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Conserved domains on  [gi|32189392|ref|NP_005800|]
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peroxiredoxin-2 [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|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 5.20e-121

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: 339.48  E-value: 5.20e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   8 IGKPAPDFKATAVV-DGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAW 86
Cdd:cd03015   1 VGKKAPDFKATAVVpNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  87 INTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTD 166
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 32189392 167 EHGEVCPAGWKPG 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 5.20e-121

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: 339.48  E-value: 5.20e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   8 IGKPAPDFKATAVV-DGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAW 86
Cdd:cd03015   1 VGKKAPDFKATAVVpNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  87 INTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTD 166
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 32189392 167 EHGEVCPAGWKPG 179
Cdd:cd03015 161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
7-198 3.12e-116

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 328.19  E-value: 3.12e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   7 RIGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAW 86
Cdd:COG0450   4 LIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAW 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  87 INTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTD 166
Cdd:COG0450  84 HETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFVD 163

                       170       180       190
                ....*....|....*....|....*....|..
gi 32189392 167 EHGEVCPAGWKPGSDTIKPNVDDSKEYFSKHN 198
Cdd:COG0450 164 KHGEVCPANWKPGDKVIIPPPDLVGKALERFP 195
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 1-195 2.98e-103

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 295.66  E-value: 2.98e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    1 MASGNARIGKPAPDFKATAVV-DGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDS 79
Cdd:PTZ00253   1 MSCGDAKINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   80 QFTHLAWINTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLV 159
Cdd:PTZ00253  81 EYAHLQWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 32189392  160 QAFQYTDEHGEVCPAGWKPGSDTIKPNVDDSKEYFS 195
Cdd:PTZ00253 161 EAFQFVEKHGEVCPANWKKGDPTMKPDPNKSKEGFF 196
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
6-188 6.21e-67

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 204.89  E-value: 6.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    6 ARIGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLA 85
Cdd:NF040737  36 IKVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKM 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   86 WINTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYT 165
Cdd:NF040737 116 WNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQHV 195

                        170       180
                 ....*....|....*....|....*
gi 32189392  166 DEHG--EVCPAGWKPGSDTIKPNVD 188
Cdd:NF040737 196 RETKgtEATPSGWQPGKPTLKPGPD 220
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 8-188 1.19e-66

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: 202.63  E-value: 1.19e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392     8 IGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWI 87
Cdd:TIGR03137   4 INTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAWH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    88 NTPRKeggLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTDE 167
Cdd:TIGR03137  84 DTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVAA 160

                         170       180
                  ....*....|....*....|..
gi 32189392   168 H-GEVCPAGWKPGSDTIKPNVD 188
Cdd:TIGR03137 161 HpGEVCPAKWKEGAETLKPSLD 182
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 8-141 2.46e-54

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: 168.94  E-value: 2.46e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392     8 IGKPAPDFKATavvDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWI 87
Cdd:pfam00578   1 VGDKAPDFELP---DGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 32189392    88 NTPRkegglgpLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQI 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 5.20e-121

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: 339.48  E-value: 5.20e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   8 IGKPAPDFKATAVV-DGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAW 86
Cdd:cd03015   1 VGKKAPDFKATAVVpNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  87 INTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTD 166
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 32189392 167 EHGEVCPAGWKPG 179
Cdd:cd03015 161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
7-198 3.12e-116

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 328.19  E-value: 3.12e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   7 RIGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAW 86
Cdd:COG0450   4 LIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAW 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  87 INTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTD 166
Cdd:COG0450  84 HETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFVD 163

                       170       180       190
                ....*....|....*....|....*....|..
gi 32189392 167 EHGEVCPAGWKPGSDTIKPNVDDSKEYFSKHN 198
Cdd:COG0450 164 KHGEVCPANWKPGDKVIIPPPDLVGKALERFP 195
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 1-195 2.98e-103

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 295.66  E-value: 2.98e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    1 MASGNARIGKPAPDFKATAVV-DGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDS 79
Cdd:PTZ00253   1 MSCGDAKINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   80 QFTHLAWINTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLV 159
Cdd:PTZ00253  81 EYAHLQWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 32189392  160 QAFQYTDEHGEVCPAGWKPGSDTIKPNVDDSKEYFS 195
Cdd:PTZ00253 161 EAFQFVEKHGEVCPANWKKGDPTMKPDPNKSKEGFF 196
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 8-196 3.82e-67

