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Conserved domains on  [gi|746032028|ref|WP_039104424|]
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peroxiredoxin C [Frischella perrara]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15000 super family cl29157
peroxiredoxin C;
1-200 5.30e-116

peroxiredoxin C;


The actual alignment was detected with superfamily member PRK15000:

Pssm-ID: 184962  Cd Length: 200  Bit Score: 328.17  E-value: 5.30e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   1 MTLVTRKAPDFTSSAVLGSGEIVNNFNFSSFTKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEF 80
Cdd:PRK15000   1 MVLVTRQAPDFTAAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  81 VHNAWRKTPQDQGGIGEVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDA 160
Cdd:PRK15000  81 VHNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 746032028 161 FQFHEEHGEVCPAQWSKGKQGMKGSPDGVASYLKQHANEL 200
Cdd:PRK15000 161 LQFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAENISSL 200
 
Name Accession Description Interval E-value
PRK15000 PRK15000
peroxiredoxin C;
1-200 5.30e-116

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 328.17  E-value: 5.30e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   1 MTLVTRKAPDFTSSAVLGSGEIVNNFNFSSFTKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEF 80
Cdd:PRK15000   1 MVLVTRQAPDFTAAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  81 VHNAWRKTPQDQGGIGEVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDA 160
Cdd:PRK15000  81 VHNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 746032028 161 FQFHEEHGEVCPAQWSKGKQGMKGSPDGVASYLKQHANEL 200
Cdd:PRK15000 161 LQFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAENISSL 200
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-198 6.59e-111

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 314.71  E-value: 6.59e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   1 MTLVTRKAPDFTSSAVLGSGeiVNNFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEF 80
Cdd:COG0450    2 MPLIGDKAPDFTAEATHGGE--FKKISLSDY-KGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  81 VHNAWRKTPQDQGGIGEVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDA 160
Cdd:COG0450   79 SHKAWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDA 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 746032028 161 FQFHEEHGEVCPAQWSKGKQGMKGSPDGVASYLKQHAN 198
Cdd:COG0450  159 LQFVDKHGEVCPANWKPGDKVIIPPPDLVGKALERFPE 196
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 4-178 4.96e-102

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: 291.72  E-value: 4.96e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   4 VTRKAPDFTSSAVLGSGEIVNnFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFVHN 83
Cdd:cd03015    1 VGKKAPDFKATAVVPNGEFKE-ISLSDY-KGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  84 AWRKTPQDQGGIGEVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDAFQF 163
Cdd:cd03015   79 AWRNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQF 158

                        170
                 ....*....|....*
gi 746032028 164 HEEHGEVCPAQWSKG 178
Cdd:cd03015  159 VEEHGEVCPANWKPG 173
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
1-190 9.45e-48

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 155.97  E-value: 9.45e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   1 MTLVTRKAPDFTSSAVLGSGeiVNNFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEF 80
Cdd:NF040737  35 MIKVGKKAPDFTAPAYYKGG--FTNVKLSDY-LGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVF 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  81 VHNAWRKTPQDQGGIGEVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDA 160
Cdd:NF040737 112 VHKMWNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQA 191

                        170       180       190
                 ....*....|....*....|....*....|..
gi 746032028 161 FQFHEEHG--EVCPAQWSKGKQGMKGSPDGVA 190
Cdd:NF040737 192 FQHVRETKgtEATPSGWQPGKPTLKPGPDLVG 223
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-139 9.92e-45

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 144.67  E-value: 9.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028    4 VTRKAPDFTSSAVLGsgeivNNFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFVHN 83
Cdd:pfam00578   1 VGDKAPDFELPDGDG-----GTVSLSDY-RGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHK 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 746032028   84 AWRKTPQdqggigeVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRH 139
Cdd:pfam00578  75 AFAEKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRY 123
 
Name Accession Description Interval E-value
PRK15000 PRK15000
peroxiredoxin C;
1-200 5.30e-116

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 328.17  E-value: 5.30e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   1 MTLVTRKAPDFTSSAVLGSGEIVNNFNFSSFTKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEF 80
Cdd:PRK15000   1 MVLVTRQAPDFTAAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  81 VHNAWRKTPQDQGGIGEVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDA 160
Cdd:PRK15000  81 VHNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 746032028 161 FQFHEEHGEVCPAQWSKGKQGMKGSPDGVASYLKQHANEL 200
Cdd:PRK15000 161 LQFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAENISSL 200
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-198 6.59e-111

