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Conserved domains on  [gi|504696391|ref|WP_014883493|]
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MULTISPECIES: glutathione peroxidase [Enterobacter]

Protein Classification

glutathione peroxidase( domain architecture ID 10793426)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
btuE PRK10606
putative glutathione peroxidase; Provisional
 1-183 7.25e-147

putative glutathione peroxidase; Provisional


:

Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 404.54  E-value: 7.25e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   1 MQTDILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLTPQYEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIK 80
Cdd:PRK10606   1 MQDSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  81 TFCSTTYGVTFPMFSKIDVNGEDRHPLYAKLIAAAPKAVAPEGSGFYERMASKGRAPLYPDDILWNFEKFLIGRDGQVVQ 160
Cdd:PRK10606  81 TYCRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTAVAPEESGFYARMVSKGRAPLYPDDILWNFEKFLVGRDGQVIQ 160

                        170       180
                 ....*....|....*....|...
gi 504696391 161 RFSPDMTPEDPIVMESIKLALAK 183
Cdd:PRK10606 161 RFSPDMTPEDPIVMESIKLALAK 183
 
Name Accession Description Interval E-value
btuE PRK10606
putative glutathione peroxidase; Provisional
 1-183 7.25e-147

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 404.54  E-value: 7.25e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   1 MQTDILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLTPQYEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIK 80
Cdd:PRK10606   1 MQDSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  81 TFCSTTYGVTFPMFSKIDVNGEDRHPLYAKLIAAAPKAVAPEGSGFYERMASKGRAPLYPDDILWNFEKFLIGRDGQVVQ 160
Cdd:PRK10606  81 TYCRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTAVAPEESGFYARMVSKGRAPLYPDDILWNFEKFLVGRDGQVIQ 160

                        170       180
                 ....*....|....*....|...
gi 504696391 161 RFSPDMTPEDPIVMESIKLALAK 183
Cdd:PRK10606 161 RFSPDMTPEDPIVMESIKLALAK 183
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 3-181 1.41e-99

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 284.28  E-value: 1.41e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   3 TDILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLTPQYEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIKTF 82
Cdd:COG0386    2 MSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  83 CSTTYGVTFPMFSKIDVNGEDRHPLYAKLIAAAPkavapegsgfyermaskgrAPLYPDDILWNFEKFLIGRDGQVVQRF 162
Cdd:COG0386   82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAP-------------------GLLGGGDIKWNFTKFLIDRDGNVVARF 142

                        170
                 ....*....|....*....
gi 504696391 163 SPDMTPEDPIVMESIKLAL 181
Cdd:COG0386  143 APTTKPEDPELEAAIEKLL 161
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 4-170 7.60e-89

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: 256.67  E-value: 7.60e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   4 DILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLTPQYEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIKTFC 83
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  84 STTYGVTFPMFSKIDVNGEDRHPLYAKLIAAAPKavapegsgfyermaskgrapLYPDDILWNFEKFLIGRDGQVVQRFS 163
Cdd:cd00340   81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPG--------------------LLGKDIKWNFTKFLVDRDGEVVKRFA 140


                 ....*..
gi 504696391 164 PDMTPED 170
Cdd:cd00340  141 PTTDPEE 147
GSHPx pfam00255
Glutathione peroxidase;
5-112 5.69e-61

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 184.48  E-value: 5.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391    5 ILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLTPQYEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIKTFCS 84
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80

                          90       100
                  ....*....|....*....|....*...
gi 504696391   85 TTYGVTFPMFSKIDVNGEDRHPLYAKLI 112
Cdd:pfam00255  81 GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 4-170 2.39e-41

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: 136.50  E-value: 2.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391    4 DILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLTPQ-YEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIKTF 82
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   83 CSTTYGVTFPMFSKIDVNGEDRHPLYAKLIaaapkavapegsgfyermASKGRAPlypddiLWNFEKFLIGRDGQVVQRF 162
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLV------------------DSSKKEP------RWNFWKYLVNPEGQVVKFW 136


                  ....*...
gi 504696391  163 SPDMTPED 170
Cdd:TIGR02540 137 RPEEPVEE 144
 
Name Accession Description Interval E-value
btuE PRK10606
putative glutathione peroxidase; Provisional
 1-183 7.25e-147

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 404.54  E-value: 7.25e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   1 MQTDILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLTPQYEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIK 80
Cdd:PRK10606   1 MQDSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  81 TFCSTTYGVTFPMFSKIDVNGEDRHPLYAKLIAAAPKAVAPEGSGFYERMASKGRAPLYPDDILWNFEKFLIGRDGQVVQ 160
Cdd:PRK10606  81 TYCRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTAVAPEESGFYARMVSKGRAPLYPDDILWNFEKFLVGRDGQVIQ 160

                        170       180
                 ....*....|....*....|...
gi 504696391 161 RFSPDMTPEDPIVMESIKLALAK 183
Cdd:PRK10606 161 RFSPDMTPEDPIVMESIKLALAK 183
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 3-181 1.41e-99

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 284.28  E-value: 1.41e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   3 TDILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLTPQYEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIKTF 82
Cdd:COG0386    2 MSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  83 CSTTYGVTFPMFSKIDVNGEDRHPLYAKLIAAAPkavapegsgfyermaskgrAPLYPDDILWNFEKFLIGRDGQVVQRF 162
Cdd:COG0386   82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAP-------------------GLLGGGDIKWNFTKFLIDRDGNVVARF 142

                        170
                 ....*....|....*....
gi 504696391 163 SPDMTPEDPIVMESIKLAL 181
Cdd:COG0386  143 APTTKPEDPELEAAIEKLL 161
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 4-170 7.60e-89

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: 256.67  E-value: 7.60e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   4 DILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLTPQYEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIKTFC 83
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  84 STTYGVTFPMFSKIDVNGEDRHPLYAKLIAAAPKavapegsgfyermaskgrapLYPDDILWNFEKFLIGRDGQVVQRFS 163
Cdd:cd00340   81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPG--------------------LLGKDIKWNFTKFLVDRDGEVVKRFA 140


                 ....*..
gi 504696391 164 PDMTPED 170
Cdd:cd00340  141 PTTDPEE 147
GSHPx pfam00255
Glutathione peroxidase;
5-112 5.69e-61

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 184.48  E-value: 5.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391    5 ILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLTPQYEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIKTFCS 84
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80

                          90       100
                  ....*....|....*....|....*...
gi 504696391   85 TTYGVTFPMFSKIDVNGEDRHPLYAKLI 112
Cdd:pfam00255  81 GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 2-172 1.46e-50

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 160.69  E-value: 1.46e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   2 QTDILNTEVTTIDGEKTTLESYKG-NVLLIVNVASKCGLTPQ-YEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEI 79
Cdd:PTZ00256  17 TKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  80 KTFCSTTYGVTFPMFSKIDVNGEDRHPLYAKLIAAAPKAVAPEGSGFYermaskgraplypddILWNFEKFLIGRDGQVV 159
Cdd:PTZ00256  97 KEYVQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNNTNEARQ---------------IPWNFAKFLIDGQGKVV 161

                        170
                 ....*....|...
gi 504696391 160 QRFSPDMTPEDPI 172
Cdd:PTZ00256 162 KYFSPKVNPNEMI 174
PLN02412 PLN02412
probable glutathione peroxidase
 5-168 2.18e-45

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 147.06  E-value: 2.18e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   5 ILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLT-PQYEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIKTFC 83
Cdd:PLN02412   9 IYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQTV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  84 STTYGVTFPMFSKIDVNGEDRHPLYAKLiaaapkavapegsgfyerMASKGraPLYPDDILWNFEKFLIGRDGQVVQRFS 163
Cdd:PLN02412  89 CTRFKAEFPIFDKVDVNGKNTAPLYKYL------------------KAEKG--GLFGDAIKWNFTKFLVSKEGKVVQRYA 148


                 ....*
gi 504696391 164 PDMTP 168
Cdd:PLN02412 149 PTTSP 153
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 10-168 2.84e-44

