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Conserved domains on  [gi|1957478451|gb|QQQ22024|]
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peroxiredoxin [Klebsiella grimontii]

Protein Classification

peroxiredoxin( domain architecture ID 11487559)

peroxiredoxin, also called thioredoxin peroxidase or alkyl hydroperoxide reductase, is a thiol-specific antioxidant protein that protects cells against reactive oxygen species

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15000 PRK15000
peroxiredoxin C;
1-200 5.09e-148

peroxiredoxin C;


:

Pssm-ID: 184962  Cd Length: 200  Bit Score: 409.06  E-value: 5.09e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   1 MVLVTRQAPDFTAAAVLGNGEIVEKFNFKQHTSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80
Cdd:PRK15000    1 MVLVTRQAPDFTAAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  81 VHNAWRNTPVDQGGIGPVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDA 160
Cdd:PRK15000   81 VHNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1957478451 161 LQFHEEHGEVCPAQWEKGKEGMAASPEGVAKYLTENVSSL 200
Cdd:PRK15000  161 LQFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAENISSL 200
 
Name Accession Description Interval E-value
PRK15000 PRK15000
peroxiredoxin C;
1-200 5.09e-148

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 409.06  E-value: 5.09e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   1 MVLVTRQAPDFTAAAVLGNGEIVEKFNFKQHTSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80
Cdd:PRK15000    1 MVLVTRQAPDFTAAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  81 VHNAWRNTPVDQGGIGPVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDA 160
Cdd:PRK15000   81 VHNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1957478451 161 LQFHEEHGEVCPAQWEKGKEGMAASPEGVAKYLTENVSSL 200
Cdd:PRK15000  161 LQFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAENISSL 200
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-196 4.16e-115

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 325.49  E-value: 4.16e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   1 MVLVTRQAPDFTAAAVLGNGeiVEKFNFKQHtSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80
Cdd:COG0450     2 MPLIGDKAPDFTAEATHGGE--FKKISLSDY-KGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  81 VHNAWRNTPVDQGGIGPVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDA 160
Cdd:COG0450    79 SHKAWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDA 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1957478451 161 LQFHEEHGEVCPAQWEKGKEGMAASPEGVAKYLTEN 196
Cdd:COG0450   159 LQFVDKHGEVCPANWKPGDKVIIPPPDLVGKALERF 194
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 4-178 7.21e-105

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: 298.65  E-value: 7.21e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   4 VTRQAPDFTAAAVLGNGEIVEKFNfkQHTSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHN 83
Cdd:cd03015     1 VGKKAPDFKATAVVPNGEFKEISL--SDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  84 AWRNTPVDQGGIGPVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDALQF 163
Cdd:cd03015    79 AWRNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQF 158

                         170
                  ....*....|....*
gi 1957478451 164 HEEHGEVCPAQWEKG 178
Cdd:cd03015   159 VEEHGEVCPANWKPG 173
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
1-191 3.04e-47

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 154.82  E-value: 3.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   1 MVLVTRQAPDFTAAAVLGNGEIVEKF-NFKqhtsGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSE 79
Cdd:NF040737   35 MIKVGKKAPDFTAPAYYKGGFTNVKLsDYL----GKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  80 FVHNAWRNTPVDQGGIGPVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVD 159
Cdd:NF040737  111 FVHKMWNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQ 190

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1957478451 160 ALQFHEEHG--EVCPAQWEKGKEGMAASPEGVAK 191
Cdd:NF040737  191 AFQHVRETKgtEATPSGWQPGKPTLKPGPDLVGK 224
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-140 1.98e-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: 146.60  E-value: 1.98e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   4 VTRQAPDFTAAAvlGNGEIVEKFNFKqhtsGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHN 83
Cdd:pfam00578   1 VGDKAPDFELPD--GDGGTVSLSDYR----GKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHK 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1957478451  84 AWRNTPVdqggigpVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQ 140
Cdd:pfam00578  75 AFAEKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
PRK15000 PRK15000
peroxiredoxin C;
1-200 5.09e-148

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 409.06  E-value: 5.09e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   1 MVLVTRQAPDFTAAAVLGNGEIVEKFNFKQHTSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80
Cdd:PRK15000    1 MVLVTRQAPDFTAAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  81 VHNAWRNTPVDQGGIGPVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDA 160
Cdd:PRK15000   81 VHNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1957478451 161 LQFHEEHGEVCPAQWEKGKEGMAASPEGVAKYLTENVSSL 200
Cdd:PRK15000  161 LQFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAENISSL 200
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-196 4.16e-115

