|
Name |
Accession |
Description |
Interval |
E-value |
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
1-158 |
1.28e-111 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 313.55 E-value: 1.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 1 MSIYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFTPQYKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEY 80
Cdd:COG0386 2 MSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 81 CEINYGVTFPMFEKIDVKGDEAHPLFKYLSKEAPGVLGSKSVKWNFTKFLVDQDGRVLKRFAPKTTPQ--QIESDISKLL 158
Cdd:COG0386 82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGDIKWNFTKFLIDRDGNVVARFAPTTKPEdpELEAAIEKLL 161
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
2-154 |
1.86e-96 |
|
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: 274.78 E-value: 1.86e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 2 SIYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFTPQYKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEYC 81
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133923694 82 EINYGVTFPMFEKIDVKGDEAHPLFKYLSKEAPGVLGsKSVKWNFTKFLVDQDGRVLKRFAPKTTPQQIESDI 154
Cdd:cd00340 81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG-KDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
2-148 |
3.02e-65 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 197.30 E-value: 3.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 2 SIYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFTPQYKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEYC 81
Cdd:PRK10606 4 SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 82 EINYGVTFPMFEKIDVKGDEAHPLFKYLSKEAPGV-----------LGSK--------SVKWNFTKFLVDQDGRVLKRFA 142
Cdd:PRK10606 84 RTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTAvapeesgfyarMVSKgraplypdDILWNFEKFLVGRDGQVIQRFS 163
|
....*.
gi 1133923694 143 PKTTPQ 148
Cdd:PRK10606 164 PDMTPE 169
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
3-109 |
1.52e-50 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 157.13 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 3 IYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFTPQYKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEYCE 82
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80
|
90 100
....*....|....*....|....*..
gi 1133923694 83 INYGVTFPMFEKIDVKGDEAHPLFKYL 109
Cdd:pfam00255 81 GGYGVTFPLFSKIEVNGEKAHPVYKFL 107
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
2-158 |
4.49e-50 |
|
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: 157.69 E-value: 4.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 2 SIYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFTPQ-YKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEY 80
Cdd:TIGR02540 1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133923694 81 CEINYGVTFPMFEKIDVKGDEAHPLFKYLSKEApgvlgSKSVKWNFTKFLVDQDGRVLKRFAPKTTPQQIESDISKLL 158
Cdd:TIGR02540 81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSS-----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
1-158 |
1.28e-111 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 313.55 E-value: 1.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 1 MSIYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFTPQYKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEY 80
Cdd:COG0386 2 MSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 81 CEINYGVTFPMFEKIDVKGDEAHPLFKYLSKEAPGVLGSKSVKWNFTKFLVDQDGRVLKRFAPKTTPQ--QIESDISKLL 158
Cdd:COG0386 82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGDIKWNFTKFLIDRDGNVVARFAPTTKPEdpELEAAIEKLL 161
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
2-154 |
1.86e-96 |
|
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: 274.78 E-value: 1.86e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 2 SIYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFTPQYKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEYC 81
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133923694 82 EINYGVTFPMFEKIDVKGDEAHPLFKYLSKEAPGVLGsKSVKWNFTKFLVDQDGRVLKRFAPKTTPQQIESDI 154
Cdd:cd00340 81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG-KDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
2-148 |
3.02e-65 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 197.30 E-value: 3.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 2 SIYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFTPQYKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEYC 81
Cdd:PRK10606 4 SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 82 EINYGVTFPMFEKIDVKGDEAHPLFKYLSKEAPGV-----------LGSK--------SVKWNFTKFLVDQDGRVLKRFA 142
Cdd:PRK10606 84 RTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTAvapeesgfyarMVSKgraplypdDILWNFEKFLVGRDGQVIQRFS 163
|
....*.
