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Conserved domains on  [gi|1834951539|ref|WP_168920406|]
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redoxin domain-containing protein [Enterobacteriaceae endosymbiont of Macroplea appendiculata]

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 4.53e-91

peroxiredoxin C;


The actual alignment was detected with superfamily member PRK15000:

Pssm-ID: 184962  Cd Length: 200  Bit Score: 265.00  E-value: 4.53e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   1 MILVTRKAPQFIAPAVLPNGDIIENFNFYKYTENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQY 80
Cdd:PRK15000    1 MVLVTRQAPDFTAAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  81 THKAWRNTDIDQGGIGHIKFIMISDIKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDA 160
Cdd:PRK15000   81 VHNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1834951539 161 IKHYKKYGQVCPAQWTSGKHSIIPTEAGIKDYLSNNLKEL 200
Cdd:PRK15000  161 LQFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAENISSL 200
 
Name Accession Description Interval E-value
PRK15000 PRK15000
peroxiredoxin C;
1-200 4.53e-91

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 265.00  E-value: 4.53e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   1 MILVTRKAPQFIAPAVLPNGDIIENFNFYKYTENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQY 80
Cdd:PRK15000    1 MVLVTRQAPDFTAAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  81 THKAWRNTDIDQGGIGHIKFIMISDIKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDA 160
Cdd:PRK15000   81 VHNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1834951539 161 IKHYKKYGQVCPAQWTSGKHSIIPTEAGIKDYLSNNLKEL 200
Cdd:PRK15000  161 LQFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAENISSL 200
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-196 5.83e-90

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 261.93  E-value: 5.83e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   1 MILVTRKAPQFIAPAVLpnGDIIENFNFYKYtENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQY 80
Cdd:COG0450     2 MPLIGDKAPDFTAEATH--GGEFKKISLSDY-KGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  81 THKAWRNTDIDQGGIGHIKFIMISDIKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDA 160
Cdd:COG0450    79 SHKAWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDA 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1834951539 161 IKHYKKYGQVCPAQWTSGKHSIIPTEAGIKDYLSNN 196
Cdd:COG0450   159 LQFVDKHGEVCPANWKPGDKVIIPPPDLVGKALERF 194
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 4-178 1.17e-84

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: 247.80  E-value: 1.17e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   4 VTRKAPQFIAPAVLPNGDIIE-NFNFYKyteNAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTH 82
Cdd:cd03015     1 VGKKAPDFKATAVVPNGEFKEiSLSDYK---GKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  83 KAWRNTDIDQGGIGHIKFIMISDIKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDAIK 162
Cdd:cd03015    78 LAWRNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQ 157

                         170
                  ....*....|....*.
gi 1834951539 163 HYKKYGQVCPAQWTSG 178
Cdd:cd03015   158 FVEEHGEVCPANWKPG 173
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-140 5.36e-37

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: 125.03  E-value: 5.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   4 VTRKAPQFiapaVLPNGDIiENFNFYKYtENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTHK 83
Cdd:pfam00578   1 VGDKAPDF----ELPDGDG-GTVSLSDY-RGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHK 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1834951539  84 AWRNtdiDQGgighIKFIMISDIKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQ 140
Cdd:pfam00578  75 AFAE---KYG----LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
PRK15000 PRK15000
peroxiredoxin C;
1-200 4.53e-91

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 265.00  E-value: 4.53e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   1 MILVTRKAPQFIAPAVLPNGDIIENFNFYKYTENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQY 80
Cdd:PRK15000    1 MVLVTRQAPDFTAAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  81 THKAWRNTDIDQGGIGHIKFIMISDIKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDA 160
Cdd:PRK15000   81 VHNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1834951539 161 IKHYKKYGQVCPAQWTSGKHSIIPTEAGIKDYLSNNLKEL 200
Cdd:PRK15000  161 LQFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAENISSL 200
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-196 5.83e-90

