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Conserved domains on  [gi|1831508098|ref|NP_001367731|]
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Peroxiredoxin prdx-2 [Caenorhabditis elegans]

Protein Classification

peroxiredoxin( domain architecture ID 10122432)

peroxiredoxin, also called thioredoxin peroxidase or alkyl hydroperoxide reductase, is a thiol-specific antioxidant protein that protects cells against reactive oxygen species

CATH:  3.40.30.10
EC:  1.11.1.-
Gene Ontology:  GO:0008379
PubMed:  15518547|12517450|10049365|15558583
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 10-181 2.33e-117

Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure.


:

Pssm-ID: 239313  Cd Length: 173  Bit Score: 330.24  E-value: 2.33e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFKTQAVV-DGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAW 88
Cdd:cd03015     1 VGKKAPDFKATAVVpNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  89 INQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVE 168
Cdd:cd03015    81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                         170
                  ....*....|...
gi 1831508098 169 KHGEVCPAGWTPG 181
Cdd:cd03015   161 EHGEVCPANWKPG 173
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 10-181 2.33e-117

Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure.


Pssm-ID: 239313  Cd Length: 173  Bit Score: 330.24  E-value: 2.33e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFKTQAVV-DGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAW 88
Cdd:cd03015     1 VGKKAPDFKATAVVpNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  89 INQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVE 168
Cdd:cd03015    81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                         170
                  ....*....|...
gi 1831508098 169 KHGEVCPAGWTPG 181
Cdd:cd03015   161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
10-199 2.69e-111

Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];


Pssm-ID: 440219  Cd Length: 196  Bit Score: 315.86  E-value: 2.69e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWI 89
Cdd:COG0450     5 IGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAWH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  90 NQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEK 169
Cdd:COG0450    85 ETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFVDK 164

                         170       180       190
                  ....*....|....*....|....*....|
gi 1831508098 170 HGEVCPAGWTPGSDTIKPGVKESQEYFKKH 199
Cdd:COG0450   165 HGEVCPANWKPGDKVIIPPPDLVGKALERF 194
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 8-196 3.71e-100

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 287.96  E-value: 3.71e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098   8 AFIGKPAPQFKTQAVV-DGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHL 86
Cdd:PTZ00253    6 AKINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  87 AWINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQF 166
Cdd:PTZ00253   86 QWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQF 165

                         170       180       190
                  ....*....|....*....|....*....|
gi 1831508098 167 VEKHGEVCPAGWTPGSDTIKPGVKESQEYF 196
Cdd:PTZ00253  166 VEKHGEVCPANWKKGDPTMKPDPNKSKEGF 195
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 10-189 1.24e-64

peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one subunit of a two-subunit complex with subunit F(TIGR03140). Usually these are found as an apparent operon. The gene has been characterized in Bacteroides fragilis, where it is important in oxidative stress defense. This gene contains two invariant cysteine residues, one near the N-terminus and one near the C-terminus, each followed immediately by a proline residue. [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 211789  Cd Length: 187  Bit Score: 197.24  E-value: 1.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWI 89
Cdd:TIGR03137   4 INTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAWH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  90 NQPRKhggLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEK 169
Cdd:TIGR03137  84 DTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVAA 160

                         170       180
                  ....*....|....*....|.
gi 1831508098 170 H-GEVCPAGWTPGSDTIKPGV 189
Cdd:TIGR03137 161 HpGEVCPAKWKEGAETLKPSL 181
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
5-188 1.16e-63

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 196.42  E-value: 1.16e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098   5 MSKAFIGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFS 84
Cdd:NF040737   33 MMMIKVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  85 HLAWINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAF 164
Cdd:NF040737  113 HKMWNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAF 192

                         170       180
                  ....*....|....*....|....*.
gi 1831508098 165 QFVE--KHGEVCPAGWTPGSDTIKPG 188
Cdd:NF040737  193 QHVRetKGTEATPSGWQPGKPTLKPG 218
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 10-143 3.43e-49

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: 155.85  E-value: 3.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFKtqaVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWI 89
Cdd:pfam00578   1 VGDKAPDFE---LPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1831508098  90 NQPrkhgglgEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQI 143
Cdd:pfam00578  78 EKY-------GLPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 10-181 2.33e-117

Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure.


