|
Name |
Accession |
Description |
Interval |
E-value |
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
9-162 |
1.26e-80 |
|
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: 235.10 E-value: 1.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 9 SVYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTKgNYAELTELSQKYADKDFKILSFPCNQFGGQMPeGDGEEMVC 88
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEP-GSNEEIKE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118783685 89 HLRSAKAEVGDVFAKIDVNGDGAHPLYKYLKHKQGGTLGDSIKWNFAKFLVNKDGQPVDRYAPTTSPSSIVKDI 162
Cdd:cd00340 79 FCETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
7-166 |
2.25e-76 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 224.96 E-value: 2.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 7 AKSVYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTKgNYAELTELSQKYADKDFKILSFPCNQFGGQMPeGDGEEM 86
Cdd:COG0386 1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEP-GSNEEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 87 --VCHLRSakaevG---DVFAKIDVNGDGAHPLYKYLKHKQGGTLGDS-IKWNFAKFLVNKDGQPVDRYAPTTSPSS--I 158
Cdd:COG0386 79 aeFCSLNY-----GvtfPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGdIKWNFTKFLIDRDGNVVARFAPTTKPEDpeL 153
|
....*...
gi 118783685 159 VKDIDKLL 166
Cdd:COG0386 154 EAAIEKLL 161
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
8-167 |
9.63e-69 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 205.99 E-value: 9.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 8 KSVYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTKGNYAELTELSQKYADKDFKILSFPCNQFGGQMPEGDGE--E 85
Cdd:PLN02412 7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEiqQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 86 MVCHLrsAKAEVgDVFAKIDVNGDGAHPLYKYLKHKQGGTLGDSIKWNFAKFLVNKDGQPVDRYAPTTSPSSIVKDIDKL 165
Cdd:PLN02412 87 TVCTR--FKAEF-PIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNL 163
|
..
gi 118783685 166 LG 167
Cdd:PLN02412 164 LG 165
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
9-166 |
2.04e-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: 141.13 E-value: 2.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 9 SVYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTKGNYAELTELSQKYADKDFKILSFPCNQFGGQMPeGDGEEMVC 88
Cdd:TIGR02540 1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEP-DSSKEIES 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118783685 89 HLRSAKAEVGDVFAKIDVNGDGAHPLYKYLKHkqggTLGDSIKWNFAKFLVNKDGQPVDRYAPTTSPSSIVKDIDKLL 166
Cdd:TIGR02540 80 FARRNYGVTFPMFSKIKILGSEAEPAFRFLVD----SSKKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
10-119 |
2.76e-40 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 131.71 E-value: 2.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 10 VYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTkGNYAELTELSQKYADKDFKILSFPCNQFGGQMPEGDGEemVCH 89
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLT-PQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEE--IKY 77
|
90 100 110
....*....|....*....|....*....|.
gi 118783685 90 LRSAKAEVG-DVFAKIDVNGDGAHPLYKYLK 119
Cdd:pfam00255 78 FCPGGYGVTfPLFSKIEVNGEKAHPVYKFLK 108
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
9-162 |
1.26e-80 |
|
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: 235.10 E-value: 1.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 9 SVYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTKgNYAELTELSQKYADKDFKILSFPCNQFGGQMPeGDGEEMVC 88
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEP-GSNEEIKE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118783685 89 HLRSAKAEVGDVFAKIDVNGDGAHPLYKYLKHKQGGTLGDSIKWNFAKFLVNKDGQPVDRYAPTTSPSSIVKDI 162
Cdd:cd00340 79 FCETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
7-166 |
2.25e-76 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 224.96 E-value: 2.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 7 AKSVYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTKgNYAELTELSQKYADKDFKILSFPCNQFGGQMPeGDGEEM 86
Cdd:COG0386 1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEP-GSNEEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 87 --VCHLRSakaevG---DVFAKIDVNGDGAHPLYKYLKHKQGGTLGDS-IKWNFAKFLVNKDGQPVDRYAPTTSPSS--I 158
Cdd:COG0386 79 aeFCSLNY-----GvtfPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGdIKWNFTKFLIDRDGNVVARFAPTTKPEDpeL 153
|
....*...
