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Conserved domains on  [gi|5453549|ref|NP_006397|]
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peroxiredoxin-4 precursor [Homo sapiens]

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
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 ...
 81-252 3.82e-114

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: 325.23  E-value: 3.82e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   81 ISKPAPYWEGTAVI-DGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAW 159
Cdd:cd03015   1 VGKKAPDFKATAVVpNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549  160 INTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTD 239
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 5453549  240 KHGEVCPAGWKPG 252
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 ...
 81-252 3.82e-114

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: 325.23  E-value: 3.82e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   81 ISKPAPYWEGTAVI-DGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAW 159
Cdd:cd03015   1 VGKKAPDFKATAVVpNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549  160 INTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTD 239
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 5453549  240 KHGEVCPAGWKPG 252
Cdd:cd03015 161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
80-271 4.90e-105

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 303.15  E-value: 4.90e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   80 KISKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAW 159
Cdd:COG0450   4 LIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAW 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549  160 INTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTD 239
Cdd:COG0450  84 HETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFVD 163

                       170       180       190
                ....*....|....*....|....*....|..
gi 5453549  240 KHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN 271
Cdd:COG0450 164 KHGEVCPANWKPGDKVIIPPPDLVGKALERFP 195
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 79-267 6.22e-93

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 272.55  E-value: 6.22e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549    79 AKISKPAPYWEGTAVI-DGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHL 157
Cdd:PTZ00253   6 AKINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   158 AWINTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQY 237
Cdd:PTZ00253  86 QWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQF 165

                        170       180       190
                 ....*....|....*....|....*....|
gi 5453549   238 TDKHGEVCPAGWKPGSETIIPDPAGKLKYF 267
Cdd:PTZ00253 166 VEKHGEVCPANWKKGDPTMKPDPNKSKEGF 195
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
79-263 2.51e-59

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 188.33  E-value: 2.51e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549    79 AKISKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLA 158
Cdd:NF040737  36 IKVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKM 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   159 WINTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYT 238
Cdd:NF040737 116 WNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQHV 195

                        170       180
                 ....*....|....*....|....*....
gi 5453549   239 --DKHGEVCPAGWKPGSETIIPDP--AGK 263
Cdd:NF040737 196 reTKGTEATPSGWQPGKPTLKPGPdlVGK 224
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 81-264 3.36e-59

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: 186.45  E-value: 3.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549     81 ISKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWI 160
Cdd:TIGR03137   4 INTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAWH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549    161 NTPRRqggLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDK 240
Cdd:TIGR03137  84 DTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVAA 160

                         170       180
                  ....*....|....*....|....*..
gi 5453549    241 H-GEVCPAGWKPGSETIIP--DPAGKL 264
Cdd:TIGR03137 161 HpGEVCPAKWKEGAETLKPslDLVGKI 187
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 81-214 2.69e-45

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: 148.53  E-value: 2.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549     81 ISKPAPYWEGTaviDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWI 160
Cdd:pfam00578   1 VGDKAPDFELP---DGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 5453549    161 NTPRrqgglgpIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQI 214
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 ...
 81-252 3.82e-114

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: 325.23  E-value: 3.82e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   81 ISKPAPYWEGTAVI-DGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAW 159
Cdd:cd03015   1 VGKKAPDFKATAVVpNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549  160 INTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTD 239
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 5453549  240 KHGEVCPAGWKPG 252
Cdd:cd03015 161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
80-271 4.90e-105

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 303.15  E-value: 4.90e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   80 KISKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAW 159
Cdd:COG0450   4 LIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAW 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549  160 INTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTD 239
Cdd:COG0450  84 HETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFVD 163

                       170       180       190
                ....*....|....*....|....*....|..
gi 5453549  240 KHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN 271
Cdd:COG0450 164 KHGEVCPANWKPGDKVIIPPPDLVGKALERFP 195
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 79-267 6.22e-93