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 325.49  E-value: 4.16e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   1 MVLVTRQAPDFTAAAVLGNGeiVEKFNFKQHtSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80
Cdd:COG0450     2 MPLIGDKAPDFTAEATHGGE--FKKISLSDY-KGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  81 VHNAWRNTPVDQGGIGPVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDA 160
Cdd:COG0450    79 SHKAWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDA 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1957478451 161 LQFHEEHGEVCPAQWEKGKEGMAASPEGVAKYLTEN 196
Cdd:COG0450   159 LQFVDKHGEVCPANWKPGDKVIIPPPDLVGKALERF 194
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 4-178 7.21e-105

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: 298.65  E-value: 7.21e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   4 VTRQAPDFTAAAVLGNGEIVEKFNfkQHTSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHN 83
Cdd:cd03015     1 VGKKAPDFKATAVVPNGEFKEISL--SDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  84 AWRNTPVDQGGIGPVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDALQF 163
Cdd:cd03015    79 AWRNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQF 158

                         170
                  ....*....|....*
gi 1957478451 164 HEEHGEVCPAQWEKG 178
Cdd:cd03015   159 VEEHGEVCPANWKPG 173
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 3-198 4.69e-67

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 206.34  E-value: 4.69e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   3 LVTRQAPDFTAAAVLgNGEIVEkFNFKQHTSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVH 82
Cdd:PTZ00137   69 LVGKLMPSFKGTALL-NDDLVQ-FNSSDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSH 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  83 NAWRNTPVDQGGIGPVKYAMVADIKREIQKAYGIEHpDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDALQ 162
Cdd:PTZ00137  147 KAWKELDVRQGGVSPLKFPLFSDISREVSKSFGLLR-DEGFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQ 225

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1957478451 163 FHEEHGEVCPAQWEKGKEGMAASPEGVAKYLTENVS 198
Cdd:PTZ00137  226 FAEKTGNVCPVNWKQGDQAMKPDSQSVKQYLSNRFN 261
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 8-192 3.31e-62

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 191.66  E-value: 3.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   8 APDFTAAAVLGNGEIvEKFNFKQHtSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWRN 87
Cdd:PTZ00253   12 APSFEEVALMPNGSF-KKISLSSY-KGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  88 TPVDQGGIGPVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDALQFHEEH 167
Cdd:PTZ00253   90 QERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFVEKH 169

                         170       180
                  ....*....|....*....|....*
gi 1957478451 168 GEVCPAQWEKGKEGMAASPEGVAKY 192
Cdd:PTZ00253  170 GEVCPANWKKGDPTMKPDPNKSKEG 194
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 7-155 6.14e-51

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: 160.79  E-value: 6.14e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   7 QAPDFTAAAVLGngeivEKFNFKQHtSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWR 86
Cdd:cd02971     1 KAPDFTLPATDG-----GEVSLSDF-KGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWA 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957478451  87 NTpvdqggIGPVKYAMVADIKREIQKAYGIEHPDE---GVALRGSFLIDANGVVRHQVVNDLSLGRNIDEML 155
Cdd:cd02971    75 EK------EGGLNFPLLSDPDGEFAKAYGVLIEKSaggGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-191 2.46e-47

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 153.60  E-value: 2.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   1 MVLVTRQAPDFTAAAvLGNGEIVEKFnfKQHTSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80
Cdd:PRK10382    1 MSLINTKIKPFKNQA-FKNGEFIEVT--EKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  81 VHNAWRNTpvdQGGIGPVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDA 160
Cdd:PRK10382   78 THKAWHSS---SETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKA 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1957478451 161 LQFHEEH-GEVCPAQWEKGKEGMAASPEGVAK 191
Cdd:PRK10382  155 AQYVASHpGEVCPAKWKEGEATLAPSLDLVGK 186
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
1-191 3.04e-47

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 154.82  E-value: 3.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   1 MVLVTRQAPDFTAAAVLGNGEIVEKF-NFKqhtsGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSE 79
Cdd:NF040737   35 MIKVGKKAPDFTAPAYYKGGFTNVKLsDYL----GKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  80 FVHNAWRNTPVDQGGIGPVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVD 159
Cdd:NF040737  111 FVHKMWNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQ 190

