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Conserved domains on  [gi|28827652|gb|AAO50670|]
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putative glutathione peroxidase [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 ...
 14-165 3.19e-87

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: 252.05  E-value: 3.19e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652  14 IHQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTeSNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFA 93
Cdd:cd00340   2 IYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28827652  94 CTRFKAEYPVFQKVRVNGQNAAPVYKFLKSKKPSFLGSRIKWNFTKFLVGKDGQVIDRYGTTVSPLSIQKDI 165
Cdd:cd00340  81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 14-165 3.19e-87

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: 252.05  E-value: 3.19e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652  14 IHQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTeSNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFA 93
Cdd:cd00340   2 IYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28827652  94 CTRFKAEYPVFQKVRVNGQNAAPVYKFLKSKKPSFLGSRIKWNFTKFLVGKDGQVIDRYGTTVSPLSIQKDI 165
Cdd:cd00340  81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 14-169 8.46e-85

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 246.53  E-value: 8.46e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652  14 IHQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTeSNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFA 93
Cdd:COG0386   4 IYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEFC 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28827652  94 CTRFKAEYPVFQKVRVNGQNAAPVYKFLKSKKPSFLGS-RIKWNFTKFLVGKDGQVIDRYGTTVSPLS--IQKDIEKAL 169
Cdd:COG0386  83 SLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGgDIKWNFTKFLIDRDGNVVARFAPTTKPEDpeLEAAIEKLL 161
PLN02412 PLN02412
probable glutathione peroxidase
 14-171 2.94e-80

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 235.27  E-value: 2.94e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652   14 IHQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTESNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFA 93
Cdd:PLN02412   9 IYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQTV 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28827652   94 CTRFKAEYPVFQKVRVNGQNAAPVYKFLKSKKPSFLGSRIKWNFTKFLVGKDGQVIDRYGTTVSPLSIQKDIEKALAQ 171
Cdd:PLN02412  89 CTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLLGQ 166
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 15-165 4.49e-46

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: 148.06  E-value: 4.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652    15 HQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTESNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFAC 94
Cdd:TIGR02540   3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28827652    95 TRFKAEYPVFQKVRVNGQNAAPVYKFL---KSKKPsflgsriKWNFTKFLVGKDGQVIDRYGTTVSPLSIQKDI 165
Cdd:TIGR02540  83 RNYGVTFPMFSKIKILGSEAEPAFRFLvdsSKKEP-------RWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEI 149
GSHPx pfam00255
Glutathione peroxidase;
14-122 1.03e-45

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 145.57  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652    14 IHQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTEsNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFA 93
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79

                          90       100
                  ....*....|....*....|....*....
gi 28827652    94 CTRFKAEYPVFQKVRVNGQNAAPVYKFLK 122
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 ...
 14-165 3.19e-87

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: 252.05  E-value: 3.19e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652  14 IHQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTeSNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFA 93
Cdd:cd00340   2 IYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28827652  94 CTRFKAEYPVFQKVRVNGQNAAPVYKFLKSKKPSFLGSRIKWNFTKFLVGKDGQVIDRYGTTVSPLSIQKDI 165
Cdd:cd00340  81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 14-169 8.46e-85

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 246.53  E-value: 8.46e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652  14 IHQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTeSNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFA 93
Cdd:COG0386   4 IYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEFC 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28827652  94 CTRFKAEYPVFQKVRVNGQNAAPVYKFLKSKKPSFLGS-RIKWNFTKFLVGKDGQVIDRYGTTVSPLS--IQKDIEKAL 169
Cdd:COG0386  83 SLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGgDIKWNFTKFLIDRDGNVVARFAPTTKPEDpeLEAAIEKLL 161
PLN02412 PLN02412
probable glutathione peroxidase
 14-171 2.94e-80

