi 499868794 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 |
3.55e-104 |
|
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: 294.42 E-value: 3.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 3 TLYSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFTPQYAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIGAFC 82
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499868794 83 ERNYGVTFPMFAKIDVKGDHAHPLYRYLTDEAPGILGlKAIKWNFTKFLIDREGRIVKRYAPSTKPDEIAADI 155
Cdd:cd00340 81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG-KDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
2-150 |
5.83e-62 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 188.83 E-value: 5.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 2 STLYSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFTPQYAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIGAF 81
Cdd:PRK10606 3 DSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 82 CERNYGVTFPMFAKIDVKGDHAHPLYRYLTDEAPGILGLKA-------------------IKWNFTKFLIDREGRIVKRY 142
Cdd:PRK10606 83 CRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTAVAPEEsgfyarmvskgraplypddILWNFEKFLVGRDGQVIQRF 162
|
....*...
gi 499868794 143 APSTKPDE 150
Cdd:PRK10606 163 SPDMTPED 170
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
3-159 |
4.35e-55 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 170.94 E-value: 4.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 3 TLYSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFT-PQYAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQI-GA 80
Cdd:PLN02412 8 SIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIqQT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499868794 81 FCERnYGVTFPMFAKIDVKGDHAHPLYRYLTDEAPGILGlKAIKWNFTKFLIDREGRIVKRYAPSTKPDEIAADIDKLL 159
Cdd:PLN02412 88 VCTR-FKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFG-DAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLL 164
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
2-159 |
1.11e-54 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 170.32 E-value: 1.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 2 STLYSFSAETLAGAPVSLDAYRG-KVLLIVNTASECGFTPQ-YAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIG 79
Cdd:PTZ00256 18 KSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 80 AFCERNYGVTFPMFAKIDVKGDHAHPLYRYLTDEAPGILG----LKAIKWNFTKFLIDREGRIVKRYAPSTKPDEIAADI 155
Cdd:PTZ00256 98 EYVQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNntneARQIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQDI 177
|
....
gi 499868794 156 DKLL 159
Cdd:PTZ00256 178 EKLL 181
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
5-159 |
1.29e-54 |
|
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: 169.25 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 5 YSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFTPQ-YAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIGAFCE 83
Cdd:TIGR02540 3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499868794 84 RNYGVTFPMFAKIDVKGDHAHPLYRYLTDEAPgilglKAIKWNFTKFLIDREGRIVKRYAPSTKPDEIAADIDKLL 159
Cdd:TIGR02540 83 RNYGVTFPMFSKIKILGSEAEPAFRFLVDSSK-----KEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
4-110 |
2.30e-53 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 164.45 E-value: 2.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 4 LYSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFTPQYAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIGAFCE 83
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80
|
90 100
....*....|....*....|....*..
gi 499868794 84 RNYGVTFPMFAKIDVKGDHAHPLYRYL 110
Cdd:pfam00255 81 GGYGVTFPLFSKIEVNGEKAHPVYKFL 107
|
|
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
3-159 |
8.70e-53 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 167.38 E-value: 8.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 3 TLYSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFTP-QYAGLQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIGAF 81
Cdd:PLN02399 78 SVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQF 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499868794 82 CERNYGVTFPMFAKIDVKGDHAHPLYRYLTDEAPGILGlKAIKWNFTKFLIDREGRIVKRYAPSTKPDEIAADIDKLL 159
Cdd:PLN02399 158 ACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLG-DLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLL 234
|
|
| PTZ00056 |
PTZ00056 |
glutathione peroxidase; Provisional |
2-159 |
2.79e-45 |
|
glutathione peroxidase; Provisional
Pssm-ID: 240248 [Multi-domain] Cd Length: 199 Bit Score: 146.92 E-value: 2.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 2 STLYSFSAETLAGAPVSLDAYRGKVLLIVNTASECGFTPQYAG-LQKLYDQYAARGFFVLGFPCNQFGKQEPGDAAQIGA 80
Cdd:PTZ00056 17 KSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDqMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 81 FCERNyGVTFPMFAKIDVKGDHAHPLYRYLTDEAPGILG----LKAIKWNFTKFLIDREGRIVKRYAPSTKPDEIAADID 156
Cdd:PTZ00056 97 FNDKN-KIKYNFFEPIEVNGENTHELFKFLKANCDSMHDengtLKAIGWNFGKFLVNKSGNVVAYFSPRTEPLELEKKIA 175
|
...
gi 499868794 157 KLL 159
Cdd:PTZ00056 176 ELL 178
|
|
| Bcp |
COG1225 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
7-159 |
1.65e-15 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 68.74 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 7 FSAETLAGAPVSLDAYRGKVLLIVNTASECGF-TPQYAGLQKLYDQYAARGFFVLGFpcnqfgkqEPGDAAQIGAFCERn 85
Cdd:COG1225 4 FTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGcTAELPELRDLYEEFKDKGVEVLGV--------SSDSDEAHKKFAEK- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499868794 86 YGVTFPMFAkiDVKGDHAhplyryltdEAPGILGLKAIkwnftkFLIDREGRIVKRYAPSTKPDEIAAD-IDKLL 159
Cdd:COG1225 75 YGLPFPLLS--DPDGEVA---------KAYGVRGTPTT------FLIDPDGKIRYVWVGPVDPRPHLEEvLEALL 132
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
3-159 |
9.09e-12 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 58.93 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 3 TLYSFSAETLAGAPVSLDAYRGKVLLIVNTASECG----FTPQyagLQKLYDQYaaRGFFVLGFPCNQfgkqepgDAAQI 78
Cdd:COG0526 7 PAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPpcraEMPV---LKELAEEY--GGVVFVGVDVDE-------NPEAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 79 GAFCERnYGVTFPMFAkidvkgDHAHPLYRYLtdeapGILGLKaikwnfTKFLIDREGRIVKRYAPSTKPDEIAADIDKL 158
Cdd:COG0526 75 KAFLKE-LGLPYPVLL------DPDGELAKAY-----GVRGIP------TTVLIDKDGKIVARHVGPLSPEELEEALEKL 136
|
.