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1957478451 160 ALQFHEEHG--EVCPAQWEKGKEGMAASPEGVAK 191
Cdd:NF040737  191 AFQHVRETKgtEATPSGWQPGKPTLKPGPDLVGK 224
PRK13189 PRK13189
peroxiredoxin; Provisional
 1-178 3.53e-46

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 151.67  E-value: 3.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   1 MVLVTRQAPDFTAAAVLGngeiveKFNFKQHTSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80
Cdd:PRK13189    8 MPLIGDKFPEFEVKTTHG------PIKLPDDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  81 VHNAWRNTPVDQGGIgPVKYAMVADIKREIQKAYGIEHPDEG-VALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVD 159
Cdd:PRK13189   82 SHIKWVEWIKEKLGV-EIEFPIIADDRGEIAKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVK 160

                         170
                  ....*....|....*....
gi 1957478451 160 ALQFHEEHGEVCPAQWEKG 178
Cdd:PRK13189  161 ALQTSDEKGVATPANWPPN 179
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 8-178 9.66e-46

Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one conserved cysteine, which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by reducing and detoxifying hydrogen peroxide, peroxynitrite, and organic hydroperoxides. As with all other PRXs, a cysteine sulfenic acid intermediate is formed upon reaction of 1-cys PRX with its substrates. Having no resolving cysteine, the oxidized enzyme is resolved by an external small-molecule or protein reductant such as thioredoxin or glutaredoxin. Similar to typical 2-cys PRX, 1-cys PRX forms a functional dimeric unit with a B-type interface, as well as a decameric structure which is stabilized in the reduced form of the enzyme. Other oligomeric forms, tetramers and hexamers, have also been reported. Mammalian 1-cys PRX is localized cellularly in the cytosol and is expressed at high levels in brain, eye, testes and lung. The seed-specific plant 1-cys PRXs protect tissues from reactive oxygen species during desiccation and are also called rehydrins.


Pssm-ID: 239314  Cd Length: 203  Bit Score: 150.00  E-value: 9.66e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   8 APDFTAAAVLGngeiveKFNFKQHTSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAW-- 85
Cdd:cd03016     5 APNFEADTTHG------PIKFHDYLGDSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWie 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  86 ---RNTPVDqggigpVKYAMVADIKREIQKAYGIEHPDEG--VALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDA 160
Cdd:cd03016    79 dieEYTGVE------IPFPIIADPDREVAKLLGMIDPDAGstLTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDA 152

                         170
                  ....*....|....*...
gi 1957478451 161 LQFHEEHGEVCPAQWEKG 178
Cdd:cd03016   153 LQLTDKHKVATPANWKPG 170
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-140 1.98e-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: 146.60  E-value: 1.98e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   4 VTRQAPDFTAAAvlGNGEIVEKFNFKqhtsGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHN 83
Cdd:pfam00578   1 VGDKAPDFELPD--GDGGTVSLSDYR----GKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHK 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1957478451  84 AWRNTPVdqggigpVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQ 140
Cdd:pfam00578  75 AFAEKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 1-186 2.18e-42

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 141.14  E-value: 2.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   1 MVLVTRQAPDFTAAAVLGngeIVEKFNFKqhtsGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80
Cdd:PRK13190    1 PVKLGQKAPDFTVNTTKG---PIDLSKYK----GKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  81 VHNAWRNTPVDQGGIgPVKYAMVADIKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDA 160
Cdd:PRK13190   74 SHIAWLRDIEERFGI-KIPFPVIADIDKELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKA 152

                         170       180
                  ....*....|....*....|....*.
gi 1957478451 161 LQFHEEHGEVCPAQWEKGKEGMAASP 186
Cdd:PRK13190  153 LQVNWKRKVATPANWQPGQEGIVPAP 178
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 7-160 3.06e-34

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


Pssm-ID: 239316 [Multi-domain]  Cd Length: 149  Bit Score: 118.53  E-value: 3.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   7 QAPDFTAAAVLGngeivEKFNFKQHTSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWR 86
Cdd:cd03018     6 KAPDFELPDQNG-----QEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957478451  87 ntpvDQGGIGpvkYAMVAD--IKREIQKAYGIEHPDEGVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDA 160
Cdd:cd03018    81 ----EENGLT---FPLLSDfwPHGEVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDLPDYDEALDA 149
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 1-175 3.59e-29