gi 1133923694 143 PKTTPQ 148
Cdd:PRK10606 164 PDMTPE 169
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
2-158 |
2.19e-60 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 184.42 E-value: 2.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 2 SIYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFT-PQYKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEY 80
Cdd:PLN02412 8 SIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133923694 81 CEINYGVTFPMFEKIDVKGDEAHPLFKYLSKEAPGVLGSkSVKWNFTKFLVDQDGRVLKRFAPKTTPQQIESDISKLL 158
Cdd:PLN02412 88 VCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGD-AIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLL 164
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
2-159 |
7.20e-57 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 176.10 E-value: 7.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 2 SIYDFEVNTLKGEEESLSKYQG-KVLLVVNTASKCGFTPQ-YKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAE 79
Cdd:PTZ00256 19 SFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIKE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 80 YCEINYGVTFPMFEKIDVKGDEAHPLFKYLSKEAPGVLGS----KSVKWNFTKFLVDQDGRVLKRFAPKTTPQQIESDIS 155
Cdd:PTZ00256 99 YVQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNNtneaRQIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQDIE 178
|
....
gi 1133923694 156 KLLK 159
Cdd:PTZ00256 179 KLLN 182
|
|
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
2-158 |
3.73e-55 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 173.55 E-value: 3.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 2 SIYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFTP-QYKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEY 80
Cdd:PLN02399 78 SVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQF 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133923694 81 CEINYGVTFPMFEKIDVKGDEAHPLFKYLSKEAPGVLGSkSVKWNFTKFLVDQDGRVLKRFAPKTTPQQIESDISKLL 158
Cdd:PLN02399 158 ACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGD-LIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLL 234
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
3-109 |
1.52e-50 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 157.13 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 3 IYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFTPQYKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEYCE 82
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80
|
90 100
....*....|....*....|....*..
gi 1133923694 83 INYGVTFPMFEKIDVKGDEAHPLFKYL 109
Cdd:pfam00255 81 GGYGVTFPLFSKIEVNGEKAHPVYKFL 107
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
2-158 |
4.49e-50 |
|
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: 157.69 E-value: 4.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 2 SIYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFTPQ-YKGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEY 80
Cdd:TIGR02540 1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133923694 81 CEINYGVTFPMFEKIDVKGDEAHPLFKYLSKEApgvlgSKSVKWNFTKFLVDQDGRVLKRFAPKTTPQQIESDISKLL 158
Cdd:TIGR02540 81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSS-----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| PTZ00056 |
PTZ00056 |
glutathione peroxidase; Provisional |
2-158 |
1.80e-46 |
|
glutathione peroxidase; Provisional
Pssm-ID: 240248 [Multi-domain] Cd Length: 199 Bit Score: 150.00 E-value: 1.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 2 SIYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCGFTPQY-KGLQEVYEKFKDRGFEVLGFPSNQFAGQEPGESNEIAEY 80
Cdd:PTZ00056 18 SIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHvDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRKF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 81 CEINyGVTFPMFEKIDVKGDEAHPLFKYLSKEAPGVLGS----KSVKWNFTKFLVDQDGRVLKRFAPKTTPQQIESDISK 156
Cdd:PTZ00056 98 NDKN-KIKYNFFEPIEVNGENTHELFKFLKANCDSMHDEngtlKAIGWNFGKFLVNKSGNVVAYFSPRTEPLELEKKIAE 176
|
..
gi 1133923694 157 LL 158
Cdd:PTZ00056 177 LL 178
|
|
| Bcp |
COG1225 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
5-159 |
1.16e-13 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 63.73 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 5 DFEVNTLKGEEESLSKYQGKVLLVVNTASKCGF-TPQYKGLQEVYEKFKDRGFEVLGFPSNqfagqepgESNEIAEYCEi 83
Cdd:COG1225 3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGcTAELPELRDLYEEFKDKGVEVLGVSSD--------SDEAHKKFAE- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133923694 84 NYGVTFPMFekIDVKGDEAhplfkylskEAPGVLGSKSVkwnftkFLVDQDGRVLKRFAPKTTP-QQIESDISKLLK 159
Cdd:COG1225 74 KYGLPFPLL--SDPDGEVA---------KAYGVRGTPTT------FLIDPDGKIRYVWVGPVDPrPHLEEVLEALLA 133
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
2-159 |
1.09e-10 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 56.24 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 2 SIYDFEVNTLKGEEESLSKYQGKVLLVVNTASKCG----FTPQykgLQEVYEKFKdrGFEVLGFPSNqfagqepgESNEI 77
Cdd:COG0526 7 PAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPpcraEMPV---LKELAEEYG--GVVFVGVDVD--------ENPEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 78 AEYCEINYGVTFPMFekIDVKGDEAHplfKYLSKEAPgvlgsksvkwnfTKFLVDQDGRVLKRFAPKTTPQQIESDISKL 157
Cdd:COG0526 74 VKAFLKELGLPYPVL--LDPDGELAK---AYGVRGIP------------TTVLIDKDGKIVARHVGPLSPEELEEALEKL 136
|
..
