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Conserved domains on  [gi|18407538|ref|NP_566128|]
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glutathione peroxidase 4 [Arabidopsis thaliana]

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 ...
 11-163 5.01e-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: 243.96  E-value: 5.01e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538  11 SVHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTEtNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAHEF 90
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18407538  91 ACERFKAEYPVFQKVRVNGQNAAPIYKFLKASKPTFLGSRIKWNFTKFLVGKDGLVIDRYGTMVTPLSIEKDI 163
Cdd:cd00340  80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 11-163 5.01e-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: 243.96  E-value: 5.01e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538  11 SVHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTEtNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAHEF 90
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18407538  91 ACERFKAEYPVFQKVRVNGQNAAPIYKFLKASKPTFLGSRIKWNFTKFLVGKDGLVIDRYGTMVTPLSIEKDI 163
Cdd:cd00340  80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 11-167 2.33e-79

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 232.66  E-value: 2.33e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538  11 SVHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTETnYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAHEF 90
Cdd:COG0386   3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQ-YEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538  91 aCE-RFKAEYPVFQKVRVNGQNAAPIYKFLKASKPTFLGS-RIKWNFTKFLVGKDGLVIDRYGTMVTPLS--IEKDIKKA 166
Cdd:COG0386  82 -CSlNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGgDIKWNFTKFLIDRDGNVVARFAPTTKPEDpeLEAAIEKL 160


                .
gi 18407538 167 L 167
Cdd:COG0386 161 L 161
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 9-167 3.71e-77

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 229.79  E-value: 3.71e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538    9 ERSVHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTETNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAH 88
Cdd:PLN02399  76 EKSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIK 155

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18407538   89 EFACERFKAEYPVFQKVRVNGQNAAPIYKFLKASKPTFLGSRIKWNFTKFLVGKDGLVIDRYGTMVTPLSIEKDIKKAL 167
Cdd:PLN02399 156 QFACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLL 234
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 11-163 7.52e-43

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: 139.59  E-value: 7.52e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538    11 SVHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTETNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAHEF 90
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18407538    91 ACERFKAEYPVFQKVRVNGQNAAPIYKFLKASKptflGSRIKWNFTKFLVGKDGLVIDRYGTMVTPLSIEKDI 163
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEI 149
GSHPx pfam00255
Glutathione peroxidase;
12-120 8.01e-43

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 138.25  E-value: 8.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538    12 VHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTEtNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAHEFA 91
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79

                          90       100
                  ....*....|....*....|....*....
gi 18407538    92 CERFKAEYPVFQKVRVNGQNAAPIYKFLK 120
Cdd:pfam00255  80 PGGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 11-163 5.01e-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: 243.96  E-value: 5.01e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538  11 SVHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTEtNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAHEF 90
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTP-QYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18407538  91 ACERFKAEYPVFQKVRVNGQNAAPIYKFLKASKPTFLGSRIKWNFTKFLVGKDGLVIDRYGTMVTPLSIEKDI 163
Cdd:cd00340  80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 11-167 2.33e-79

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 232.66  E-value: 2.33e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538  11 SVHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTETnYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAHEF 90
Cdd:COG0386   3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQ-YEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538  91 aCE-RFKAEYPVFQKVRVNGQNAAPIYKFLKASKPTFLGS-RIKWNFTKFLVGKDGLVIDRYGTMVTPLS--IEKDIKKA 166
Cdd:COG0386  82 -CSlNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGgDIKWNFTKFLIDRDGNVVARFAPTTKPEDpeLEAAIEKL 160


                .
gi 18407538 167 L 167
Cdd:COG0386 161 L 161
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 9-167 3.71e-77

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 229.79  E-value: 3.71e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538    9 ERSVHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTETNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAH 88
Cdd:PLN02399  76 EKSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIK 155

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18407538   89 EFACERFKAEYPVFQKVRVNGQNAAPIYKFLKASKPTFLGSRIKWNFTKFLVGKDGLVIDRYGTMVTPLSIEKDIKKAL 167
Cdd:PLN02399 156 QFACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLL 234
PLN02412 PLN02412
probable glutathione peroxidase
 10-170 9.04e-77

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 226.41  E-value: 9.04e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538   10 RSVHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTETNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAHE 89
Cdd:PLN02412   7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538   90 FACERFKAEYPVFQKVRVNGQNAAPIYKFLKASKPTFLGSRIKWNFTKFLVGKDGLVIDRYGTMVTPLSIEKDIKKALED 169
Cdd:PLN02412  87 TVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLLGQ 166


                 .
gi 18407538  170 A 170
Cdd:PLN02412 167 A 167
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 7-167 3.70e-55

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 171.87  E-value: 3.70e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538    7 VPERSVHQFTVKDSSGKDLNMSIYQG-KVLLIVNVASKCGFTETNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQ 85
Cdd:PTZ00256  15 PPTKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538   86 EAHEFACERFKAEYPVFQKVRVNGQNAAPIYKFLKASKPTFLGS-----RIKWNFTKFLVGKDGLVIDRYGTMVTPLSIE 160
Cdd:PTZ00256  95 EIKEYVQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNNtnearQIPWNFAKFLIDGQGKVVKYFSPKVNPNEMI 174


                 ....*..
gi 18407538  161 KDIKKAL 167
Cdd:PTZ00256 175 QDIEKLL 181
btuE PRK10606
putative glutathione peroxidase; Provisional
 17-167 2.08e-46