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 272.55  E-value: 6.22e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549    79 AKISKPAPYWEGTAVI-DGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHL 157
Cdd:PTZ00253   6 AKINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   158 AWINTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQY 237
Cdd:PTZ00253  86 QWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQF 165

                        170       180       190
                 ....*....|....*....|....*....|
gi 5453549   238 TDKHGEVCPAGWKPGSETIIPDPAGKLKYF 267
Cdd:PTZ00253 166 VEKHGEVCPANWKKGDPTMKPDPNKSKEGF 195
PRK15000 PRK15000
peroxiredoxin C;
81-267 1.74e-59

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 187.58  E-value: 1.74e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549    81 ISKPAPYWEGTAVI-DGEFKE-LKLTDY-RGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHL 157
Cdd:PRK15000   4 VTRQAPDFTAAAVLgSGEIVDkFNFKQHtNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   158 AWINTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQY 237
Cdd:PRK15000  84 AWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDALQF 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 5453549   238 TDKHGEVCPAGWKPGSETIIPDPAGKLKYF 267
Cdd:PRK15000 164 HEEHGDVCPAQWEKGKEGMNASPDGVAKYL 193
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
79-263 2.51e-59

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 188.33  E-value: 2.51e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549    79 AKISKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLA 158
Cdd:NF040737  36 IKVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKM 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   159 WINTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYT 238
Cdd:NF040737 116 WNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQHV 195

                        170       180
                 ....*....|....*....|....*....
gi 5453549   239 --DKHGEVCPAGWKPGSETIIPDP--AGK 263
Cdd:NF040737 196 reTKGTEATPSGWQPGKPTLKPGPdlVGK 224
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 81-264 3.36e-59

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: 186.45  E-value: 3.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549     81 ISKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWI 160
Cdd:TIGR03137   4 INTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAWH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549    161 NTPRRqggLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDK 240
Cdd:TIGR03137  84 DTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVAA 160

                         170       180
                  ....*....|....*....|....*..
gi 5453549    241 H-GEVCPAGWKPGSETIIP--DPAGKL 264
Cdd:TIGR03137 161 HpGEVCPAKWKEGAETLKPslDLVGKI 187
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 81-269 4.11e-59

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 188.62  E-value: 4.11e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549    81 ISKPAPYWEGTAVIDGEFKELKLTDY-RGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAW 159
Cdd:PTZ00137  70 VGKLMPSFKGTALLNDDLVQFNSSDYfKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAW 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   160 INTPRRQGGLGPIRIPLLSDLTHQISKDYGVyLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTD 239
Cdd:PTZ00137 150 KELDVRQGGVSPLKFPLFSDISREVSKSFGL-LRDEGFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQFAE 228

                        170       180       190
                 ....*....|....*....|....*....|
gi 5453549   240 KHGEVCPAGWKPGSETIIPDPAGKLKYFDK 269
Cdd:PTZ00137 229 KTGNVCPVNWKQGDQAMKPDSQSVKQYLSN 258
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 93-229 3.07e-53

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: 169.27  E-value: 3.07e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   93 VIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWINTprrqggLGPI 172
Cdd:cd02971   7 LPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEK------EGGL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549  173 RIPLLSDLTHQISKDYGVYLEDS---GHTLRGLFIIDDKGILRQITLNDLPVGRSVDETL 229
Cdd:cd02971  81 NFPLLSDPDGEFAKAYGVLIEKSaggGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
PRK13189 PRK13189
peroxiredoxin; Provisional
 105-262 1.02e-46

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 155.53  E-value: 1.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   105 DYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWINTPRRQGGLgPIRIPLLSDLTHQI 184
Cdd:PRK13189  32 DYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKWVEWIKEKLGV-EIEFPIIADDRGEI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   185 SKDYGVYLEDSG-HTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGS----ETIIPd 259
Cdd:PRK13189 111 AKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQTSDEKGVATPANWPPNDlikdKVIVP- 189


                 ...
gi 5453549   260 PAG 262
Cdd:PRK13189 190 PAS 192
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 81-214 2.69e-45

