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Conserved domains on  [gi|1002277198|ref|XP_015642936|]
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probable phospholipid hydroperoxide glutathione peroxidase [Oryza sativa Japonica Group]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 49-234 1.74e-125

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member PLN02399:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 236  Bit Score: 354.98  E-value: 1.74e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  49 SAAVPVVAAPSRrwaPGVAYATAATGKSVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTTANYTELSHLYEKYKT 128
Cdd:PLN02399   54 SPNSPGFLSKSR---SFGVYARAATEKSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198 129 QGFEILAFPCNQFGAQEPGSNPQIKQFACTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSAGGFLGDLVKWNFEKFLVDKT 208
Cdd:PLN02399  131 QGFEILAFPCNQFGGQEPGSNPEIKQFACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKN 210

                         170       180
                  ....*....|....*....|....*.
gi 1002277198 209 GKVVERYPPTTSPFQIEKDIQKLLAA 234
Cdd:PLN02399  211 GKVVERYPPTTSPFQIEKDIQKLLAA 236
 
Name Accession Description Interval E-value
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 49-234 1.74e-125

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 354.98  E-value: 1.74e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  49 SAAVPVVAAPSRrwaPGVAYATAATGKSVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTTANYTELSHLYEKYKT 128
Cdd:PLN02399   54 SPNSPGFLSKSR---SFGVYARAATEKSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198 129 QGFEILAFPCNQFGAQEPGSNPQIKQFACTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSAGGFLGDLVKWNFEKFLVDKT 208
Cdd:PLN02399  131 QGFEILAFPCNQFGGQEPGSNPEIKQFACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKN 210

                         170       180
                  ....*....|....*....|....*.
gi 1002277198 209 GKVVERYPPTTSPFQIEKDIQKLLAA 234
Cdd:PLN02399  211 GKVVERYPPTTSPFQIEKDIQKLLAA 236
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 76-228 1.95e-93

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: 270.54  E-value: 1.95e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  76 SVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGlTTANYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQIKQF 155
Cdd:cd00340     1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCG-FTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002277198 156 ACTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSAGGFLGDLVKWNFEKFLVDKTGKVVERYPPTTSPFQIEKDI 228
Cdd:cd00340    80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 76-232 9.43e-86

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 251.53  E-value: 9.43e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  76 SVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTtANYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQIKQF 155
Cdd:COG0386     3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198 156 ACTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSAGGFLGD-LVKWNFEKFLVDKTGKVVERYPPTTSP--FQIEKDIQKLL 232
Cdd:COG0386    82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGgDIKWNFTKFLIDRDGNVVARFAPTTKPedPELEAAIEKLL 161
GSHPx pfam00255
Glutathione peroxidase;
77-185 4.29e-51

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 161.75  E-value: 4.29e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  77 VHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTTaNYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQIKQFA 156
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79

                          90       100
                  ....*....|....*....|....*....
gi 1002277198 157 CTRFKAEFPIFDKVDVNGPNTAPIYKFLK 185
Cdd:pfam00255  80 PGGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 76-232 4.99e-47

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: 152.68  E-value: 4.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  76 SVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTTANYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQIKQF 155
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002277198 156 ACTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSAggflGDLVKWNFEKFLVDKTGKVVERYPPTTSPFQIEKDIQKLL 232
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
 
Name Accession Description Interval E-value
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 49-234 1.74e-125

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 354.98  E-value: 1.74e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  49 SAAVPVVAAPSRrwaPGVAYATAATGKSVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTTANYTELSHLYEKYKT 128
Cdd:PLN02399   54 SPNSPGFLSKSR---SFGVYARAATEKSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198 129 QGFEILAFPCNQFGAQEPGSNPQIKQFACTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSAGGFLGDLVKWNFEKFLVDKT 208
Cdd:PLN02399  131 QGFEILAFPCNQFGGQEPGSNPEIKQFACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKN 210

                         170       180
                  ....*....|....*....|....*.
gi 1002277198 209 GKVVERYPPTTSPFQIEKDIQKLLAA 234
Cdd:PLN02399  211 GKVVERYPPTTSPFQIEKDIQKLLAA 236
PLN02412 PLN02412
probable glutathione peroxidase
 72-234 2.03e-98

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 283.80  E-value: 2.03e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  72 ATGKSVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTTANYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQ 151
Cdd:PLN02412    4 ESPKSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198 152 IKQFACTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSAGGFLGDLVKWNFEKFLVDKTGKVVERYPPTTSPFQIEKDIQKL 231
Cdd:PLN02412   84 IQQTVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNL 163


                  ...
gi 1002277198 232 LAA 234
Cdd:PLN02412  164 LGQ 166
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 76-228 1.95e-93