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 206.34  E-value: 3.82e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    8 IGKPAPDFKATAVVDGAFKEVKLSDY-KGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAW 86
Cdd:PTZ00137  70 VGKLMPSFKGTALLNDDLVQFNSSDYfKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAW 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   87 INTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKtDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTD 166
Cdd:PTZ00137 150 KELDVRQGGVSPLKFPLFSDISREVSKSFGLLR-DEGFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQFAE 228

                        170       180       190
                 ....*....|....*....|....*....|
gi 32189392  167 EHGEVCPAGWKPGSDTIKPNVDDSKEYFSK 196
Cdd:PTZ00137 229 KTGNVCPVNWKQGDQAMKPDSQSVKQYLSN 258
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
6-188 6.21e-67

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 204.89  E-value: 6.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    6 ARIGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLA 85
Cdd:NF040737  36 IKVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKM 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   86 WINTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYT 165
Cdd:NF040737 116 WNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQHV 195

                        170       180
                 ....*....|....*....|....*
gi 32189392  166 DEHG--EVCPAGWKPGSDTIKPNVD 188
Cdd:NF040737 196 RETKgtEATPSGWQPGKPTLKPGPD 220
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 8-188 1.19e-66

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: 202.63  E-value: 1.19e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392     8 IGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWI 87
Cdd:TIGR03137   4 INTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAWH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    88 NTPRKeggLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTDE 167
Cdd:TIGR03137  84 DTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVAA 160

                         170       180
                  ....*....|....*....|..
gi 32189392   168 H-GEVCPAGWKPGSDTIKPNVD 188
Cdd:TIGR03137 161 HpGEVCPAKWKEGAETLKPSLD 182
PRK15000 PRK15000
peroxiredoxin C;
8-197 8.87e-66

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 200.67  E-value: 8.87e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    8 IGKPAPDFKATAVVdGAFKEVKLSDYK----GKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTH 83
Cdd:PRK15000   4 VTRQAPDFTAAAVL-GSGEIVDKFNFKqhtnGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   84 LAWINTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQ 163
Cdd:PRK15000  83 NAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDALQ 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 32189392  164 YTDEHGEVCPAGWKPGSDTIKPNVDDSKEYFSKH 197
Cdd:PRK15000 163 FHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAEN 196
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 11-156 4.16e-61

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: 186.60  E-value: 4.16e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  11 PAPDFKATAVVdgaFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWINTp 90
Cdd:cd02971   1 KAPDFTLPATD---GGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEK- 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32189392  91 rkeggLGPLNIPLLADVTRRLSEDYGVLKTDE---GIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEAL 156
Cdd:cd02971  77 -----EGGLNFPLLSDPDGEFAKAYGVLIEKSaggGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
PRK13189 PRK13189
peroxiredoxin; Provisional
 7-192 8.84e-55

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 173.63  E-value: 8.84e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    7 RIGKPAPDFKATAVvdgaFKEVKLSD-YKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLA 85
Cdd:PRK13189  10 LIGDKFPEFEVKTT----HGPIKLPDdYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   86 WINTPRKEGGLgPLNIPLLADVTRRLSEDYGVLKTDEG-IAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQY 164
Cdd:PRK13189  86 WVEWIKEKLGV-EIEFPIIADDRGEIAKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQT 164

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 32189392  165 TDEHGEVCPAGWKPGS----DTIKP---NVDDSKE 192
Cdd:PRK13189 165 SDEKGVATPANWPPNDlikdKVIVPpasSVEEAKK 199
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 8-141 2.46e-54

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: 168.94  E-value: 2.46e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392     8 IGKPAPDFKATavvDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWI 87
Cdd:pfam00578   1 VGDKAPDFELP---DGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 32189392    88 NTPRkegglgpLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQI 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 7.35e-54

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: 170.41  E-value: 7.35e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   8 IGKPAPDFKAtavvDGAFKEVKLSDYKG-KYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAW 86
Cdd:cd03016   1 LGDTAPNFEA----DTTHGPIKFHDYLGdSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKW 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  87 INTPrKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGI--AYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQY 164
Cdd:cd03016  77 IEDI-EEYTGVEIPFPIIADPDREVAKLLGMIDPDAGStlTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQL 155