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 261.93  E-value: 5.83e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   1 MILVTRKAPQFIAPAVLpnGDIIENFNFYKYtENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQY 80
Cdd:COG0450     2 MPLIGDKAPDFTAEATH--GGEFKKISLSDY-KGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  81 THKAWRNTDIDQGGIGHIKFIMISDIKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDA 160
Cdd:COG0450    79 SHKAWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDA 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1834951539 161 IKHYKKYGQVCPAQWTSGKHSIIPTEAGIKDYLSNN 196
Cdd:COG0450   159 LQFVDKHGEVCPANWKPGDKVIIPPPDLVGKALERF 194
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 4-178 1.17e-84

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: 247.80  E-value: 1.17e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   4 VTRKAPQFIAPAVLPNGDIIE-NFNFYKyteNAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTH 82
Cdd:cd03015     1 VGKKAPDFKATAVVPNGEFKEiSLSDYK---GKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  83 KAWRNTDIDQGGIGHIKFIMISDIKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDAIK 162
Cdd:cd03015    78 LAWRNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQ 157

                         170
                  ....*....|....*.
gi 1834951539 163 HYKKYGQVCPAQWTSG 178
Cdd:cd03015   158 FVEEHGEVCPANWKPG 173
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 3-195 8.63e-58

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 182.84  E-value: 8.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   3 LVTRKAPQFIAPAVLpNGDIIEnFNFYKYTENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTH 82
Cdd:PTZ00137   69 LVGKLMPSFKGTALL-NDDLVQ-FNSSDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSH 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  83 KAWRNTDIDQGGIGHIKFIMISDIKKNIQQQYGIEHPNlGIALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDAIK 162
Cdd:PTZ00137  147 KAWKELDVRQGGVSPLKFPLFSDISREVSKSFGLLRDE-GFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQ 225

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1834951539 163 HYKKYGQVCPAQWTSGKHSIIPTEAGIKDYLSN 195
Cdd:PTZ00137  226 FAEKTGNVCPVNWKQGDQAMKPDSQSVKQYLSN 258
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 8-197 3.24e-48

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 156.22  E-value: 3.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   8 APQFIAPAVLPNGdiienfNFYKYTENAI----TVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTHK 83
Cdd:PTZ00253   12 APSFEEVALMPNG------SFKKISLSSYkgkwVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  84 AWRNTDIDQGGIGHIKFIMISDIKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDAIKH 163
Cdd:PTZ00253   86 QWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQF 165

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1834951539 164 YKKYGQVCPAQWTSGKHSIIPTEAGIKDYLSNNL 197
Cdd:PTZ00253  166 VEKHGEVCPANWKKGDPTMKPDPNKSKEGFFSKA 199
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 7-155 5.10e-43

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: 140.76  E-value: 5.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   7 KAPQFIAPAVLPngdiiENFNFYKYtENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTHKAWR 86
Cdd:cd02971     1 KAPDFTLPATDG-----GEVSLSDF-KGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWA 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834951539  87 NTdidqggIGHIKFIMISDIKKNIQQQYGIEHPNL---GIALRATFIIDEKHIIKHQTVNDLFFGRNIHETL 155
Cdd:cd02971    75 EK------EGGLNFPLLSDPDGEFAKAYGVLIEKSaggGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 20-184 4.18e-40

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: 135.36  E-value: 4.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  20 GDIIENF---------NFYKYTENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTHKAWRNtDI 90
Cdd:cd03016     2 GDTAPNFeadtthgpiKFHDYLGDSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIE-DI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  91 DQGGIGHIKFIMISDIKKNIQQQYGIEHPNLGIAL--RATFIIDEKHIIK-----HQTVndlffGRNIHETLRIIDAIKH 163
Cdd:cd03016    81 EEYTGVEIPFPIIADPDREVAKLLGMIDPDAGSTLtvRAVFIIDPDKKIRlilyyPATT-----GRNFDEILRVVDALQL 155

