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Conserved domains on  [gi|1011956832|ref|WP_062763528|]
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peroxiredoxin [Tistrella mobilis]

Protein Classification

peroxiredoxin( domain architecture ID 10786284)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
2-160 8.24e-113

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440442  Cd Length: 160  Bit Score: 316.65  E-value: 8.24e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   2 TISIGDKIPAATLVEMTADGPNKVSTDELFAGRTVAVFAVPGAFTPTCSARHLPGFVEQADQIAAKGVDEIVCISVNDAF 81
Cdd:COG0678     1 TIKVGDKLPDVTFKTRTADGPEDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832  82 VMGAWGKAQGVDGKVRLLADGNGDLTKALGLTLDGTGFGMGLRSQRYSMLVKDGVVTQLNVE-KPGAFEVSDAGTLLGQL 160
Cdd:COG0678    81 VMNAWGKAQGAEGKITMLADGNGEFTKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVEpAPGPFEVSDAETLLAQL 160
 
Name Accession Description Interval E-value
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
2-160 8.24e-113

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 316.65  E-value: 8.24e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   2 TISIGDKIPAATLVEMTADGPNKVSTDELFAGRTVAVFAVPGAFTPTCSARHLPGFVEQADQIAAKGVDEIVCISVNDAF 81
Cdd:COG0678     1 TIKVGDKLPDVTFKTRTADGPEDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832  82 VMGAWGKAQGVDGKVRLLADGNGDLTKALGLTLDGTGFGMGLRSQRYSMLVKDGVVTQLNVE-KPGAFEVSDAGTLLGQL 160
Cdd:COG0678    81 VMNAWGKAQGAEGKITMLADGNGEFTKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVEpAPGPFEVSDAETLLAQL 160
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 5-157 4.59e-85

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 246.32  E-value: 4.59e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   5 IGDKIPAATLVEMTADGPNKVSTDELFAGRTVAVFAVPGAFTPTCSARHLPGFVEQADQIAAKGVDEIVCISVNDAFVMG 84
Cdd:cd03013     1 VGDKLPNVTLFEYVPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011956832  85 AWGKAQGVDGKVRLLADGNGDLTKALGLTLDGTGFGMGLRSQRYSMLVKDGVVTQLNVEK-PGAFEVSDAGTLL 157
Cdd:cd03013    81 AWGKALGAKDKIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEdPGDVEVSSAENVL 154
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 6-157 1.85e-39

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 130.57  E-value: 1.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   6 GDKIPAATLVEMTADGpNKVSTDElFAGRTVAVFAVPGAFTPTCSARHlPGFVEQADQIAAKGVDEIVCISVNDAF-VMG 84
Cdd:pfam08534   3 GDKAPDFTLPDAATDG-NTVSLSD-FKGKKVVLNFWPGAFCPTCSAEH-PYLEKLNELYKEKGVDVVAVNSDNDAFfVKR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011956832  85 AWGKAqgvDGKVRLLADGNGDLTKALGLTLDGtGFGMGLRSQRYSMLVKDGVVTQLNVEKPGAFEVSDAGTLL 157
Cdd:pfam08534  80 FWGKE---GLPFPFLSDGNAAFTKALGLPIEE-DASAGLRSPRYAVIDEDGKVVYLFVGPEPGVDVSDAEAVL 148
PRK13599 PRK13599
peroxiredoxin;
5-145 3.80e-05

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 42.01  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   5 IGDKIPAATLveMTADGPNKVSTDelFAGRTVAVFAVPGAFTPTCSARHLPgFVEQADQIAAKGVdEIVCISVNDAFVMG 84
Cdd:PRK13599    4 LGEKFPSMEV--VTTQGVKRLPED--YAGKWFVLFSHPADFTPVCTTEFVE-FARKANDFKELNT-ELIGLSVDQVFSHI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1011956832  85 AW----GKAQGVDGKVRLLADGNGDLTKALGLTLDGTgfgmGLRSQRYSMLVKDGVVTQLNVEKP 145
Cdd:PRK13599   78 KWvewiKDNTNIAIPFPVIADDLGKVSNQLGMIHPGK----GTNTVRAVFIVDDKGTIRLIMYYP 138
 
Name Accession Description Interval E-value
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
2-160 8.24e-113

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 316.65  E-value: 8.24e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   2 TISIGDKIPAATLVEMTADGPNKVSTDELFAGRTVAVFAVPGAFTPTCSARHLPGFVEQADQIAAKGVDEIVCISVNDAF 81
Cdd:COG0678     1 TIKVGDKLPDVTFKTRTADGPEDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832  82 VMGAWGKAQGVDGKVRLLADGNGDLTKALGLTLDGTGFGMGLRSQRYSMLVKDGVVTQLNVE-KPGAFEVSDAGTLLGQL 160
Cdd:COG0678    81 VMNAWGKAQGAEGKITMLADGNGEFTKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVEpAPGPFEVSDAETLLAQL 160
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 5-157 4.59e-85

