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Conserved domains on  [gi|1721911867|ref|XP_030206490|]
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peroxiredoxin-2 [Gadus morhua]

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 ...
 8-179 1.28e-120

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: 338.33  E-value: 1.28e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   8 IGKPAPAFTTTAVVN-GEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAW 86
Cdd:cd03015     1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  87 INTPRKQGGLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQHTD 166
Cdd:cd03015    81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                         170
                  ....*....|...
gi 1721911867 167 KFGEVCPAGWKPG 179
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 ...
 8-179 1.28e-120

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: 338.33  E-value: 1.28e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   8 IGKPAPAFTTTAVVN-GEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAW 86
Cdd:cd03015     1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  87 INTPRKQGGLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQHTD 166
Cdd:cd03015    81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                         170
                  ....*....|...
gi 1721911867 167 KFGEVCPAGWKPG 179
Cdd:cd03015   161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
5-196 6.67e-113

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 319.71  E-value: 6.67e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   5 SAQIGKPAPAFTTTAVVNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHL 84
Cdd:COG0450     2 MPLIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  85 AWINTPRKQGGLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQH 164
Cdd:COG0450    82 AWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQF 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1721911867 165 TDKFGEVCPAGWKPGNDTIVPDIKKSKEFFSK 196
Cdd:COG0450   162 VDKHGEVCPANWKPGDKVIIPPPDLVGKALER 193
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 1-195 1.52e-106

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 304.13  E-value: 1.52e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   1 MSAGSAQIGKPAPAFTTTAVV-NGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDS 79
Cdd:PTZ00253    1 MSCGDAKINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  80 QFSHLAWINTPRKQGGLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLV 159
Cdd:PTZ00253   81 EYAHLQWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLL 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1721911867 160 QAFQHTDKFGEVCPAGWKPGNDTIVPDIKKSKEFFS 195
Cdd:PTZ00253  161 EAFQFVEKHGEVCPANWKKGDPTMKPDPNKSKEGFF 196
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 8-187 3.83e-63

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: 193.39  E-value: 3.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   8 IGKPAPAFTTTAVVNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAWI 87
Cdd:TIGR03137   4 INTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAWH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  88 NTPRKqggLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQHTDK 167
Cdd:TIGR03137  84 DTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVAA 160

                         170       180
                  ....*....|....*....|.
gi 1721911867 168 F-GEVCPAGWKPGNDTIVPDI 187
Cdd:TIGR03137 161 HpGEVCPAKWKEGAETLKPSL 181
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
6-185 4.78e-62

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 192.18  E-value: 4.78e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   6 AQIGKPAPAFTTTAVVNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLA 85
Cdd:NF040737   36 IKVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  86 WINTPRKQGGLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQHT 165
Cdd:NF040737  116 WNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQHV 195

                         170       180
                  ....*....|....*....|..
gi 1721911867 166 --DKFGEVCPAGWKPGNDTIVP 185
Cdd:NF040737  196 reTKGTEATPSGWQPGKPTLKP 217
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 8-141 1.63e-52

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: 164.32  E-value: 1.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   8 IGKPAPAFTttaVVNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAWI 87
Cdd:pfam00578   1 VGDKAPDFE---LPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1721911867  88 NTPRkqgglgpMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQI 141
Cdd:pfam00578  78 EKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 8-179 1.28e-120

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: 338.33  E-value: 1.28e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   8 IGKPAPAFTTTAVVN-GEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAW 86
Cdd:cd03015     1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  87 INTPRKQGGLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQHTD 166
Cdd:cd03015    81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                         170
                  ....*....|...
gi 1721911867 167 KFGEVCPAGWKPG 179
Cdd:cd03015   161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
5-196 6.67e-113

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 319.71  E-value: 6.67e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   5 SAQIGKPAPAFTTTAVVNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHL 84
Cdd:COG0450     2 MPLIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  85 AWINTPRKQGGLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQH 164
Cdd:COG0450    82 AWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQF 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1721911867 165 TDKFGEVCPAGWKPGNDTIVPDIKKSKEFFSK 196
Cdd:COG0450   162 VDKHGEVCPANWKPGDKVIIPPPDLVGKALER 193
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 1-195 1.52e-106

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 304.13  E-value: 1.52e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   1 MSAGSAQIGKPAPAFTTTAVV-NGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDS 79
Cdd:PTZ00253    1 MSCGDAKINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  80 QFSHLAWINTPRKQGGLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLV 159
Cdd:PTZ00253   81 EYAHLQWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLL 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1721911867 160 QAFQHTDKFGEVCPAGWKPGNDTIVPDIKKSKEFFS 195
Cdd:PTZ00253  161 EAFQFVEKHGEVCPANWKKGDPTMKPDPNKSKEGFF 196
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 5-197 2.24e-63

