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Conserved domains on  [gi|519048201|ref|WP_020204076|]
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glutathione peroxidase [Cupriavidus sp. WS]

Protein Classification

glutathione peroxidase( domain architecture ID 10786287)

glutathione peroxidase is a hybrid protein containing peroxiredoxin (PRX) and glutaredoxin (GRX) domains, similar to Marichromatium gracile glutathione amide-dependent peroxidase that catalyzes the oxidation of glutathione amide (GASH) to produce glutathione amide disulfide (GASSAG)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
5-163 5.02e-109

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440442  Cd Length: 160  Bit Score: 310.48  E-value: 5.02e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201   5 REGQRVPNVSFRVRENNEWKTVTTADLFEGKTIALFSLPGAFTPTCSSTHLPRYNELAPVFAKHGVDAILCVSVNDTFVM 84
Cdd:COG0678    3 KVGDKLPDVTFKTRTADGPEDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDAFVM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201  85 NEWAKDQESEN-IVMIPDGNGEFTEGMGMLVDKTDLGFGKRSWRYSMLVKDGVVEKMFIEPeePGDPFKVSDADTMLGYI 163
Cdd:COG0678   83 NAWGKAQGAEGkITMLADGNGEFTKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVEP--APGPFEVSDAETLLAQL 160
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 164-242 5.87e-40

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 TIGR02190:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 79  Bit Score: 132.66  E-value: 5.87e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519048201  164 APDARKPDQVVVFSKVGCSFCAKAKQMLSDNGYEYIDVPLEHKVRGKVLGAVSGNMTAPQIFINGSLVGDAEALEAYLA 242
Cdd:TIGR02190   1 APQARKPESVVVFTKPGCPFCAKAKATLKEKGYDFEEIPLGNDARGRSLRAVTGATTVPQVFIGGKLIGGSDELEAYLA 79
 
Name Accession Description Interval E-value
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
5-163 5.02e-109

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 310.48  E-value: 5.02e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201   5 REGQRVPNVSFRVRENNEWKTVTTADLFEGKTIALFSLPGAFTPTCSSTHLPRYNELAPVFAKHGVDAILCVSVNDTFVM 84
Cdd:COG0678    3 KVGDKLPDVTFKTRTADGPEDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDAFVM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201  85 NEWAKDQESEN-IVMIPDGNGEFTEGMGMLVDKTDLGFGKRSWRYSMLVKDGVVEKMFIEPeePGDPFKVSDADTMLGYI 163
Cdd:COG0678   83 NAWGKAQGAEGkITMLADGNGEFTKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVEP--APGPFEVSDAETLLAQL 160
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 6-160 1.21e-72

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: 218.20  E-value: 1.21e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201   6 EGQRVPNVSFRVRENNEWKTVTTADLFEGKTIALFSLPGAFTPTCSSTHLPRYNELAPVFAKHGVDAILCVSVNDTFVMN 85
Cdd:cd03013    1 VGDKLPNVTLFEYVPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519048201  86 EWAKDQESEN-IVMIPDGNGEFTEGMGMLVDKTDLGFGKRSWRYSMLVKDGVVEKMFIEPEepGDPFKVSDADTML 160
Cdd:cd03013   81 AWGKALGAKDkIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEED--PGDVEVSSAENVL 154
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 164-242 5.87e-40

Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to an N-terminal peroxiredoxin-like domain.


Pssm-ID: 131245 [Multi-domain]  Cd Length: 79  Bit Score: 132.66  E-value: 5.87e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519048201  164 APDARKPDQVVVFSKVGCSFCAKAKQMLSDNGYEYIDVPLEHKVRGKVLGAVSGNMTAPQIFINGSLVGDAEALEAYLA 242
Cdd:TIGR02190   1 APQARKPESVVVFTKPGCPFCAKAKATLKEKGYDFEEIPLGNDARGRSLRAVTGATTVPQVFIGGKLIGGSDELEAYLA 79
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 171-242 2.43e-32

Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that 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. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -> GSH reductase -> GSH -> GRX domain of hybrid -> PRX domain of hybrid -> peroxide substrate.


Pssm-ID: 239327 [Multi-domain]  Cd Length: 72  Bit Score: 112.99  E-value: 2.43e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519048201 171 DQVVVFSKVGCSFCAKAKQMLSDNGYEYIDVPLEHKVRGKVLGAVSGNMTAPQIFINGSLVGDAEALEAYLA 242
Cdd:cd03029    1 ESVSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGRSLRAVTGAMTVPQVFIDGELIGGSDDLEKYFA 72
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 6-160 1.05e-31