gi 1133923694 158 LK 159
Cdd:COG0526 137 LA 138
|
|
| AhpC-TSA |
pfam00578 |
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
5-137 |
3.02e-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: 51.84 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 5 DFEVNTLKGEEESLSKYQGKVLLVVNTASkcGFTP----QYKGLQEVYEKFKDRGFEVLGFPSNqfagqEPGESNEIAEy 80
Cdd:pfam00578 7 DFELPDGDGGTVSLSDYRGKWVVLFFYPA--DWTPvcttELPALADLYEEFKKLGVEVLGVSVD-----SPESHKAFAE- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1133923694 81 ceiNYGVTFPMFekIDVKGDEAHplfKYlskeapGVLGSKSVKWNFTKFLVDQDGRV 137
Cdd:pfam00578 79 ---KYGLPFPLL--SDPDGEVAR---AY------GVLNEEEGGALRATFVIDPDGKV 121
|
|
| TlpA_like_family |
cd02966 |
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
5-142 |
3.93e-08 |
|
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: 48.77 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 5 DFEVNTLKGEEESLSKYQGKVLLVVNTASKCGF----TPQykgLQEVYEKFKDRGFEVLGfpsnqFAGQEPGESNeIAEY 80
Cdd:cd02966 1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPcraeMPE---LEALAKEYKDDGVEVVG-----VNVDDDDPAA-VKAF 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133923694 81 CEiNYGVTFPMFEkidvkgDEAHPLFKYLskeapGVLGsksvkWNFTkFLVDQDGRVLKRFA 142
Cdd:cd02966 72 LK-KYGITFPVLL------DPDGELAKAY-----GVRG-----LPTT-FLIDRDGRIRARHV 115
|
|
| Redoxin |
pfam08534 |
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
13-141 |
3.02e-05 |
|
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 13 GEEESLSKYQGKVLLVVNTASKcgFTP----QYKGLQEVYEKFKDRGFEVLG-------FPSNQFAGQEpgesneiaeyc 81
Cdd:pfam08534 18 GNTVSLSDFKGKKVVLNFWPGA--FCPtcsaEHPYLEKLNELYKEKGVDVVAvnsdndaFFVKRFWGKE----------- 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133923694 82 einyGVTFPMFekIDVKGDEAHPLFKYLSKEAPGVLGSKSVkwnftkFLVDQDGRVLKRF 141
Cdd:pfam08534 85 ----GLPFPFL--SDGNAAFTKALGLPIEEDASAGLRSPRY------AVIDEDGKVVYLF 132
|
|
| PRX_BCP |
cd03017 |
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ... |
5-60 |
4.17e-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: 38.30 E-value: 4.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133923694 5 DFEVNTLKGEEESLSKYQGKVLLVV-----NTAskcGFTPQYKGLQEVYEKFKDRGFEVLG 60
Cdd:cd03017 5 DFTLPDQDGETVSLSDLRGKPVVLYfypkdDTP---GCTKEACDFRDLYEEFKALGAVVIG 62
|
|
| TryX_like_TryX_NRX |
cd03009 |
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ... |
13-59 |
1.85e-03 |
|
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.
Pssm-ID: 239307 [Multi-domain] Cd Length: 131 Bit Score: 36.49 E-value: 1.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1133923694 13 GEEESLSKYQGKVLLVVNTASKC----GFTPQykgLQEVYEKFKDRG--FEVL 59
Cdd:cd03009 8 GGKVPVSSLEGKTVGLYFSASWCppcrAFTPK---LVEFYEKLKESGknFEIV 57
|
|
| Sco1 |
COG1999 |
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ... |
129-159 |
4.72e-03 |
|
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441602 Cd Length: 156 Bit Score: 35.65 E-value: 4.72e-03
10 20 30
....*....|....*....|....*....|.
gi 1133923694 129 FLVDQDGRVLKRFAPKTTPQQIESDISKLLK 159
Cdd:COG1999 125 YLVDPDGRLRGYYPAGEDPEELAADLKALLE 155
|
|
| |
