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Conserved domains on  [gi|1869213705|ref|WP_179267994|]
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redoxin domain-containing protein [Halorarum salinum]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 2-165 2.31e-35

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03018:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 149  Bit Score: 120.46  E-value: 2.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705   2 LQTGDDAPAVTAPmatpdaaseaergnytSDDVAEFDLESALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDAD 81
Cdd:cd03018     1 LEVGDKAPDFELP----------------DQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  82 VYGVSADTPWSLLAFVDEYDLGYPLVSGFNDP--VIAEFGVEREDgplAGIANRAVFVVDADRRITYTWSAD--EPLTFP 157
Cdd:cd03018    65 VLGISVDSPFSLRAWAEENGLTFPLLSDFWPHgeVAKAYGVFDED---LGVAERAVFVIDRDGIIRYAWVSDdgEPRDLP 141


                  ....*...
gi 1869213705 158 DTDELADE 165
Cdd:cd03018   142 DYDEALDA 149
 
Name Accession Description Interval E-value
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 2-165 2.31e-35

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: 120.46  E-value: 2.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705   2 LQTGDDAPAVTAPmatpdaaseaergnytSDDVAEFDLESALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDAD 81
Cdd:cd03018     1 LEVGDKAPDFELP----------------DQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  82 VYGVSADTPWSLLAFVDEYDLGYPLVSGFNDP--VIAEFGVEREDgplAGIANRAVFVVDADRRITYTWSAD--EPLTFP 157
Cdd:cd03018    65 VLGISVDSPFSLRAWAEENGLTFPLLSDFWPHgeVAKAYGVFDED---LGVAERAVFVIDRDGIIRYAWVSDdgEPRDLP 141


                  ....*...
gi 1869213705 158 DTDELADE 165
Cdd:cd03018   142 DYDEALDA 149
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 5-146 7.17e-25

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: 93.06  E-value: 7.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705   5 GDDAPAVTAPmatpdaaseaergnytSDDVAEFDLeSALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDADVYG 84
Cdd:pfam00578   2 GDKAPDFELP----------------DGDGGTVSL-SDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLG 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1869213705  85 VSADTPWSLLAFVDEYDLGYPLVSGFNDPVIAEFGVEREDgplAGIANRAVFVVDADRRITY 146
Cdd:pfam00578  65 VSVDSPESHKAFAEKYGLPFPLLSDPDGEVARAYGVLNEE---EGGALRATFVIDPDGKVRY 123
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
41-169 1.96e-21

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 84.53  E-value: 1.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  41 SALRDGPVALAFFpGVYSRTCTRELCGLRDWRADLADIDADVYGVSADTPWSLLAFVDEYDLGYPLVSGFNDPVIAEFGV 120
Cdd:COG1225    17 SDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPFPLLSDPDGEVAKAYGV 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1869213705 121 EREdgplagianRAVFVVDADRRITYTWSADepltFPDTDELADEIRAA 169
Cdd:COG1225    96 RGT---------PTTFLIDPDGKIRYVWVGP----VDPRPHLEEVLEAL 131
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 31-165 6.02e-11

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 59.19  E-value: 6.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  31 SDDVAEFDLESALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDADVYGVSADTPWSLLAFVdEYD--------L 102
Cdd:PTZ00137   84 NDDLVQFNSSDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAWK-ELDvrqggvspL 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1869213705 103 GYPLVSGFNDPVIAEFGVEREDgplaGIANRAVFVVDADRRITYTW--------SADEPLTFPDTDELADE 165
Cdd:PTZ00137  163 KFPLFSDISREVSKSFGLLRDE----GFSHRASVLVDKAGVVKHVAvydlglgrSVDETLRLFDAVQFAEK 229
 
Name Accession Description Interval E-value
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 2-165 2.31e-35

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: 120.46  E-value: 2.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705   2 LQTGDDAPAVTAPmatpdaaseaergnytSDDVAEFDLESALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDAD 81
Cdd:cd03018     1 LEVGDKAPDFELP----------------DQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  82 VYGVSADTPWSLLAFVDEYDLGYPLVSGFNDP--VIAEFGVEREDgplAGIANRAVFVVDADRRITYTWSAD--EPLTFP 157
Cdd:cd03018    65 VLGISVDSPFSLRAWAEENGLTFPLLSDFWPHgeVAKAYGVFDED---LGVAERAVFVIDRDGIIRYAWVSDdgEPRDLP 141


                  ....*...
gi 1869213705 158 DTDELADE 165
Cdd:cd03018   142 DYDEALDA 149
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 30-162 8.27e-29

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: 103.40  E-value: 8.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  30 TSDDVAEFDLeSALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDADVYGVSADTPWSLLAFVDEY-DLGYPLVS 108
Cdd:cd02971     8 PATDGGEVSL-SDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKEgGLNFPLLS 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1869213705 109 GFNDPVIAEFGVEREDGPLAGIANRAVFVVDADRRITYTWSADEPlTFPDTDEL 162
Cdd:cd02971    87 DPDGEFAKAYGVLIEKSAGGGLAARATFIIDPDGKIRYVEVEPLP-TGRNAEEL 139
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 5-146 7.17e-25