                         170       180
                  ....*....|....*....|.
gi 1834951539 164 YKKYGQVCPAQWTSGKHSIIP 184
Cdd:cd03016   156 TDKHKVATPANWKPGDDVIVP 176
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-140 5.36e-37

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: 125.03  E-value: 5.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   4 VTRKAPQFiapaVLPNGDIiENFNFYKYtENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTHK 83
Cdd:pfam00578   1 VGDKAPDF----ELPDGDG-GTVSLSDY-RGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHK 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1834951539  84 AWRNtdiDQGgighIKFIMISDIKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQ 140
Cdd:pfam00578  75 AFAE---KYG----LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-185 2.77e-34

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 120.09  E-value: 2.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   1 MILVTRKAPQFIAPAvLPNGDIIENFNfyKYTENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQY 80
Cdd:PRK10382    1 MSLINTKIKPFKNQA-FKNGEFIEVTE--KDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  81 THKAWRNTdidQGGIGHIKFIMISDIKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDA 160
Cdd:PRK10382   78 THKAWHSS---SETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKA 154

                         170       180
                  ....*....|....*....|....*.
gi 1834951539 161 IKHYKKY-GQVCPAQWTSGKHSIIPT 185
Cdd:PRK10382  155 AQYVASHpGEVCPAKWKEGEATLAPS 180
PRK13189 PRK13189
peroxiredoxin; Provisional
 1-199 2.05e-32

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 116.24  E-value: 2.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   1 MILVTRKAPQFiaPAVLPNGDIienfNFYKYTENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQY 80
Cdd:PRK13189    8 MPLIGDKFPEF--EVKTTHGPI----KLPDDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  81 THKAWRNTDIDQGGIgHIKFIMISDIKKNIQQQYGIEHPNLG-IALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIID 159
Cdd:PRK13189   82 SHIKWVEWIKEKLGV-EIEFPIIADDRGEIAKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1834951539 160 AIKHYKKYGQVCPAQWTSG----KHSIIP---TEAGIKDYLSNNLKE 199
Cdd:PRK13189  161 ALQTSDEKGVATPANWPPNdlikDKVIVPpasSVEEAKKRLEAKEKG 207
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 1-193 1.58e-30

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 110.71  E-value: 1.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   1 MILVTRKAPQFiapAVLPNGDIIenfNFYKYtENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQY 80
Cdd:PRK13190    1 PVKLGQKAPDF---TVNTTKGPI---DLSKY-KGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  81 THKAWRnTDIDQGGIGHIKFIMISDIKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDA 160
Cdd:PRK13190   74 SHIAWL-RDIEERFGIKIPFPVIADIDKELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKA 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1834951539 161 IKHYKKYGQVCPAQWTSGKHSIIPTEAGIKDYL 193
Cdd:PRK13190  153 LQVNWKRKVATPANWQPGQEGIVPAPSTLDEAE 185
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 7-160 4.79e-30

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: 108.13  E-value: 4.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   7 KAPQFIAPAVlpNGdiiENFNFYKYTENAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTHKAWR 86
Cdd:cd03018     6 KAPDFELPDQ--NG---QEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834951539  87 ntdiDQGGIGhikFIMISD--IKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDA 160
Cdd:cd03018    81 ----EENGLT---FPLLSDfwPHGEVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDLPDYDEALDA 149
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 38-191 3.40e-24

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 94.91  E-value: 3.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  38 VIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTHKAWRNTdIDQGGIGHIKFIMISDIKKNIQQQYGIE 117
Cdd:PRK13191   37 VLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMW-IEKNLKVEVPFPIIADPMGNVAKRLGMI 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834951539 118 HPNLGIA-LRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDAIKHYKKYGQVCPAQWTS----GKHSIIPTEAGIKD 191
Cdd:PRK13191  116 HAESSTAtVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLVDKAGVVTPANWPNneliGDKVINPAPRTIKD 194
PRK13599 PRK13599
peroxiredoxin;
38-184 7.18e-23

