|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
1-236 |
6.33e-155 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 429.32 E-value: 6.33e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 1 MVSMTTSSSSYGTFSTVVNSSRPNSSATFLVPSLKFSTGISNFANLSNGFSLKSPINPGFLFKSRPFTVQARAAAEKTVH 80
Cdd:PLN02399 1 MVSLTTSSSSYASFKTVFNSSPPPPSMAFLVPSLKSSTGISKSAFLSNGFSLKSPNSPGFLSKSRSFGVYARAATEKSVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 81 DFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSEIKQFACT 160
Cdd:PLN02399 81 DFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQFACT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17104619 161 RFKAEFPIFDKVDVNGPSTAPIYEFLKSNAGGFLGGLIKWNFEKFLIDKKGKVVERYPPTTSPFQIEKDIQKLLAA 236
Cdd:PLN02399 161 RFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLLAA 236
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
78-230 |
3.31e-90 |
|
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: 262.45 E-value: 3.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 78 TVHDFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSEIKQF 157
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17104619 158 ACTRFKAEFPIFDKVDVNGPSTAPIYEFLKSNAGGFLGGLIKWNFEKFLIDKKGKVVERYPPTTSPFQIEKDI 230
Cdd:cd00340 80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
78-234 |
2.73e-86 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 252.69 E-value: 2.73e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 78 TVHDFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSEIKQF 157
Cdd:COG0386 3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 158 ACTRFKAEFPIFDKVDVNGPSTAPIYEFLKSNAGGFLG-GLIKWNFEKFLIDKKGKVVERYPPTTSP--FQIEKDIQKLL 234
Cdd:COG0386 82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGgGDIKWNFTKFLIDRDGNVVARFAPTTKPedPELEAAIEKLL 161
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
79-187 |
9.46e-47 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 150.58 E-value: 9.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 79 VHDFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSEIKQFA 158
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
|
90 100
....*....|....*....|....*....
gi 17104619 159 CTRFKAEFPIFDKVDVNGPSTAPIYEFLK 187
Cdd:pfam00255 80 PGGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
80-234 |
2.95e-45 |
|
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: 148.45 E-value: 2.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 80 HDFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSEIKQFAC 159
Cdd:TIGR02540 3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17104619 160 TRFKAEFPIFDKVDVNGPSTAPIYEFLKSNAggflGGLIKWNFEKFLIDKKGKVVERYPPTTSPFQIEKDIQKLL 234
Cdd:TIGR02540 83 RNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
1-236 |
6.33e-155 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 429.32 E-value: 6.33e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 1 MVSMTTSSSSYGTFSTVVNSSRPNSSATFLVPSLKFSTGISNFANLSNGFSLKSPINPGFLFKSRPFTVQARAAAEKTVH 80
Cdd:PLN02399 1 MVSLTTSSSSYASFKTVFNSSPPPPSMAFLVPSLKSSTGISKSAFLSNGFSLKSPNSPGFLSKSRSFGVYARAATEKSVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 81 DFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSEIKQFACT 160
Cdd:PLN02399 81 DFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQFACT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17104619 161 RFKAEFPIFDKVDVNGPSTAPIYEFLKSNAGGFLGGLIKWNFEKFLIDKKGKVVERYPPTTSPFQIEKDIQKLLAA 236
Cdd:PLN02399 161 RFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLLAA 236
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
74-236 |
2.50e-92 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 268.40 E-value: 2.50e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 74 AAEKTVHDFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSE 153
Cdd:PLN02412 4 ESPKSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 154 IKQFACTRFKAEFPIFDKVDVNGPSTAPIYEFLKSNAGGFLGGLIKWNFEKFLIDKKGKVVERYPPTTSPFQIEKDIQKL 233
Cdd:PLN02412 84 IQQTVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNL 163
|
...
gi 17104619 234 LAA 236
Cdd:PLN02412 164 LGQ 166
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
78-230 |
3.31e-90 |
|
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: 262.45 E-value: 3.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 78 TVHDFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSEIKQF 157
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17104619 158 ACTRFKAEFPIFDKVDVNGPSTAPIYEFLKSNAGGFLGGLIKWNFEKFLIDKKGKVVERYPPTTSPFQIEKDI 230
Cdd:cd00340 80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
78-234 |
2.73e-86 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 252.69 E-value: 2.73e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 78 TVHDFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSEIKQF 157
Cdd:COG0386 3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 158 ACTRFKAEFPIFDKVDVNGPSTAPIYEFLKSNAGGFLG-GLIKWNFEKFLIDKKGKVVERYPPTTSP--FQIEKDIQKLL 234
Cdd:COG0386 82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGgGDIKWNFTKFLIDRDGNVVARFAPTTKPedPELEAAIEKLL 161
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
75-236 |
3.96e-65 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 199.99 E-value: 3.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 75 AEKTVHDFTVKDIDGKDVALNKFKG-KVMLIVNVASRCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSE 153
Cdd:PTZ00256 16 PTKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 154 IKQFACTRFKAEFPIFDKVDVNGPSTAPIYEFLKSNAGGFLGGL-----IKWNFEKFLIDKKGKVVERYPPTTSPFQIEK 228
Cdd:PTZ00256 96 IKEYVQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNNTnearqIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQ 175
|
....*...