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 107.62  E-value: 3.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   1 MVLVTRQAPDFTAAAVLGNGEIVEKFnfkqhtSGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80
Cdd:PRK13191    6 IPLIGEKFPEMEVITTHGKIKLPDDY------KGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  81 VHNAWRNTPVDQGGIgPVKYAMVADIKREIQKAYGIEHPDEGVA-LRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVD 159
Cdd:PRK13191   80 SHIEWVMWIEKNLKV-EVPFPIIADPMGNVAKRLGMIHAESSTAtVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIR 158

                         170
                  ....*....|....*.
gi 1957478451 160 ALQFHEEHGEVCPAQW 175
Cdd:PRK13191  159 ALQLVDKAGVVTPANW 174
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
8-156 1.44e-26

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 98.40  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   8 APDFTAAAVlgNGEIVEKFNFKqhtsGKATVLFFWpMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWrn 87
Cdd:COG1225     1 APDFTLPDL--DGKTVSLSDLR----GKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKF-- 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1957478451  88 tpVDQGGIgpvKYAMVADIKREIQKAYGIehpdegVALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLR 156
Cdd:COG1225    72 --AEKYGL---PFPLLSDPDGEVAKAYGV------RGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
PRK13599 PRK13599
peroxiredoxin;
33-175 2.78e-25

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 97.48  E-value: 2.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  33 SGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWRNTPVDQGGIgPVKYAMVADIKREIQK 112
Cdd:PRK13599   27 AGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNTNI-AIPFPVIADDLGKVSN 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1957478451 113 AYGIEHPDEGV-ALRGSFLIDANGVVRHQVVNDLSLGRNIDEMLRMVDALQFHEEHGEVCPAQW 175
Cdd:PRK13599  106 QLGMIHPGKGTnTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQYGVALPEKW 169
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 7-139 1.34e-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: 91.07  E-value: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   7 QAPDFTAAAVLGngeivEKFNFKQHTsGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWR 86
Cdd:cd03017     2 KAPDFTLPDQDG-----ETVSLSDLR-GKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1957478451  87 NtpvDQGgigpVKYAMVADIKREIQKAYGIEHPDEGV---ALRGSFLIDANGVVRH 139
Cdd:cd03017    76 E---KYG----LPFPLLSDPDGKLAKAYGVWGEKKKKymgIERSTFLIDPDGKIVK 124
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 8-155 1.15e-17

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 75.87  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   8 APDFTAAAVLGNGEIVEKFNFKqhtsGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSE--FVHNAW 85
Cdd:pfam08534   6 APDFTLPDAATDGNTVSLSDFK----GKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDafFVKRFW 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1957478451  86 rntpvdqgGIGPVKYAMVADIKREIQKAYGI---EHPDEGVALRGSFLIDANGVVRH--QVVNDLSLGRNIDEML 155
Cdd:pfam08534  82 --------GKEGLPFPFLSDGNAAFTKALGLpieEDASAGLRSPRYAVIDEDGKVVYlfVGPEPGVDVSDAEAVL 148
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 34-142 8.15e-10

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: 54.16  E-value: 8.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  34 GKATVLFFW-----PmdftfvCPSELIAFDKRYEEFQKRGVEVVGVSFDsEFVHNAWRNTpVDQGGIgpvKYAMVADIKR 108
Cdd:cd02966    19 GKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNVD-DDDPAAVKAF-LKKYGI---TFPVLLDPDG 87

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1957478451 109 EIQKAYGIehpdegVALRGSFLIDANGVVRHQVV 142
Cdd:cd02966    88 ELAKAYGV------RGLPTTFLIDRDGRIRARHV 115
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 160-194 3.75e-09

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: 50.28  E-value: 3.75e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1957478451 160 ALQFHEEHGEVCPAQWEKGKEGMAASP----EGVAKYLT 194
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIVPPPatqeEAVKRYLE 39
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-156 5.65e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 52.38  E-value: 5.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   1 MVLVTRQAPDFTAAAVLGngeivEKFNFKQHtSGKATVLFFW-----PmdftfvCPSELIAFDKRYEEFqkRGVEVVGVS 75
Cdd:COG0526     1 MKAVGKPAPDFTLTDLDG-----KPLSLADL-KGKPVLVNFWatwcpP------CRAEMPVLKELAEEY--GGVVFVGVD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  76 FDSEfvHNAWRNTPVDQGgigpVKYAMVADIKREIQKAYGIEH-PDegvalrgSFLIDANGVVRHQVVNDLSlGRNIDEM 154
Cdd:COG0526    67 VDEN--PEAVKAFLKELG----LPYPVLLDPDGELAKAYGVRGiPT-------TVLIDKDGKIVARHVGPLS-PEELEEA 132