gi 499868794 159 L 159
Cdd:COG0526 137 L 137
|
|
| TlpA_like_family |
cd02966 |
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
7-143 |
4.30e-11 |
|
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: 56.48 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 7 FSAETLAGAPVSLDAYRGKVLLIVNTASECGF----TPQyagLQKLYDQYAARGFFVLGFpcNqfgkQEPGDAAQIGAFc 82
Cdd:cd02966 2 FSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPcraeMPE---LEALAKEYKDDGVEVVGV--N----VDDDDPAAVKAF- 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499868794 83 ERNYGVTFPMFakIDVKGDhahplyrylTDEAPGILGLkaikwnFTKFLIDREGRIVKRYA 143
Cdd:cd02966 72 LKKYGITFPVL--LDPDGE---------LAKAYGVRGL------PTTFLIDRDGRIRARHV 115
|
|
| AhpC-TSA |
pfam00578 |
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
6-141 |
1.17e-09 |
|
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: 53.00 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 6 SFSAETLAGAPVSLDAYRGKVLLIVNTASecGFTP----QYAGLQKLYDQYAARGFFVLGFPCNqfgkqepgDAAQIGAF 81
Cdd:pfam00578 7 DFELPDGDGGTVSLSDYRGKWVVLFFYPA--DWTPvcttELPALADLYEEFKKLGVEVLGVSVD--------SPESHKAF 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 82 CERnYGVTFPMFAkiDVKGDHAHpLYRYLTDEAPGILGlkaikwnfTKFLIDREGRIVKR 141
Cdd:pfam00578 77 AEK-YGLPFPLLS--DPDGEVAR-AYGVLNEEEGGALR--------ATFVIDPDGKVRYI 124
|
|
| Redoxin |
pfam08534 |
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
6-159 |
2.99e-07 |
|
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 46.98 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 6 SFSAETLAGAPVSLDAYRGKVLLIVNTASecGFTP----QYAGLQKLYDQYAARGFFVLGFPCNQfgkqepgDAAQIGAF 81
Cdd:pfam08534 10 TLPDAATDGNTVSLSDFKGKKVVLNFWPG--AFCPtcsaEHPYLEKLNELYKEKGVDVVAVNSDN-------DAFFVKRF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499868794 82 CERnYGVTFPMFAkiDVKGDHAHPLYRYLTDEAPGILGLKAIkwnftkFLIDREGRIVKRYAPSTKPDEIaADIDKLL 159
Cdd:pfam08534 81 WGK-EGLPFPFLS--DGNAAFTKALGLPIEEDASAGLRSPRY------AVIDEDGKVVYLFVGPEPGVDV-SDAEAVL 148
|
|
| PRX_family |
cd02971 |
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ... |
6-159 |
1.40e-06 |
|
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They 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 TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis.
Pssm-ID: 239269 [Multi-domain] Cd Length: 140 Bit Score: 45.23 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 6 SFSAETLAGAPVSLDAYRGKVLLIV-----NTAsecGFTPQYAGLQKLYDQYAARGFFVLGFPCNqfgkqepgDAAQIGA 80
Cdd:cd02971 4 DFTLPATDGGEVSLSDFKGKWVVLFfypkdFTP---VCTTELCAFRDLAEEFAKGGAEVLGVSVD--------SPFSHKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 81 FCERNYGVTFPMFAkiDVKGDHAhplyryltdEAPGILGLKAIKWNFTK---FLIDREGRIVKRYapsTKPDEIAADIDK 157
Cdd:cd02971 73 WAEKEGGLNFPLLS--DPDGEFA---------KAYGVLIEKSAGGGLAAratFIIDPDGKIRYVE---VEPLPTGRNAEE 138
|
..
gi 499868794 158 LL 159
Cdd:cd02971 139 LL 140
|
|
| PRX_BCP |
cd03017 |
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ... |
6-155 |
8.46e-06 |
|
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: 42.92 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868794 6 SFSAETLAGAPVSLDAYRGKVLLIV-----NTAsecGFTPQYAGLQKLYDQYAARGFFVLGFpcnqfgkqEPGDAAQIGA 80
Cdd:cd03017 5 DFTLPDQDGETVSLSDLRGKPVVLYfypkdDTP---GCTKEACDFRDLYEEFKALGAVVIGV--------SPDSVESHAK 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499868794 81 FCERnYGVTFPMFAkiDVKGDHAhplyryltdEAPGILGLKAIKWNFTK---FLIDREGRIVKRYaPSTKPDEIAADI 155
Cdd:cd03017 74 FAEK-YGLPFPLLS--DPDGKLA---------KAYGVWGEKKKKYMGIErstFLIDPDGKIVKVW-RKVKPKGHAEEV 138
|
|
| Sco1 |
COG1999 |
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ... |
130-159 |
3.98e-05 |
|
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441602 Cd Length: 156 Bit Score: 41.42 E-value: 3.98e-05
10 20 30
....*....|....*....|....*....|
gi 499868794 130 FLIDREGRIVKRYAPSTKPDEIAADIDKLL 159
Cdd:COG1999 125 YLVDPDGRLRGYYPAGEDPEELAADLKALL 154
|
|
| |
