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Conserved domains on  [gi|78706776|ref|NP_001027191|]
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peroxiredoxin 5, isoform B [Drosophila melanogaster]

Protein Classification

peroxiredoxin family protein( domain architecture ID 10122413)

peroxiredoxin family protein such as peroxiredoxin 5, a thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively, playing a role in cell protection against oxidative stress by detoxifying peroxides

CATH:  3.40.30.10
EC:  1.11.1.-
Gene Ontology:  GO:0004601
PubMed:  15518547|12517450|15558583|10049365
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 37-187 5.05e-80

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: 234.76  E-value: 5.05e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776  37 VGDSLPSVDLFED--SPANKINTGDLVNGKKVIIFGVPGAFTPGCSKTHLPGYVSSADELKSKqGVDEIVCVSVNDPFVM 114
Cdd:cd03013   1 VGDKLPNVTLFEYvpGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAK-GVDEVICVSVNDPFVM 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706776 115 SAWGKEHGAAGKVRLLADPAGGFTKALDVTIDLPPLG-GVRSKRYSLVVENGKVTELNVEPDGTGLSCSLANNI 187
Cdd:cd03013  80 KAWGKALGAKDKIRFLADGNGEFTKALGLTLDLSAAGgGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENV 153
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 37-187 5.05e-80

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: 234.76  E-value: 5.05e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776  37 VGDSLPSVDLFED--SPANKINTGDLVNGKKVIIFGVPGAFTPGCSKTHLPGYVSSADELKSKqGVDEIVCVSVNDPFVM 114
Cdd:cd03013   1 VGDKLPNVTLFEYvpGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAK-GVDEVICVSVNDPFVM 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706776 115 SAWGKEHGAAGKVRLLADPAGGFTKALDVTIDLPPLG-GVRSKRYSLVVENGKVTELNVEPDGTGLSCSLANNI 187
Cdd:cd03013  80 KAWGKALGAKDKIRFLADGNGEFTKALGLTLDLSAAGgGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENV 153
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
34-176 1.81e-78

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 231.13  E-value: 1.81e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776  34 MVKVGDSLPSVDLF---EDSPANkINTGDLVNGKKVIIFGVPGAFTPGCSKTHLPGYVSSADELKSKqGVDEIVCVSVND 110
Cdd:COG0678   1 TIKVGDKLPDVTFKtrtADGPED-VTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAK-GVDEIACVSVND 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706776 111 PFVMSAWGKEHGAAGKVRLLADPAGGFTKALDVTIDLPPLG-GVRSKRYSLVVENGKVTELNVEPDG 176
Cdd:COG0678  79 AFVMNAWGKAQGAEGKITMLADGNGEFTKALGLEVDKSALGfGKRSQRYAMLVEDGVVKKLNVEPAP 145
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 36-177 1.54e-38

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 129.41  E-value: 1.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776    36 KVGDSLPSVDLFE-DSPANKINTGDLvNGKKVIIFGVPGAFTPGCSKTHLpgYVSSADELKSKQGVDEIVCVSVNDPF-V 113
Cdd:pfam08534   1 KAGDKAPDFTLPDaATDGNTVSLSDF-KGKKVVLNFWPGAFCPTCSAEHP--YLEKLNELYKEKGVDVVAVNSDNDAFfV 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706776   114 MSAWGKEHGaagKVRLLADPAGGFTKALDVTIDLPPLGGVRSKRYSLVVENGKVTELNVEPDGT 177
Cdd:pfam08534  78 KRFWGKEGL---PFPFLSDGNAAFTKALGLPIEEDASAGLRSPRYAVIDEDGKVVYLFVGPEPG 138
tpx PRK00522
thiol peroxidase;
30-175 1.28e-03

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 37.96  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776   30 TSAAMVKVGDSLPSV-----DLFEDSPANkintgdlVNGKKVIIFGVPGAFTPGCSKThlpgyVSSADELKSKQGVDEIV 104
Cdd:PRK00522  13 VAGSLPQVGDKAPDFtlvanDLSDVSLAD-------FAGKRKVLNIFPSIDTGVCATS-----VRKFNQEAAELDNTVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776  105 CVSVNDPFVMSAWGKEHGAAGKVRL--LADPAggFTKALDVTIDLPPLGGVRSkRYSLVV-ENGKVT------ELNVEPD 175
Cdd:PRK00522  81 CISADLPFAQKRFCGAEGLENVITLsdFRDHS--FGKAYGVAIAEGPLKGLLA-RAVFVLdENNKVVyselvpEITNEPD 157
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 37-187 5.05e-80