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: 93.06  E-value: 7.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705   5 GDDAPAVTAPmatpdaaseaergnytSDDVAEFDLeSALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDADVYG 84
Cdd:pfam00578   2 GDKAPDFELP----------------DGDGGTVSL-SDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLG 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1869213705  85 VSADTPWSLLAFVDEYDLGYPLVSGFNDPVIAEFGVEREDgplAGIANRAVFVVDADRRITY 146
Cdd:pfam00578  65 VSVDSPESHKAFAEKYGLPFPLLSDPDGEVARAYGVLNEE---EGGALRATFVIDPDGKVRY 123
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 6-149 1.94e-24

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: 92.23  E-value: 1.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705   6 DDAPAVTAPmatpdaaseaergnytSDDVAEFDLeSALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDADVYGV 85
Cdd:cd03017     1 DKAPDFTLP----------------DQDGETVSL-SDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGV 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1869213705  86 SADTPWSLLAFVDEYDLGYPLVSgfnDP---VIAEFGVEREDGPLAGIANRAVFVVDADRRITYTWS 149
Cdd:cd03017    64 SPDSVESHAKFAEKYGLPFPLLS---DPdgkLAKAYGVWGEKKKKYMGIERSTFLIDPDGKIVKVWR 127
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
41-169 1.96e-21

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 84.53  E-value: 1.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  41 SALRDGPVALAFFpGVYSRTCTRELCGLRDWRADLADIDADVYGVSADTPWSLLAFVDEYDLGYPLVSGFNDPVIAEFGV 120
Cdd:COG1225    17 SDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPFPLLSDPDGEVAKAYGV 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1869213705 121 EREdgplagianRAVFVVDADRRITYTWSADepltFPDTDELADEIRAA 169
Cdd:COG1225    96 RGT---------PTTFLIDPDGKIRYVWVGP----VDPRPHLEEVLEAL 131
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 3-162 4.20e-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: 4.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705   3 QTGDDAPAVTAPMATPDaaseaerGNytsddvaEFDLeSALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDADV 82
Cdd:pfam08534   1 KAGDKAPDFTLPDAATD-------GN-------TVSL-SDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  83 YGVSADT-PWSLLAFVDEYDLGYPLVSGFNDPVIAEFGVEREDGPLAGIANRAVFVVDADRRITYTWSADEP-LTFPDTD 160
Cdd:pfam08534  66 VAVNSDNdAFFVKRFWGKEGLPFPFLSDGNAAFTKALGLPIEEDASAGLRSPRYAVIDEDGKVVYLFVGPEPgVDVSDAE 145


                  ..
gi 1869213705 161 EL 162
Cdd:pfam08534 146 AV 147
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 48-139 1.24e-11

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: 59.44  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  48 VALAFFPGVYSRTCTRELCGLRDWRADLADIDADVYGVSADTPWSLLAFVDEY-------DLGYPLVSGFNDPVIAEFGV 120
Cdd:cd03015    32 VVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAWRNTPrkegglgKINFPLLADPKKKISRDYGV 111

                          90
                  ....*....|....*....
gi 1869213705 121 EREDgplAGIANRAVFVVD 139
Cdd:cd03015   112 LDEE---EGVALRGTFIID 127
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 31-165 6.02e-11

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 59.19  E-value: 6.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  31 SDDVAEFDLESALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDADVYGVSADTPWSLLAFVdEYD--------L 102
Cdd:PTZ00137   84 NDDLVQFNSSDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAWK-ELDvrqggvspL 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1869213705 103 GYPLVSGFNDPVIAEFGVEREDgplaGIANRAVFVVDADRRITYTW--------SADEPLTFPDTDELADE 165
Cdd:PTZ00137  163 KFPLFSDISREVSKSFGLLRDE----GFSHRASVLVDKAGVVKHVAvydlglgrSVDETLRLFDAVQFAEK 229
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 2-120 1.43e-09

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 53.79  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705   2 LQTGDDAPAVTAPmatpdaaseAERGNYTSddVAEFdlesalRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDAD 81
Cdd:PRK09437    4 LKAGDIAPKFSLP---------DQDGEQVS--LTDF------QGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVV 66

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1869213705  82 VYGVSADTPWSLLAFVDEYDLGYPLVSGFNDPVIAEFGV 120
Cdd:PRK09437   67 VLGISTDKPEKLSRFAEKELLNFTLLSDEDHQVAEQFGV 105
tpx PRK00522
thiol peroxidase;
107-160 6.11e-09

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 52.21  E-value: 6.11e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1869213705 107 VSGFNDPVIAE-FGVEREDGPLAGIANRAVFVVDADRRITYTWSADEPLTFPDTD 160
Cdd:PRK00522  105 LSDFRDHSFGKaYGVAIAEGPLKGLLARAVFVLDENNKVVYSELVPEITNEPDYD 159
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-144 1.44e-08

