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Conserved domains on  [gi|1379540456|gb|PUE70029|]
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glutathione peroxidase [Xanthomonas vasicola pv. vasculorum]

Protein Classification

glutathione peroxidase( domain architecture ID 10785352)

glutathione peroxidase catalyzes the reduction of hydroperoxides using GSH as a specific electron donor

CATH:  3.40.30.10
EC:  1.11.1.-
Gene Ontology:  GO:0043295|GO:0004602
PubMed:  11215509
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 4-172 2.18e-98

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


:

Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 281.20  E-value: 2.18e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   4 TLYDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTPQYEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIAQFC 83
Cdd:COG0386     3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEFC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  84 QLTYDVTFPMFAKIPVTGDQAHPLYQTLTSTHPHTTGDGPmreklagygiapnpapgILWNFEKFLIGRDGKIIDRFAPD 163
Cdd:COG0386    83 SLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGD-----------------IKWNFTKFLIDRDGNVVARFAPT 145


                  ....*....
gi 1379540456 164 IPADDARLR 172
Cdd:COG0386   146 TKPEDPELE 154
 
Name Accession Description Interval E-value
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 4-172 2.18e-98

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 281.20  E-value: 2.18e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   4 TLYDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTPQYEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIAQFC 83
Cdd:COG0386     3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEFC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  84 QLTYDVTFPMFAKIPVTGDQAHPLYQTLTSTHPHTTGDGPmreklagygiapnpapgILWNFEKFLIGRDGKIIDRFAPD 163
Cdd:COG0386    83 SLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGD-----------------IKWNFTKFLIDRDGNVVARFAPT 145


                  ....*....
gi 1379540456 164 IPADDARLR 172
Cdd:COG0386   146 TKPEDPELE 154
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 4-168 2.50e-84

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: 245.12  E-value: 2.50e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   4 TLYDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTPQYEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIAQFC 83
Cdd:cd00340     1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  84 QLTYDVTFPMFAKIPVTGDQAHPLYQTLTSTHPhttgdgpmreklagygiaPNPAPGILWNFEKFLIGRDGKIIDRFAPD 163
Cdd:cd00340    81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAP------------------GLLGKDIKWNFTKFLVDRDGEVVKRFAPT 142


                  ....*
gi 1379540456 164 IPADD 168
Cdd:cd00340   143 TDPEE 147
btuE PRK10606
putative glutathione peroxidase; Provisional
 1-168 7.83e-79

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 232.36  E-value: 7.83e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   1 MSQTLYDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTPQYEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIA 80
Cdd:PRK10606    1 MQDSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  81 QFCQLTYDVTFPMFAKIPVTGDQAHPLYQTLTSTHPH--TTGDGPMREKLAGYGIAPNPAPGILWNFEKFLIGRDGKIID 158
Cdd:PRK10606   81 TYCRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTavAPEESGFYARMVSKGRAPLYPDDILWNFEKFLVGRDGQVIQ 160

                         170
                  ....*....|
gi 1379540456 159 RFAPDIPADD 168
Cdd:PRK10606  161 RFSPDMTPED 170
GSHPx pfam00255
Glutathione peroxidase;
5-111 3.35e-47

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 149.81  E-value: 3.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   5 LYDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTPQYEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIAQFCQ 84
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80

                          90       100
                  ....*....|....*....|....*..
gi 1379540456  85 LTYDVTFPMFAKIPVTGDQAHPLYQTL 111
Cdd:pfam00255  81 GGYGVTFPLFSKIEVNGEKAHPVYKFL 107
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 6-170 1.66e-42

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: 139.20  E-value: 1.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   6 YDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTPQ-YEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIAQFCQ 84
Cdd:TIGR02540   3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  85 LTYDVTFPMFAKIPVTGDQAHPLYQTLTSthphTTGDGPMreklagygiapnpapgilWNFEKFLIGRDGKIIDRFAPDI 164
Cdd:TIGR02540  83 RNYGVTFPMFSKIKILGSEAEPAFRFLVD----SSKKEPR------------------WNFWKYLVNPEGQVVKFWRPEE 140


                  ....*.
gi 1379540456 165 PADDAR 170
Cdd:TIGR02540 141 PVEEIR 146
 
Name Accession Description Interval E-value
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 4-172 2.18e-98

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 281.20  E-value: 2.18e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   4 TLYDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTPQYEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIAQFC 83
Cdd:COG0386     3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEFC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  84 QLTYDVTFPMFAKIPVTGDQAHPLYQTLTSTHPHTTGDGPmreklagygiapnpapgILWNFEKFLIGRDGKIIDRFAPD 163
Cdd:COG0386    83 SLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGD-----------------IKWNFTKFLIDRDGNVVARFAPT 145