Pssm-ID: 239313  Cd Length: 173  Bit Score: 330.24  E-value: 2.33e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFKTQAVV-DGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAW 88
Cdd:cd03015     1 VGKKAPDFKATAVVpNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  89 INQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVE 168
Cdd:cd03015    81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                         170
                  ....*....|...
gi 1831508098 169 KHGEVCPAGWTPG 181
Cdd:cd03015   161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
10-199 2.69e-111

Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];


Pssm-ID: 440219  Cd Length: 196  Bit Score: 315.86  E-value: 2.69e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWI 89
Cdd:COG0450     5 IGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAWH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  90 NQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEK 169
Cdd:COG0450    85 ETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFVDK 164

                         170       180       190
                  ....*....|....*....|....*....|
gi 1831508098 170 HGEVCPAGWTPGSDTIKPGVKESQEYFKKH 199
Cdd:COG0450   165 HGEVCPANWKPGDKVIIPPPDLVGKALERF 194
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 8-196 3.71e-100

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 287.96  E-value: 3.71e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098   8 AFIGKPAPQFKTQAVV-DGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHL 86
Cdd:PTZ00253    6 AKINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  87 AWINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQF 166
Cdd:PTZ00253   86 QWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQF 165

                         170       180       190
                  ....*....|....*....|....*....|
gi 1831508098 167 VEKHGEVCPAGWTPGSDTIKPGVKESQEYF 196
Cdd:PTZ00253  166 VEKHGEVCPANWKKGDPTMKPDPNKSKEGF 195
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 10-189 1.24e-64

peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one subunit of a two-subunit complex with subunit F(TIGR03140). Usually these are found as an apparent operon. The gene has been characterized in Bacteroides fragilis, where it is important in oxidative stress defense. This gene contains two invariant cysteine residues, one near the N-terminus and one near the C-terminus, each followed immediately by a proline residue. [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 211789  Cd Length: 187  Bit Score: 197.24  E-value: 1.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWI 89
Cdd:TIGR03137   4 INTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAWH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  90 NQPRKhggLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEK 169
Cdd:TIGR03137  84 DTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVAA 160

                         170       180
                  ....*....|....*....|.
gi 1831508098 170 H-GEVCPAGWTPGSDTIKPGV 189
Cdd:TIGR03137 161 HpGEVCPAKWKEGAETLKPSL 181
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
5-188 1.16e-63

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 196.42  E-value: 1.16e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098   5 MSKAFIGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFS 84
Cdd:NF040737   33 MMMIKVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  85 HLAWINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAF 164
Cdd:NF040737  113 HKMWNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAF 192

                         170       180
                  ....*....|....*....|....*.
gi 1831508098 165 QFVE--KHGEVCPAGWTPGSDTIKPG 188
Cdd:NF040737  193 QHVRetKGTEATPSGWQPGKPTLKPG 218
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 9-198 9.05e-59

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 185.15  E-value: 9.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098   9 FIGKPAPQFKTQAVVDGEFVDVSLSDY-KGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLA 87
Cdd:PTZ00137   69 LVGKLMPSFKGTALLNDDLVQFNSSDYfKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  88 WINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKeDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFV 167
Cdd:PTZ00137  149 WKELDVRQGGVSPLKFPLFSDISREVSKSFGLLR-DEGFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQFA 227

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1831508098 168 EKHGEVCPAGWTPGSDTIKPGVKESQEYFKK 198
Cdd:PTZ00137  228 EKTGNVCPVNWKQGDQAMKPDSQSVKQYLSN 258
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 13-158 4.40e-58

Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They 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 TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis.


Pssm-ID: 239269 [Multi-domain]  Cd Length: 140  Bit Score: 178.90  E-value: 4.40e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  13 PAPQFKTQAVVDGEfvdVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWINqp 92
Cdd:cd02971     1 KAPDFTLPATDGGE---VSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAE-- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831508098  93 rKHGGLgemNIPVLADTNHQISRDYGVLKEDE---GIAFRGLFIIDPSQNLRQITINDLPVGRSVDETL 158
Cdd:cd02971    76 -KEGGL---NFPLLSDPDGEFAKAYGVLIEKSaggGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
PRK15000 PRK15000
peroxiredoxin C;
9-199 9.45e-53

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 167.54  E-value: 9.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098   9 FIGKPAPQFKTQAVV-DGEFVD-VSLSDY-KGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSH 85
Cdd:PRK15000    3 LVTRQAPDFTAAAVLgSGEIVDkFNFKQHtNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  86 LAWINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQ 165
Cdd:PRK15000   83 NAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDALQ 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1831508098 166 FVEKHGEVCPAGWTPGsdtiKPGVKESQEYFKKH 199
Cdd:PRK15000  163 FHEEHGDVCPAQWEKG----KEGMNASPDGVAKY 192
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 10-187 3.71e-51

Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one conserved cysteine, which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by reducing and detoxifying hydrogen peroxide, peroxynitrite, and organic hydroperoxides. As with all other PRXs, a cysteine sulfenic acid intermediate is formed upon reaction of 1-cys PRX with its substrates. Having no resolving cysteine, the oxidized enzyme is resolved by an external small-molecule or protein reductant such as thioredoxin or glutaredoxin. Similar to typical 2-cys PRX, 1-cys PRX forms a functional dimeric unit with a B-type interface, as well as a decameric structure which is stabilized in the reduced form of the enzyme. Other oligomeric forms, tetramers and hexamers, have also been reported. Mammalian 1-cys PRX is localized cellularly in the cytosol and is expressed at high levels in brain, eye, testes and lung. The seed-specific plant 1-cys PRXs protect tissues from reactive oxygen species during desiccation and are also called rehydrins.


Pssm-ID: 239314  Cd Length: 203  Bit Score: 163.48  E-value: 3.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFKtqavVDGEFVDVSLSDYKG-KYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAW 88
Cdd:cd03016     1 LGDTAPNFE----ADTTHGPIKFHDYLGdSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  89 INQPRKHGGlGEMNIPVLADTNHQISRDYGVLKEDEGIAF--RGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQF 166
Cdd:cd03016    77 IEDIEEYTG-VEIPFPIIADPDREVAKLLGMIDPDAGSTLtvRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQL 155

                         170       180
                  ....*....|....*....|.
gi 1831508098 167 VEKHGEVCPAGWTPGSDTIKP 187
Cdd:cd03016   156 TDKHKVATPANWKPGDDVIVP 176
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 10-143 3.43e-49

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: 155.85  E-value: 3.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFKtqaVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWI 89
Cdd:pfam00578   1 VGDKAPDFE---LPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1831508098  90 NQPrkhgglgEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQI 143
Cdd:pfam00578  78 EKY-------GLPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
PRK13189 PRK13189
peroxiredoxin; Provisional
 1-189 3.76e-49

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 158.99  E-value: 3.76e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098   1 MYRQMSKAFIGKPAPQFKtqavVDGEFVDVSLSD-YKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAAST 79
Cdd:PRK13189    2 EYEEIRMPLIGDKFPEFE----VKTTHGPIKLPDdYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  80 DSVFSHLAWINQPRKHGGLgEMNIPVLADTNHQISRDYGVLKEDEG-IAFRGLFIIDPSQNLRQITINDLPVGRSVDETL 158
Cdd:PRK13189   78 DQVFSHIKWVEWIKEKLGV-EIEFPIIADDRGEIAKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEIL 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1831508098 159 RLVQAFQFVEKHGEVCPAGWTPGsDTIKPGV 189
Cdd:PRK13189  157 RLVKALQTSDEKGVATPANWPPN-DLIKDKV 186
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 8-187 2.51e-48

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 155.92  E-value: 2.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098   8 AFIGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLA 87
Cdd:PRK10382    2 SLINTKIKPFKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  88 WinqprkHGG---LGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAF 164
Cdd:PRK10382   82 W------HSSsetIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAA 155

                         170       180
                  ....*....|....*....|....
gi 1831508098 165 QFVEKH-GEVCPAGWTPGSDTIKP 187
Cdd:PRK10382  156 QYVASHpGEVCPAKWKEGEATLAP 179
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 30-187 4.58e-46

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 150.77  E-value: 4.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  30 VSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWINQPRKHGGLgEMNIPVLADT 109
Cdd:PRK13190   20 IDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWLRDIEERFGI-KIPFPVIADI 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831508098 110 NHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEKHGEVCPAGWTPGSDTIKP 187
Cdd:PRK13190   99 DKELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQVNWKRKVATPANWQPGQEGIVP 176
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 34-178 9.60e-35

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 121.88  E-value: 9.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  34 DYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWINQPRKHGGLgEMNIPVLADTNHQI 113
Cdd:PRK13191   30 DYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMWIEKNLKV-EVPFPIIADPMGNV 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831508098 114 SRDYGVLKEDEGIA-FRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEKHGEVCPAGW 178
Cdd:PRK13191  109 AKRLGMIHAESSTAtVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLVDKAGVVTPANW 174
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 10-159 3.07e-34

Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective 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. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers.


