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Conserved domains on  [gi|54650156|dbj|BAD66880|]
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peroxiredoxin [Entamoeba moshkovskii]

Protein Classification

peroxiredoxin( domain architecture ID 10122432)

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

CATH:  3.40.30.10
EC:  1.11.1.-
Gene Ontology:  GO:0008379
PubMed:  15518547|12517450|10049365|15558583
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 27-199 1.13e-99

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: 286.32  E-value: 1.13e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  27 IGKETPQFKAAAYHPDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:cd03015   1 VGKKAPDFKATAVVPNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156 107 CETEKKNGGVGKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFTD 186
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 54650156 187 QHGAVCPLNWKPG 199
Cdd:cd03015 161 EHGEVCPANWKPG 173
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 27-199 1.13e-99

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: 286.32  E-value: 1.13e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  27 IGKETPQFKAAAYHPDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:cd03015   1 VGKKAPDFKATAVVPNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156 107 CETEKKNGGVGKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFTD 186
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 54650156 187 QHGAVCPLNWKPG 199
Cdd:cd03015 161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
27-217 4.14e-91

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 265.40  E-value: 4.14e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  27 IGKETPQFKAAAYHPDGtIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:COG0450   5 IGDKAPDFTAEATHGGE-FKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAW 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156 107 CETEKKNGGVGKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFTD 186
Cdd:COG0450  84 HETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFVD 163

                       170       180       190
                ....*....|....*....|....*....|.
gi 54650156 187 QHGAVCPLNWKPGNDTIEPSHDGIKKYLSSH 217
Cdd:COG0450 164 KHGEVCPANWKPGDKVIIPPPDLVGKALERF 194
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 25-216 1.44e-73

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 221.32  E-value: 1.44e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156   25 AEIGKETPQFKAAAYHPDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQ 104
Cdd:PTZ00253   6 AKINHPAPSFEEVALMPNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  105 AWCETEKKNGGVGKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQF 184
Cdd:PTZ00253  86 QWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQF 165

                        170       180       190
                 ....*....|....*....|....*....|..
gi 54650156  185 TDQHGAVCPLNWKPGNDTIEPSHDGIKKYLSS 216
Cdd:PTZ00253 166 VEKHGEVCPANWKKGDPTMKPDPNKSKEGFFS 197
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 27-212 1.53e-54

peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one subunit of a two-subunit complex with subunit F(TIGR03140). Usually these are found as an apparent operon. The gene has been characterized in Bacteroides fragilis, where it is important in oxidative stress defense. This gene contains two invariant cysteine residues, one near the N-terminus and one near the C-terminus, each followed immediately by a proline residue. [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 211789  Cd Length: 187  Bit Score: 172.59  E-value: 1.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156    27 IGKETPQFKAAAYHpDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:TIGR03137   4 INTEIKPFKATAYH-NGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAW 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156   107 CETEKKnggVGKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFTD 186
Cdd:TIGR03137  83 HDTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVA 159

                         170       180
                  ....*....|....*....|....*..
gi 54650156   187 QH-GAVCPLNWKPGNDTIEPSHDGIKK 212
Cdd:TIGR03137 160 AHpGEVCPAKWKEGAETLKPSLDLVGK 186
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 27-161 6.33e-46

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: 148.14  E-value: 6.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156    27 IGKETPQFKAaayhPDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:pfam00578   1 VGDKAPDFEL----PDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 54650156   107 CETEkknggvgKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYI 161
Cdd:pfam00578  77 AEKY-------GLPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 27-199 1.13e-99

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: 286.32  E-value: 1.13e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  27 IGKETPQFKAAAYHPDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:cd03015   1 VGKKAPDFKATAVVPNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156 107 CETEKKNGGVGKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFTD 186
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 54650156 187 QHGAVCPLNWKPG 199
Cdd:cd03015 161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
27-217 4.14e-91

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 265.40  E-value: 4.14e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  27 IGKETPQFKAAAYHPDGtIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:COG0450   5 IGDKAPDFTAEATHGGE-FKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAW 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156 107 CETEKKNGGVGKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFTD 186
Cdd:COG0450  84 HETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFVD 163

                       170       180       190
                ....*....|....*....|....*....|.
gi 54650156 187 QHGAVCPLNWKPGNDTIEPSHDGIKKYLSSH 217
Cdd:COG0450 164 KHGEVCPANWKPGDKVIIPPPDLVGKALERF 194
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 25-216 1.44e-73