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 196.71  E-value: 2.24e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   5 SAQIGKPAPAFTTTAVVNGEFKDVSLSSY-QGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSH 83
Cdd:PTZ00137   67 SSLVGKLMPSFKGTALLNDDLVQFNSSDYfKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSH 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  84 LAWINTPRKQGGLGPMNIPLLADLTHSISRDYGVLKeDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQ 163
Cdd:PTZ00137  147 KAWKELDVRQGGVSPLKFPLFSDISREVSKSFGLLR-DEGFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQ 225

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1721911867 164 HTDKFGEVCPAGWKPGNDTIVPDIKKSKEFFSKQ 197
Cdd:PTZ00137  226 FAEKTGNVCPVNWKQGDQAMKPDSQSVKQYLSNR 259
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 8-187 3.83e-63

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: 193.39  E-value: 3.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   8 IGKPAPAFTTTAVVNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAWI 87
Cdd:TIGR03137   4 INTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAWH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  88 NTPRKqggLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQHTDK 167
Cdd:TIGR03137  84 DTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVAA 160

                         170       180
                  ....*....|....*....|.
gi 1721911867 168 F-GEVCPAGWKPGNDTIVPDI 187
Cdd:TIGR03137 161 HpGEVCPAKWKEGAETLKPSL 181
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
6-185 4.78e-62

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 192.18  E-value: 4.78e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   6 AQIGKPAPAFTTTAVVNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLA 85
Cdd:NF040737   36 IKVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  86 WINTPRKQGGLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQHT 165
Cdd:NF040737  116 WNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQHV 195

                         170       180
                  ....*....|....*....|..
gi 1721911867 166 --DKFGEVCPAGWKPGNDTIVP 185
Cdd:NF040737  196 reTKGTEATPSGWQPGKPTLKP 217
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 11-156 4.35e-59

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: 181.59  E-value: 4.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  11 PAPAFTTTAVVngeFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAWINTP 90
Cdd:cd02971     1 KAPDFTLPATD---GGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721911867  91 RKqgglgpMNIPLLADLTHSISRDYGVLKEDQ---GIAYRGLFVIDDKGILRQITINDLPVGRSVDETL 156
Cdd:cd02971    78 GG------LNFPLLSDPDGEFAKAYGVLIEKSaggGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
PRK15000 PRK15000
peroxiredoxin C;
8-181 1.09e-58

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 182.95  E-value: 1.09e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   8 IGKPAPAFTTTAVV-NGEF-KDVSLSSY-QGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHL 84
Cdd:PRK15000    4 VTRQAPDFTAAAVLgSGEIvDKFNFKQHtNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  85 AWINTPRKQGGLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQH 164
Cdd:PRK15000   84 AWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDALQF 163

                         170
                  ....*....|....*..
gi 1721911867 165 TDKFGEVCPAGWKPGND 181
Cdd:PRK15000  164 HEEHGDVCPAQWEKGKE 180
PRK13189 PRK13189
peroxiredoxin; Provisional
 7-192 4.32e-53

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 169.01  E-value: 4.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   7 QIGKPAPAFTttavVNGEFKDVSLSS-YQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLA 85
Cdd:PRK13189   10 LIGDKFPEFE----VKTTHGPIKLPDdYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  86 WINTPRKQGGLgPMNIPLLADLTHSISRDYGVLKEDQG-IAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQH 164
Cdd:PRK13189   86 WVEWIKEKLGV-EIEFPIIADDRGEIAKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQT 164

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1721911867 165 TDKFGEVCPAGWKPGN----DTIVP------DIKKSKE 192
Cdd:PRK13189  165 SDEKGVATPANWPPNDlikdKVIVPpassveEAKKRLE 202
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 8-141 1.63e-52

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: 164.32  E-value: 1.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   8 IGKPAPAFTttaVVNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAWI 87
Cdd:pfam00578   1 VGDKAPDFE---LPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1721911867  88 NTPRkqgglgpMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQI 141
Cdd:pfam00578  78 EKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 8-197 1.78e-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: 164.25  E-value: 1.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   8 IGKPAPAFT--TTavvNGEFKdvsLSSYQG-KYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHL 84
Cdd:cd03016     1 LGDTAPNFEadTT---HGPIK---FHDYLGdSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  85 AWINTPRKQGGlGPMNIPLLADLTHSISRDYGVLKEDQGI--AYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAF 162
Cdd:cd03016    75 KWIEDIEEYTG-VEIPFPIIADPDREVAKLLGMIDPDAGStlTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDAL 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1721911867 163 QHTDKFGEVCPAGWKPGNDTIVP---DIKKSKEFFSKQ 197
Cdd:cd03016   154 QLTDKHKVATPANWKPGDDVIVPpsvSDEEAKKKFPKG 191
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-187 8.23e-49