Pssm-ID: 239316 [Multi-domain]  Cd Length: 149  Bit Score: 118.53  E-value: 3.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFktqAVVDGEFVDVSLSDYKG-KYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAW 88
Cdd:cd03018     3 VGDKAPDF---ELPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAW 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831508098  89 inqpRKHGGLgemNIPVLADTNHQ--ISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRS---VDETLR 159
Cdd:cd03018    80 ----AEENGL---TFPLLSDFWPHgeVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDlpdYDEALD 148
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 12-159 3.73e-34

Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.


Pssm-ID: 239315  Cd Length: 140  Bit Score: 118.03  E-value: 3.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  12 KPAPQFKTQAVvDGEfvDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWINq 91
Cdd:cd03017     1 DKAPDFTLPDQ-DGE--TVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAE- 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831508098  92 prKHGglgeMNIPVLADTNHQISRDYGVLKEDE---GIAFRGLFIIDPSQNLRQItINDLPVGRSVDETLR 159
Cdd:cd03017    77 --KYG----LPFPLLSDPDGKLAKAYGVWGEKKkkyMGIERSTFLIDPDGKIVKV-WRKVKPKGHAEEVLE 140
PRK13599 PRK13599
peroxiredoxin;
16-189 5.02e-31

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 112.50  E-value: 5.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  16 QFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWINQPRKH 95
Cdd:PRK13599    7 KFPSMEVVTTQGVKRLPEDYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  96 GGLgEMNIPVLADTNHQISRDYGVLKEDEGI-AFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEKHGEVC 174
Cdd:PRK13599   87 TNI-AIPFPVIADDLGKVSNQLGMIHPGKGTnTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQYGVAL 165

                         170
                  ....*....|....*
gi 1831508098 175 PAGWtPGSDTIKPGV 189
Cdd:PRK13599  166 PEKW-PNNYLIKDHV 179
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
14-159 1.44e-29

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 106.10  E-value: 1.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  14 APQFKTQAVvDGEfvDVSLSDYKGKYVVLFFYPlDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWInqpR 93
Cdd:COG1225     1 APDFTLPDL-DGK--TVSLSDLRGKPVVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFA---E 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831508098  94 KHGglgeMNIPVLADTNHQISRDYGVLkedegiAFRGLFIIDPSQNLRQITINDLPVGRSVDETLR 159
Cdd:COG1225    74 KYG----LPFPLLSDPDGEVAKAYGVR------GTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 10-147 1.27e-15

Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing peroxidatic and resolving cysteines, similar to the homodimeric thiol specific antioxidant (TSA) protein also known as TRX-dependent thiol peroxidase (Tpx). Tpx is a bacterial periplasmic peroxidase which differs from other PRXs in that it shows substrate specificity toward alkyl hydroperoxides over hydrogen peroxide. As with all other PRXs, the peroxidatic cysteine (N-terminal) of Tpx is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Tpx is able to resolve this intermediate by forming an intramolecular disulfide bond with a conserved C-terminal cysteine (the resolving cysteine), which can then be reduced by thioredoxin. This differs from the typical 2-cys PRX which resolves the oxidized cysteine by forming an intermolecular disulfide bond with the resolving cysteine from the other subunit of the homodimer. Atypical 2-cys PRX homodimers have a loop-based interface (A-type for alternate), in contrast with the B-type interface of typical 2-cys and 1-cys PRXs.


Pssm-ID: 239312 [Multi-domain]  Cd Length: 143  Bit Score: 70.31  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFKtqaVVDGEFVDVSLSDYKGKYVVLFFYP-LDfTFVCPTEIIAFSDRAEEFKaiNTVVLAASTDSVFSHLAW 88
Cdd:cd03014     2 VGDKAPDFT---LVTSDLSEVSLADFAGKVKVISVFPsID-TPVCATQTKRFNKEAAKLD--NTVVLTISADLPFAQKRW 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  89 InqprkhGGLGEMNIPVLADTN-HQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITIND 147
Cdd:cd03014    76 C------GAEGVDNVTTLSDFRdHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYVELVP 129
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 11-135 1.07e-14