gi 118783685 159 VKDIDKLL 166
Cdd:COG0386 154 EAAIEKLL 161
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
8-167 |
9.63e-69 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 205.99 E-value: 9.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 8 KSVYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTKGNYAELTELSQKYADKDFKILSFPCNQFGGQMPEGDGE--E 85
Cdd:PLN02412 7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEiqQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 86 MVCHLrsAKAEVgDVFAKIDVNGDGAHPLYKYLKHKQGGTLGDSIKWNFAKFLVNKDGQPVDRYAPTTSPSSIVKDIDKL 165
Cdd:PLN02412 87 TVCTR--FKAEF-PIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNL 163
|
..
gi 118783685 166 LG 167
Cdd:PLN02412 164 LG 165
|
|
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
8-166 |
1.58e-66 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 202.82 E-value: 1.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 8 KSVYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTKGNYAELTELSQKYADKDFKILSFPCNQFGGQMPEGDGEEMV 87
Cdd:PLN02399 77 KSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQ 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118783685 88 CHLRSAKAEVgDVFAKIDVNGDGAHPLYKYLKHKQGGTLGDSIKWNFAKFLVNKDGQPVDRYAPTTSPSSIVKDIDKLL 166
Cdd:PLN02399 157 FACTRFKAEF-PIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLL 234
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
6-166 |
1.03e-48 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 155.69 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 6 NAKSVYDFTVKDSQGADVSLEKYRG-KVLLIVNIASQCGLTKGNYAELTELSQKYADKDFKILSFPCNQFGGQMPEGDGE 84
Cdd:PTZ00256 16 PTKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 85 --EMVchlrsaKAEVG---DVFAKIDVNGDGAHPLYKYLK-----HKQGGTLGDSIKWNFAKFLVNKDGQPVDRYAPTTS 154
Cdd:PTZ00256 96 ikEYV------QKKFNvdfPLFQKIEVNGENTHEIYKYLRrnselFQNNTNEARQIPWNFAKFLIDGQGKVVKYFSPKVN 169
|
170
....*....|..
gi 118783685 155 PSSIVKDIDKLL 166
Cdd:PTZ00256 170 PNEMIQDIEKLL 181
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
9-166 |
2.04e-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: 141.13 E-value: 2.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 9 SVYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTKGNYAELTELSQKYADKDFKILSFPCNQFGGQMPeGDGEEMVC 88
Cdd:TIGR02540 1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEP-DSSKEIES 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118783685 89 HLRSAKAEVGDVFAKIDVNGDGAHPLYKYLKHkqggTLGDSIKWNFAKFLVNKDGQPVDRYAPTTSPSSIVKDIDKLL 166
Cdd:TIGR02540 80 FARRNYGVTFPMFSKIKILGSEAEPAFRFLVD----SSKKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| PTZ00056 |
PTZ00056 |
glutathione peroxidase; Provisional |
8-167 |
4.40e-43 |
|
glutathione peroxidase; Provisional
Pssm-ID: 240248 [Multi-domain] Cd Length: 199 Bit Score: 141.91 E-value: 4.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 8 KSVYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTKGNYAELTELSQKYADKDFKILSFPCNQFGGQmpEGDGEEMV 87
Cdd:PTZ00056 17 KSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQ--EFPNTKDI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 88 CHLRSAKAEVGDVFAKIDVNGDGAHPLYKYLK------HKQGGTLgDSIKWNFAKFLVNKDGQPVDRYAPTTSPSSIVKD 161
Cdd:PTZ00056 95 RKFNDKNKIKYNFFEPIEVNGENTHELFKFLKancdsmHDENGTL-KAIGWNFGKFLVNKSGNVVAYFSPRTEPLELEKK 173
|
....*.