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 157.07  E-value: 8.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   1 MSAGSAQIgKPapaFTTTAVVNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQ 80
Cdd:PRK10382    1 MSLINTKI-KP---FKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  81 FSHLAWINTPRKqggLGPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQ 160
Cdd:PRK10382   77 FTHKAWHSSSET---IAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIK 153

                         170       180
                  ....*....|....*....|....*...
gi 1721911867 161 AFQHTDKF-GEVCPAGWKPGNDTIVPDI 187
Cdd:PRK10382  154 AAQYVASHpGEVCPAKWKEGEATLAPSL 181
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 8-185 4.03e-44

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 145.77  E-value: 4.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   8 IGKPAPAFTttavVNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAWI 87
Cdd:PRK13190    4 LGQKAPDFT----VNTTKGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  88 NTPRKQGGLgPMNIPLLADLTHSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQHTDK 167
Cdd:PRK13190   80 RDIEERFGI-KIPFPVIADIDKELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQVNWK 158

                         170
                  ....*....|....*...
gi 1721911867 168 FGEVCPAGWKPGNDTIVP 185
Cdd:PRK13190  159 RKVATPANWQPGQEGIVP 176
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 33-183 1.34e-36

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 126.88  E-value: 1.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  33 YQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAWINTPRKQGGLgPMNIPLLADLTHSIS 112
Cdd:PRK13191   31 YKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMWIEKNLKV-EVPFPIIADPMGNVA 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721911867 113 RDYGVLKEDQGIA-YRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQHTDKFGEVCPAGWkPGNDTI 183
Cdd:PRK13191  110 KRLGMIHAESSTAtVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLVDKAGVVTPANW-PNNELI 180
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 7-157 2.76e-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: 118.92  E-value: 2.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   7 QIGKPAPAFTttaVVNGEFKDVSLSSYQG-KYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLA 85
Cdd:cd03018     2 EVGDKAPDFE---LPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721911867  86 WintpRKQGGLgpmNIPLLADL-TH-SISRDYGVLKEDQGIAYRGLFVIDDKGILRQITINDLPVGRS---VDETLR 157
Cdd:cd03018    79 W----AEENGL---TFPLLSDFwPHgEVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDlpdYDEALD 148
PRK13599 PRK13599
peroxiredoxin;
33-180 1.73e-33

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 118.66  E-value: 1.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  33 YQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAWINTPRKQGGLgPMNIPLLADLTHSIS 112
Cdd:PRK13599   26 YAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNTNI-AIPFPVIADDLGKVS 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721911867 113 RDYGVLKEDQGI-AYRGLFVIDDKGILRQITINDLPVGRSVDETLRLVQAFQHTDKFGEVCPAGWkPGN 180
Cdd:PRK13599  105 NQLGMIHPGKGTnTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQYGVALPEKW-PNN 172
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 10-157 2.71e-33

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: 115.72  E-value: 2.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  10 KPAPAFTTTavvNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAWINt 89
Cdd:cd03017     1 DKAPDFTLP---DQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAE- 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721911867  90 prKQGglgpMNIPLLADLTHSISRDYGVLKEDQ---GIAYRGLFVIDDKGILRQItINDLPVGRSVDETLR 157
Cdd:cd03017    77 --KYG----LPFPLLSDPDGKLAKAYGVWGEKKkkyMGIERSTFLIDPDGKIVKV-WRKVKPKGHAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
12-157 8.81e-30

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 106.87  E-value: 8.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  12 APAFTTTAVvNGefKDVSLSSYQGKYVILFFYPlDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSHLAWIntpR 91
Cdd:COG1225     1 APDFTLPDL-DG--KTVSLSDLRGKPVVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFA---E 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721911867  92 KQGglgpMNIPLLADLTHSISRDYGVLKEdqgiayRGLFVIDDKGILRQITINDLPVGRSVDETLR 157
Cdd:COG1225    74 KYG----LPFPLLSDPDGEVAKAYGVRGT------PTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 7-139 1.98e-17