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 314.71  E-value: 6.59e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   1 MTLVTRKAPDFTSSAVLGSGeiVNNFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEF 80
Cdd:COG0450    2 MPLIGDKAPDFTAEATHGGE--FKKISLSDY-KGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  81 VHNAWRKTPQDQGGIGEVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDA 160
Cdd:COG0450   79 SHKAWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDA 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 746032028 161 FQFHEEHGEVCPAQWSKGKQGMKGSPDGVASYLKQHAN 198
Cdd:COG0450  159 LQFVDKHGEVCPANWKPGDKVIIPPPDLVGKALERFPE 196
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 4-178 4.96e-102

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: 291.72  E-value: 4.96e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   4 VTRKAPDFTSSAVLGSGEIVNnFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFVHN 83
Cdd:cd03015    1 VGKKAPDFKATAVVPNGEFKE-ISLSDY-KGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  84 AWRKTPQDQGGIGEVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDAFQF 163
Cdd:cd03015   79 AWRNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQF 158

                        170
                 ....*....|....*
gi 746032028 164 HEEHGEVCPAQWSKG 178
Cdd:cd03015  159 VEEHGEVCPANWKPG 173
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 2-198 8.91e-67

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 205.57  E-value: 8.91e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   2 TLVTRKAPDFTSSAVLGsGEIVNnFNFSSFTKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFV 81
Cdd:PTZ00137  68 SLVGKLMPSFKGTALLN-DDLVQ-FNSSDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFS 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  82 HNAWRKTPQDQGGIGEVKFPIVADIKHAIMQAYGIEHPEaGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDAF 161
Cdd:PTZ00137 146 HKAWKELDVRQGGVSPLKFPLFSDISREVSKSFGLLRDE-GFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAV 224

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 746032028 162 QFHEEHGEVCPAQWSKGKQGMKGSPDGVASYLKQHAN 198
Cdd:PTZ00137 225 QFAEKTGNVCPVNWKQGDQAMKPDSQSVKQYLSNRFN 261
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 8-188 6.24e-66

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 201.29  E-value: 6.24e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   8 APDFTSSAVLGSGEIvNNFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFVHNAWRK 87
Cdd:PTZ00253  12 APSFEEVALMPNGSF-KKISLSSY-KGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWTL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  88 TPQDQGGIGEVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDAFQFHEEH 167
Cdd:PTZ00253  90 QERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFVEKH 169

                        170       180
                 ....*....|....*....|.
gi 746032028 168 GEVCPAQWSKGKQGMKGSPDG 188
Cdd:PTZ00253 170 GEVCPANWKKGDPTMKPDPNK 190
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 7-155 2.25e-52

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: 164.64  E-value: 2.25e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   7 KAPDFTSSAVLGsgeivNNFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFVHNAWR 86
Cdd:cd02971    1 KAPDFTLPATDG-----GEVSLSDF-KGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWA 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746032028  87 KTpqdqggIGEVKFPIVADIKHAIMQAYGIEHPEA---GVALRASYFIDKSGIVRHETVNDLPIGRNIDEML 155
Cdd:cd02971   75 EK------EGGLNFPLLSDPDGEFAKAYGVLIEKSaggGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
1-190 9.45e-48

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 155.97  E-value: 9.45e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   1 MTLVTRKAPDFTSSAVLGSGeiVNNFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEF 80
Cdd:NF040737  35 MIKVGKKAPDFTAPAYYKGG--FTNVKLSDY-LGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVF 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  81 VHNAWRKTPQDQGGIGEVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDA 160
Cdd:NF040737 112 VHKMWNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQA 191

                        170       180       190
                 ....*....|....*....|....*....|..
gi 746032028 161 FQFHEEHG--EVCPAQWSKGKQGMKGSPDGVA 190
Cdd:NF040737 192 FQHVRETKgtEATPSGWQPGKPTLKPGPDLVG 223
PRK13189 PRK13189
peroxiredoxin; Provisional
 1-178 3.04e-45

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 149.36  E-value: 3.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   1 MTLVTRKAPDFTssAVLGSGEIvnnfNFSSFTKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEF 80
Cdd:PRK13189   8 MPLIGDKFPEFE--VKTTHGPI----KLPDDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  81 VHNAWRKTPQDQGGIgEVKFPIVADIKHAIMQAYGIEHPEAG-VALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVD 159
Cdd:PRK13189  82 SHIKWVEWIKEKLGV-EIEFPIIADDRGEIAKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVK 160

                        170
                 ....*....|....*....
gi 746032028 160 AFQFHEEHGEVCPAQWSKG 178
Cdd:PRK13189 161 ALQTSDEKGVATPANWPPN 179
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-139 9.92e-45

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 144.67  E-value: 9.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028    4 VTRKAPDFTSSAVLGsgeivNNFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFVHN 83
Cdd:pfam00578   1 VGDKAPDFELPDGDG-----GTVSLSDY-RGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHK 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 746032028   84 AWRKTPQdqggigeVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRH 139
Cdd:pfam00578  75 AFAEKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRY 123
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 7-178 9.23e-43

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: 142.29  E-value: 9.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   7 KAPDFTSSAVLGsgeivnNFNFSSFTKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFVHNAWR 86
Cdd:cd03016    4 TAPNFEADTTHG------PIKFHDYLGDSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  87 KTPQDQGGIgEVKFPIVADIKHAIMQAYGIEHPEAG--VALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDAFQFH 164
Cdd:cd03016   78 EDIEEYTGV-EIPFPIIADPDREVAKLLGMIDPDAGstLTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQLT 156

                        170
                 ....*....|....
gi 746032028 165 EEHGEVCPAQWSKG 178
Cdd:cd03016  157 DKHKVATPANWKPG 170
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 1-195 1.58e-41

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 139.22  E-value: 1.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   1 MTLVTRKAPDFTSSAVLGSgeivnnFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEF 80
Cdd:PRK13190   1 PVKLGQKAPDFTVNTTKGP------IDLSKY-KGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  81 VHNAWRKTPQDQGGIgEVKFPIVADIKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDA 160
Cdd:PRK13190  74 SHIAWLRDIEERFGI-KIPFPVIADIDKELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKA 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 746032028 161 FQFHEEHGEVCPAQWSKGKQGMKGSPDGVASYLKQ 195
Cdd:PRK13190 153 LQVNWKRKVATPANWQPGQEGIVPAPSTLDEAEMR 187
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 32-189 6.58e-38

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 129.34  E-value: 6.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  32 TKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFVHNAWRKTPQDqggIGEVKFPIVADIKHAIM 111
Cdd:PRK10382  29 TEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAWHSSSET---IAKIKYAMIGDPTGALT 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746032028 112 QAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDAFQFHEEH-GEVCPAQWSKGKQGMKGSPDGV 189
Cdd:PRK10382 106 RNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHpGEVCPAKWKEGEATLAPSLDLV 184
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 7-160 1.29e-34

Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers.


Pssm-ID: 239316 [Multi-domain]  Cd Length: 149  Bit Score: 119.69  E-value: 1.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   7 KAPDFTSSAVLGSGeivnnFNFSSFTKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFVHNAWR 86
Cdd:cd03018    6 KAPDFELPDQNGQE-----VRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746032028  87 ktpqDQGGIGevkFPIVADI-KH-AIMQAYGIEHPEAGVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDA 160
Cdd:cd03018   81 ----EENGLT---FPLLSDFwPHgEVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDLPDYDEALDA 149
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 1-175 1.30e-31

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 114.17  E-value: 1.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   1 MTLVTRKAPDFTSSAVLGSGEIVNNFnfssftKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEF 80
Cdd:PRK13191   6 IPLIGEKFPEMEVITTHGKIKLPDDY------KGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  81 VHNAWRKTPQDQGGIgEVKFPIVADIKHAIMQAYGIEHPEAGVA-LRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVD 159
Cdd:PRK13191  80 SHIEWVMWIEKNLKV-EVPFPIIADPMGNVAKRLGMIHAESSTAtVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIR 158

                        170
                 ....*....|....*.
gi 746032028 160 AFQFHEEHGEVCPAQW 175
Cdd:PRK13191 159 ALQLVDKAGVVTPANW 174
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
8-156 6.27e-28

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 102.25  E-value: 6.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   8 APDFTSSAVLGsgeivNNFNFSSFtKGKYAVVFFWpMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFVHNAWRK 87
Cdd:COG1225    1 APDFTLPDLDG-----KTVSLSDL-RGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAE 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746032028  88 tpqDQGgigeVKFPIVADIKHAIMQAYGIehpeagVALRASYFIDKSGIVRHETVNDLPIGRNIDEMLR 156
Cdd:COG1225   74 ---KYG----LPFPLLSDPDGEVAKAYGV------RGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
PRK13599 PRK13599
peroxiredoxin;
34-175 1.62e-27

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 103.64  E-value: 1.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  34 GKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFVHNAWRKTPQDQGGIgEVKFPIVADIKHAIMQA 113
Cdd:PRK13599  28 GKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNTNI-AIPFPVIADDLGKVSNQ 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746032028 114 YGIEHPEAGV-ALRASYFIDKSGIVRHETVNDLPIGRNIDEMLRIVDAFQFHEEHGEVCPAQW 175
Cdd:PRK13599 107 LGMIHPGKGTnTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQYGVALPEKW 169
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 7-156 3.48e-23

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: 89.91  E-value: 3.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   7 KAPDFTSSAVLGsgeivNNFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSEFVHNAWR 86
Cdd:cd03017    2 KAPDFTLPDQDG-----ETVSLSDL-RGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFA 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746032028  87 ktpQDQGgigeVKFPIVADIKHAIMQAYGI---EHPEAGVALRASYFIDKSGIVRHETVNDLPIGrNIDEMLR 156
Cdd:cd03017   76 ---EKYG----LPFPLLSDPDGKLAKAYGVwgeKKKKYMGIERSTFLIDPDGKIVKVWRKVKPKG-HAEEVLE 140
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 7-139 7.30e-22

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 86.65  E-value: 7.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028    7 KAPDFTSSAVLGSGeivNNFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMDSE--FVHNA 84
Cdd:pfam08534   5 KAPDFTLPDAATDG---NTVSLSDF-KGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDafFVKRF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 746032028   85 WRKTPqdqggigeVKFPIVADIKHAIMQAYGI---EHPEAGVALRASYFIDKSGIVRH 139
Cdd:pfam08534  81 WGKEG--------LPFPFLSDGNAAFTKALGLpieEDASAGLRSPRYAVIDEDGKVVY 130
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 33-139 8.26e-12

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: 59.56  E-value: 8.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  33 KGKYAVVFFW-----PmdftfvCPSEIIAFDHRFEEFKKRGVEVIGISMDsEFVHNAWRKTPQDQGgigeVKFPIVADIK 107
Cdd:cd02966   18 KGKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNVD-DDDPAAVKAFLKKYG----ITFPVLLDPD 86

                         90       100       110
                 ....*....|....*....|....*....|..
gi 746032028 108 HAIMQAYGIehpeagVALRASYFIDKSGIVRH 139
Cdd:cd02966   87 GELAKAYGV------RGLPTTFLIDRDGRIRA 112
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-139 1.11e-10

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 57.01  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   1 MTLVTRKAPDFTSSAVLGsgeivNNFNFSSFtKGKYAVVFFW-----PmdftfvCPSEIIAFDHRFEEFKkrGVEVIGIS 75
Cdd:COG0526    1 MKAVGKPAPDFTLTDLDG-----KPLSLADL-KGKPVLVNFWatwcpP------CRAEMPVLKELAEEYG--GVVFVGVD 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746032028  76 MDSEfvHNAWRKTPQDQGgigeVKFPIVADIKHAIMQAYGIEhpeagvALRASYFIDKSGIVRH 139
Cdd:COG0526   67 VDEN--PEAVKAFLKELG----LPYPVLLDPDGELAKAYGVR------GIPTTVLIDKDGKIVA 118
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 160-194 1.30e-07

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: 46.43  E-value: 1.30e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 746032028  160 AFQFHEEHGEVCPAQWSKGKQGM---KGSPD-GVASYLK 194
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIvppPATQEeAVKRYLE 39
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 7-129 7.15e-07

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: 46.97  E-value: 7.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   7 KAPDFTSSAVLGsgeivNNFNFSSFTKGKYAVVFFwpmdFT-FVCPS---EIIAFDHRFEEFKKRGVEVIGISMDSEFVH 82
Cdd:cd02970    1 TAPDFELPDAGG-----ETVTLSALLGEGPVVVVF----YRgFGCPFcreYLRALSKLLPELDALGVELVAVGPESPEKL 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 746032028  83 NAWRKTPqdqggigEVKFPIVADIKHAIMQAYGIEHPEAGVALRASY 129
Cdd:cd02970   72 EAFDKGK-------FLPFPVYADPDRKLYRALGLVRSLPWSNTPRAL 111
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
4-137 2.51e-05

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 43.07  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   4 VTRKAPDFTSSAVLGsgeivNNFNFSSFtKGKYAVVFFWPmdfTFV--CPSEIIAFDHRFEEFKKRGVEVIGISMD-SEF 80
Cdd:PRK03147  37 VGKEAPNFVLTDLEG-----KKIELKDL-KGKGVFLNFWG---TWCkpCEKEMPYMNELYPKYKEKGVEIIAVNVDeTEL 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 746032028  81 -VHNAwrktpQDQGGigeVKFPIVADIKHAIMQAYGIehpeagVALRASYFIDKSGIV 137
Cdd:PRK03147 108 aVKNF-----VNRYG---LTFPVAIDKGRQVIDAYGV------GPLPTTFLIDKDGKV 151
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 7-145 4.46e-05