                  ....*....
gi 1379540456 164 IPADDARLR 172
Cdd:COG0386   146 TKPEDPELE 154
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 4-168 2.50e-84

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: 245.12  E-value: 2.50e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   4 TLYDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTPQYEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIAQFC 83
Cdd:cd00340     1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  84 QLTYDVTFPMFAKIPVTGDQAHPLYQTLTSTHPhttgdgpmreklagygiaPNPAPGILWNFEKFLIGRDGKIIDRFAPD 163
Cdd:cd00340    81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAP------------------GLLGKDIKWNFTKFLVDRDGEVVKRFAPT 142


                  ....*
gi 1379540456 164 IPADD 168
Cdd:cd00340   143 TDPEE 147
btuE PRK10606
putative glutathione peroxidase; Provisional
 1-168 7.83e-79

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 232.36  E-value: 7.83e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   1 MSQTLYDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTPQYEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIA 80
Cdd:PRK10606    1 MQDSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  81 QFCQLTYDVTFPMFAKIPVTGDQAHPLYQTLTSTHPH--TTGDGPMREKLAGYGIAPNPAPGILWNFEKFLIGRDGKIID 158
Cdd:PRK10606   81 TYCRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTavAPEESGFYARMVSKGRAPLYPDDILWNFEKFLVGRDGQVIQ 160

                         170
                  ....*....|
gi 1379540456 159 RFAPDIPADD 168
Cdd:PRK10606  161 RFSPDMTPED 170
GSHPx pfam00255
Glutathione peroxidase;
5-111 3.35e-47

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 149.81  E-value: 3.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   5 LYDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTPQYEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIAQFCQ 84
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80

                          90       100
                  ....*....|....*....|....*..
gi 1379540456  85 LTYDVTFPMFAKIPVTGDQAHPLYQTL 111
Cdd:pfam00255  81 GGYGVTFPLFSKIEVNGEKAHPVYKFL 107
PLN02412 PLN02412
probable glutathione peroxidase
 2-162 3.35e-45

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 146.67  E-value: 3.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   2 SQTLYDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLT-PQYEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIA 80
Cdd:PLN02412    6 PKSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  81 QFCQLTYDVTFPMFAKIPVTGDQAHPLYQTLTSTHPHTTGDgpmreklagygiapnpapGILWNFEKFLIGRDGKIIDRF 160
Cdd:PLN02412   86 QTVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGD------------------AIKWNFTKFLVSKEGKVVQRY 147


                  ..
gi 1379540456 161 AP 162
Cdd:PLN02412  148 AP 149
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 2-164 8.70e-44

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 143.36  E-value: 8.70e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   2 SQTLYDIPVTHIEGEPATLADYRG-KVLLVVNVASKCGLTPQ-YEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEI 79
Cdd:PTZ00256   17 TKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  80 AQFCQLTYDVTFPMFAKIPVTGDQAHPLYQTLtsthphttgdgpmREKLAGYGIAPNPAPGILWNFEKFLIGRDGKIIDR 159
Cdd:PTZ00256   97 KEYVQKKFNVDFPLFQKIEVNGENTHEIYKYL-------------RRNSELFQNNTNEARQIPWNFAKFLIDGQGKVVKY 163


                  ....*
gi 1379540456 160 FAPDI 164
Cdd:PTZ00256  164 FSPKV 168
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 3-162 7.41e-43

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 142.73  E-value: 7.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   3 QTLYDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTP-QYEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIAQ 81
Cdd:PLN02399   77 KSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQ 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  82 FCQLTYDVTFPMFAKIPVTGDQAHPLYQTLTSTHPHTTGDgpmreklagygiapnpapGILWNFEKFLIGRDGKIIDRFA 161
Cdd:PLN02399  157 FACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGD------------------LIKWNFEKFLVDKNGKVVERYP 218


                  .
gi 1379540456 162 P 162
Cdd:PLN02399  219 P 219
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 6-170 1.66e-42

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: 139.20  E-value: 1.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   6 YDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTPQ-YEGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEIAQFCQ 84
Cdd:TIGR02540   3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  85 LTYDVTFPMFAKIPVTGDQAHPLYQTLTSthphTTGDGPMreklagygiapnpapgilWNFEKFLIGRDGKIIDRFAPDI 164
Cdd:TIGR02540  83 RNYGVTFPMFSKIKILGSEAEPAFRFLVD----SSKKEPR------------------WNFWKYLVNPEGQVVKFWRPEE 140