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 235.27  E-value: 2.94e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652   14 IHQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTESNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFA 93
Cdd:PLN02412   9 IYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQTV 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28827652   94 CTRFKAEYPVFQKVRVNGQNAAPVYKFLKSKKPSFLGSRIKWNFTKFLVGKDGQVIDRYGTTVSPLSIQKDIEKALAQ 171
Cdd:PLN02412  89 CTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLLGQ 166
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 14-170 2.43e-78

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 232.87  E-value: 2.43e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652   14 IHQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTESNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFA 93
Cdd:PLN02399  79 VHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQFA 158

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28827652   94 CTRFKAEYPVFQKVRVNGQNAAPVYKFLKSKKPSFLGSRIKWNFTKFLVGKDGQVIDRYGTTVSPLSIQKDIEKALA 170
Cdd:PLN02399 159 CTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLLA 235
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 14-171 1.17e-54

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 170.71  E-value: 1.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652   14 IHQFTVKDSSGKEVDLSVYQG-KVLLVVNVASKCGFTESNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQF 92
Cdd:PTZ00256  20 FFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIKEY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652   93 ACTRFKAEYPVFQKVRVNGQNAAPVYKFLKSKKPSFLGS-----RIKWNFTKFLVGKDGQVIDRYGTTVSPLSIQKDIEK 167
Cdd:PTZ00256 100 VQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNNtnearQIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQDIEK 179


                 ....
gi 28827652  168 ALAQ 171
Cdd:PTZ00256 180 LLNA 183
btuE PRK10606
putative glutathione peroxidase; Provisional
 14-171 1.51e-50

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 160.32  E-value: 1.51e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652   14 IHQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTEsNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFA 93
Cdd:PRK10606   5 ILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTP-QYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652   94 CTRFKAEYPVFQKVRVNGQNAAPVYKFLKSKKPSFLGSR--------------------IKWNFTKFLVGKDGQVIDRYG 153
Cdd:PRK10606  84 RTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTAVAPEesgfyarmvskgraplypddILWNFEKFLVGRDGQVIQRFS 163

                        170       180
                 ....*....|....*....|
gi 28827652  154 TTVSPLS--IQKDIEKALAQ 171
Cdd:PRK10606 164 PDMTPEDpiVMESIKLALAK 183
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 15-165 4.49e-46

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: 148.06  E-value: 4.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652    15 HQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTESNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFAC 94
Cdd:TIGR02540   3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28827652    95 TRFKAEYPVFQKVRVNGQNAAPVYKFL---KSKKPsflgsriKWNFTKFLVGKDGQVIDRYGTTVSPLSIQKDI 165
Cdd:TIGR02540  83 RNYGVTFPMFSKIKILGSEAEPAFRFLvdsSKKEP-------RWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEI 149
GSHPx pfam00255
Glutathione peroxidase;
14-122 1.03e-45

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 145.57  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652    14 IHQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTEsNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFA 93
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79

                          90       100
                  ....*....|....*....|....*....
gi 28827652    94 CTRFKAEYPVFQKVRVNGQNAAPVYKFLK 122
Cdd:pfam00255  80 PGGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 14-169 3.23e-43

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 142.30  E-value: 3.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652   14 IHQFTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTESNYTQLTELYRKYKDQGFVVLAFPCNQFLSQEPGTSEEAHQFA 93
Cdd:PTZ00056  19 IYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRKFN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652   94 cTRFKAEYPVFQKVRVNGQNAAPVYKFLKSKKPSFLG-----SRIKWNFTKFLVGKDGQVIDRYGTTVSPLSIQKDIEKA 168
Cdd:PTZ00056  99 -DKNKIKYNFFEPIEVNGENTHELFKFLKANCDSMHDengtlKAIGWNFGKFLVNKSGNVVAYFSPRTEPLELEKKIAEL 177


                 .
gi 28827652  169 L 169
Cdd:PTZ00056 178 L 178
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
17-173 2.54e-10