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 75.10  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   7 QIGKPAPAFTTTAVvNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLG--ASTDSQFSHL 84
Cdd:pfam08534   1 KAGDKAPDFTLPDA-ATDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAvnSDNDAFFVKR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1721911867  85 AWintprKQGGLgpmNIPLLADLTHSISRDYGV-LKED--QGIAYRGLFVIDDKGILR 139
Cdd:pfam08534  80 FW-----GKEGL---PFPFLSDGNAAFTKALGLpIEEDasAGLRSPRYAVIDEDGKVV 129
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 7-145 5.93e-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: 68.38  E-value: 5.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   7 QIGKPAPAFTttaVVNGEFKDVSLSSYQGKYVILFFYP-LDfTFVCPTEIVAFSDRAEEFRKIgcEVLGASTDSQFSHLA 85
Cdd:cd03014     1 KVGDKAPDFT---LVTSDLSEVSLADFAGKVKVISVFPsID-TPVCATQTKRFNKEAAKLDNT--VVLTISADLPFAQKR 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721911867  86 WINTPrkqgglGPMNIPLLADL-THSISRDYGVLKEDQGIAYRGLFVIDDKGILRQITIND 145
Cdd:cd03014    75 WCGAE------GVDNVTTLSDFrDHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYVELVP 129
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 7-141 3.44e-14

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 66.88  E-value: 3.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   7 QIGKPAPAFTttaVVNGEFKDVSLSSYQGKYVILFFYPLDFTFVCPTEIVAFSDRAEEFRKIGCEVLGASTD-----SQF 81
Cdd:PRK09437    5 KAGDIAPKFS---LPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDkpeklSRF 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721911867  82 ShlawintpRKQGglgpMNIPLLADLTHSISRDYGVLKEDQ--GIAYRGL----FVIDDKGILRQI 141
Cdd:PRK09437   82 A--------EKEL----LNFTLLSDEDHQVAEQFGVWGEKKfmGKTYDGIhrisFLIDADGKIEHV 135
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 161-196 8.15e-12

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: 57.60  E-value: 8.15e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1721911867 161 AFQHTDKFGEVCPAGWKPGNDTIVPDIK----KSKEFFSK 196
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIVPPPAtqeeAVKRYLEG 40
tpx PRK00522
thiol peroxidase;
7-133 1.21e-09

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 54.91  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   7 QIGKPAPAFTttaVVNGEFKDVSLSSYQGKYVILFFYP-LDfTFVCPTEIVAFSDRAEEFRkiGCEVLGASTDSQFSHLA 85
Cdd:PRK00522   19 QVGDKAPDFT---LVANDLSDVSLADFAGKRKVLNIFPsID-TGVCATSVRKFNQEAAELD--NTVVLCISADLPFAQKR 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1721911867  86 WIntprkqGGLGPMNIPLLADL-THSISRDYGVLKEDQ---GIAYRGLFVID 133
Cdd:PRK00522   93 FC------GAEGLENVITLSDFrDHSFGKAYGVAIAEGplkGLLARAVFVLD 138
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 14-141 1.61e-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: 42.61  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  14 AFTTTAVvngEFKDVSLSSYQGKYVILFFY-----PldftfvCPTEIVAFSDRAEEFRKIGCEVLGASTDSQFSH--LAW 86
Cdd:cd02966     1 DFSLPDL---DGKPVSLSDLKGKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAavKAF 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1721911867  87 IntprKQGGLgpmNIPLLADLTHSISRDYGVlkedqgiayRGL---FVIDDKGILRQI 141
Cdd:cd02966    72 L----KKYGI---TFPVLLDPDGELAKAYGV---------RGLpttFLIDRDGRIRAR 113
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 9-146 9.77e-04

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: 38.37  E-value: 9.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867   9 GKPAPAFTTTAVVNGEFkdvSLSSYQ-GKYVILFFypldFTFVCP------TEIVAFsdrAEEFRKIGCEVLGASTDSQF 81
Cdd:cd02969     1 GSPAPDFSLPDTDGKTY---SLADFAdGKALVVMF----ICNHCPyvkaieDRLNRL---AKEYGAKGVAVVAINSNDIE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721911867  82 SH--------LAWIntprKQGGLgpmNIPLLADLTHSISRDYG--------VLKEDQGIAYRGlfVIDD--KGILRQITI 143
Cdd:cd02969    71 AYpedspenmKAKA----KEHGY---PFPYLLDETQEVAKAYGaactpdffLFDPDGKLVYRG--RIDDsrPGNDPPVTG 141


                  ...
gi 1721911867 144 NDL 146
Cdd:cd02969   142 RDL 144
 
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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