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Conserved domains on  [gi|4505591|ref|NP_002565|]
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peroxiredoxin-1 [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 ...
 8-180 8.46e-124

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: 346.41  E-value: 8.46e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    8 IGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAW 87
Cdd:cd03015   1 VGKKAPDFKATAVVPNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591   88 VNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTD 167
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 4505591  168 KHGEVCPAGWKPG 180
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 ...
 8-180 8.46e-124

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: 346.41  E-value: 8.46e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    8 IGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAW 87
Cdd:cd03015   1 VGKKAPDFKATAVVPNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591   88 VNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTD 167
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 4505591  168 KHGEVCPAGWKPG 180
Cdd:cd03015 161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
7-197 1.68e-113

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 321.25  E-value: 1.68e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    7 KIGHPAPNFKATAVMPdGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLA 86
Cdd:COG0450   4 LIGDKAPDFTAEATHG-GEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591   87 WVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFT 166
Cdd:COG0450  83 WHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFV 162

                       170       180       190
                ....*....|....*....|....*....|.
gi 4505591  167 DKHGEVCPAGWKPGSDTIKPDVQKSKEYFSK 197
Cdd:COG0450 163 DKHGEVCPANWKPGDKVIIPPPDLVGKALER 193
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 1-196 2.40e-109

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 311.07  E-value: 2.40e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     1 MSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDS 80
Cdd:PTZ00253   1 MSCGDAKINHPAPSFEEVALMPNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    81 HFCHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLV 160
Cdd:PTZ00253  81 EYAHLQWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 4505591   161 QAFQFTDKHGEVCPAGWKPGSDTIKPDVQKSKEYFS 196
Cdd:PTZ00253 161 EAFQFVEKHGEVCPANWKKGDPTMKPDPNKSKEGFF 196
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
6-186 1.82e-61

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 191.03  E-value: 1.82e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     6 AKIGHPAPNFKATAVMpDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHL 85
Cdd:NF040737  36 IKVGKKAPDFTAPAYY-KGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHK 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    86 AWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQF 165
Cdd:NF040737 115 MWNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQH 194

                        170       180
                 ....*....|....*....|...
gi 4505591   166 T--DKHGEVCPAGWKPGSDTIKP 186
Cdd:NF040737 195 VreTKGTEATPSGWQPGKPTLKP 217
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 8-186 6.59e-61

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: 187.99  E-value: 6.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591      8 IGHPAPNFKATAVMpDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAW 87
Cdd:TIGR03137   4 INTEIKPFKATAYH-NGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAW 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     88 VNTPKKqggLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTD 167
Cdd:TIGR03137  83 HDTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVA 159

                         170       180
                  ....*....|....*....|
gi 4505591    168 KH-GEVCPAGWKPGSDTIKP 186
Cdd:TIGR03137 160 AHpGEVCPAKWKEGAETLKP 179
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 8-142 8.48e-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: 167.79  E-value: 8.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591      8 IGHPAPNFKAtavmPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAW 87
Cdd:pfam00578   1 VGDKAPDFEL----PDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 4505591     88 VNTPKkqgglgpMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQI 142
Cdd:pfam00578  77 AEKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 8-180 8.46e-124

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: 346.41  E-value: 8.46e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    8 IGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAW 87
Cdd:cd03015   1 VGKKAPDFKATAVVPNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591   88 VNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTD 167
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 4505591  168 KHGEVCPAGWKPG 180
Cdd:cd03015 161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
7-197 1.68e-113

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 321.25  E-value: 1.68e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    7 KIGHPAPNFKATAVMPdGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLA 86
Cdd:COG0450   4 LIGDKAPDFTAEATHG-GEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591   87 WVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFT 166
Cdd:COG0450  83 WHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFV 162