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 32189392 165 TDEHGEVCPAGWKPGSDTIKP---NVDDSKEYFSKH 197
Cdd:cd03016 156 TDKHKVATPANWKPGDDVIVPpsvSDEEAKKKFPKG 191
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-188 4.93e-50

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 160.15  E-value: 4.93e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    1 MASGNARIgKPapdFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQ 80
Cdd:PRK10382   1 MSLINTKI-KP---FKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   81 FTHLAWINTPRKeggLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQ 160
Cdd:PRK10382  77 FTHKAWHSSSET---IAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIK 153

                        170       180
                 ....*....|....*....|....*....
gi 32189392  161 AFQYTDEH-GEVCPAGWKPGSDTIKPNVD 188
Cdd:PRK10382 154 AAQYVASHpGEVCPAKWKEGEATLAPSLD 182
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 7-185 2.76e-44

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 146.15  E-value: 2.76e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    7 RIGKPAPDFKatavVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAW 86
Cdd:PRK13190   3 KLGQKAPDFT----VNTTKGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   87 INTPRKEGGLgPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTD 166
Cdd:PRK13190  79 LRDIEERFGI-KIPFPVIADIDKELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQVNW 157

                        170
                 ....*....|....*....
gi 32189392  167 EHGEVCPAGWKPGSDTIKP 185
Cdd:PRK13190 158 KRKVATPANWQPGQEGIVP 176
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 7-157 5.27e-38

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: 128.16  E-value: 5.27e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   7 RIGKPAPDFkatAVVDGAFKEVKLSDYKG-KYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLA 85
Cdd:cd03018   2 EVGDKAPDF---ELPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRA 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32189392  86 WIntpRKEGglgpLNIPLLAD--VTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRS---VDEALR 157
Cdd:cd03018  79 WA---EENG----LTFPLLSDfwPHGEVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDlpdYDEALD 148
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 8-187 5.35e-37

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 127.66  E-value: 5.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    8 IGKPAPDFKatavVDGAFKEVKLSD-YKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAW 86
Cdd:PRK13191   9 IGEKFPEME----VITTHGKIKLPDdYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   87 INTPRKEGGLgPLNIPLLADVTRRLSEDYGVLKTDEGIA-YRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYT 165
Cdd:PRK13191  85 VMWIEKNLKV-EVPFPIIADPMGNVAKRLGMIHAESSTAtVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLV 163

                        170       180
                 ....*....|....*....|..
gi 32189392  166 DEHGEVCPAGWkPGSDTIKPNV 187
Cdd:PRK13191 164 DKAGVVTPANW-PNNELIGDKV 184
PRK13599 PRK13599
peroxiredoxin;
32-187 3.41e-35

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 123.28  E-value: 3.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   32 DYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWINTPRKEGGLgPLNIPLLADVTRRL 111
Cdd:PRK13599  25 DYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNTNI-AIPFPVIADDLGKV 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32189392  112 SEDYGVLKTDEGI-AYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTDEHGEVCPAGWkPGSDTIKPNV 187
Cdd:PRK13599 104 SNQLGMIHPGKGTnTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQYGVALPEKW-PNNYLIKDHV 179
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 10-157 7.59e-35

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: 119.96  E-value: 7.59e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  10 KPAPDFKATAVvDGafKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWINt 89
Cdd:cd03017   1 DKAPDFTLPDQ-DG--ETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAE- 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32189392  90 prKEGglgpLNIPLLADVTRRLSEDYGVLKTDE---GIAYRGLFIIDGKGVLRQITVNDLPVGrSVDEALR 157
Cdd:cd03017  77 --KYG----LPFPLLSDPDGKLAKAYGVWGEKKkkyMGIERSTFLIDPDGKIVKVWRKVKPKG-HAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
12-157 1.38e-33

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 116.50  E-value: 1.38e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  12 APDFKATAVvDGafKEVKLSDYKGKYVVLFFYPlDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWIntpR 91
Cdd:COG1225   1 APDFTLPDL-DG--KTVSLSDLRGKPVVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFA---E 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32189392  92 KEGglgpLNIPLLADVTRRLSEDYGVLKTdegiayRGLFIIDGKGVLRQITVNDLPVGRSVDEALR 157
Cdd:COG1225  74 KYG----LPFPLLSDPDGEVAKAYGVRGT------PTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 9-147 1.01e-16

