NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|398364659|ref|NP_012899|]
View 

glutathione peroxidase GPX1 [Saccharomyces cerevisiae S288C]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 4-155 4.30e-82

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: 238.95  E-value: 4.30e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   4 FYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFCQ 83
Cdd:cd00340    2 IYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFCE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398364659  84 DKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSGiKMIKWNFEKFVVDRNGKVVKRFSCMTRPLELCPII 155
Cdd:cd00340   82 TNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG-KDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 4-155 4.30e-82

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: 238.95  E-value: 4.30e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   4 FYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFCQ 83
Cdd:cd00340    2 IYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFCE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398364659  84 DKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSGiKMIKWNFEKFVVDRNGKVVKRFSCMTRPLELCPII 155
Cdd:cd00340   82 TNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG-KDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 1-159 4.27e-79

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 231.50  E-value: 4.27e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   1 MQEFYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINK 80
Cdd:COG0386    1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659  81 FCQDKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSGIKMIKWNFEKFVVDRNGKVVKRFSCMTRPL--ELCPIIEEL 158
Cdd:COG0386   81 FCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGDIKWNFTKFLIDRDGNVVARFAPTTKPEdpELEAAIEKL 160


                 .
gi 398364659 159 L 159
Cdd:COG0386  161 L 161
GSHPx pfam00255
Glutathione peroxidase;
4-111 1.07e-62

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 188.33  E-value: 1.07e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659    4 FYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFCQ 83
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80

                          90       100
                  ....*....|....*....|....*...
gi 398364659   84 DKYGVTFPILHKIRCNGQKQDPVYKFLK 111
Cdd:pfam00255  81 GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 5-159 1.71e-46

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 151.59  E-value: 1.71e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   5 YSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTP-QYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFCQ 83
Cdd:PLN02399  80 HDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQFAC 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364659  84 DKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSGiKMIKWNFEKFVVDRNGKVVKRFSCMTRPLELCPIIEELL 159
Cdd:PLN02399 160 TRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLG-DLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLL 234
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 3-140 1.27e-36

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: 123.79  E-value: 1.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659    3 EFYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQ-YKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKF 81
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 398364659   82 CQDKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSgksgiKMIKWNFEKFVVDRNGKVVK 140
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSK-----KEPRWNFWKYLVNPEGQVVK 134
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 4-155 4.30e-82

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: 238.95  E-value: 4.30e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   4 FYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFCQ 83
Cdd:cd00340    2 IYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFCE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398364659  84 DKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSGiKMIKWNFEKFVVDRNGKVVKRFSCMTRPLELCPII 155
Cdd:cd00340   82 TNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLG-KDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 1-159 4.27e-79

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 231.50  E-value: 4.27e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   1 MQEFYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINK 80
Cdd:COG0386    1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659  81 FCQDKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSGIKMIKWNFEKFVVDRNGKVVKRFSCMTRPL--ELCPIIEEL 158
Cdd:COG0386   81 FCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGDIKWNFTKFLIDRDGNVVARFAPTTKPEdpELEAAIEKL 160


                 .
gi 398364659 159 L 159
Cdd:COG0386  161 L 161
GSHPx pfam00255
Glutathione peroxidase;
4-111 1.07e-62

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 188.33  E-value: 1.07e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659    4 FYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFCQ 83
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80

                          90       100
                  ....*....|....*....|....*...
gi 398364659   84 DKYGVTFPILHKIRCNGQKQDPVYKFLK 111
Cdd:pfam00255  81 GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 5-159 1.71e-46

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 151.59  E-value: 1.71e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   5 YSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTP-QYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFCQ 83
Cdd:PLN02399  80 HDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQFAC 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364659  84 DKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSGiKMIKWNFEKFVVDRNGKVVKRFSCMTRPLELCPIIEELL 159
Cdd:PLN02399 160 TRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLG-DLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLL 234
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 4-161 3.28e-44

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 144.13  E-value: 3.28e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   4 FYSFSPIDENGNPFPFNSLRN-KVVLIVNVASHCAFTPQ-YKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKF 81
Cdd:PTZ00256  20 FFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIKEY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659  82 CQDKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSG----IKMIKWNFEKFVVDRNGKVVKRFSCMTRPLELCPIIEE 157
Cdd:PTZ00256 100 VQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNntneARQIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQDIEK 179


                 ....
gi 398364659 158 LLNQ 161
Cdd:PTZ00256 180 LLNA 183
PLN02412 PLN02412
probable glutathione peroxidase
 2-161 1.34e-42

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 139.35  E-value: 1.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   2 QEFYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFT-PQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINK 80
Cdd:PLN02412   7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659  81 FCQDKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSGiKMIKWNFEKFVVDRNGKVVKRFSCMTRPLELCPIIEELLN 160
Cdd:PLN02412  87 TVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFG-DAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLLG 165


                 .
gi 398364659 161 Q 161
Cdd:PLN02412 166 Q 166
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 4-160 3.10e-41

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 136.91  E-value: 3.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   4 FYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQY-KELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFc 82
Cdd:PTZ00056  19 IYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHvDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRKF- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659  83 QDKYGVTFPILHKIRCNGQKQDPVYKFLK---NSVSGKSG-IKMIKWNFEKFVVDRNGKVVKRFSCMTRPLELCPIIEEL 158
Cdd:PTZ00056  98 NDKNKIKYNFFEPIEVNGENTHELFKFLKancDSMHDENGtLKAIGWNFGKFLVNKSGNVVAYFSPRTEPLELEKKIAEL 177


                 ..
gi 398364659 159 LN 160
Cdd:PTZ00056 178 LG 179
btuE PRK10606
putative glutathione peroxidase; Provisional
 19-143 6.33e-38