                       170       180       190
                ....*....|....*....|....*....|.
gi 4505591  167 DKHGEVCPAGWKPGSDTIKPDVQKSKEYFSK 197
Cdd:COG0450 163 DKHGEVCPANWKPGDKVIIPPPDLVGKALER 193
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 1-196 2.40e-109

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 311.07  E-value: 2.40e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     1 MSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDS 80
Cdd:PTZ00253   1 MSCGDAKINHPAPSFEEVALMPNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    81 HFCHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLV 160
Cdd:PTZ00253  81 EYAHLQWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 4505591   161 QAFQFTDKHGEVCPAGWKPGSDTIKPDVQKSKEYFS 196
Cdd:PTZ00253 161 EAFQFVEKHGEVCPANWKKGDPTMKPDPNKSKEGFF 196
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 8-198 2.05e-64

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 199.40  E-value: 2.05e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     8 IGHPAPNFKATAVMpDGQFKDISLSDY-KGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLA 86
Cdd:PTZ00137  70 VGKLMPSFKGTALL-NDDLVQFNSSDYfKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKA 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    87 WVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKaDEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFT 166
Cdd:PTZ00137 149 WKELDVRQGGVSPLKFPLFSDISREVSKSFGLLR-DEGFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQFA 227

                        170       180       190
                 ....*....|....*....|....*....|..
gi 4505591   167 DKHGEVCPAGWKPGSDTIKPDVQKSKEYFSKQ 198
Cdd:PTZ00137 228 EKTGNVCPVNWKQGDQAMKPDSQSVKQYLSNR 259
PRK15000 PRK15000
peroxiredoxin C;
12-197 1.71e-62

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 192.58  E-value: 1.71e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    12 APNFKATAVMPDGQF-KDISLSDY-KGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVN 89
Cdd:PRK15000   8 APDFTAAAVLGSGEIvDKFNFKQHtNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWRN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    90 TPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTDKH 169
Cdd:PRK15000  88 TPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDALQFHEEH 167

                        170       180
                 ....*....|....*....|....*...
gi 4505591   170 GEVCPAGWKPGSDTIKPDVQKSKEYFSK 197
Cdd:PRK15000 168 GDVCPAQWEKGKEGMNASPDGVAKYLAE 195
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
6-186 1.82e-61

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 191.03  E-value: 1.82e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     6 AKIGHPAPNFKATAVMpDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHL 85
Cdd:NF040737  36 IKVGKKAPDFTAPAYY-KGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHK 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    86 AWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQF 165
Cdd:NF040737 115 MWNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQH 194

                        170       180
                 ....*....|....*....|...
gi 4505591   166 T--DKHGEVCPAGWKPGSDTIKP 186
Cdd:NF040737 195 VreTKGTEATPSGWQPGKPTLKP 217
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 8-186 6.59e-61

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: 187.99  E-value: 6.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591      8 IGHPAPNFKATAVMpDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAW 87
Cdd:TIGR03137   4 INTEIKPFKATAYH-NGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAW 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     88 VNTPKKqggLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTD 167
Cdd:TIGR03137  83 HDTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVA 159

                         170       180
                  ....*....|....*....|
gi 4505591    168 KH-GEVCPAGWKPGSDTIKP 186
Cdd:TIGR03137 160 AHpGEVCPAKWKEGAETLKP 179
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 11-157 6.60e-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: 186.21  E-value: 6.60e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591   11 PAPNFKATAVmpdgQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVnt 90
Cdd:cd02971   1 KAPDFTLPAT----DGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWA-- 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591   91 pKKQGGLgpmNIPLVSDPKRTIAQDYGVLKADE---GISFRGLFIIDDKGILRQITVNDLPVGRSVDETL 157
Cdd:cd02971  75 -EKEGGL---NFPLLSDPDGEFAKAYGVLIEKSaggGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 8-186 1.18e-56