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: 148.53  E-value: 2.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549     81 ISKPAPYWEGTaviDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWI 160
Cdd:pfam00578   1 VGDKAPDFELP---DGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 5453549    161 NTPRrqgglgpIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQI 214
Cdd:pfam00578  78 EKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 81-264 9.00e-45

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 149.37  E-value: 9.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549    81 ISKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWI 160
Cdd:PRK10382   4 INTKIKPFKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAWH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   161 NTPRRqggLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDK 240
Cdd:PRK10382  84 SSSET---IAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVAS 160

                        170       180
                 ....*....|....*....|....*..
gi 5453549   241 H-GEVCPAGWKPGSETIIP--DPAGKL 264
Cdd:PRK10382 161 HpGEVCPAKWKEGEATLAPslDLVGKI 187
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 102-269 9.75e-45

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: 150.00  E-value: 9.75e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549  102 KLTDYRG-KYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWINTPRRQGGlGPIRIPLLSDL 180
Cdd:cd03016  18 KFHDYLGdSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEDIEEYTG-VEIPFPIIADP 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549  181 THQISKDYGVYLEDSGHTL--RGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIP 258
Cdd:cd03016  97 DREVAKLLGMIDPDAGSTLtvRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQLTDKHKVATPANWKPGDDVIVP 176

                       170
                ....*....|....*
gi 5453549  259 ----DPAGKLKYFDK 269
Cdd:cd03016 177 psvsDEEAKKKFPKG 191
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 103-261 1.55e-41

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 141.53  E-value: 1.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   103 LTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWINTPRRQGGLgPIRIPLLSDLTH 182
Cdd:PRK13190  22 LSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWLRDIEERFGI-KIPFPVIADIDK 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5453549   183 QISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPA 261
Cdd:PRK13190 101 ELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQVNWKRKVATPANWQPGQEGIVPAPS 179
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 101-256 1.19e-38

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 134.59  E-value: 1.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   101 LKLTD-YRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWINTPRRQGGLgPIRIPLLSD 179
Cdd:PRK13191  25 IKLPDdYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMWIEKNLKV-EVPFPIIAD 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5453549   180 LTHQISKDYG-VYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWkPGSETI 256
Cdd:PRK13191 104 PMGNVAKRLGmIHAESSTATVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLVDKAGVVTPANW-PNNELI 180
PRK13599 PRK13599
peroxiredoxin;
105-249 1.95e-33

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 120.97  E-value: 1.95e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   105 DYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWINTPRRQGGLgPIRIPLLSDLTHQI 184
Cdd:PRK13599  25 DYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNTNI-AIPFPVIADDLGKV 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453549   185 SKDYGVYLEDSG-HTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGW 249
Cdd:PRK13599 104 SNQLGMIHPGKGtNTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQYGVALPEKW 169
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 80-230 9.24e-29

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: 106.97  E-value: 9.24e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   80 KISKPAPYWEgtaVIDGEFKELKLTDYRG-KYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLA 158
Cdd:cd03018   2 EVGDKAPDFE---LPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRA 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5453549  159 WintpRRQGGLgpiRIPLLSDL-TH-QISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRS---VDETLR 230
Cdd:cd03018  79 W----AEENGL---TFPLLSDFwPHgEVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDlpdYDEALD 148
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 99-230 8.68e-26

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: 98.77  E-value: 8.68e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   99 KELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWINtprRQGglgpIRIPLLS 178
Cdd:cd03017  14 ETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAE---KYG----LPFPLLS 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5453549  179 DLTHQISKDYGVYLEDSGHTL---RGLFIIDDKGILRQItLNDLPVGRSVDETLR 230
Cdd:cd03017  87 DPDGKLAKAYGVWGEKKKKYMgieRSTFLIDPDGKIVKV-WRKVKPKGHAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
85-230 2.42e-23