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: 270.54  E-value: 1.95e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  76 SVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGlTTANYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQIKQF 155
Cdd:cd00340     1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCG-FTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002277198 156 ACTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSAGGFLGDLVKWNFEKFLVDKTGKVVERYPPTTSPFQIEKDI 228
Cdd:cd00340    80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 76-232 9.43e-86

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


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 251.53  E-value: 9.43e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  76 SVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTtANYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQIKQF 155
Cdd:COG0386     3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198 156 ACTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSAGGFLGD-LVKWNFEKFLVDKTGKVVERYPPTTSP--FQIEKDIQKLL 232
Cdd:COG0386    82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGgDIKWNFTKFLIDRDGNVVARFAPTTKPedPELEAAIEKLL 161
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 75-234 1.18e-72

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 219.25  E-value: 1.18e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  75 KSVHDFTVKDIDGKDVALSKFKGR-ALLIVNVASQCGLTTANYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQIK 153
Cdd:PTZ00256   18 KSFFEFEAIDIDGQLVQLSKFKGKkAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198 154 QFACTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSAGGFLGDL-----VKWNFEKFLVDKTGKVVERYPPTTSPFQIEKDI 228
Cdd:PTZ00256   98 EYVQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNNTnearqIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQDI 177


                  ....*.
gi 1002277198 229 QKLLAA 234
Cdd:PTZ00256  178 EKLLNA 183
btuE PRK10606
putative glutathione peroxidase; Provisional
 76-221 2.97e-52

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 167.26  E-value: 2.97e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  76 SVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTtANYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQIKQF 155
Cdd:PRK10606    4 SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLT-PQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198 156 ACTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSA--------GGFLGDLVK------------WNFEKFLVDKTGKVVERY 215
Cdd:PRK10606   83 CRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAptavapeeSGFYARMVSkgraplypddilWNFEKFLVGRDGQVIQRF 162


                  ....*.
gi 1002277198 216 PPTTSP 221
Cdd:PRK10606  163 SPDMTP 168
GSHPx pfam00255
Glutathione peroxidase;
77-185 4.29e-51

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 161.75  E-value: 4.29e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  77 VHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTTaNYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQIKQFA 156
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79

                          90       100
                  ....*....|....*....|....*....
gi 1002277198 157 CTRFKAEFPIFDKVDVNGPNTAPIYKFLK 185
Cdd:pfam00255  80 PGGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 75-232 5.18e-49

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 159.25  E-value: 5.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  75 KSVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTTANYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQIKQ 154
Cdd:PTZ00056   17 KSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198 155 FAcTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSAGGFL---GDL--VKWNFEKFLVDKTGKVVERYPPTTSPFQIEKDIQ 229
Cdd:PTZ00056   97 FN-DKNKIKYNFFEPIEVNGENTHELFKFLKANCDSMHdenGTLkaIGWNFGKFLVNKSGNVVAYFSPRTEPLELEKKIA 175


                  ...
gi 1002277198 230 KLL 232
Cdd:PTZ00056  176 ELL 178
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 76-232 4.99e-47

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: 152.68  E-value: 4.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  76 SVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTTANYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQIKQF 155
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002277198 156 ACTRFKAEFPIFDKVDVNGPNTAPIYKFLKSSAggflGDLVKWNFEKFLVDKTGKVVERYPPTTSPFQIEKDIQKLL 232
Cdd:TIGR02540  81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
79-234 1.00e-10

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 57.57  E-value: 1.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  79 DFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTTANYTELSHLYEKYKTQGFEILAFpcnqfgaqEPGSNPQIKQFAcT 158
Cdd:COG1225     3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGV--------SSDSDEAHKKFA-E 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002277198 159 RFKAEFPIFdkVDVNGpNTAPIYKflkssaggflgdlVKWNFEKFLVDKTGKVVERYpptTSPFQIEKDIQKLLAA 234
Cdd:COG1225    74 KYGLPFPLL--SDPDG-EVAKAYG-------------VRGTPTTFLIDPDGKIRYVW---VGPVDPRPHLEEVLEA 130
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 72-234 1.15e-07

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 49.30  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  72 ATGKSVHDFTVKDIDGKDVALSKFKGRALLiVNV-ASQCGLTTANYTELSHLYEKYKtqGFEILAFPCNQfgaqepgSNP 150
Cdd:COG0526     3 AVGKPAPDFTLTDLDGKPLSLADLKGKPVL-VNFwATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVDE-------NPE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198 151 QIKQFAcTRFKAEFPIFdkVDVNGpntaPIYKFLKSSAggflgdlvkwnF-EKFLVDKTGKVVERYPPTTSPFQIEKDIQ 229
Cdd:COG0526    73 AVKAFL-KELGLPYPVL--LDPDG----ELAKAYGVRG-----------IpTTVLIDKDGKIVARHVGPLSPEELEEALE 134