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: 177.73  E-value: 1.18e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    8 IGHPAPNFKATAVMpdgqfKDISLSDYKG-KYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLA 86
Cdd:cd03016   1 LGDTAPNFEADTTH-----GPIKFHDYLGdSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591   87 WVNTPKKQGGlGPMNIPLVSDPKRTIAQDYGVLKADEGISF--RGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQ 164
Cdd:cd03016  76 WIEDIEEYTG-VEIPFPIIADPDREVAKLLGMIDPDAGSTLtvRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQ 154

                       170       180
                ....*....|....*....|..
gi 4505591  165 FTDKHGEVCPAGWKPGSDTIKP 186
Cdd:cd03016 155 LTDKHKVATPANWKPGDDVIVP 176
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 8-142 8.48e-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: 167.79  E-value: 8.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591      8 IGHPAPNFKAtavmPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAW 87
Cdd:pfam00578   1 VGDKAPDFEL----PDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 4505591     88 VNTPKkqgglgpMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQI 142
Cdd:pfam00578  77 AEKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
PRK13189 PRK13189
peroxiredoxin; Provisional
 8-188 2.55e-53

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 169.78  E-value: 2.55e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     8 IGHPAPNFKATAVmpdgqFKDISLSD-YKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLA 86
Cdd:PRK13189  11 IGDKFPEFEVKTT-----HGPIKLPDdYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    87 WVNTPKKQGGLgPMNIPLVSDPKRTIAQDYGVLKADEG-ISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQF 165
Cdd:PRK13189  86 WVEWIKEKLGV-EIEFPIIADDRGEIAKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQT 164

                        170       180
                 ....*....|....*....|...
gi 4505591   166 TDKHGEVCPAGWKPGsDTIKPDV 188
Cdd:PRK13189 165 SDEKGVATPANWPPN-DLIKDKV 186
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-188 8.48e-47

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 152.06  E-value: 8.48e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     1 MSSGNAKIghpAPnFKATAvMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDS 80
Cdd:PRK10382   1 MSLINTKI---KP-FKNQA-FKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    81 HFCHLAWVNTPKKqggLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLV 160
Cdd:PRK10382  76 HFTHKAWHSSSET---IAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKI 152

                        170       180
                 ....*....|....*....|....*....
gi 4505591   161 QAFQFTDKH-GEVCPAGWKPGSDTIKPDV 188
Cdd:PRK10382 153 KAAQYVASHpGEVCPAKWKEGEATLAPSL 181
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 7-186 5.61e-45

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 148.08  E-value: 5.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     7 KIGHPAPNFKA-TAVMPdgqfkdISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHL 85
Cdd:PRK13190   3 KLGQKAPDFTVnTTKGP------IDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    86 AWVNTPKKQGGLgPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQF 165
Cdd:PRK13190  77 AWLRDIEERFGI-KIPFPVIADIDKELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQV 155

                        170       180
                 ....*....|....*....|.
gi 4505591   166 TDKHGEVCPAGWKPGSDTIKP 186
Cdd:PRK13190 156 NWKRKVATPANWQPGQEGIVP 176
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 33-177 9.10e-40

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 134.97  E-value: 9.10e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    33 DYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVNTPKKQGGLgPMNIPLVSDPKRTI 112
Cdd:PRK13191  30 DYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMWIEKNLKV-EVPFPIIADPMGNV 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505591   113 AQDYGVLKADEGIS-FRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGW 177
Cdd:PRK13191 109 AKRLGMIHAESSTAtVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLVDKAGVVTPANW 174
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 7-158 2.75e-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: 128.93  E-value: 2.75e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    7 KIGHPAPNFkataVMPDGQFKDISLSDYKG-KYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHL 85
Cdd:cd03018   2 EVGDKAPDF----ELPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLR 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505591   86 AWvntpKKQGGLgpmNIPLVSD--PKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRS---VDETLR 158
Cdd:cd03018  78 AW----AEENGL---TFPLLSDfwPHGEVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDlpdYDEALD 148
PRK13599 PRK13599
peroxiredoxin;
33-188 6.86e-35