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 127.97  E-value: 6.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659  19 FNSLRNKVVLIVNVASHCAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFCQDKYGVTFPILHKIRC 98
Cdd:PRK10606  20 LEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYCRTTWGVTFPMFSKIEV 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398364659  99 NGQKQDPVYKFL-----KNSVSGKSGI--KM------------IKWNFEKFVVDRNGKVVKRFS 143
Cdd:PRK10606 100 NGEGRHPLYQKLiaaapTAVAPEESGFyaRMvskgraplypddILWNFEKFLVGRDGQVIQRFS 163
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 3-140 1.27e-36

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: 123.79  E-value: 1.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659    3 EFYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQ-YKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKF 81
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 398364659   82 CQDKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSgksgiKMIKWNFEKFVVDRNGKVVK 140
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSK-----KEPRWNFWKYLVNPEGQVVK 134
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
7-161 7.77e-12

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 59.11  E-value: 7.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   7 FSPIDENGNPFPFNSLRNKVVLIVNVASHCAF-TPQYKELEYLYEKYKSHGLVIVAFpcgqfgnqEFEKDKEINKFCqDK 85
Cdd:COG1225    4 FTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGcTAELPELRDLYEEFKDKGVEVLGV--------SSDSDEAHKKFA-EK 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364659  86 YGVTFPILHkircngqkqDPvykflKNSVSGKSGIKMIKWNFekfVVDRNGKVVKRFscmTRPLELCPIIEELLNQ 161
Cdd:COG1225   75 YGLPFPLLS---------DP-----DGEVAKAYGVRGTPTTF---LIDPDGKIRYVW---VGPVDPRPHLEEVLEA 130
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 2-161 1.58e-08

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 50.46  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   2 QEFYSFSPIDENGNPFPFNSLRNKVVLiVNV-ASHC----AFTPqykELEYLYEKYKshGLVIVAFpcgqfgNQEfEKDK 76
Cdd:COG0526    6 KPAPDFTLTDLDGKPLSLADLKGKPVL-VNFwATWCppcrAEMP---VLKELAEEYG--GVVFVGV------DVD-ENPE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659  77 EINKFcQDKYGVTFPILhkircngqkQDPVYKFlknsvsgksgikMIKWNF----EKFVVDRNGKVVKRFSCMTRPLELC 152
Cdd:COG0526   73 AVKAF-LKELGLPYPVL---------LDPDGEL------------AKAYGVrgipTTVLIDKDGKIVARHVGPLSPEELE 130


                 ....*....
gi 398364659 153 PIIEELLNQ 161
Cdd:COG0526  131 EALEKLLAK 139
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 6-142 6.53e-07

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 46.21  E-value: 6.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659    6 SFSPIDENGNPFPFNSLRNKVVLIVNVAShcAFTP----QYKELEYLYEKYKSHGLVIVAfpCGQfGNQEFEkdkeINKF 81
Cdd:pfam08534  10 TLPDAATDGNTVSLSDFKGKKVVLNFWPG--AFCPtcsaEHPYLEKLNELYKEKGVDVVA--VNS-DNDAFF----VKRF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364659   82 CqDKYGVTFPILHkircngqkqDPVYKFLKN-----SVSGKSGIKMIKWnfekFVVDRNGKVVKRF 142
Cdd:pfam08534  81 W-GKEGLPFPFLS---------DGNAAFTKAlglpiEEDASAGLRSPRY----AVIDEDGKVVYLF 132
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 6-141 1.56e-06

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: 44.91  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659    6 SFSPIDENGNPFPFNSLRNKVVLIVNVAShcAFTP----QYKELEYLYEKYKSHGLVIVAFPCgqfgnqefEKDKEINKF 81
Cdd:pfam00578   7 DFELPDGDGGTVSLSDYRGKWVVLFFYPA--DWTPvcttELPALADLYEEFKKLGVEVLGVSV--------DSPESHKAF 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398364659   82 CqDKYGVTFPILHkircngqkqDPvykflKNSVSGKSGIKMIKWNFEK---FVVDRNGKVVKR 141
Cdd:pfam00578  77 A-EKYGLPFPLLS---------DP-----DGEVARAYGVLNEEEGGALratFVIDPDGKVRYI 124
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
7-140 6.31e-03

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 35.36  E-value: 6.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659   7 FSPIDENGNPFPFNSLRNKVVLIVNVASHCAftPQYKELEY---LYEKYKSHGLVIVAFPCGqfgnqefEKDKEINKFCq 83
Cdd:PRK03147  44 FVLTDLEGKKIELKDLKGKGVFLNFWGTWCK--PCEKEMPYmneLYPKYKEKGVEIIAVNVD-------ETELAVKNFV- 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 398364659  84 DKYGVTFPILHkircngQKQDpvykflknSVSGKSGIKMIKwnfEKFVVDRNGKVVK 140
Cdd:PRK03147 114 NRYGLTFPVAI------DKGR--------QVIDAYGVGPLP---TTFLIDKDGKVVK 153
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 21-93 8.37e-03

TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.


Pssm-ID: 239310 [Multi-domain]  Cd Length: 126  Bit Score: 34.59  E-value: 8.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364659  21 SLRNKVVLI-------VNvashCAFTPQYkeLEYLYEKYKSHGLVIVAFPCGQFGnqeFEKDKEINKFCQDKYGVTFPIL 93
Cdd:cd03012   20 QLRGKVVLLdfwtyccIN----CLHTLPY--LTDLEQKYKDDGLVVIGVHSPEFA---FERDLANVKSAVLRYGITYPVA 90
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH