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Conserved domains on  [gi|17157991|ref|NP_477510|]
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thioredoxin peroxidase 1, isoform A [Drosophila melanogaster]

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
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 ...
 4-175 1.68e-115

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: 325.23  E-value: 1.68e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   4 LQKPAPAFAGTAVVN-GVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAW 82
Cdd:cd03015   1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991  83 INTPRKQGGLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQYTD 162
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 17157991 163 KYGEVCPANWKPG 175
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 ...
 4-175 1.68e-115

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: 325.23  E-value: 1.68e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   4 LQKPAPAFAGTAVVN-GVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAW 82
Cdd:cd03015   1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991  83 INTPRKQGGLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQYTD 162
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 17157991 163 KYGEVCPANWKPG 175
Cdd:cd03015 161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-191 1.73e-110

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 313.55  E-value: 1.73e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   1 MPQLQKPAPAFAGTAVVNGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHL 80
Cdd:COG0450   2 MPLIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991  81 AWINTPRKQGGLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQY 160
Cdd:COG0450  82 AWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQF 161

                       170       180       190
                ....*....|....*....|....*....|.
gi 17157991 161 TDKYGEVCPANWKPGQKTMVADPTKSKEYFE 191
Cdd:COG0450 162 VDKHGEVCPANWKPGDKVIIPPPDLVGKALE 192
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 3-193 1.49e-103

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 296.43  E-value: 1.49e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991    3 QLQKPAPAFAGTAVV-NGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLA 81
Cdd:PTZ00253   7 KINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   82 WINTPRKQGGLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQYT 161
Cdd:PTZ00253  87 WTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFV 166

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17157991  162 DKYGEVCPANWKPGQKTMVADPTKSKEYFETT 193
Cdd:PTZ00253 167 EKHGEVCPANWKKGDPTMKPDPNKSKEGFFSK 198
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
1-179 3.50e-59

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 184.86  E-value: 3.50e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991    1 MPQLQKPAPAFAGTAVVNGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHL 80
Cdd:NF040737  35 MIKVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHK 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   81 AWINTPRKQGGLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQY 160
Cdd:NF040737 115 MWNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQH 194

                        170       180
                 ....*....|....*....|.
gi 17157991  161 T--DKYGEVCPANWKPGQKTM 179
Cdd:NF040737 195 VreTKGTEATPSGWQPGKPTL 215
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 1-179 6.86e-56

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: 174.90  E-value: 6.86e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991     1 MPQLQKPAPAFAGTAVVNGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHL 80
Cdd:TIGR03137   1 MSLINTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991    81 AWINTPRKqggLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQY 160
Cdd:TIGR03137  81 AWHDTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQY 157

                         170       180
                  ....*....|....*....|
gi 17157991   161 TDKY-GEVCPANWKPGQKTM 179
Cdd:TIGR03137 158 VAAHpGEVCPAKWKEGAETL 177
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 6-137 2.72e-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: 148.53  E-value: 2.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991     6 KPAPAFAGTavvNGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAWINT 85
Cdd:pfam00578   3 DKAPDFELP---DGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17157991    86 PrkqgglgSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQI 137
Cdd:pfam00578  80 Y-------GLPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 4-175 1.68e-115

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: 325.23  E-value: 1.68e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   4 LQKPAPAFAGTAVVN-GVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAW 82
Cdd:cd03015   1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991  83 INTPRKQGGLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQYTD 162
Cdd:cd03015  81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|...
gi 17157991 163 KYGEVCPANWKPG 175
Cdd:cd03015 161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-191 1.73e-110

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 313.55  E-value: 1.73e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   1 MPQLQKPAPAFAGTAVVNGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHL 80
Cdd:COG0450   2 MPLIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991  81 AWINTPRKQGGLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQY 160
Cdd:COG0450  82 AWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQF 161

                       170       180       190
                ....*....|....*....|....*....|.
gi 17157991 161 TDKYGEVCPANWKPGQKTMVADPTKSKEYFE 191
Cdd:COG0450 162 VDKHGEVCPANWKPGDKVIIPPPDLVGKALE 192
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 3-193 1.49e-103

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 296.43  E-value: 1.49e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991    3 QLQKPAPAFAGTAVV-NGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLA 81
Cdd:PTZ00253   7 KINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   82 WINTPRKQGGLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQYT 161
Cdd:PTZ00253  87 WTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFV 166

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17157991  162 DKYGEVCPANWKPGQKTMVADPTKSKEYFETT 193
Cdd:PTZ00253 167 EKHGEVCPANWKKGDPTMKPDPNKSKEGFFSK 198
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
1-179 3.50e-59

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 184.86  E-value: 3.50e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991    1 MPQLQKPAPAFAGTAVVNGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHL 80
Cdd:NF040737  35 MIKVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHK 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   81 AWINTPRKQGGLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQY 160
Cdd:NF040737 115 MWNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQH 194

                        170       180
                 ....*....|....*....|.
gi 17157991  161 T--DKYGEVCPANWKPGQKTM 179
Cdd:NF040737 195 VreTKGTEATPSGWQPGKPTL 215
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 7-152 7.56e-57

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: 175.81  E-value: 7.56e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   7 PAPAFAGTAVVngvFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAWINTp 86
Cdd:cd02971   1 KAPDFTLPATD---GGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEK- 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17157991  87 rkqggLGSMDIPLLADKSMKVARDYGVLDEE---TGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETL 152
Cdd:cd02971  77 -----EGGLNFPLLSDPDGEFAKAYGVLIEKsagGGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 6-193 3.12e-56

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 178.22  E-value: 3.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991    6 KPAPAFAGTAVVNGVFKDIKLSDY-KGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAWIN 84
Cdd:PTZ00137  72 KLMPSFKGTALLNDDLVQFNSSDYfKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAWKE 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   85 TPRKQGGLGSMDIPLLADKSMKVARDYGVLDEEtGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQYTDKY 164
Cdd:PTZ00137 152 LDVRQGGVSPLKFPLFSDISREVSKSFGLLRDE-GFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQFAEKT 230

                        170       180
                 ....*....|....*....|....*....
gi 17157991  165 GEVCPANWKPGQKTMVADPTKSKEYFETT 193
Cdd:PTZ00137 231 GNVCPVNWKQGDQAMKPDSQSVKQYLSNR 259
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 1-179 6.86e-56

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: 174.90  E-value: 6.86e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991     1 MPQLQKPAPAFAGTAVVNGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHL 80
Cdd:TIGR03137   1 MSLINTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991    81 AWINTPRKqggLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQY 160
Cdd:TIGR03137  81 AWHDTSEA---IGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQY 157

                         170       180
                  ....*....|....*....|
gi 17157991   161 TDKY-GEVCPANWKPGQKTM 179
Cdd:TIGR03137 158 VAAHpGEVCPAKWKEGAETL 177
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 24-188 4.52e-55

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: 173.50  E-value: 4.52e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991  24 IKLSDYKG-KYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAWINTPRKQGGlGSMDIPLLAD 102
Cdd:cd03016  17 IKFHDYLGdSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEDIEEYTG-VEIPFPIIAD 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991 103 KSMKVARDYGVLDEETGIPF--RGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQYTDKYGEVCPANWKPGQKTMV 180
Cdd:cd03016  96 PDREVAKLLGMIDPDAGSTLtvRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQLTDKHKVATPANWKPGDDVIV 175


                ....*...
gi 17157991 181 AdPTKSKE 188
Cdd:cd03016 176 P-PSVSDE 182
PRK15000 PRK15000
peroxiredoxin C;
1-190 1.61e-54

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 172.17  E-value: 1.61e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991    1 MPQLQKPAPAFAGTAVV-NG-VFKDIKLSDY-KGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQF 77
Cdd:PRK15000   1 MVLVTRQAPDFTAAAVLgSGeIVDKFNFKQHtNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   78 THLAWINTPRKQGGLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQA 157
Cdd:PRK15000  81 VHNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDA 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 17157991  158 FQYTDKYGEVCPANWKPGQKTMVADPTKSKEYF 190
Cdd:PRK15000 161 LQFHEEHGDVCPAQWEKGKEGMNASPDGVAKYL 193
PRK13189 PRK13189
peroxiredoxin; Provisional
 1-175 6.33e-52

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 165.93  E-value: 6.33e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991    1 MPQLQKPAPAFAgtavVNGVFKDIKLSD-YKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTH 79
Cdd:PRK13189   8 MPLIGDKFPEFE----VKTTHGPIKLPDdYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   80 LAWINTPRKQGGLgSMDIPLLADKSMKVARDYGVLDEETG-IPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAF 158
Cdd:PRK13189  84 IKWVEWIKEKLGV-EIEFPIIADDRGEIAKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKAL 162

                        170
                 ....*....|....*..
gi 17157991  159 QYTDKYGEVCPANWKPG 175
Cdd:PRK13189 163 QTSDEKGVATPANWPPN 179
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 6-137 2.72e-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: 148.53  E-value: 2.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991     6 KPAPAFAGTavvNGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAWINT 85
Cdd:pfam00578   3 DKAPDFELP---DGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17157991    86 PrkqgglgSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQI 137
Cdd:pfam00578  80 Y-------GLPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 1-184 1.61e-45

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 149.23  E-value: 1.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991    1 MPQLQKPAPAFAgtavVNGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHL 80
Cdd:PRK13190   1 PVKLGQKAPDFT----VNTTKGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   81 AWINTPRKQGGLgSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQY 160
Cdd:PRK13190  77 AWLRDIEERFGI-KIPFPVIADIDKELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQV 155

                        170       180
                 ....*....|....*....|....
gi 17157991  161 TDKYGEVCPANWKPGQKTMVADPT 184
Cdd:PRK13190 156 NWKRKVATPANWQPGQEGIVPAPS 179
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-179 1.67e-39

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 133.19  E-value: 1.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991    1 MPQLQKPAPAFAGTAVVNGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHL 80
Cdd:PRK10382   1 MSLINTKIKPFKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   81 AWINTPRKqggLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQY 160
Cdd:PRK10382  81 AWHSSSET---IAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQY 157

                        170       180
                 ....*....|....*....|
gi 17157991  161 TDKY-GEVCPANWKPGQKTM 179
Cdd:PRK10382 158 VASHpGEVCPAKWKEGEATL 177
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 24-172 1.31e-38

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 131.89  E-value: 1.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   24 IKLSD-YKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAWINTPRKQGGLgSMDIPLLAD 102
Cdd:PRK13191  25 IKLPDdYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMWIEKNLKV-EVPFPIIAD 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17157991  103 KSMKVARDYGVLDEETGIP-FRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQYTDKYGEVCPANW 172
Cdd:PRK13191 104 PMGNVAKRLGMIHAESSTAtVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLVDKAGVVTPANW 174
PRK13599 PRK13599
peroxiredoxin;
28-172 2.11e-32

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 115.97  E-value: 2.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   28 DYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAWINTPRKQGGLgSMDIPLLADKSMKV 107
Cdd:PRK13599  25 DYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNTNI-AIPFPVIADDLGKV 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17157991  108 ARDYGVLDEETGI-PFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQYTDKYGEVCPANW 172
Cdd:PRK13599 104 SNQLGMIHPGKGTnTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQYGVALPEKW 169
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 7-147 1.21e-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: 109.29  E-value: 1.21e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   7 PAPAFAgtaVVNGVFKDIKLSDYKG-KYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAWint 85
Cdd:cd03018   6 KAPDFE---LPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAW--- 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17157991  86 pRKQGGLGsmdIPLLADKSMK--VARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRS 147
Cdd:cd03018  80 -AEENGLT---FPLLSDFWPHgeVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRD 139
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 6-153 1.23e-29

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: 106.48  E-value: 1.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   6 KPAPAFAGTAVvNGvfKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAWINt 85
Cdd:cd03017   1 DKAPDFTLPDQ-DG--ETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAE- 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17157991  86 prKQGglgsMDIPLLADKSMKVARDYGVLDE---ETGIPFRGLFIIDDKQNLRQITVNDLPVGrSVEETLR 153
Cdd:cd03017  77 --KYG----LPFPLLSDPDGKLAKAYGVWGEkkkKYMGIERSTFLIDPDGKIVKVWRKVKPKG-HAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
8-153 5.57e-27

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 99.55  E-value: 5.57e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   8 APAFAGTAVvNGvfKDIKLSDYKGKYLVLFFYPlDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAWIntpR 87
Cdd:COG1225   1 APDFTLPDL-DG--KTVSLSDLRGKPVVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFA---E 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17157991  88 KQGglgsMDIPLLADKSMKVARDYGVLDEetgipfRGLFIIDDKQNLRQITVNDLPVGRSVEETLR 153
Cdd:COG1225  74 KYG----LPFPLLSDPDGEVAKAYGVRGT------PTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 6-143 6.88e-14

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 65.85  E-value: 6.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991     6 KPAPAFAGTAVVNGvFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDS-QFTHLAWIn 84
Cdd:pfam08534   4 DKAPDFTLPDAATD-GNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNdAFFVKRFW- 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17157991    85 tprKQGGLgsmDIPLLADKSMKVARDYGV---LDEETGIPFRGLFIIDDKQNLRQITVNDLP 143
Cdd:pfam08534  82 ---GKEGL---PFPFLSDGNAAFTKALGLpieEDASAGLRSPRYAVIDEDGKVVYLFVGPEP 137
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 157-192 3.30e-13

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: 61.07  E-value: 3.30e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 17157991   157 AFQYTDKYGEVCPANWKPGQKTMVADPT----KSKEYFET 192
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIVPPPAtqeeAVKRYLEG 40
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 8-131 2.71e-09

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: 53.36  E-value: 2.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   8 APAFAgtaVVNGVFKDIKLSDYKGKYLVLFFYP-LDfTFVCPTEIIAFSESAAEFRKINCEVIgcSTDSQFTHLAWINTP 86
Cdd:cd03014   6 APDFT---LVTSDLSEVSLADFAGKVKVISVFPsID-TPVCATQTKRFNKEAAKLDNTVVLTI--SADLPFAQKRWCGAE 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17157991  87 rkqgGLGSMdIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDK 131
Cdd:cd03014  80 ----GVDNV-TTLSDFRDHSFGKAYGVLIKDLGLLARAVFVIDEN 119
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 24-137 5.15e-07

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 47.24  E-value: 5.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991   24 IKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTD-----SQFThlawintpRKQgglgSMDIP 98
Cdd:PRK09437  23 VSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDkpeklSRFA--------EKE----LLNFT 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 17157991   99 LLADKSMKVARDYGVLDEET-------GIpFRGLFIIDDKQNLRQI 137
Cdd:PRK09437  91 LLSDEDHQVAEQFGVWGEKKfmgktydGI-HRISFLIDADGKIEHV 135
tpx PRK00522
thiol peroxidase;
2-129 1.60e-06

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 46.05  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991    2 PQLQKPAPAFAgtaVVNGVFKDIKLSDYKGKYLVLFFYP-LDfTFVCPTEIIAFSESAAEFRkiNCEVIGCSTDSQFTHL 80
Cdd:PRK00522  18 PQVGDKAPDFT---LVANDLSDVSLADFAGKRKVLNIFPsID-TGVCATSVRKFNQEAAELD--NTVVLCISADLPFAQK 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17157991   81 AWINTPrkqgGLGSMdIPLLADKSMKVARDYGVLDEE---TGIPFRGLFIID 129
Cdd:PRK00522  92 RFCGAE----GLENV-ITLSDFRDHSFGKAYGVAIAEgplKGLLARAVFVLD 138
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 22-137 2.52e-06

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: 44.53  E-value: 2.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991  22 KDIKLSDYKGKYLVLFFY-----PldftfvCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTH--LAWIntprKQGGLgs 94
Cdd:cd02966  10 KPVSLSDLKGKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAavKAFL----KKYGI-- 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 17157991  95 mDIPLLADKSMKVARDYGVldeeTGIPFrgLFIIDDKQNLRQI 137
Cdd:cd02966  78 -TFPVLLDPDGELAKAYGV----RGLPT--TFLIDRDGRIRAR 113
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 26-123 2.38e-03

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: 36.95  E-value: 2.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17157991  26 LSDYKGKYLVLFFYPldfTFVCP---TEIIAFSESAAEFRKINCEVIGCSTDSqfthLAWINTPRKQGGLgsmDIPLLAD 102
Cdd:cd02970  18 SALLGEGPVVVVFYR---GFGCPfcrEYLRALSKLLPELDALGVELVAVGPES----PEKLEAFDKGKFL---PFPVYAD 87

                        90       100
                ....*....|....*....|.
gi 17157991 103 KSMKVARDYGVLDEETGIPFR 123
Cdd:cd02970  88 PDRKLYRALGLVRSLPWSNTP 108
 
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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