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: 234.76  E-value: 5.05e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776  37 VGDSLPSVDLFED--SPANKINTGDLVNGKKVIIFGVPGAFTPGCSKTHLPGYVSSADELKSKqGVDEIVCVSVNDPFVM 114
Cdd:cd03013   1 VGDKLPNVTLFEYvpGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAK-GVDEVICVSVNDPFVM 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706776 115 SAWGKEHGAAGKVRLLADPAGGFTKALDVTIDLPPLG-GVRSKRYSLVVENGKVTELNVEPDGTGLSCSLANNI 187
Cdd:cd03013  80 KAWGKALGAKDKIRFLADGNGEFTKALGLTLDLSAAGgGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENV 153
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
34-176 1.81e-78

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 231.13  E-value: 1.81e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776  34 MVKVGDSLPSVDLF---EDSPANkINTGDLVNGKKVIIFGVPGAFTPGCSKTHLPGYVSSADELKSKqGVDEIVCVSVND 110
Cdd:COG0678   1 TIKVGDKLPDVTFKtrtADGPED-VTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAK-GVDEIACVSVND 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706776 111 PFVMSAWGKEHGAAGKVRLLADPAGGFTKALDVTIDLPPLG-GVRSKRYSLVVENGKVTELNVEPDG 176
Cdd:COG0678  79 AFVMNAWGKAQGAEGKITMLADGNGEFTKALGLEVDKSALGfGKRSQRYAMLVEDGVVKKLNVEPAP 145
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 36-177 1.54e-38

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 129.41  E-value: 1.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776    36 KVGDSLPSVDLFE-DSPANKINTGDLvNGKKVIIFGVPGAFTPGCSKTHLpgYVSSADELKSKQGVDEIVCVSVNDPF-V 113
Cdd:pfam08534   1 KAGDKAPDFTLPDaATDGNTVSLSDF-KGKKVVLNFWPGAFCPTCSAEHP--YLEKLNELYKEKGVDVVAVNSDNDAFfV 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706776   114 MSAWGKEHGaagKVRLLADPAGGFTKALDVTIDLPPLGGVRSKRYSLVVENGKVTELNVEPDGT 177
Cdd:pfam08534  78 KRFWGKEGL---PFPFLSDGNAAFTKALGLPIEEDASAGLRSPRYAVIDEDGKVVYLFVGPEPG 138
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 41-178 1.73e-36

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: 123.81  E-value: 1.73e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776  41 LPSVDLFeDSPANKINTGDLvNGKKVIIFGVPGAFTPGCSkTHLPGYVSSADELksKQGVDEIVCVSVNDPFVMSAWGKE 120
Cdd:cd02971   2 APDFTLP-ATDGGEVSLSDF-KGKWVVLFFYPKDFTPVCT-TELCAFRDLAEEF--AKGGAEVLGVSVDSPFSHKAWAEK 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 78706776 121 HGAAgKVRLLADPAGGFTKALDVTIDLPPLGGvRSKRYSLVV-ENGKVTELNVEPDGTG 178
Cdd:cd02971  77 EGGL-NFPLLSDPDGEFAKAYGVLIEKSAGGG-LAARATFIIdPDGKIRYVEVEPLPTG 133
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 37-169 3.71e-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: 68.40  E-value: 3.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776    37 VGDSLPSVDLfEDSPANKINTGDLvNGKKVIIFGVPGAFTPGCsKTHLPGYVSSADELKsKQGVdEIVCVSVNDPFVMSA 116
Cdd:pfam00578   1 VGDKAPDFEL-PDGDGGTVSLSDY-RGKWVVLFFYPADWTPVC-TTELPALADLYEEFK-KLGV-EVLGVSVDSPESHKA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 78706776   117 WGKEHGAagKVRLLADPAGGFTKALDVTIDLPPLGgvrsKRYSLVV-ENGKVTE 169
Cdd:pfam00578  76 FAEKYGL--PFPLLSDPDGEVARAYGVLNEEEGGA----LRATFVIdPDGKVRY 123
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 35-176 1.39e-09