                  ..
gi 1957478451 155 LR 156
Cdd:COG0526   133 LE 134
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
2-137 4.17e-07

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 48.08  E-value: 4.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   2 VLVTRQAPDFTAAAVlgNGEIVEKFNFKqhtsGKATVLFFWPmdfTFV--CPSELIAFDKRYEEFQKRGVEVVGVSFD-S 78
Cdd:PRK03147   35 VQVGKEAPNFVLTDL--EGKKIELKDLK----GKGVFLNFWG---TWCkpCEKEMPYMNELYPKYKEKGVEIIAVNVDeT 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  79 EF-VHNAwrntpVDQGGigpVKYAMVADIKREIQKAYGIehpdegVALRGSFLIDANGVV 137
Cdd:PRK03147  106 ELaVKNF-----VNRYG---LTFPVAIDKGRQVIDAYGV------GPLPTTFLIDKDGKV 151
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 7-146 4.83e-06

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: 44.50  E-value: 4.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   7 QAPDFTAaaVLGNGEIVEKFNFKqhtsGKATVLFFWPMDFTFVCPSELIAFDKRYEEFQkrGVEVVGVSFDSEFVHNAWR 86
Cdd:cd03014     5 KAPDFTL--VTSDLSEVSLADFA----GKVKVISVFPSIDTPVCATQTKRFNKEAAKLD--NTVVLTISADLPFAQKRWC 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957478451  87 NTpvdqggIGPVKYAMVAD-IKREIQKAYGIEHPDEGVALRGSFLIDANGVVRH-QVVNDLS 146
Cdd:cd03014    77 GA------EGVDNVTTLSDfRDHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYvELVPEIT 132
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 7-138 3.36e-05

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 42.35  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   7 QAPDFTAAAVLGNgeiveKFNFKQHTSGKATVLFFwpmdFT-FVCPS---ELIAFDKRYEEFQKRGVEVVGVSFDSEFvh 82
Cdd:cd02970     1 TAPDFELPDAGGE-----TVTLSALLGEGPVVVVF----YRgFGCPFcreYLRALSKLLPELDALGVELVAVGPESPE-- 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1957478451  83 nawRNTPVDQGgiGPVKYAMVADIKREIQKAYGIE-----------------------HPDEGVALRGSFLIDANGVVR 138
Cdd:cd02970    70 ---KLEAFDKG--KFLPFPVYADPDRKLYRALGLVrslpwsntpralwknaaigfrgnDEGDGLQLPGVFVIGPDGTIL 143
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 6-138 2.30e-04

Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF.


Pssm-ID: 239267 [Multi-domain]  Cd Length: 171  Bit Score: 40.30  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451   6 RQAPDFTAAAVLGNgeiveKFNFKQHTSGKATVLFFwpmdFTFVCP------SELIAFDKryeEFQKRGVEVVGVS---- 75
Cdd:cd02969     2 SPAPDFSLPDTDGK-----TYSLADFADGKALVVMF----ICNHCPyvkaieDRLNRLAK---EYGAKGVAVVAINsndi 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1957478451  76 ----FDS-----EFVHNawrntpvdqGGIgpvKYAMVADIKREIQKAYGIEH-PDegvalrgSFLIDANGVVR 138
Cdd:cd02969    70 eaypEDSpenmkAKAKE---------HGY---PFPYLLDETQEVAKAYGAACtPD-------FFLFDPDGKLV 123
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 34-137 1.18e-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: 36.90  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957478451  34 GKATVLFFWP------MDFTfvcpSELIAFDKRYEEfqKRGVEVVGVSFDSEFvhNAWRNTpVDQGGIGPVKYAMVADIK 107
Cdd:pfam13905   1 GKVVLLYFGAswckpcRRFT----PLLKELYEKLKK--KKNVEIVFVSLDRDL--EEFKDY-LKKMPKDWLSVPFDDDER 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1957478451 108 REIQKAYGIEH-PdegvALrgsFLIDANGVV 137
Cdd:pfam13905  72 NELKRKYGVNAiP----TL---VLLDPNGEV 95
 
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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