                  ....*.
gi 1379540456 165 PADDAR 170
Cdd:TIGR02540 141 PVEEIR 146
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 1-162 7.35e-32

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 113.41  E-value: 7.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   1 MSQTLYDIPVTHIEGEPATLADYRGKVLLVVNVASKCGLTPQY-EGLEALYRDKRAQGLEVLAFPANDFNGQEPGSEAEI 79
Cdd:PTZ00056   15 LRKSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHvDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  80 AQFCQlTYDVTFPMFAKIPVTGDQAHPLYQTLTSTHPHttgdgpMREKlagygiaPNPAPGILWNFEKFLIGRDGKIIDR 159
Cdd:PTZ00056   95 RKFND-KNKIKYNFFEPIEVNGENTHELFKFLKANCDS------MHDE-------NGTLKAIGWNFGKFLVNKSGNVVAY 160


                  ...
gi 1379540456 160 FAP 162
Cdd:PTZ00056  161 FSP 163
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
13-168 1.61e-07

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 47.94  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  13 IEGEPATLADYRGKVLLVVNVASKCGL-TPQYEGLEALYRDKRAQGLEVLAFPANDfngqepgsEAEIAQFCQlTYDVTF 91
Cdd:COG1225     9 LDGKTVSLSDLRGKPVVLYFYATWCPGcTAELPELRDLYEEFKDKGVEVLGVSSDS--------DEAHKKFAE-KYGLPF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1379540456  92 PMFAkipvtgDQAHPLYQTltsthphttgdgpmreklagYGIAPNPApgilwnfeKFLIGRDGKIIDRFAPDIPADD 168
Cdd:COG1225    80 PLLS------DPDGEVAKA--------------------YGVRGTPT--------TFLIDPDGKIRYVWVGPVDPRP 122
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 3-170 7.90e-06

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 43.53  E-value: 7.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   3 QTLYDIPVTHIEGEPATLADYRGKVLLvVNV-ASKCG----LTPQyegLEALYrdKRAQGLEVLAFPANDfngqepgSEA 77
Cdd:COG0526     6 KPAPDFTLTDLDGKPLSLADLKGKPVL-VNFwATWCPpcraEMPV---LKELA--EEYGGVVFVGVDVDE-------NPE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  78 EIAQFCQlTYDVTFPMFAKipvtgdqahplyqtltsthphttGDGPMREKLAGYGIaPnpapgilwnfEKFLIGRDGKII 157
Cdd:COG0526    73 AVKAFLK-ELGLPYPVLLD-----------------------PDGELAKAYGVRGI-P----------TTVLIDKDGKIV 117

                         170
                  ....*....|...
gi 1379540456 158 DRFAPDIPADDAR 170
Cdd:COG0526   118 ARHVGPLSPEELE 130
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 7-94 4.34e-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: 41.07  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456   7 DIPVTHIEGEPATLADYRGKVlLVVNV-ASKCGltP-QYE--GLEALYRDKRAQGLEVLAFPANDFNgqepgsEAEIAQF 82
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKV-VLVNFwASWCP--PcRAEmpELEALAKEYKDDGVEVVGVNVDDDD------PAAVKAF 71

                          90
                  ....*....|..
gi 1379540456  83 CQlTYDVTFPMF 94
Cdd:cd02966    72 LK-KYGITFPVL 82
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 14-95 8.34e-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: 37.59  E-value: 8.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  14 EGEPATLADYRGKVLLVVNVASK----CglTPQYEGLEALYRDKRAQGLEVLAFPANdfngqepgSEAEIAQFCQlTYDV 89
Cdd:pfam00578  14 DGGTVSLSDYRGKWVVLFFYPADwtpvC--TTELPALADLYEEFKKLGVEVLGVSVD--------SPESHKAFAE-KYGL 82


                  ....*.
gi 1379540456  90 TFPMFA 95
Cdd:pfam00578  83 PFPLLS 88
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
10-158 4.31e-03

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 36.13  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540456  10 VTHIEGEPATLADYRGKVLLVVNVASKCGLT----PQYEGLEALYRDkraQGLEVLAFPANdfngqepgsEAEIA--QFC 83
Cdd:PRK03147   46 LTDLEGKKIELKDLKGKGVFLNFWGTWCKPCekemPYMNELYPKYKE---KGVEIIAVNVD---------ETELAvkNFV 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1379540456  84 QlTYDVTFPMfakipvtgdqahplyqtltsthPHTTGdgpmREKLAGYGIAPNPApgilwnfeKFLIGRDGKIID 158
Cdd:PRK03147  114 N-RYGLTFPV----------------------AIDKG----RQVIDAYGVGPLPT--------TFLIDKDGKVVK 153
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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