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: 1.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776  35 VKVGDSLPSVDLfEDSPANKINTGDLVNGKKVIIFGVPGAFTPGCSKtHLPGYVSSADELkSKQGVdEIVCVSVNDPFVM 114
Cdd:cd03018   1 LEVGDKAPDFEL-PDQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTK-ELCALRDSLELF-EAAGA-EVLGISVDSPFSL 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78706776 115 SAWGKEHGAagKVRLLAD--PAGGFTKALDVTIDLPplgGVrSKRYSLVV-ENGKVTELNVEPDG 176
Cdd:cd03018  77 RAWAEENGL--TFPLLSDfwPHGEVAKAYGVFDEDL---GV-AERAVFVIdRDGIIRYAWVSDDG 135
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 39-176 2.31e-07

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: 47.93  E-value: 2.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776  39 DSLPSVDLfEDSPANKINTGDLVnGKKVIIFGVPGAFTPGCSKtHLPGYVSSADELKsKQGVdEIVCVSVNDPFVMSAWG 118
Cdd:cd03017   1 DKAPDFTL-PDQDGETVSLSDLR-GKPVVLYFYPKDDTPGCTK-EACDFRDLYEEFK-ALGA-VVIGVSPDSVESHAKFA 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78706776 119 KEHGAagKVRLLADPAGGFTKALDVTIDLPPLGGvRSKRYSLVV-ENGKVTEL--NVEPDG 176
Cdd:cd03017  76 EKYGL--PFPLLSDPDGKLAKAYGVWGEKKKKYM-GIERSTFLIdPDGKIVKVwrKVKPKG 133
tpx PRK00522
thiol peroxidase;
30-175 1.28e-03

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 37.96  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776   30 TSAAMVKVGDSLPSV-----DLFEDSPANkintgdlVNGKKVIIFGVPGAFTPGCSKThlpgyVSSADELKSKQGVDEIV 104
Cdd:PRK00522  13 VAGSLPQVGDKAPDFtlvanDLSDVSLAD-------FAGKRKVLNIFPSIDTGVCATS-----VRKFNQEAAELDNTVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776  105 CVSVNDPFVMSAWGKEHGAAGKVRL--LADPAggFTKALDVTIDLPPLGGVRSkRYSLVV-ENGKVT------ELNVEPD 175
Cdd:PRK00522  81 CISADLPFAQKRFCGAEGLENVITLsdFRDHS--FGKAYGVAIAEGPLKGLLA-RAVFVLdENNKVVyselvpEITNEPD 157
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 36-175 1.95e-03

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: 36.79  E-value: 1.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776  36 KVGDSLPSVDLFeDSPANKINTGDLVnGKKVIIFGVPGAFTPGCSKT--HLpgyvssADELKSKQGVDeIVCVSVNDPFV 113
Cdd:cd03014   1 KVGDKAPDFTLV-TSDLSEVSLADFA-GKVKVISVFPSIDTPVCATQtkRF------NKEAAKLDNTV-VLTISADLPFA 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776 114 MSAWGKEHGAAgKVRLLADPAGG-FTKALDVTIdlPPLGgvRSKRYSLVV-ENGKVT------ELNVEPD 175
Cdd:cd03014  72 QKRWCGAEGVD-NVTTLSDFRDHsFGKAYGVLI--KDLG--LLARAVFVIdENGKVIyvelvpEITDEPD 136
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 54-143 1.97e-03

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: 37.48  E-value: 1.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706776  54 KINTGDLvNGKKVIIFGVPGAFTPGCSkTHLPGYVSSADELKsKQGVdEIVCVSVNDPFVMSAW---GKEHGAAGKVR-- 128
Cdd:cd03015  21 EISLSDY-KGKWVVLFFYPLDFTFVCP-TEIIAFSDRYEEFK-KLNA-EVLGVSTDSHFSHLAWrntPRKEGGLGKINfp 96

                        90
                ....*....|....*
gi 78706776 129 LLADPAGGFTKALDV 143
Cdd:cd03015  97 LLADPKKKISRDYGV 111
 
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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