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Conserved domains on  [gi|193209493|ref|NP_509615|]
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Glutathione peroxidase [Caenorhabditis elegans]

Protein Classification

glutathione peroxidase( domain architecture ID 10085912)

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|GO:0006979
PubMed:  11215509|23201771|10049365|15558583
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 39-203 9.08e-60

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: 184.64  E-value: 9.08e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493  39 SIYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQQYTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHELMNGI 118
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493 119 MYVRPgngwkphQNLHIYGKLDTNGDNQHPIYEFVKESCPQTVdkigktdelmynpirASDITWNFEKFLIDRNGQPRFR 198
Cdd:cd00340   81 ETNYG-------VTFPMFAKIDVNGENAHPLYKYLKEEAPGLL---------------GKDIKWNFTKFLVDRDGEVVKR 138


                 ....*
gi 193209493 199 FHPTA 203
Cdd:cd00340  139 FAPTT 143
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 39-203 9.08e-60

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: 184.64  E-value: 9.08e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493  39 SIYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQQYTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHELMNGI 118
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493 119 MYVRPgngwkphQNLHIYGKLDTNGDNQHPIYEFVKESCPQTVdkigktdelmynpirASDITWNFEKFLIDRNGQPRFR 198
Cdd:cd00340   81 ETNYG-------VTFPMFAKIDVNGENAHPLYKYLKEEAPGLL---------------GKDIKWNFTKFLVDRDGEVVKR 138


                 ....*
gi 193209493 199 FHPTA 203
Cdd:cd00340  139 FAPTT 143
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 39-218 1.08e-48

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 156.78  E-value: 1.08e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493  39 SIYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQQYTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHEL---- 114
Cdd:COG0386    3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIaefc 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493 115 -MNgimyvrpgngwkphqnlhiYG-------KLDTNGDNQHPIYEFVKESCPqtvdkigktdelmyNPIRASDITWNFEK 186
Cdd:COG0386   83 sLN-------------------YGvtfpmfaKIDVNGPNAHPLYKYLKEEAP--------------GLLGGGDIKWNFTK 129

                        170       180       190
                 ....*....|....*....|....*....|..
gi 193209493 187 FLIDRNGQPRFRFHPTAWSHGDVVTPFIEQLL 218
Cdd:COG0386  130 FLIDRDGNVVARFAPTTKPEDPELEAAIEKLL 161
btuE PRK10606
putative glutathione peroxidase; Provisional
 38-219 9.94e-40

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 134.90  E-value: 9.94e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493  38 QSIYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQQYTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHELMNg 117
Cdd:PRK10606   3 DSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKT- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493 118 imYVRPGNGwkphQNLHIYGKLDTNGDNQHPIYEFVKESCPQTVDKIGKT-DELMYN----PIRASDITWNFEKFLIDRN 192
Cdd:PRK10606  82 --YCRTTWG----VTFPMFSKIEVNGEGRHPLYQKLIAAAPTAVAPEESGfYARMVSkgraPLYPDDILWNFEKFLVGRD 155

                        170       180
                 ....*....|....*....|....*..
gi 193209493 193 GQPRFRFHPTAWSHGDVVTPFIEQLLA 219
Cdd:PRK10606 156 GQVIQRFSPDMTPEDPIVMESIKLALA 182
GSHPx pfam00255
Glutathione peroxidase;
40-154 4.14e-37

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 125.54  E-value: 4.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493   40 IYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQQYTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHElmngIM 119
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEE----IK 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 193209493  120 YVRPGnGWKPhqNLHIYGKLDTNGDNQHPIYEFVK 154
Cdd:pfam00255  77 YFCPG-GYGV--TFPLFSKIEVNGEKAHPVYKFLK 108
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 39-194 1.34e-20