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 73.17  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392     9 GKPAPDFKATAV-VDGafKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDS-QFTHLAW 86
Cdd:pfam08534   3 GDKAPDFTLPDAaTDG--NTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNdAFFVKRF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32189392    87 INtprKEGglgpLNIPLLADVTRRLSEDYGV---LKTDEGIAYRGLFIIDGKGVLRQITVNDLP 147
Cdd:pfam08534  81 WG---KEG----LPFPFLSDGNAAFTKALGLpieEDASAGLRSPRYAVIDEDGKVVYLFVGPEP 137
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 8-139 3.18e-14

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: 66.45  E-value: 3.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   8 IGKPAPDFKataVVDGAFKEVKLSDYKGKYVVLFFYP-LDfTFVCPTEIIAFSNRAEDFRKLgcEVLGVSVDSQFTHLAW 86
Cdd:cd03014   2 VGDKAPDFT---LVTSDLSEVSLADFAGKVKVISVFPsID-TPVCATQTKRFNKEAAKLDNT--VVLTISADLPFAQKRW 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 32189392  87 INTPrkegglGPLNIPLLAD-VTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLR 139
Cdd:cd03014  76 CGAE------GVDNVTTLSDfRDHSFGKAYGVLIKDLGLLARAVFVIDENGKVI 123
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 9-141 2.79e-12

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 61.49  E-value: 2.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    9 GKPAPDFkatAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVD-----SQFTh 83
Cdd:PRK09437   7 GDIAPKF---SLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDkpeklSRFA- 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32189392   84 lawintpRKEGglgpLNIPLLADVTRRLSEDYGVL-------KTDEGIaYRGLFIIDGKGVLRQI 141
Cdd:PRK09437  83 -------EKEL----LNFTLLSDEDHQVAEQFGVWgekkfmgKTYDGI-HRISFLIDADGKIEHV 135
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 161-196 3.50e-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: 58.37  E-value: 3.50e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 32189392   161 AFQYTDEHGEVCPAGWKPGSDTIKPNVDD----SKEYFSK 196
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIVPPPATqeeaVKRYLEG 40
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 8-139 1.34e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 54.31  E-value: 1.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   8 IGKPAPDFKATAVvDGafKEVKLSDYKGKYVVLFFYpldFTFvCPT------EIIAFSNRAEDFrklgcEVLGVSVDSQF 81
Cdd:COG0526   4 VGKPAPDFTLTDL-DG--KPLSLADLKGKPVLVNFW---ATW-CPPcraempVLKELAEEYGGV-----VFVGVDVDENP 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32189392  82 ThlAWINTPRKEGglgpLNIPLLADVTRRLSEDYGVLKTDEgiayrgLFIIDGKGVLR 139
Cdd:COG0526  72 E--AVKAFLKELG----LPYPVLLDPDGELAKAYGVRGIPT------TVLIDKDGKIV 117
tpx PRK00522
thiol peroxidase;
8-139 1.93e-08

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 51.44  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    8 IGKPAPDFKataVVDGAFKEVKLSDYKGKYVVLFFYP-LDfTFVCPTEIIAFSNRAEDFRklGCEVLGVSVDSQFTHLAW 86
Cdd:PRK00522  20 VGDKAPDFT---LVANDLSDVSLADFAGKRKVLNIFPsID-TGVCATSVRKFNQEAAELD--NTVVLCISADLPFAQKRF 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32189392   87 INTprkEGglgplniplLADVT-------RRLSEDYGVLKTDE---GIAYRGLFIIDGKGVLR 139
Cdd:PRK00522  94 CGA---EG---------LENVItlsdfrdHSFGKAYGVAIAEGplkGLLARAVFVLDENNKVV 144
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 19-141 6.56e-08