                  ....*
gi 1002277198 230 KLLAA 234
Cdd:COG0526   135 KLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 79-215 8.24e-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: 46.46  E-value: 8.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  79 DFTVKDIDGKDVALSKFKGRALLiVNV-ASQCGLTTANYTELSHLYEKYKTQGFEILAFpcnqfgAQEPGSNPQIKQFAc 157
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVVL-VNFwASWCPPCRAEMPELEALAKEYKDDGVEVVGV------NVDDDDPAAVKAFL- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002277198 158 TRFKAEFPIFdkVDVNGpNTAPIYKflkssaggflgdlVKWNFEKFLVDKTGKVVERY 215
Cdd:cd02966    73 KKYGITFPVL--LDPDG-ELAKAYG-------------VRGLPTTFLIDRDGRIRARH 114
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 72-215 2.67e-06

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 45.82  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  72 ATGKSVHDFTVKDI--DGKDVALSKFKGRALLIVNVAS-QCGLTTANYTELSHLYEKYKTQGFEILAFPCNQ--FGAQEp 146
Cdd:pfam08534   1 KAGDKAPDFTLPDAatDGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNdaFFVKR- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002277198 147 gsnpqikqfACTRFKAEFPIFdkVDVNGpntapiyKFLKSSAGGFLGDLVKWNFEK--FLVDKTGKVVERY 215
Cdd:pfam08534  80 ---------FWGKEGLPFPFL--SDGNA-------AFTKALGLPIEEDASAGLRSPryAVIDEDGKVVYLF 132
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
71-213 4.78e-06

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 45.38  E-value: 4.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  71 AATGKSVHDFTVKDIDGKDVALSKFKGRALLIVNVASQCGLTTANYTELSHLYEKYKTQGFEILAFPCNqfgaqepGSNP 150
Cdd:PRK03147   35 VQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVD-------ETEL 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002277198 151 QIKQFAcTRFKAEFPI-FDKVD--VNGPNTAPiykfLKSSaggflgdlvkwnfekFLVDKTGKVVE 213
Cdd:PRK03147  108 AVKNFV-NRYGLTFPVaIDKGRqvIDAYGVGP----LPTT---------------FLIDKDGKVVK 153
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 74-214 9.37e-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: 43.75  E-value: 9.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  74 GKSVHDFTVKDIDGKDVALSKFKGRALLIVNVAS-QCGLTTANYTELSHLYEKYKTQGFEILAFPCNqfgaqepgSNPQI 152
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSVD--------SPESH 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002277198 153 KQFAcTRFKAEFPIFdkVDVNGpNTAPIYKFLKSSAGGFLGDLvkwnfekFLVDKTGKVVER 214
Cdd:pfam00578  74 KAFA-EKYGLPFPLL--SDPDG-EVARAYGVLNEEEGGALRAT-------FVIDPDGKVRYI 124
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 81-234 5.68e-05

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 42.20  E-value: 5.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  81 TVKDIDGKDVALSKFKGRALLIVNVASQCG----LTTANyteLSHLYEKYKTQG---FEILAF---PCN----------- 139
Cdd:COG1999     4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPdvcpTTLAN---LAQVQEALGEDGgddVQVLFIsvdPERdtpevlkayae 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198 140 QFGAQE----PGSNPQIKQFAcTRFKAefpIFDKVDVNGpntapiYKFLKSSaggflgdlvkwNFekFLVDKTGKVVERY 215
Cdd:COG1999    81 AFGAPRwiglTGDPEEIAALA-KAFGV---YYEKVPDGD------YTFDHSA-----------AV--YLVDPDGRLRGYY 137

                         170
                  ....*....|....*....
gi 1002277198 216 PPTTSPFQIEKDIQKLLAA 234
Cdd:COG1999   138 PAGEDPEELAADLKALLEE 156
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 74-165 8.25e-05

Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF.


Pssm-ID: 239267 [Multi-domain]  Cd Length: 171  Bit Score: 41.84  E-value: 8.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002277198  74 GKSVHDFTVKDIDGKDVALSKF-KGRALLIVNVASQCGLTTANYTELSHLYEKYKTQGFEILAFPCNQFGAQEPGSNPQI 152
Cdd:cd02969     1 GSPAPDFSLPDTDGKTYSLADFaDGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPENM 80

                          90
                  ....*....|...
gi 1002277198 153 KQFAcTRFKAEFP 165
Cdd:cd02969    81 KAKA-KEHGYPFP 92
 
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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