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 221.32  E-value: 1.44e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156   25 AEIGKETPQFKAAAYHPDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQ 104
Cdd:PTZ00253   6 AKINHPAPSFEEVALMPNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  105 AWCETEKKNGGVGKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQF 184
Cdd:PTZ00253  86 QWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQF 165

                        170       180       190
                 ....*....|....*....|....*....|..
gi 54650156  185 TDQHGAVCPLNWKPGNDTIEPSHDGIKKYLSS 216
Cdd:PTZ00253 166 VEKHGEVCPANWKKGDPTMKPDPNKSKEGFFS 197
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 27-215 5.30e-63

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 196.71  E-value: 5.30e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156   27 IGKETPQFKAAAYhPDGTIKEVDISEY-KGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQA 105
Cdd:PTZ00137  70 VGKLMPSFKGTAL-LNDDLVQFNSSDYfKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKA 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  106 WCETEKKNGGVGKLNFPLISDIKKCISISYGMLNVQaGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFT 185
Cdd:PTZ00137 149 WKELDVRQGGVSPLKFPLFSDISREVSKSFGLLRDE-GFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQFA 227

                        170       180       190
                 ....*....|....*....|....*....|
gi 54650156  186 DQHGAVCPLNWKPGNDTIEPSHDGIKKYLS 215
Cdd:PTZ00137 228 EKTGNVCPVNWKQGDQAMKPDSQSVKQYLS 257
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 27-212 1.53e-54

peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one subunit of a two-subunit complex with subunit F(TIGR03140). Usually these are found as an apparent operon. The gene has been characterized in Bacteroides fragilis, where it is important in oxidative stress defense. This gene contains two invariant cysteine residues, one near the N-terminus and one near the C-terminus, each followed immediately by a proline residue. [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 211789  Cd Length: 187  Bit Score: 172.59  E-value: 1.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156    27 IGKETPQFKAAAYHpDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:TIGR03137   4 INTEIKPFKATAYH-NGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAW 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156   107 CETEKKnggVGKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFTD 186
Cdd:TIGR03137  83 HDTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVA 159

                         170       180
                  ....*....|....*....|....*..
gi 54650156   187 QH-GAVCPLNWKPGNDTIEPSHDGIKK 212
Cdd:TIGR03137 160 AHpGEVCPAKWKEGAETLKPSLDLVGK 186
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 32-176 2.86e-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: 162.33  E-value: 2.86e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  32 PQFKAaayhPDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAWCETEk 111
Cdd:cd02971   3 PDFTL----PATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKE- 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54650156 112 knggvGKLNFPLISDIKKCISISYGMLN---VQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETI 176
Cdd:cd02971  78 -----GGLNFPLLSDPDGEFAKAYGVLIeksAGGGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
PRK15000 PRK15000
peroxiredoxin C;
27-217 1.07e-50

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 163.31  E-value: 1.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156   27 IGKETPQFKAAAYHPDGTIKE-VDISEY-KGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQ 104
Cdd:PRK15000   4 VTRQAPDFTAAAVLGSGEIVDkFNFKQHtNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  105 AWCETEKKNGGVGKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQF 184
Cdd:PRK15000  84 AWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDALQF 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 54650156  185 TDQHGAVCPLNWKPGNDTIEPSHDGIKKYLSSH 217
Cdd:PRK15000 164 HEEHGDVCPAQWEKGKEGMNASPDGVAKYLAEN 196
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 27-205 9.20e-47

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: 153.08  E-value: 9.20e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  27 IGKETPQFKAaayhpDGTIKEVDISEYKGKYLVLLF-YPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQA 105
Cdd:cd03016   1 LGDTAPNFEA-----DTTHGPIKFHDYLGDSWGILFsHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156 106 WCETEKKNGGVgKLNFPLISDIKKCISISYGMLNVQAGISR--RGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQ 183
Cdd:cd03016  76 WIEDIEEYTGV-EIPFPIIADPDREVAKLLGMIDPDAGSTLtvRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQ 154

                       170       180
                ....*....|....*....|..
gi 54650156 184 FTDQHGAVCPLNWKPGNDTIEP 205
Cdd:cd03016 155 LTDKHKVATPANWKPGDDVIVP 176
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 27-161 6.33e-46

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: 148.14  E-value: 6.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156    27 IGKETPQFKAaayhPDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:pfam00578   1 VGDKAPDFEL----PDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 54650156   107 CETEkknggvgKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYI 161
Cdd:pfam00578  77 AEKY-------GLPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
PRK13189 PRK13189
peroxiredoxin; Provisional
 27-205 1.47e-45