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 122.51  E-value: 6.86e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    33 DYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVNTPKKQGGLgPMNIPLVSDPKRTI 112
Cdd:PRK13599  25 DYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNTNI-AIPFPVIADDLGKV 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505591   113 AQDYGVLKADEGI-SFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGWkPGSDTIKPDV 188
Cdd:PRK13599 104 SNQLGMIHPGKGTnTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQYGVALPEKW-PNNYLIKDHV 179
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 11-158 6.07e-34

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


Pssm-ID: 239315  Cd Length: 140  Bit Score: 117.65  E-value: 6.07e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591   11 PAPNFKAtavmPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVnt 90
Cdd:cd03017   2 KAPDFTL----PDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFA-- 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505591   91 pKKQGglgpMNIPLVSDPKRTIAQDYGVLKADE---GISFRGLFIIDDKGILRQITVNDLPVGrSVDETLR 158
Cdd:cd03017  76 -EKYG----LPFPLLSDPDGKLAKAYGVWGEKKkkyMGIERSTFLIDPDGKIVKVWRKVKPKG-HAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
12-158 5.17e-30

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 107.26  E-value: 5.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591   12 APNFKATAVmpDGqfKDISLSDYKGKYVVFFFYPlDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVntp 91
Cdd:COG1225   1 APDFTLPDL--DG--KTVSLSDLRGKPVVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFA--- 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505591   92 KKQGglgpMNIPLVSDPKRTIAQDYGVLKadegisFRGLFIIDDKGILRQITVNDLPVGRSVDETLR 158
Cdd:COG1225  73 EKYG----LPFPLLSDPDGEVAKAYGVRG------TPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 7-148 1.20e-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: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591      7 KIGHPAPNFKATAVMPDGQfkDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDShfcHLA 86
Cdd:pfam08534   1 KAGDKAPDFTLPDAATDGN--TVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDN---DAF 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505591     87 WVNTPKKQGGLgpmNIPLVSDPKRTIAQDYGV---LKADEGISFRGLFIIDDKGILRQITVNDLP 148
Cdd:pfam08534  76 FVKRFWGKEGL---PFPFLSDGNAAFTKALGLpieEDASAGLRSPRYAVIDEDGKVVYLFVGPEP 137
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 162-197 2.52e-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: 58.75  E-value: 2.52e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 4505591    162 AFQFTDKHGEVCPAGWKPGSDTIKP----DVQKSKEYFSK 197
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIVPppatQEEAVKRYLEG 40
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 7-140 4.87e-12

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: 60.68  E-value: 4.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    7 KIGHPAPNFKATavmpDGQFKDISLSDYKGKYVVFFFYP-LDfTFVCPTEIIAFSDRAEEFKKLNcqVIGASVDSHFCHL 85
Cdd:cd03014   1 KVGDKAPDFTLV----TSDLSEVSLADFAGKVKVISVFPsID-TPVCATQTKRFNKEAAKLDNTV--VLTISADLPFAQK 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4505591   86 AWVNTPkkqgglGPMNIPLVSDPK-RTIAQDYGVLKADEGISFRGLFIIDDKGILR 140
Cdd:cd03014  74 RWCGAE------GVDNVTTLSDFRdHSFGKAYGVLIKDLGLLARAVFVIDENGKVI 123
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 7-142 5.19e-12

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 61.11  E-value: 5.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     7 KIGHPAPNFKatavMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDShfchla 86
Cdd:PRK09437   5 KAGDIAPKFS----LPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDK------ 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505591    87 wvntPKKQGGLGP---MNIPLVSDPKRTIAQDYGVL-------KADEGIsFRGLFIIDDKGILRQI 142
Cdd:PRK09437  75 ----PEKLSRFAEkelLNFTLLSDEDHQVAEQFGVWgekkfmgKTYDGI-HRISFLIDADGKIEHV 135
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 8-140 1.54e-08