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 91.31  E-value: 7.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  38 VIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTHKAWRNTDIDQGGIgHIKFIMISDIKKNIQQQYGIE 117
Cdd:PRK13599   32 VLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNTNI-AIPFPVIADDLGKVSNQLGMI 110

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834951539 118 HPNLGI-ALRATFIIDEKHIIKHQTVNDLFFGRNIHETLRIIDAIKHYKKYGQVCPAQWTSG----KHSIIP 184
Cdd:PRK13599  111 HPGKGTnTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQYGVALPEKWPNNylikDHVIVP 182
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 7-139 4.53e-19

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: 79.13  E-value: 4.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   7 KAPQFIAPAvlpngDIIENFNFYKYTeNAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTHKAWR 86
Cdd:cd03017     2 KAPDFTLPD-----QDGETVSLSDLR-GKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834951539  87 NtdiDQGgighIKFIMISDIKKNIQQQYGI---EHPNLGIALRATFIIDEKHIIKH 139
Cdd:cd03017    76 E---KYG----LPFPLLSDPDGKLAKAYGVwgeKKKKYMGIERSTFLIDPDGKIVK 124
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
37-156 2.97e-18

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 77.21  E-value: 2.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  37 TVIFFWPlDFTYVCPSEIITFNKYYNEFDKRNVKLLGISCDSQYTHKAWRNTDidqggigHIKFIMISDIKKNIQQQYGI 116
Cdd:COG1225    24 VVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKY-------GLPFPLLSDPDGEVAKAYGV 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1834951539 117 EhpnlgiALRATFIIDEKHIIKHQTVNDLFFGRNIHETLR 156
Cdd:COG1225    96 R------GTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 7-139 5.63e-12

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 60.85  E-value: 5.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   7 KAPQFIAPAVLPNGdiiENFNFYKYTeNAITVIFFWPLDFTYVCPSEIITFNKYYNEFDKRNVKLLGISC--DSQYTHKA 84
Cdd:pfam08534   5 KAPDFTLPDAATDG---NTVSLSDFK-GKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSdnDAFFVKRF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1834951539  85 WrntdidqgGIGHIKFIMISDIKKNIQQQYGI---EHPNLGIALRATFIIDEKHIIKH 139
Cdd:pfam08534  81 W--------GKEGLPFPFLSDGNAAFTKALGLpieEDASAGLRSPRYAVIDEDGKVVY 130
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 160-195 9.19e-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: 44.12  E-value: 9.19e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1834951539 160 AIKHYKKYGQVCPAQWTSGKHSIIP----TEAGIKDYLSN 195
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIVPppatQEEAVKRYLEG 40
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 7-140 1.79e-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: 42.96  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539   7 KAPQFiapaVLPNGDIiENFNFYKYTENaITVIFFWP-LDfTYVCPSEIITFNKYYNEFDkrNVKLLGISCDSQYTHKAW 85
Cdd:cd03014     5 KAPDF----TLVTSDL-SEVSLADFAGK-VKVISVFPsID-TPVCATQTKRFNKEAAKLD--NTVVLTISADLPFAQKRW 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834951539  86 RNTdidqggIGHIKFIMISD-IKKNIQQQYGIEHPNLGIALRATFIIDEKHIIKHQ 140
Cdd:cd03014    76 CGA------EGVDNVTTLSDfRDHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYV 125
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 36-140 1.96e-03

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: 36.83  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834951539  36 ITVIFFWpldFTY--VCPSEIITFNKYYNEFDKRNVKLLGISCDSQyTHKAWRNTdIDQGGIghiKFIMISDIKKNIQQQ 113
Cdd:cd02966    21 VVLVNFW---ASWcpPCRAEMPELEALAKEYKDDGVEVVGVNVDDD-DPAAVKAF-LKKYGI---TFPVLLDPDGELAKA 92

                          90       100
                  ....*....|....*....|....*..
gi 1834951539 114 YGIehpnlgIALRATFIIDEKHIIKHQ 140
Cdd:cd02966    93 YGV------RGLPTTFLIDRDGRIRAR 113
 
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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