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 55.26  E-value: 2.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652  17 FTVKDSSGKEVDLSVYQGKVLLVVNVASKCGF--TESNytQLTELYRKYKDQGFVVLAfpcnqfLSQEpgtSEEAHQFAC 94
Cdd:COG1225   4 FTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGctAELP--ELRDLYEEFKDKGVEVLG------VSSD---SDEAHKKFA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652  95 TRFKAEYPVF----QKVrvngQNAAPVYKFlkskkPSFlgsrikwnftkFLVGKDGQVIDRYgttVSPLSIQKDIEKALA 170
Cdd:COG1225  73 EKYGLPFPLLsdpdGEV----AKAYGVRGT-----PTT-----------FLIDPDGKIRYVW---VGPVDPRPHLEEVLE 129


                ...
gi 28827652 171 QEL 173
Cdd:COG1225 130 ALL 132
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 16-105 6.66e-09

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: 51.08  E-value: 6.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652  16 QFTVKDSSGKEVDLSVYQGKVLlVVNV-ASKCGFTESNYTQLTELYRKYKDQGFVVLAfpcnqfLSQEPGTSEEAHQFAc 94
Cdd:cd02966   1 DFSLPDLDGKPVSLSDLKGKVV-LVNFwASWCPPCRAEMPELEALAKEYKDDGVEVVG------VNVDDDDPAAVKAFL- 72

                        90
                ....*....|.
gi 28827652  95 TRFKAEYPVFQ 105
Cdd:cd02966  73 KKYGITFPVLL 83
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 17-171 5.47e-08

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 49.30  E-value: 5.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652  17 FTVKDSSGKEVDLSVYQGKVLLvVNV-ASKCGFTESNYTQLTELYRKYKdqGFVVLafpcnqFLSQEpGTSEEAHQFAcT 95
Cdd:COG0526  11 FTLTDLDGKPLSLADLKGKPVL-VNFwATWCPPCRAEMPVLKELAEEYG--GVVFV------GVDVD-ENPEAVKAFL-K 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28827652  96 RFKAEYPVFQKVRVNGQNAAPVYKFlkskkPSFlgsrikwnftkFLVGKDGQVIDRYGTTVSPLSIQKDIEKALAQ 171
Cdd:COG0526  80 ELGLPYPVLLDPDGELAKAYGVRGI-----PTT-----------VLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 17-104 1.59e-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: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652    17 FTVKDSSGKEVDLSVYQGKVLLVVNVASK-CGFTESNYTQLTELYRKYKDQGFVVLAFPCNqflsqepgtSEEAHQFACT 95
Cdd:pfam00578   8 FELPDGDGGTVSLSDYRGKWVVLFFYPADwTPVCTTELPALADLYEEFKKLGVEVLGVSVD---------SPESHKAFAE 78


                  ....*....
gi 28827652    96 RFKAEYPVF 104
Cdd:pfam00578  79 KYGLPFPLL 87
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 24-169 1.74e-03

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 36.96  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827652    24 GKEVDLSVYQGKVLLVVNVASK-CGFTESNYTQLTELYRKYKDQGFVVLAFpcnqflsqepGTSEEAhqFACTRFKAEYP 102
Cdd:pfam08534  18 GNTVSLSDFKGKKVVLNFWPGAfCPTCSAEHPYLEKLNELYKEKGVDVVAV----------NSDNDA--FFVKRFWGKEG 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28827652   103 VfqKVRVN-GQNAAPVYKF---LKSKKPSFLGSRikwnfTKFLVGKDGQVIDRYgTTVSPLSIQKDIEKAL 169
Cdd:pfam08534  86 L--PFPFLsDGNAAFTKALglpIEEDASAGLRSP-----RYAVIDEDGKVVYLF-VGPEPGVDVSDAEAVL 148
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
17-72 4.14e-03

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 36.13  E-value: 4.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 28827652   17 FTVKDSSGKEVDLSVYQGKVLLVVNVASKCGFTESNYTQLTELYRKYKDQGFVVLA 72
Cdd:PRK03147  44 FVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIA 99
 
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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