gi 17104619 229 DIQKLLAA 236
Cdd:PTZ00256 176 DIEKLLNA 183
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
78-223 |
4.60e-52 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 166.87 E-value: 4.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 78 TVHDFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSEIKQF 157
Cdd:PRK10606 4 SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTP-QYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 158 ACTRFKAEFPIFDKVDVNGPSTAPIYEFL--------KSNAGGFLGGL------------IKWNFEKFLIDKKGKVVERY 217
Cdd:PRK10606 83 CRTTWGVTFPMFSKIEVNGEGRHPLYQKLiaaaptavAPEESGFYARMvskgraplypddILWNFEKFLVGRDGQVIQRF 162
|
....*.
gi 17104619 218 PPTTSP 223
Cdd:PRK10606 163 SPDMTP 168
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
79-187 |
9.46e-47 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 150.58 E-value: 9.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 79 VHDFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSEIKQFA 158
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
|
90 100
....*....|....*....|....*....
gi 17104619 159 CTRFKAEFPIFDKVDVNGPSTAPIYEFLK 187
Cdd:pfam00255 80 PGGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
80-234 |
2.95e-45 |
|
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: 148.45 E-value: 2.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 80 HDFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSEIKQFAC 159
Cdd:TIGR02540 3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17104619 160 TRFKAEFPIFDKVDVNGPSTAPIYEFLKSNAggflGGLIKWNFEKFLIDKKGKVVERYPPTTSPFQIEKDIQKLL 234
Cdd:TIGR02540 83 RNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| PTZ00056 |
PTZ00056 |
glutathione peroxidase; Provisional |
75-234 |
1.57e-44 |
|
glutathione peroxidase; Provisional
Pssm-ID: 240248 [Multi-domain] Cd Length: 199 Bit Score: 148.08 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 75 AEKTVHDFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGFQEPGSNSEI 154
Cdd:PTZ00056 15 LRKSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 155 KQFAcTRFKAEFPIFDKVDVNGPSTAPIYEFLKSNA------GGFLGGlIKWNFEKFLIDKKGKVVERYPPTTSPFQIEK 228
Cdd:PTZ00056 95 RKFN-DKNKIKYNFFEPIEVNGENTHELFKFLKANCdsmhdeNGTLKA-IGWNFGKFLVNKSGNVVAYFSPRTEPLELEK 172
|
....*.
gi 17104619 229 DIQKLL 234
Cdd:PTZ00056 173 KIAELL 178
|
|
| Bcp |
COG1225 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
81-236 |
1.54e-09 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 54.49 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 81 DFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSSNYSELSHLYEKYKTQGFEILAFpcnqfgfqEPGSNSEIKQFAcT 160
Cdd:COG1225 3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGV--------SSDSDEAHKKFA-E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 161 RFKAEFPIFdkVDVNG-----------PSTapiyeflksnaggflgglikwnfekFLIDKKGKVVERYpptTSPFQIEKD 229
Cdd:COG1225 74 KYGLPFPLL--SDPDGevakaygvrgtPTT-------------------------FLIDPDGKIRYVW---VGPVDPRPH 123
|
....*..
gi 17104619 230 IQKLLAA 236
Cdd:COG1225 124 LEEVLEA 130
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
74-236 |
2.82e-08 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 51.23 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 74 AAEKTVHDFTVKDIDGKDVALNKFKGKVMLiVNV-ASRCGLTSSNYSELSHLYEKYKtqGFEILAFPCNQfgfqepgSNS 152
Cdd:COG0526 3 AVGKPAPDFTLTDLDGKPLSLADLKGKPVL-VNFwATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVDE-------NPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 153 EIKQFAcTRFKAEFPIF--------DKVDVNG-PSTapiyeflksnaggflgglikwnfekFLIDKKGKVVERYPPTTSP 223
Cdd:COG0526 73 AVKAFL-KELGLPYPVLldpdgelaKAYGVRGiPTT-------------------------VLIDKDGKIVARHVGPLSP 126
|
170
....*....|...