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 51.62  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705   1 MLQTGDDAPAVTAPMatpdaaseaergnYTSDDVAEFDLeSALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDA 80
Cdd:COG0450     2 MPLIGDKAPDFTAEA-------------THGGEFKKISL-SDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGV 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1869213705  81 DVYGVSADTPWSLLAFVD-------EYDLGYPLVSgfnDP--VIAE-FGVEREDgplAGIANRAVFVVDADRRI 144
Cdd:COG0450    68 EVIGLSVDSVFSHKAWHEtikekggIVKIKFPIIA---DPtgKIARaYGMLHPE---DGVAVRGVFIIDPDGKI 135
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
2-147 1.44e-06

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 45.85  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705   2 LQTGDDAPAVTApmatpdaaseaergnyTSDDVAEFDLeSALRDGPVALAFFPGVYSRTCTRELcglRDWRADLADID-A 80
Cdd:COG2077    18 PKVGDKAPDFTL----------------VDTDLSDVTL-SDFAGKRKVLNIVPSLDTPVCATST---RKFNEEAAKLDnV 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1869213705  81 DVYGVSADTPWSLLAFVDEYDL-GYPLVSGFNDPVIAE-FGVEREDGPLAGIANRAVFVVDADRRITYT 147
Cdd:COG2077    78 VVLTISADLPFAQKRFCGAEGIdNVVTLSDFRDRSFGKdYGVLIKEGPLLGLLARAVFVLDENGKVVYT 146
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 52-141 2.77e-05

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 42.67  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  52 FFPGVYSRTCTRELCGLRDWRADLADIDADVYGVSADTPWSLLAFVDEYD----LGYPLVSGFNDPVIAEFGVEREDgpl 127
Cdd:PRK10382   38 FYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAWHSSSEtiakIKYAMIGDPTGALTRNFDNMRED--- 114

                          90
                  ....*....|....
gi 1869213705 128 AGIANRAVFVVDAD 141
Cdd:PRK10382  115 EGLADRATFVVDPQ 128
PRK15000 PRK15000
peroxiredoxin C;
18-154 1.37e-04

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 40.81  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  18 PDAASEAERGNytSDDVAEFDLESALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDADVYGVSADTPWSLLAF- 96
Cdd:PRK15000    9 PDFTAAAVLGS--GEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWr 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1869213705  97 ---VDEYDLG---YPLVSGFNDPVIAEFGVERedgPLAGIANRAVFVVDADRRITYTWSADEPL 154
Cdd:PRK15000   87 ntpVDKGGIGpvkYAMVADVKREIQKAYGIEH---PDEGVALRGSFLIDANGIVRHQVVNDLPL 147
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 36-148 2.59e-04

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: 39.26  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  36 EFDLESALRDGPVALAFFPGVYSRTCTRELCGLRDWRADLADIDADVYGVSADTPWSLLAFVDEYDLGYPLVSgfnDP-- 113
Cdd:cd02970    14 TVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESPEKLEAFDKGKFLPFPVYA---DPdr 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1869213705 114 -VIAEFGVERE-----------DGPLAGIANR---------AVFVVDADRRITYTW 148
Cdd:cd02970    91 kLYRALGLVRSlpwsntpralwKNAAIGFRGNdegdglqlpGVFVIGPDGTILFAH 146
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 3-162 4.94e-04

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: 38.33  E-value: 4.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705   3 QTGDDAPAVTApmatpdaaseaergnyTSDDVAEFDLESALrDGPVALAFFPGVYSRTC---TRELcglrdwRADLADID 79
Cdd:cd03014     1 KVGDKAPDFTL----------------VTSDLSEVSLADFA-GKVKVISVFPSIDTPVCatqTKRF------NKEAAKLD 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  80 -ADVYGVSADTPWSLLAFVDEYDL-GYPLVSGFNDPVIAE-FGVEREDgplAGIANRAVFVVDADRRITYTWSADEPLTF 156
Cdd:cd03014    58 nTVVLTISADLPFAQKRWCGAEGVdNVTTLSDFRDHSFGKaYGVLIKD---LGLLARAVFVIDENGKVIYVELVPEITDE 134


                  ....*.
gi 1869213705 157 PDTDEL 162
Cdd:cd03014   135 PDYEAA 140
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 48-145 4.11e-03

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 36.42  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869213705  48 VALAFFPGVYSRTCTRELCGLRDWRADLADIDADVYGVSADTPWSLLAFVDEY-------DLGYPLVSGFNDPVIAEFGV 120
Cdd:PTZ00253   39 VVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWTLQErkkgglgTMAIPMLADKTKSIARSYGV 118

                          90       100
                  ....*....|....*....|....*...
gi 1869213705 121 EREDgplAGIANRAVFVVDAD---RRIT 145
Cdd:PTZ00253  119 LEEE---QGVAYRGLFIIDPKgmlRQIT 143
 
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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