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 92.24  E-value: 2.42e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   85 APYWEGTAViDGefKELKLTDYRGKYLVFFFYPlDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWIntpR 164
Cdd:COG1225   1 APDFTLPDL-DG--KTVSLSDLRGKPVVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFA---E 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453549  165 RQGglgpIRIPLLSDLTHQISKDYGVYledsghTLRGLFIIDDKGILRQITLNDLPVGRSVDETLR 230
Cdd:COG1225  74 KYG----LPFPLLSDPDGEVAKAYGVR------GTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 234-269 1.90e-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: 60.30  E-value: 1.90e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 5453549    234 AFQYTDKHGEVCPAGWKPGSETIIPDPA----GKLKYFDK 269
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIVPPPAtqeeAVKRYLEG 40
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 95-220 1.35e-10

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 58.15  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549     95 DGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDS-QFTHLAWINTPrrqgglgPIR 173
Cdd:pfam08534  15 ATDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNdAFFVKRFWGKE-------GLP 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 5453549    174 IPLLSDLTHQISKDYGVYLED---SGHTLRGLFIIDDKGILRQITLNDLP 220
Cdd:pfam08534  88 FPFLSDGNAAFTKALGLPIEEdasAGLRSPRYAVIDEDGKVVYLFVGPEP 137
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 92-218 3.96e-10

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: 56.82  E-value: 3.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   92 AVIDGEFKELKLTDYRGKYLVFFFYP-LDfTFVCPTEIIAFGDRLEEFRsiNTEVVACSVDSQFTHLAWINTPrrqgglG 170
Cdd:cd03014  10 TLVTSDLSEVSLADFAGKVKVISVFPsID-TPVCATQTKRFNKEAAKLD--NTVVLTISADLPFAQKRWCGAE------G 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 5453549  171 PIRIPLLSDL-THQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLND 218
Cdd:cd03014  81 VDNVTTLSDFrDHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYVELVP 129
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 95-214 1.58e-08

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 52.63  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549    95 DGEfkELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVD-----SQFTHLAWINtprrqggl 169
Cdd:PRK09437  19 DGE--QVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDkpeklSRFAEKELLN-------- 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 5453549   170 gpirIPLLSDLTHQISKDYGVYLEDS--GHTLRGL----FIIDDKGILRQI 214
Cdd:PRK09437  89 ----FTLLSDEDHQVAEQFGVWGEKKfmGKTYDGIhrisFLIDADGKIEHV 135
tpx PRK00522
thiol peroxidase;
93-206 9.71e-04

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 39.11  E-value: 9.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549    93 VIDGEFKELKLTDYRGKYLVFFFYP-LDfTFVCPTEIIAFGDRLEEFRsiNTEVVACSVDSQFTHLAWIntprrqGGLGP 171
Cdd:PRK00522  29 LVANDLSDVSLADFAGKRKVLNIFPsID-TGVCATSVRKFNQEAAELD--NTVVLCISADLPFAQKRFC------GAEGL 99

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 5453549   172 IRIPLLSDL-THQISKDYGVYLEDS---GHTLRGLFIID 206
Cdd:PRK00522 100 ENVITLSDFrDHSFGKAYGVAIAEGplkGLLARAVFVLD 138
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 99-234 2.37e-03

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 37.57  E-value: 2.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453549   99 KELKLTDYRGKY-LVFFFYpldfTF---VCPTEIIAFG---DRLEEFRSINTEVVACSVDSQF-------THLAWINTPR 164
Cdd:COG1999  11 KPVTLADLRGKPvLVFFGY----TScpdVCPTTLANLAqvqEALGEDGGDDVQVLFISVDPERdtpevlkAYAEAFGAPR 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5453549  165 RQGGLGPiripllSDLTHQISKDYGVYLEDSG-------HTLRgLFIIDDKGILRQItlndLPVGRSVDETLRLVQA 234
Cdd:COG1999  87 WIGLTGD------PEEIAALAKAFGVYYEKVPdgdytfdHSAA-VYLVDPDGRLRGY----YPAGEDPEELAADLKA 152
 
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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