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 146.58  E-value: 2.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  10 VTTIDGEKTTLESYKGNVLLIVNVASKCGLTP-QYEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIKTFCSTTYG 88
Cdd:PLN02399  84 VKDIDGKDVALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQFACTRFK 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  89 VTFPMFSKIDVNGEDRHPLYAKLIAAApkavapegSGFYErmaskgraplypDDILWNFEKFLIGRDGQVVQRFSPDMTP 168
Cdd:PLN02399 164 AEFPIFDKVDVNGPSTAPVYQFLKSNA--------GGFLG------------DLIKWNFEKFLVDKNGKVVERYPPTTSP 223
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 4-170 2.39e-41

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: 136.50  E-value: 2.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391    4 DILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLTPQ-YEQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIKTF 82
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   83 CSTTYGVTFPMFSKIDVNGEDRHPLYAKLIaaapkavapegsgfyermASKGRAPlypddiLWNFEKFLIGRDGQVVQRF 162
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLV------------------DSSKKEP------RWNFWKYLVNPEGQVVKFW 136


                  ....*...
gi 504696391  163 SPDMTPED 170
Cdd:TIGR02540 137 RPEEPVEE 144
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 5-175 5.32e-36

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 124.19  E-value: 5.32e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   5 ILNTEVTTIDGEKTTLESYKGNVLLIVNVASKCGLTPQY-EQLENIQKAWEKDGFTVLGFPCNQFLGQEPGSEEEIKTFc 83
Cdd:PTZ00056  19 IYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHvDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRKF- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  84 STTYGVTFPMFSKIDVNGEDRHPLYAKLiaaapKAVAPEgsgFYERmasKGRAplypDDILWNFEKFLIGRDGQVVQRFS 163
Cdd:PTZ00056  98 NDKNKIKYNFFEPIEVNGENTHELFKFL-----KANCDS---MHDE---NGTL----KAIGWNFGKFLVNKSGNVVAYFS 162

                        170
                 ....*....|....
gi 504696391 164 PDMTPED--PIVME 175
Cdd:PTZ00056 163 PRTEPLEleKKIAE 176
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
9-183 7.86e-07

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 46.40  E-value: 7.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   9 EVTTIDGEKTTLESYKGNVLLIVNVASKCGL-TPQYEQLENIQKAWEKDGFTVLGFpcnqflgqEPGSEEEIKTFCStTY 87
Cdd:COG1225    5 TLPDLDGKTVSLSDLRGKPVVLYFYATWCPGcTAELPELRDLYEEFKDKGVEVLGV--------SSDSDEAHKKFAE-KY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391  88 GVTFPMFSkiDVNGEdrhplyakliaaapkavapegsgfyerMASKGRAPLYPDDilwnfekFLIGRDGQVVQRFSPDMT 167
Cdd:COG1225   76 GLPFPLLS--DPDGE---------------------------VAKAYGVRGTPTT-------FLIDPDGKIRYVWVGPVD 119

                        170
                 ....*....|....*.
gi 504696391 168 PeDPIVMESIKLALAK 183
Cdd:COG1225  120 P-RPHLEEVLEALLAE 134
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 9-102 9.92e-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: 39.91  E-value: 9.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391   9 EVTTIDGEKTTLESYKGNVLLiVNV-ASKCGltP-QYE--QLENIQKAWEKDGFTVLGfpcnqfLGQEPGSEEEIKTFcS 84
Cdd:cd02966    3 SLPDLDGKPVSLSDLKGKVVL-VNFwASWCP--PcRAEmpELEALAKEYKDDGVEVVG------VNVDDDDPAAVKAF-L 72

                         90
                 ....*....|....*...
gi 504696391  85 TTYGVTFPMFskIDVNGE 102
Cdd:cd02966   73 KKYGITFPVL--LDPDGE 88
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 9-102 6.66e-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: 37.97  E-value: 6.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696391    9 EVTTIDGEKTTLESYKGNVLLIVNVASK----CglTPQYEQLENIQKAWEKDGFTVLGFPCNqflgqepgSEEEIKTFCs 84
Cdd:pfam00578   9 ELPDGDGGTVSLSDYRGKWVVLFFYPADwtpvC--TTELPALADLYEEFKKLGVEVLGVSVD--------SPESHKAFA- 77

                          90
                  ....*....|....*...
gi 504696391   85 TTYGVTFPMFSkiDVNGE 102
Cdd:pfam00578  78 EKYGLPFPLLS--DPDGE 93
 
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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