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 150.52  E-value: 1.47e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156   27 IGKETPQFKAAAYHpdGTIKEVDisEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:PRK13189  11 IGDKFPEFEVKTTH--GPIKLPD--DYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  107 CETEKKNGGVgKLNFPLISDIKKCISISYGMLNVQAG-ISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFT 185
Cdd:PRK13189  87 VEWIKEKLGV-EIEFPIIADDRGEIAKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQTS 165

                        170       180
                 ....*....|....*....|
gi 54650156  186 DQHGAVCPLNWKPGNDTIEP 205
Cdd:PRK13189 166 DEKGVATPANWPPNDLIKDK 185
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 27-205 5.81e-44

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 146.15  E-value: 5.81e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156   27 IGKETPQFKAAAyhpdgTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:PRK13190   4 LGQKAPDFTVNT-----TKGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  107 CETEKKNGGVgKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFTD 186
Cdd:PRK13190  79 LRDIEERFGI-KIPFPVIADIDKELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQVNW 157

                        170
                 ....*....|....*....
gi 54650156  187 QHGAVCPLNWKPGNDTIEP 205
Cdd:PRK13190 158 KRKVATPANWQPGQEGIVP 176
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 34-212 2.96e-37

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 128.18  E-value: 2.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156   34 FKAAAYHpDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAWCETEKKn 113
Cdd:PRK10382  11 FKNQAFK-NGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAWHSSSET- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  114 ggVGKLNFPLISDIKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFTDQH-GAVC 192
Cdd:PRK10382  89 --IAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHpGEVC 166

                        170       180
                 ....*....|....*....|
gi 54650156  193 PLNWKPGNDTIEPSHDGIKK 212
Cdd:PRK10382 167 PAKWKEGEATLAPSLDLVGK 186
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 26-181 3.22e-37

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: 127.00  E-value: 3.22e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  26 EIGKETPQFKAaayhPDGTIKEVDISEYKG-KYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQ 104
Cdd:cd03018   2 EVGDKAPDFEL----PDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLR 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 54650156 105 AWCEtekKNGgvgkLNFPLISD--IKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKA 181
Cdd:cd03018  78 AWAE---ENG----LTFPLLSDfwPHGEVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDLPDYDEALDA 149
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 27-203 4.64e-35

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 123.42  E-value: 4.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156   27 IGKETPQFKAAAYHpdGTIKEVDisEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:PRK13191   9 IGEKFPEMEVITTH--GKIKLPD--DYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  107 CETEKKNGGVgKLNFPLISDIKKCISISYGMLNVQAGISR-RGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFT 185
Cdd:PRK13191  85 VMWIEKNLKV-EVPFPIIADPMGNVAKRLGMIHAESSTATvRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLV 163

                        170
                 ....*....|....*...
gi 54650156  186 DQHGAVCPLNWkPGNDTI 203
Cdd:PRK13191 164 DKAGVVTPANW-PNNELI 180
PRK13599 PRK13599
peroxiredoxin;
27-204 9.54e-34

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 120.20  E-value: 9.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156   27 IGKETPQFKAAAYHPDGTIKEvdisEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAW 106
Cdd:PRK13599   4 LGEKFPSMEVVTTQGVKRLPE----DYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  107 CETEKKNGGVgKLNFPLISDIKKCISISYGMLNVQAGISR-RGYVIIDDKGIVRYIQINDDGIGRSTDETIRIVKAIQFT 185
Cdd:PRK13599  80 VEWIKDNTNI-AIPFPVIADDLGKVSNQLGMIHPGKGTNTvRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTA 158

                        170
                 ....*....|....*....
gi 54650156  186 DQHGAVCPLNWkPGNDTIE 204
Cdd:PRK13599 159 DQYGVALPEKW-PNNYLIK 176
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 32-164 1.88e-28

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: 104.17  E-value: 1.88e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  32 PQFKAaayhPDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAWCetEK 111
Cdd:cd03017   4 PDFTL----PDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFA--EK 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 54650156 112 KNggvgkLNFPLISDIKKCISISYG---MLNVQAGISRRGYVIIDDKGIVRYIQIN 164
Cdd:cd03017  78 YG-----LPFPLLSDPDGKLAKAYGvwgEKKKKYMGIERSTFLIDPDGKIVKVWRK 128
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
32-177 1.53e-23