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 149.92  E-value: 2.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538   17 VKDSSGKDLNMSIYQGKVLLIVNVASKCGFTEtNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAHEFACERFK 96
Cdd:PRK10606  10 VTTIDGEVTTLEKYAGNVLLIVNVASKCGLTP-QYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYCRTTWG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538   97 AEYPVFQKVRVNGQNAAPIYKFLKASKPTFLGSR--------------------IKWNFTKFLVGKDGLVIDRYGTMVTP 156
Cdd:PRK10606  89 VTFPMFSKIEVNGEGRHPLYQKLIAAAPTAVAPEesgfyarmvskgraplypddILWNFEKFLVGRDGQVIQRFSPDMTP 168

                        170
                 ....*....|...
gi 18407538  157 LS--IEKDIKKAL 167
Cdd:PRK10606 169 EDpiVMESIKLAL 181
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 3-168 3.46e-44

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 144.61  E-value: 3.46e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538    3 ASASVPERSVHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTETNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPG 82
Cdd:PTZ00056  10 VSKDELRKSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538   83 TSQEAHEFAcERFKAEYPVFQKVRVNGQNAAPIYKFLKASKPTFLG-----SRIKWNFTKFLVGKDGLVIDRYGTMVTPL 157
Cdd:PTZ00056  90 NTKDIRKFN-DKNKIKYNFFEPIEVNGENTHELFKFLKANCDSMHDengtlKAIGWNFGKFLVNKSGNVVAYFSPRTEPL 168

                        170
                 ....*....|.
gi 18407538  158 SIEKDIKKALE 168
Cdd:PTZ00056 169 ELEKKIAELLG 179
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 11-163 7.52e-43

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: 139.59  E-value: 7.52e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538    11 SVHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTETNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAHEF 90
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18407538    91 ACERFKAEYPVFQKVRVNGQNAAPIYKFLKASKptflGSRIKWNFTKFLVGKDGLVIDRYGTMVTPLSIEKDI 163
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEI 149
GSHPx pfam00255
Glutathione peroxidase;
12-120 8.01e-43

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 138.25  E-value: 8.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538    12 VHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTEtNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAHEFA 91
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79

                          90       100
                  ....*....|....*....|....*....
gi 18407538    92 CERFKAEYPVFQKVRVNGQNAAPIYKFLK 120
Cdd:pfam00255  80 PGGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 14-103 8.26e-07

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: 45.69  E-value: 8.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538  14 QFTVKDSSGKDLNMSIYQGKVLLiVNV-ASKCGFTETNYTQLTELYRKYKDQDFEILAfpcnqfLYQEPGTSQEAHEFAc 92
Cdd:cd02966   1 DFSLPDLDGKPVSLSDLKGKVVL-VNFwASWCPPCRAEMPELEALAKEYKDDGVEVVG------VNVDDDDPAAVKAFL- 72

                        90
                ....*....|.
gi 18407538  93 ERFKAEYPVFQ 103
Cdd:cd02966  73 KKYGITFPVLL 83
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
15-170 6.11e-06

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 43.70  E-value: 6.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538  15 FTVKDSSGKDLNMSIYQGKVLLIVNVASKCGF--TETNytQLTELYRKYKDQDFEILAFPCNqflyqepgtSQEAHEFAC 92
Cdd:COG1225   4 FTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGctAELP--ELRDLYEEFKDKGVEVLGVSSD---------SDEAHKKFA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538  93 ERFKAEYPVFqkvrvngqnAAPIYKFLKA----SKPTFlgsrikwnftkFLVGKDGLVIDRYGTMVTPlsiEKDIKKALE 168
Cdd:COG1225  73 EKYGLPFPLL---------SDPDGEVAKAygvrGTPTT-----------FLIDPDGKIRYVWVGPVDP---RPHLEEVLE 129


                ..
gi 18407538 169 DA 170
Cdd:COG1225 130 AL 131
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 15-168 9.43e-06

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 43.14  E-value: 9.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538  15 FTVKDSSGKDLNMSIYQGKVLLiVNV-ASKCGFTETNYTQLTELYRKYKdqDFEILAFPCNQflyqepgTSQEAHEFAcE 93
Cdd:COG0526  11 FTLTDLDGKPLSLADLKGKPVL-VNFwATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVDE-------NPEAVKAFL-K 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18407538  94 RFKAEYPVFQKVRVNGQNAAPIYKFlkaskPTFlgsrikwnftkFLVGKDGLVIDRYGTMVTPLSIEKDIKKALE 168
Cdd:COG0526  80 ELGLPYPVLLDPDGELAKAYGVRGI-----PTT-----------VLIDKDGKIVARHVGPLSPEELEEALEKLLA 138
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 15-102 8.02e-03

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: 34.51  E-value: 8.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407538    15 FTVKDSSGKDLNMSIYQGKVLLIVNVASK-CGFTETNYTQLTELYRKYKDQDFEILAFPCNqflyqepgtSQEAHEFACE 93
Cdd:pfam00578   8 FELPDGDGGTVSLSDYRGKWVVLFFYPADwTPVCTTELPALADLYEEFKKLGVEVLGVSVD---------SPESHKAFAE 78


                  ....*....
gi 18407538    94 RFKAEYPVF 102
Cdd:pfam00578  79 KYGLPFPLL 87
 
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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