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: 49.16  E-value: 6.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  19 AVVDGAFKEVKLSDYKGKYVVLFFY-----PldftfvCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTH--LAWIntpR 91
Cdd:cd02966   3 SLPDLDGKPVSLSDLKGKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAavKAFL---K 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32189392  92 KEGglgpLNIPLLADVTRRLSEDYGVlktdegiayRGL---FIIDGKGVLRQI 141
Cdd:cd02966  74 KYG----ITFPVLLDPDGELAKAYGV---------RGLpttFLIDRDGRIRAR 113
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
6-141 2.57e-07

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 48.46  E-value: 2.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392    6 ARIGKPAPDFkatAVVDGAFKEVKLSDYKGKYVVLFFYPldfTFV--CPTEIIAFSNRAEDFRKLGCEVLGVSVDSqfTH 83
Cdd:PRK03147  35 VQVGKEAPNF---VLTDLEGKKIELKDLKGKGVFLNFWG---TWCkpCEKEMPYMNELYPKYKEKGVEIIAVNVDE--TE 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   84 LAWINTPRKEGglgpLNIPLLADVTRRLSEDYGV--LKTDegiayrglFIIDGKGVLRQI 141
Cdd:PRK03147 107 LAVKNFVNRYG----LTFPVAIDKGRQVIDAYGVgpLPTT--------FLIDKDGKVVKV 154
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 9-161 3.33e-06

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: 45.31  E-value: 3.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392   9 GKPAPDFKATAvVDGafKEVKLSDY-KGKYVVLFFypldFTFVCP------TEIIAFsnrAEDFRKLGCEVLGVSVDSQF 81
Cdd:cd02969   1 GSPAPDFSLPD-TDG--KTYSLADFaDGKALVVMF----ICNHCPyvkaieDRLNRL---AKEYGAKGVAVVAINSNDIE 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  82 TH--------LAWIntprKEGGlgpLNIPLLADVTRRLSEDYGVLKTDEgiayrgLFIIDGKGVLR---QI----TVNDL 146
Cdd:cd02969  71 AYpedspenmKAKA----KEHG---YPFPYLLDETQEVAKAYGAACTPD------FFLFDPDGKLVyrgRIddsrPGNDP 137

                       170
                ....*....|....*.
gi 32189392 147 PV-GRSVDEALRLVQA 161
Cdd:cd02969 138 PVtGRDLRAALDALLA 153
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 30-139 3.22e-05

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two 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. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 42.35  E-value: 3.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  30 LSDYKGKYVVLFFYPldfTFVCP---TEIIAFSNRAEDFRKLGCEVLGVSVDSqfthlaWINTpRKEGGLGPLNIPLLAD 106
Cdd:cd02970  18 SALLGEGPVVVVFYR---GFGCPfcrEYLRALSKLLPELDALGVELVAVGPES------PEKL-EAFDKGKFLPFPVYAD 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32189392 107 VTRRLSEDYGVLKT-----------------------DEGIAYRGLFIIDGKGVLR 139
Cdd:cd02970  88 PDRKLYRALGLVRSlpwsntpralwknaaigfrgndeGDGLQLPGVFVIGPDGTIL 143
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 26-161 1.97e-04

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 40.27  E-value: 1.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189392  26 KEVKLSDYKGKYVVLFFyplDFTF---VCPTEIIAFSNRAEDFRKLGCE---VLGVSVDSQF-------THLAWINTPRK 92
Cdd:COG1999  11 KPVTLADLRGKPVLVFF---GYTScpdVCPTTLANLAQVQEALGEDGGDdvqVLFISVDPERdtpevlkAYAEAFGAPRW 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32189392  93 EGGLGPlnipllADVTRRLSEDYGV-LKTDEGIAYR-----GLFIIDGKGVLRQItvndLPVGRSVDEALRLVQA 161
Cdd:COG1999  88 IGLTGD------PEEIAALAKAFGVyYEKVPDGDYTfdhsaAVYLVDPDGRLRGY----YPAGEDPEELAADLKA 152
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 11-80 5.33e-04

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 38.74  E-value: 5.33e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32189392  11 PAPDFKataVVDGAFKEVKLSDYKGKYVVLFFYpldFTF---VCPTEIIAFSN-----RAEDFRKLgcEVLGVSVDSQ 80
Cdd:cd02968   1 IGPDFT---LTDQDGRPVTLSDLKGKPVLVYFG---YTHcpdVCPTTLANLAQalkqlGADGGDDV--QVVFISVDPE 70
 
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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