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 91.47  E-value: 1.53e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  32 PQFKAaayhPDGTIKEVDISEYKGKYLVLLFYPlDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVYCHQAWCETEk 111
Cdd:COG1225   2 PDFTL----PDLDGKTVSLSDLRGKPVVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKY- 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54650156 112 knggvgKLNFPLISDIKKCISISYGMLNVqagisrRGYVIIDDKGIVRYIQINDDGIGRSTDETIR 177
Cdd:COG1225  76 ------GLPFPLLSDPDGEVAKAYGVRGT------PTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 28-166 4.92e-14

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 66.62  E-value: 4.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156    28 GKETPQFKAAAYHPDGtiKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSV--DSVYCHQA 105
Cdd:pfam08534   3 GDKAPDFTLPDAATDG--NTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSdnDAFFVKRF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54650156   106 WceteKKNGgvgkLNFPLISDIKKCISISYG---MLNVQAGISRRGYVIIDDKGIVRYIQINDD 166
Cdd:pfam08534  81 W----GKEG----LPFPFLSDGNAAFTKALGlpiEEDASAGLRSPRYAVIDEDGKVVYLFVGPE 136
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 26-166 1.32e-12

Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing peroxidatic and resolving cysteines, similar to the homodimeric thiol specific antioxidant (TSA) protein also known as TRX-dependent thiol peroxidase (Tpx). Tpx is a bacterial periplasmic peroxidase which differs from other PRXs in that it shows substrate specificity toward alkyl hydroperoxides over hydrogen peroxide. As with all other PRXs, the peroxidatic cysteine (N-terminal) of Tpx is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Tpx is able to resolve this intermediate by forming an intramolecular disulfide bond with a conserved C-terminal cysteine (the resolving cysteine), which can then be reduced by thioredoxin. This differs from the typical 2-cys PRX which resolves the oxidized cysteine by forming an intermolecular disulfide bond with the resolving cysteine from the other subunit of the homodimer. Atypical 2-cys PRX homodimers have a loop-based interface (A-type for alternate), in contrast with the B-type interface of typical 2-cys and 1-cys PRXs.


Pssm-ID: 239312 [Multi-domain]  Cd Length: 143  Bit Score: 62.60  E-value: 1.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  26 EIGKETPQFKAAayhpDGTIKEVDISEYKGKYLVLLFYP-LDwSSVCPTELIGYSEIFSQFKELNceVLGVSVDSVYCHQ 104
Cdd:cd03014   1 KVGDKAPDFTLV----TSDLSEVSLADFAGKVKVISVFPsID-TPVCATQTKRFNKEAAKLDNTV--VLTISADLPFAQK 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54650156 105 AWCETEkknggvGKLNFPLISD-IKKCISISYGMLNVQAGISRRGYVIIDDKGIVRYIQINDD 166
Cdd:cd03014  74 RWCGAE------GVDNVTTLSDfRDHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYVELVPE 130
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 181-216 8.66e-10

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: 52.21  E-value: 8.66e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 54650156   181 AIQFTDQHGAVCPLNWKPGNDTIEP----SHDGIKKYLSS 216
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIVPppatQEEAVKRYLEG 40
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 28-158 2.75e-07

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 48.40  E-value: 2.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156   28 GKETPQFKAaayhPDGTIKEVDISEYKGKYLVLLFYPLDWSSVCPTELIGYSEIFSQFKELNCEVLGVSVDSVychqawc 107
Cdd:PRK09437   7 GDIAPKFSL----PDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKP------- 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54650156  108 E-----TEKKNggvgkLNFPLISDIKKCISISYG-------MLNVQAGISRRGYvIIDDKGIV 158
Cdd:PRK09437  76 EklsrfAEKEL-----LNFTLLSDEDHQVAEQFGvwgekkfMGKTYDGIHRISF-LIDADGKI 132
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 41-163 4.09e-05

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: 41.45  E-value: 4.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650156  41 PDGTIKEVDISEYKGKYLVLLFypldWSSVCP---TELIGYSEIFSQFKELNCEVLGVSVDSvYCHQAWCETEKKNGgvg 117
Cdd:cd02966   5 PDLDGKPVSLSDLKGKVVLVNF----WASWCPpcrAEMPELEALAKEYKDDGVEVVGVNVDD-DDPAAVKAFLKKYG--- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 54650156 118 kLNFPLISDIKKCISISYGmlnvqagisRRGY---VIIDDKGIVRYIQI 163
Cdd:cd02966  77 -ITFPVLLDPDGELAKAYG---------VRGLpttFLIDRDGRIRARHV 115
 
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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