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 68.17  E-value: 1.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  11 GKPAPQFKTQAVvDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKA--INTVVLAASTDSVFSHLAW 88
Cdd:pfam08534   3 GDKAPDFTLPDA-ATDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEkgVDVVAVNSDNDAFFVKRFW 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831508098  89 inqpRKHGGlgemNIPVLADTNHQISRDYGV-LKED--EGIAFRGLFIID 135
Cdd:pfam08534  82 ----GKEGL----PFPFLSDGNAAFTKALGLpIEEDasAGLRSPRYAVID 123
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 5-143 3.55e-13

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 64.19  E-value: 3.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098   5 MSKAFIGKPAPQFKTQAVvDGEFVdvSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFS 84
Cdd:PRK09437    1 MNPLKAGDIAPKFSLPDQ-DGEQV--SLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831508098  85 HLAWINQPrkhgglgEMNIPVLADTNHQISRDYGVL-------KEDEGIaFRGLFIIDPSQNLRQI 143
Cdd:PRK09437   78 LSRFAEKE-------LLNFTLLSDEDHQVAEQFGVWgekkfmgKTYDGI-HRISFLIDADGKIEHV 135
tpx PRK00522
thiol peroxidase;
10-141 4.39e-11

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 58.76  E-value: 4.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFKtqaVVDGEFVDVSLSDYKGKYVVLFFYP-LDfTFVCPTEIIAFSDRAEEFKaiNTVVLAASTDSVFSHLAW 88
Cdd:PRK00522   20 VGDKAPDFT---LVANDLSDVSLADFAGKRKVLNIFPsID-TGVCATSVRKFNQEAAELD--NTVVLCISADLPFAQKRF 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831508098  89 InqprkhGGLGEMNIPVLAD-TNHQISRDYGVLKEDE---GIAFRGLFIIDPSQNLR 141
Cdd:PRK00522   94 C------GAEGLENVITLSDfRDHSFGKAYGVAIAEGplkGLLARAVFVLDENNKVV 144
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 163-198 1.28e-10

C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols. The C-terminal domain is crucial for providing the extra cysteine necessary for dimerization of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine, upstream of this domain; and glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulfide to the sulfhydryl and consequent activation of the enzyme. The domain is associated with family AhpC-TSA, pfam00578, which carries the catalytic cysteine.


Pssm-ID: 431271  Cd Length: 40  Bit Score: 54.13  E-value: 1.28e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1831508098 163 AFQFVEKHGEVCPAGWTPGSDTIKPGVKE----SQEYFKK 198
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIVPPPATqeeaVKRYLEG 40
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 10-141 4.22e-07

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 47.38  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  10 IGKPAPQFktqAVVDGEFVDVSLSDYKGKYVVLFFY-----PldftfvCPTEIIAFSDRAEEFKAINtvVLAASTDSvfS 84
Cdd:COG0526     4 VGKPAPDF---TLTDLDGKPLSLADLKGKPVLVNFWatwcpP------CRAEMPVLKELAEEYGGVV--FVGVDVDE--N 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  85 HLAWINQPRKHGglgeMNIPVLADTNHQISRDYGVlkedegiafRGL---FIIDPSQNLR 141
Cdd:COG0526    71 PEAVKAFLKELG----LPYPVLLDPDGELAKAYGV---------RGIpttVLIDKDGKIV 117
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 30-143 1.02e-05

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 42.99  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098  30 VSLSDYKGKYVVLFFY-----PldftfvCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSH--LAWInqpRKHGglgeMN 102
Cdd:cd02966    12 VSLSDLKGKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAavKAFL---KKYG----IT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1831508098 103 IPVLADTNHQISRDYGVlkedegiafRGL---FIIDPSQNLRQI 143
Cdd:cd02966    79 FPVLLDPDGELAKAYGV---------RGLpttFLIDRDGRIRAR 113
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
1-119 6.58e-04

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 38.83  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508098   1 MYRQMSKAFIGKPAPQFktqAVVDGEFVDVSLSDYKGKYVVLFFYPldfTFV--CPTEIIAFSDRAEEFKAINTVVLAAS 78
Cdd:PRK03147   28 FFADKEKVQVGKEAPNF---VLTDLEGKKIELKDLKGKGVFLNFWG---TWCkpCEKEMPYMNELYPKYKEKGVEIIAVN 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1831508098  79 TDSvfSHLAWINQPRKHGglgeMNIPVLADTNHQISRDYGV 119
Cdd:PRK03147  102 VDE--TELAVKNFVNRYG----LTFPVAIDKGRQVIDAYGV 136
 
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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