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 246.32  E-value: 4.59e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   5 IGDKIPAATLVEMTADGPNKVSTDELFAGRTVAVFAVPGAFTPTCSARHLPGFVEQADQIAAKGVDEIVCISVNDAFVMG 84
Cdd:cd03013     1 VGDKLPNVTLFEYVPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011956832  85 AWGKAQGVDGKVRLLADGNGDLTKALGLTLDGTGFGMGLRSQRYSMLVKDGVVTQLNVEK-PGAFEVSDAGTLL 157
Cdd:cd03013    81 AWGKALGAKDKIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEdPGDVEVSSAENVL 154
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 6-157 1.85e-39

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 130.57  E-value: 1.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   6 GDKIPAATLVEMTADGpNKVSTDElFAGRTVAVFAVPGAFTPTCSARHlPGFVEQADQIAAKGVDEIVCISVNDAF-VMG 84
Cdd:pfam08534   3 GDKAPDFTLPDAATDG-NTVSLSD-FKGKKVVLNFWPGAFCPTCSAEH-PYLEKLNELYKEKGVDVVAVNSDNDAFfVKR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011956832  85 AWGKAqgvDGKVRLLADGNGDLTKALGLTLDGtGFGMGLRSQRYSMLVKDGVVTQLNVEKPGAFEVSDAGTLL 157
Cdd:pfam08534  80 FWGKE---GLPFPFLSDGNAAFTKALGLPIEE-DASAGLRSPRYAVIDEDGKVVYLFVGPEPGVDVSDAEAVL 148
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 8-157 1.15e-34

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: 118.03  E-value: 1.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   8 KIPAATLvemTADGPNKVSTDElFAGRTVAVFAVPGAFTPTCSArHLPGFVEQADQIAaKGVDEIVCISVNDAFVMGAWG 87
Cdd:cd02971     1 KAPDFTL---PATDGGEVSLSD-FKGKWVVLFFYPKDFTPVCTT-ELCAFRDLAEEFA-KGGAEVLGVSVDSPFSHKAWA 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011956832  88 KAQGVDgKVRLLADGNGDLTKALGLTLDGTGFGMglRSQRYSMLV-KDGVVTQLNVEKPGafEVSDAGTLL 157
Cdd:cd02971    75 EKEGGL-NFPLLSDPDGEFAKAYGVLIEKSAGGG--LAARATFIIdPDGKIRYVEVEPLP--TGRNAEELL 140
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 5-138 5.11e-15

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: 67.25  E-value: 5.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   5 IGDKIPAATLveMTADGpNKVSTDElFAGRTVAVFAVPGAFTPTCsARHLPGFVEQADQIAAKGVdEIVCISVNDAFVMG 84
Cdd:pfam00578   1 VGDKAPDFEL--PDGDG-GTVSLSD-YRGKWVVLFFYPADWTPVC-TTELPALADLYEEFKKLGV-EVLGVSVDSPESHK 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1011956832  85 AWGKAQGVdgKVRLLADGNGDLTKALGLTLDGTGFGmglrsQRYSMLV-KDGVVT 138
Cdd:pfam00578  75 AFAEKYGL--PFPLLSDPDGEVARAYGVLNEEEGGA-----LRATFVIdPDGKVR 122
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 3-138 7.69e-10

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: 54.20  E-value: 7.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   3 ISIGDKIPAATLVEMTADgpnKVSTDELFAGRTVAVFAVPGAFTPTCSARhLPGFVEQADQIAAKGVdEIVCISVNDAFV 82
Cdd:cd03018     1 LEVGDKAPDFELPDQNGQ---EVRLSEFRGRKPVVLVFFPLAFTPVCTKE-LCALRDSLELFEAAGA-EVLGISVDSPFS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1011956832  83 MGAWGKAQGVDgkVRLLADGN--GDLTKALGLTLDGTGFgmglrSQRYSMLV-KDGVVT 138
Cdd:cd03018    76 LRAWAEENGLT--FPLLSDFWphGEVAKAYGVFDEDLGV-----AERAVFVIdRDGIIR 127
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 4-119 1.52e-08

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: 50.66  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   4 SIGDKIPAATLVemTADGpNKVSTDElFAGRTVAVFAVPGAFTPTCSArhlpgFVEQADQIAAKGVD-EIVCISVNDAFV 82
Cdd:cd03014     1 KVGDKAPDFTLV--TSDL-SEVSLAD-FAGKVKVISVFPSIDTPVCAT-----QTKRFNKEAAKLDNtVVLTISADLPFA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1011956832  83 MGAWGKAQGVDgKVRLLAD-GNGDLTKALGLTLDGTGF 119
Cdd:cd03014    72 QKRWCGAEGVD-NVTTLSDfRDHSFGKAYGVLIKDLGL 108
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 7-139 5.10e-08