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: 84.50  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493   39 SIYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQQ-YTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHELMNg 117
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIES- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193209493  118 imYVRPGNGwkphQNLHIYGKLDTNGDNQHPIYEFVkescpqtVDKIGKtdelmynpirasDITWNFEKFLIDRNGQ 194
Cdd:TIGR02540  80 --FARRNYG----VTFPMFSKIKILGSEAEPAFRFL-------VDSSKK------------EPRWNFWKYLVNPEGQ 131
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 39-203 9.08e-60

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: 184.64  E-value: 9.08e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493  39 SIYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQQYTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHELMNGI 118
Cdd:cd00340    1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493 119 MYVRPgngwkphQNLHIYGKLDTNGDNQHPIYEFVKESCPQTVdkigktdelmynpirASDITWNFEKFLIDRNGQPRFR 198
Cdd:cd00340   81 ETNYG-------VTFPMFAKIDVNGENAHPLYKYLKEEAPGLL---------------GKDIKWNFTKFLVDRDGEVVKR 138


                 ....*
gi 193209493 199 FHPTA 203
Cdd:cd00340  139 FAPTT 143
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 39-218 1.08e-48

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 156.78  E-value: 1.08e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493  39 SIYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQQYTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHEL---- 114
Cdd:COG0386    3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIaefc 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493 115 -MNgimyvrpgngwkphqnlhiYG-------KLDTNGDNQHPIYEFVKESCPqtvdkigktdelmyNPIRASDITWNFEK 186
Cdd:COG0386   83 sLN-------------------YGvtfpmfaKIDVNGPNAHPLYKYLKEEAP--------------GLLGGGDIKWNFTK 129

                        170       180       190
                 ....*....|....*....|....*....|..
gi 193209493 187 FLIDRNGQPRFRFHPTAWSHGDVVTPFIEQLL 218
Cdd:COG0386  130 FLIDRDGNVVARFAPTTKPEDPELEAAIEKLL 161
btuE PRK10606
putative glutathione peroxidase; Provisional
 38-219 9.94e-40

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 134.90  E-value: 9.94e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493  38 QSIYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQQYTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHELMNg 117
Cdd:PRK10606   3 DSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKT- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493 118 imYVRPGNGwkphQNLHIYGKLDTNGDNQHPIYEFVKESCPQTVDKIGKT-DELMYN----PIRASDITWNFEKFLIDRN 192
Cdd:PRK10606  82 --YCRTTWG----VTFPMFSKIEVNGEGRHPLYQKLIAAAPTAVAPEESGfYARMVSkgraPLYPDDILWNFEKFLVGRD 155

                        170       180
                 ....*....|....*....|....*..
gi 193209493 193 GQPRFRFHPTAWSHGDVVTPFIEQLLA 219
Cdd:PRK10606 156 GQVIQRFSPDMTPEDPIVMESIKLALA 182
GSHPx pfam00255
Glutathione peroxidase;
40-154 4.14e-37

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 125.54  E-value: 4.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493   40 IYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQQYTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHElmngIM 119
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEE----IK 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 193209493  120 YVRPGnGWKPhqNLHIYGKLDTNGDNQHPIYEFVK 154
Cdd:pfam00255  77 YFCPG-GYGV--TFPLFSKIEVNGEKAHPVYKFLK 108
PLN02412 PLN02412
probable glutathione peroxidase
 34-202 3.09e-36

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 125.49  E-value: 3.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493  34 KDTNQSIYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQ-QYTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENH 112
Cdd:PLN02412   3 EESPKSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDsNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493 113 ELMNGIMYVRPGngwkphqNLHIYGKLDTNGDNQHPIYEFVKescpqtVDKIGktdelmynpIRASDITWNFEKFLIDRN 192
Cdd:PLN02412  83 EIQQTVCTRFKA-------EFPIFDKVDVNGKNTAPLYKYLK------AEKGG---------LFGDAIKWNFTKFLVSKE 140

                        170
                 ....*....|
gi 193209493 193 GQPRFRFHPT 202
Cdd:PLN02412 141 GKVVQRYAPT 150
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 36-219 1.07e-35