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: 41.80  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   7 KAPDFTSSAVLGSgeivnNFNFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKkrGVEVIGISMDSEFVHNAWR 86
Cdd:cd03014    5 KAPDFTLVTSDLS-----EVSLADF-AGKVKVISVFPSIDTPVCATQTKRFNKEAAKLD--NTVVLTISADLPFAQKRWC 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746032028  87 KTPqdqgGIGEVKfpIVAD-IKHAIMQAYGIEHPEAGVALRASYFIDKSGIVRH-ETVNDL 145
Cdd:cd03014   77 GAE----GVDNVT--TLSDfRDHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYvELVPEI 131
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 24-100 4.90e-05

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 41.78  E-value: 4.90e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746032028  24 NNFNFSSFTKGKYAVVFFWPMDFTFVCPSEII-AFDHRFEEFKKRGV-EVIGISMDSEFVHNAWRKtpqDQGGIGEVKF 100
Cdd:cd03013   19 NPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLpGYVENADELKAKGVdEVICVSVNDPFVMKAWGK---ALGAKDKIRF 94
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 6-155 8.50e-05

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: 41.46  E-value: 8.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   6 RKAPDFTSSAVLGsgeivNNFNFSSFTKGKYAVVFFwpmdFTFVCP------SEIIAFDhrfEEFKKRGVEVIGISMDSE 79
Cdd:cd02969    2 SPAPDFSLPDTDG-----KTYSLADFADGKALVVMF----ICNHCPyvkaieDRLNRLA---KEYGAKGVAVVAINSNDI 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  80 FVHN-----AWRKTPQDQGgigeVKFPIVADIKHAIMQAYGIEH-PEAgvalrasYFIDKSGIVRHE-------TVNDLP 146
Cdd:cd02969   70 EAYPedspeNMKAKAKEHG----YPFPYLLDETQEVAKAYGAACtPDF-------FLFDPDGKLVYRgriddsrPGNDPP 138

                        170
                 ....*....|....
gi 746032028 147 IGRN-----IDEML 155
Cdd:cd02969  139 VTGRdlraaLDALL 152
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 7-139 2.30e-03

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 37.22  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   7 KAPDFTssavL--GSGEIVNnfnFSSFtKGKYAVVFFWPMDFTFVCPSEIIAFDHRFEEFKKRGVEVIGISMD-----SE 79
Cdd:PRK09437   9 IAPKFS----LpdQDGEQVS---LTDF-QGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDkpeklSR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746032028  80 FVHnawRKtpqdqggigEVKFPIVADIKHAIMQAYGI--EHPEAGVAL----RASYFIDKSGIVRH 139
Cdd:PRK09437  81 FAE---KE---------LLNFTLLSDEDHQVAEQFGVwgEKKFMGKTYdgihRISFLIDADGKIEH 134
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 34-137 3.48e-03

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 35.36  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028   34 GKYAVVFFWP------MDFTfvcpSEIIAFDHRFEefKKRGVEVIGISMDSEFvhNAWRKTPQDQGGiGEVKFPIVADIK 107
Cdd:pfam13905   1 GKVVLLYFGAswckpcRRFT----PLLKELYEKLK--KKKNVEIVFVSLDRDL--EEFKDYLKKMPK-DWLSVPFDDDER 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 746032028  108 HAIMQAYGIEH-PEAgvalrasYFIDKSGIV 137
Cdd:pfam13905  72 NELKRKYGVNAiPTL-------VLLDPNGEV 95
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 33-139 6.91e-03

TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.


Pssm-ID: 239310 [Multi-domain]  Cd Length: 126  Bit Score: 35.36  E-value: 6.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746032028  33 KGKYAVVFFWpmdfTFVCPS--EIIAFDHRFEE-FKKRGVEVIGI---SMDSEFVHNAWRKTPQDQGgigeVKFPIVADI 106
Cdd:cd03012   22 RGKVVLLDFW----TYCCINclHTLPYLTDLEQkYKDDGLVVIGVhspEFAFERDLANVKSAVLRYG----ITYPVANDN 93

                         90       100       110
                 ....*....|....*....|....*....|....
gi 746032028 107 KHAIMQAYGIEH-PeagvalrASYFIDKSGIVRH 139
Cdd:cd03012   94 DYATWRAYGNQYwP-------ALYLIDPTGNVRH 120
 
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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