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: 49.08  E-value: 5.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   7 DKIPAATLvemTADGPNKVSTDElFAGRTVAVFAVPGAFTPTCSaRHLPGFVEQADQIAAKGVdEIVCISVNDAFVMGAW 86
Cdd:cd03017     1 DKAPDFTL---PDQDGETVSLSD-LRGKPVVLYFYPKDDTPGCT-KEACDFRDLYEEFKALGA-VVIGVSPDSVESHAKF 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1011956832  87 GKAQGVdgKVRLLADGNGDLTKALGLTLDGTGFGMGlrSQRYSMLV-KDGVVTQ 139
Cdd:cd03017    75 AEKYGL--PFPLLSDPDGKLAKAYGVWGEKKKKYMG--IERSTFLIdPDGKIVK 124
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 5-142 3.31e-07

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: 47.50  E-value: 3.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   5 IGDKIPAATLVEMTADGPNKVSTDELFAGRTVAVFAVPGAFT---PTcsarHLPGFVEQADQIAAKGVdEIVCISVNDAF 81
Cdd:cd03015     1 VGKKAPDFKATAVVPNGEFKEISLSDYKGKWVVLFFYPLDFTfvcPT----EIIAFSDRYEEFKKLNA-EVLGVSTDSHF 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011956832  82 VMGAW---GKAQGVDGKVR--LLADGNGDLTKALGLTLDGTGFgmglrSQRYSMLV-KDGVVTQLNV 142
Cdd:cd03015    76 SHLAWrntPRKEGGLGKINfpLLADPKKKISRDYGVLDEEEGV-----ALRGTFIIdPEGIIRHITV 137
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-111 2.65e-06

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 45.07  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   1 MTISIGDKIPaatlvEMTAD-----GPNKVSTDElFAGRTVAVFAVPGAFTPTCsarhlP----GFVEQADQIAAKGVdE 71
Cdd:COG0450     1 MMPLIGDKAP-----DFTAEathggEFKKISLSD-YKGKWVVLFFHPADFTFVC-----PtelgAFAKRYEEFKKLGV-E 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1011956832  72 IVCISVNDAFVMGAWG---KAQGVDGKVR--LLADGNGDLTKALG 111
Cdd:COG0450    69 VIGLSVDSVFSHKAWHetiKEKGGIVKIKfpIIADPTGKIARAYG 113
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 8-112 1.72e-05

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


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 42.35  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   8 KIPAATLveMTADGpNKVSTDELFAGRTVAVFAVPGAFTPTCsARHLPGFVEQADQIAAKGVDEIvcisvndAFVMGAWG 87
Cdd:cd02970     1 TAPDFEL--PDAGG-ETVTLSALLGEGPVVVVFYRGFGCPFC-REYLRALSKLLPELDALGVELV-------AVGPESPE 69

                          90       100
                  ....*....|....*....|....*....
gi 1011956832  88 KAQGVDGKVRL----LADGNGDLTKALGL 112
Cdd:cd02970    70 KLEAFDKGKFLpfpvYADPDRKLYRALGL 98
PRK13599 PRK13599
peroxiredoxin;
5-145 3.80e-05

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 42.01  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   5 IGDKIPAATLveMTADGPNKVSTDelFAGRTVAVFAVPGAFTPTCSARHLPgFVEQADQIAAKGVdEIVCISVNDAFVMG 84
Cdd:PRK13599    4 LGEKFPSMEV--VTTQGVKRLPED--YAGKWFVLFSHPADFTPVCTTEFVE-FARKANDFKELNT-ELIGLSVDQVFSHI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1011956832  85 AW----GKAQGVDGKVRLLADGNGDLTKALGLTLDGTgfgmGLRSQRYSMLVKDGVVTQLNVEKP 145
Cdd:PRK13599   78 KWvewiKDNTNIAIPFPVIADDLGKVSNQLGMIHPGK----GTNTVRAVFIVDDKGTIRLIMYYP 138
tpx PRK00522
thiol peroxidase;
4-138 1.38e-03

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 37.19  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011956832   4 SIGDKIPAATLVemtADGPNKVSTDElFAGRTVAVFAVPGAFTPTCSARhlpgfVEQADQIAAKGVDEIV-CISVNDAFV 82
Cdd:PRK00522   19 QVGDKAPDFTLV---ANDLSDVSLAD-FAGKRKVLNIFPSIDTGVCATS-----VRKFNQEAAELDNTVVlCISADLPFA 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1011956832  83 MGAWGKAQGVDGKVRLLADGNGDLTKALGLTLDgTGFGMGLRSQRYSMLVKDGVVT 138
Cdd:PRK00522   90 QKRFCGAEGLENVITLSDFRDHSFGKAYGVAIA-EGPLKGLLARAVFVLDENNKVV 144
 
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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