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 126.17  E-value: 1.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493  36 TNQSIYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYT-QQYTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHEL 114
Cdd:PLN02399  75 TEKSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTsSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEI 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493 115 MNGIMYvrpgngwKPHQNLHIYGKLDTNGDNQHPIYEFVKESCPQTVDKIgktdelmynpirasdITWNFEKFLIDRNGQ 194
Cdd:PLN02399 155 KQFACT-------RFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDL---------------IKWNFEKFLVDKNGK 212

                        170       180       190
                 ....*....|....*....|....*....|
gi 193209493 195 PRFRFHPTAwshgdvvTPF-----IEQLLA 219
Cdd:PLN02399 213 VVERYPPTT-------SPFqiekdIQKLLA 235
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 32-218 2.13e-29

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 107.92  E-value: 2.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493  32 QCKDTNQSIYDFQVETLQGEYTDLSQYRG-QVLLMVNVATFCAYT-QQYTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPA 109
Cdd:PTZ00256  12 QIQPPTKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTsDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPW 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493 110 ENHELMNgimYVRPgngwKPHQNLHIYGKLDTNGDNQHPIYEFVKESCPQTVDKIGKTDElmynpirasdITWNFEKFLI 189
Cdd:PTZ00256  92 DEPEIKE---YVQK----KFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNNTNEARQ----------IPWNFAKFLI 154

                        170       180
                 ....*....|....*....|....*....
gi 193209493 190 DRNGQPRFRFHPTAwsHGDVVTPFIEQLL 218
Cdd:PTZ00256 155 DGQGKVVKYFSPKV--NPNEMIQDIEKLL 181
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 39-194 4.43e-26

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 99.93  E-value: 4.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493  39 SIYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQQYTD-FNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHEL--- 114
Cdd:PTZ00056  18 SIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDqMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIrkf 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493 115 --MNGIMYvrpgngwkphqnlHIYGKLDTNGDNQHPIYEFVKESCPQTVDKIGKTdelmynpiraSDITWNFEKFLIDRN 192
Cdd:PTZ00056  98 ndKNKIKY-------------NFFEPIEVNGENTHELFKFLKANCDSMHDENGTL----------KAIGWNFGKFLVNKS 154


                 ..
gi 193209493 193 GQ 194
Cdd:PTZ00056 155 GN 156
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 39-194 1.34e-20

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: 84.50  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209493   39 SIYDFQVETLQGEYTDLSQYRGQVLLMVNVATFCAYTQQ-YTDFNPLIEKYQSQGFTLIAFPCNQFYLQEPAENHELMNg 117
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIES- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193209493  118 imYVRPGNGwkphQNLHIYGKLDTNGDNQHPIYEFVkescpqtVDKIGKtdelmynpirasDITWNFEKFLIDRNGQ 194
Cdd:TIGR02540  80 --FARRNYG----VTFPMFSKIKILGSEAEPAFRFL-------VDSSKK------------EPRWNFWKYLVNPEGQ 131
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
42-97 1.63e-06

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 46.01  E-value: 1.63e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 193209493  42 DFQVETLQGEYTDLSQYRGQVLLMVNVATFCAY-TQQYTDFNPLIEKYQSQGFTLIA 97
Cdd:COG1225    3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGcTAELPELRDLYEEFKDKGVEVLG 59
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 42-97 3.86e-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: 41.84  E-value: 3.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193209493  42 DFQVETLQGEYTDLSQYRGQVLLmVNV-ATFCAYTQQYT-DFNPLIEKYQSQGFTLIA 97
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVL-VNFwASWCPPCRAEMpELEALAKEYKDDGVEVVG 57
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 42-97 2.99e-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: 39.51  E-value: 2.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 193209493   42 DFQVETLQGEYTDLSQYRGQ-VLLMVNVATFCAY-TQQYTDFNPLIEKYQSQGFTLIA 97
Cdd:pfam00578   7 DFELPDGDGGTVSLSDYRGKwVVLFFYPADWTPVcTTELPALADLYEEFKKLGVEVLG 64
 
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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