gi 17104619 224 FQIEKDIQKLLAA 236
Cdd:COG0526 127 EELEEALEKLLAK 139
|
|
| TlpA_like_family |
cd02966 |
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
81-217 |
4.30e-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: 49.93 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 81 DFTVKDIDGKDVALNKFKGKVMLiVNV-ASRCGLTSSNYSELSHLYEKYKTQGFEILAFpcNqfgfQEPGSNSEIKQFAc 159
Cdd:cd02966 1 DFSLPDLDGKPVSLSDLKGKVVL-VNFwASWCPPCRAEMPELEALAKEYKDDGVEVVGV--N----VDDDDPAAVKAFL- 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 17104619 160 TRFKAEFPIFdkVDVNGpSTAPIYeflksnaggflgGLIKWnFEKFLIDKKGKVVERY 217
Cdd:cd02966 73 KKYGITFPVL--LDPDG-ELAKAY------------GVRGL-PTTFLIDRDGRIRARH 114
|
|
| PRK03147 |
PRK03147 |
thiol-disulfide oxidoreductase ResA; |
59-215 |
3.45e-07 |
|
thiol-disulfide oxidoreductase ResA;
Pssm-ID: 179545 [Multi-domain] Cd Length: 173 Bit Score: 48.85 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 59 GFLFKSRPFTVQARAAAEKTVHDFTVKDIDGKDVALNKFKGKVMLIVNVASRCGLTSSNYSELSHLYEKYKTQGFEILAF 138
Cdd:PRK03147 21 GYTIYSNFFADKEKVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 139 PCNqfgfqepGSNSEIKQFAcTRFKAEFPI-FDK----VDVNGPSTAPIyeflksnaggflgglikwnfeKFLIDKKGKV 213
Cdd:PRK03147 101 NVD-------ETELAVKNFV-NRYGLTFPVaIDKgrqvIDAYGVGPLPT---------------------TFLIDKDGKV 151
|
..
gi 17104619 214 VE 215
Cdd:PRK03147 152 VK 153
|
|
| Sco1 |
COG1999 |
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ... |
83-236 |
1.68e-06 |
|
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441602 Cd Length: 156 Bit Score: 46.43 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 83 TVKDIDGKDVALNKFKGKVMLIVNVASRCG----LTSSNYSELSHLYEKYKTQGFEILAF---PCN-------QFG--FQ 146
Cdd:COG1999 4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPdvcpTTLANLAQVQEALGEDGGDDVQVLFIsvdPERdtpevlkAYAeaFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 147 EP------GSNSEIKQFAcTRFKAefpIFDKVDVNGpstapiYEFLKSNaggflgglikwNFekFLIDKKGKVVERYPPT 220
Cdd:COG1999 84 APrwigltGDPEEIAALA-KAFGV---YYEKVPDGD------YTFDHSA-----------AV--YLVDPDGRLRGYYPAG 140
|
170
....*....|....*.
gi 17104619 221 TSPFQIEKDIQKLLAA 236
Cdd:COG1999 141 EDPEELAADLKALLEE 156
|
|
| AhpC-TSA |
pfam00578 |
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
81-216 |
3.91e-05 |
|
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: 41.83 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 81 DFTVKDIDGKDVALNKFKGKVMLIVNVASR-CGLTSSNYSELSHLYEKYKTQGFEILAFPCNqfgfqepgSNSEIKQFAc 159
Cdd:pfam00578 7 DFELPDGDGGTVSLSDYRGKWVVLFFYPADwTPVCTTELPALADLYEEFKKLGVEVLGVSVD--------SPESHKAFA- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 17104619 160 TRFKAEFPIFdkVDVNGpSTAPIYEFLKSNAGGFLGGLikwnfekFLIDKKGKVVER 216
Cdd:pfam00578 78 EKYGLPFPLL--SDPDG-EVARAYGVLNEEEGGALRAT-------FVIDPDGKVRYI 124
|
|
| Redoxin |
pfam08534 |
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
74-217 |
4.55e-05 |
|
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 42.36 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17104619 74 AAEKTVHDFTVKDI--DGKDVALNKFKGKVMLIVNVASR-CGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGFqepgs 150
Cdd:pfam08534 1 KAGDKAPDFTLPDAatDGNTVSLSDFKGKKVVLNFWPGAfCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAF----- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17104619 151 nsEIKQFaCTRFKAEFPIFdkVDVNGpstapiyEFLKSnaggfLGGLIKWNFEK-------FLIDKKGKVVERY 217
Cdd:pfam08534 76 --FVKRF-WGKEGLPFPFL--SDGNA-------AFTKA-----LGLPIEEDASAglrspryAVIDEDGKVVYLF 132
|
|
| |