gi 118783685 162 IDKLLG 167
Cdd:PTZ00056 174 IAELLG 179
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
9-155 |
7.28e-43 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 140.68 E-value: 7.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 9 SVYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTKgNYAELTELSQKYADKDFKILSFPCNQFGGQMPeGDGEEMVC 88
Cdd:PRK10606 4 SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTP-QYEQLENIQKAWADQGFVVLGFPCNQFLGQEP-GSDEEIKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 89 HLRSAKAEVGDVFAKIDVNGDGAHPLYKYLKHKQGGTLG--------------------DSIKWNFAKFLVNKDGQPVDR 148
Cdd:PRK10606 82 YCRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTAVApeesgfyarmvskgraplypDDILWNFEKFLVGRDGQVIQR 161
|
....*..
gi 118783685 149 YAPTTSP 155
Cdd:PRK10606 162 FSPDMTP 168
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
10-119 |
2.76e-40 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 131.71 E-value: 2.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 10 VYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTkGNYAELTELSQKYADKDFKILSFPCNQFGGQMPEGDGEemVCH 89
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLT-PQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEE--IKY 77
|
90 100 110
....*....|....*....|....*....|.
gi 118783685 90 LRSAKAEVG-DVFAKIDVNGDGAHPLYKYLK 119
Cdd:pfam00255 78 FCPGGYGVTfPLFSKIEVNGEKAHPVYKFLK 108
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
8-167 |
2.39e-07 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 47.38 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 8 KSVYDFTVKDSQGADVSLEKYRGKVLLIVNIASQCGltkgnyaeltelsqkyadkdfkilsfPCNQfggQMPegdgeemv 87
Cdd:COG0526 6 KPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCP--------------------------PCRA---EMP-------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118783685 88 cHLRSAKAEVGDV-FAKIDVNGDGAHPLYKYLKHKQGGTLGDSIKWNFAK----------FLVNKDGQPVDRYAPTTSPS 156
Cdd:COG0526 49 -VLKELAEEYGGVvFVGVDVDENPEAVKAFLKELGLPYPVLLDPDGELAKaygvrgipttVLIDKDGKIVARHVGPLSPE 127
|
170
....*....|.
gi 118783685 157 SIVKDIDKLLG 167
Cdd:COG0526 128 ELEEALEKLLA 138
|
|
| Bcp |
COG1225 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
12-67 |
6.28e-07 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 46.01 E-value: 6.28e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 118783685 12 DFTVKDSQGADVSLEKYRGKVLLIVNIASQCGLTKGNYAELTELSQKYADKDFKIL 67
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 ... |
12-67 |
1.51e-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: 44.92 E-value: 1.51e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 118783685 12 DFTVKDSQGADVSLEKYRGKVLLiVNI-ASQCGLTKGNYAELTELSQKYADKDFKIL 67
Cdd:cd02966 1 DFSLPDLDGKPVSLSDLKGKVVL-VNFwASWCPPCRAEMPELEALAKEYKDDGVEVV 56
|
|
| AhpC-TSA |
pfam00578 |
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
12-67 |
2.32e-03 |
|
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: 36.05 E-value: 2.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 118783685 12 DFTVKDSQGADVSLEKYRGKVLLIVNIAS-QCGLTKGNYAELTELSQKYADKDFKIL 67
Cdd:pfam00578 7 DFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVL 63
|
|
| PRX_like1 |
cd02969 |
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ... |
12-68 |
3.06e-03 |
|
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: 36.45 E-value: 3.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 118783685 12 DFTVKDSQGADVSLEKYR-GKVLLIVNIASQCGLTKGNYAELTELSQKYADKDFKILS 68
Cdd:cd02969 6 DFSLPDTDGKTYSLADFAdGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVA 63
|
|
| |