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 51.23  E-value: 1.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591    8 IGHPAPNFKatavMPDGQFKDISLSDYKGKYVVFFFY-----PldftfvCPTEIIAFSDRAEEFKKLncQVIGASVDSHf 82
Cdd:COG0526   4 VGKPAPDFT----LTDLDGKPLSLADLKGKPVLVNFWatwcpP------CRAEMPVLKELAEEYGGV--VFVGVDVDEN- 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4505591   83 cHLAWVNTPKKQGglgpMNIPLVSDPKRTIAQDYGVlkadEGISFrgLFIIDDKGILR 140
Cdd:COG0526  71 -PEAVKAFLKELG----LPYPVLLDPDGELAKAYGV----RGIPT--TVLIDKDGKIV 117
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 21-142 4.27e-07

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


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 46.85  E-value: 4.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591   21 MPDGQFKDISLSDYKGKYVVfffypLDF--TF--VCPTEIIAFSDRAEEFKKLNCQVIGASVDShFCHLAWVNTPKKQGg 96
Cdd:cd02966   4 LPDLDGKPVSLSDLKGKVVL-----VNFwaSWcpPCRAEMPELEALAKEYKDDGVEVVGVNVDD-DDPAAVKAFLKKYG- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4505591   97 lgpMNIPLVSDPKRTIAQDYGVlkadegisfRGL---FIIDDKGILRQI 142
Cdd:cd02966  77 ---ITFPVLLDPDGELAKAYGV---------RGLpttFLIDRDGRIRAR 113
tpx PRK00522
thiol peroxidase;
7-134 1.45e-06

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 46.43  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     7 KIGHPAPNFKATAvmpdGQFKDISLSDYKGKYVVFFFYP-LDfTFVCPTEIIAFSDRAEEFKklNCQVIGASVDSHFCHL 85
Cdd:PRK00522  19 QVGDKAPDFTLVA----NDLSDVSLADFAGKRKVLNIFPsID-TGVCATSVRKFNQEAAELD--NTVVLCISADLPFAQK 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4505591    86 AWVntpkkqGGLGPMNIPLVSDPK-RTIAQDYGVLKADE---GISFRGLFIID 134
Cdd:PRK00522  92 RFC------GAEGLENVITLSDFRdHSFGKAYGVAIAEGplkGLLARAVFVLD 138
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
6-142 2.91e-04

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 39.99  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591     6 AKIGHPAPNFkataVMPDGQFKDISLSDYKGKYVVFFFYPldfTFV--CPTEIIAFSDRAEEFKKLNCQVIGASVDShfC 83
Cdd:PRK03147  35 VQVGKEAPNF----VLTDLEGKKIELKDLKGKGVFLNFWG---TWCkpCEKEMPYMNELYPKYKEKGVEIIAVNVDE--T 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4505591    84 HLAwVNTPKKQGGLgpmNIPLVSDPKRTIAQDYGVlkadegISFRGLFIIDDKGILRQI 142
Cdd:PRK03147 106 ELA-VKNFVNRYGL---TFPVAIDKGRQVIDAYGV------GPLPTTFLIDKDGKVVKV 154
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 29-121 8.87e-04

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: 38.11  E-value: 8.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505591   29 ISLSDY--KGKYVVFFFYpldfTFVCP---TEIIAFSDRAEEFKKLNCQVIGASVDShfchlaWVNTPKKQGGLGPmNIP 103
Cdd:cd02970  15 VTLSALlgEGPVVVVFYR----GFGCPfcrEYLRALSKLLPELDALGVELVAVGPES------PEKLEAFDKGKFL-PFP 83

                        90
                ....*....|....*...
gi 4505591  104 LVSDPKRTIAQDYGVLKA 121
Cdd:cd02970  84 VYADPDRKLYRALGLVRS 101
 
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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