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 113.62  E-value: 1.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201    6 EGQRVPNVSFrVRENNEWKTVTTADlFEGKTIALFSLPGAFTPTCSSTHlPRYNELAPVFAKHGVDAILCVSVNDTF-VM 84
Cdd:pfam08534   2 AGDKAPDFTL-PDAATDGNTVSLSD-FKGKKVVLNFWPGAFCPTCSAEH-PYLEKLNELYKEKGVDVVAVNSDNDAFfVK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519048201   85 NEWAKdqESENIVMIPDGNGEFTEGMGMLVDKtDLGFGKRSWRYSMLVKDGVVEKMFIEPEepgDPFKVSDADTML 160
Cdd:pfam08534  79 RFWGK--EGLPFPFLSDGNAAFTKALGLPIEE-DASAGLRSPRYAVIDEDGKVVYLFVGPE---PGVDVSDAEAVL 148
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
172-242 1.01e-16

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 72.15  E-value: 1.01e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519048201 172 QVVVFSKVGCSFCAKAKQMLSDNG--YEYIDVPLEHKVRGKVLgAVSGNMTAPQIFINGSLVG--DAEALEAYLA 242
Cdd:COG0695    1 KVTLYTTPGCPYCARAKRLLDEKGipYEEIDVDEDPEAREELR-ERSGRRTVPVIFIGGEHLGgfDEGELDALLA 74
Glutaredoxin pfam00462
Glutaredoxin;
173-231 5.27e-15

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 67.14  E-value: 5.27e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519048201  173 VVVFSKVGCSFCAKAKQMLSDNG--YEYIDVPLEHKVRgKVLGAVSGNMTAPQIFINGSLV 231
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGvdFEEIDVDEDPEIR-EELKELSGWPTVPQVFIDGEHI 60
PRK10638 PRK10638
glutaredoxin 3; Provisional
 173-243 1.29e-08

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 50.59  E-value: 1.29e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519048201 173 VVVFSKVGCSFCAKAKQMLSDNGYEYIDVPLE-HKVRGKVLGAVSGNMTAPQIFINGSLVGDAEALEAYLAR 243
Cdd:PRK10638   4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPIDgDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDAR 75
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 173-228 5.19e-05

Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature.


Pssm-ID: 469116 [Multi-domain]  Cd Length: 70  Bit Score: 40.14  E-value: 5.19e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 519048201 173 VVVFSKVGCSFCAKAKQMLSDNG--YEYIDVPLEHKVRGKVLGAVSGNMTAPQIFING 228
Cdd:NF041212   1 VVIYTKPGCPYCAAAKEDLARRGipFEEIDVSKDPEALEEMLRLTGGERIVPVIVEGG 58
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 7-100 1.21e-04

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 41.76  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201   7 GQRVPNVSFrvrenNEWKTVTTADLFEGKTIALFSLPGAFTPTCSSTHLP---RYNElapvFAKHGVDaILCVSVNDTFV 83
Cdd:PRK13190   5 GQKAPDFTV-----NTTKGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAfsrRYED----FKKLGVE-LVGLSVDSIYS 74

                         90
                 ....*....|....*..
gi 519048201  84 MNEWAKDQESENIVMIP 100
Cdd:PRK13190  75 HIAWLRDIEERFGIKIP 91
 
Name Accession Description Interval E-value
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
5-163 5.02e-109

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 310.48  E-value: 5.02e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201   5 REGQRVPNVSFRVRENNEWKTVTTADLFEGKTIALFSLPGAFTPTCSSTHLPRYNELAPVFAKHGVDAILCVSVNDTFVM 84
Cdd:COG0678    3 KVGDKLPDVTFKTRTADGPEDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDAFVM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201  85 NEWAKDQESEN-IVMIPDGNGEFTEGMGMLVDKTDLGFGKRSWRYSMLVKDGVVEKMFIEPeePGDPFKVSDADTMLGYI 163
Cdd:COG0678   83 NAWGKAQGAEGkITMLADGNGEFTKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVEP--APGPFEVSDAETLLAQL 160
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 6-160 1.21e-72

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: 218.20  E-value: 1.21e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201   6 EGQRVPNVSFRVRENNEWKTVTTADLFEGKTIALFSLPGAFTPTCSSTHLPRYNELAPVFAKHGVDAILCVSVNDTFVMN 85
Cdd:cd03013    1 VGDKLPNVTLFEYVPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519048201  86 EWAKDQESEN-IVMIPDGNGEFTEGMGMLVDKTDLGFGKRSWRYSMLVKDGVVEKMFIEPEepGDPFKVSDADTML 160
Cdd:cd03013   81 AWGKALGAKDkIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEED--PGDVEVSSAENVL 154
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 164-242 5.87e-40

Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to an N-terminal peroxiredoxin-like domain.


Pssm-ID: 131245 [Multi-domain]  Cd Length: 79  Bit Score: 132.66  E-value: 5.87e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519048201  164 APDARKPDQVVVFSKVGCSFCAKAKQMLSDNGYEYIDVPLEHKVRGKVLGAVSGNMTAPQIFINGSLVGDAEALEAYLA 242
Cdd:TIGR02190   1 APQARKPESVVVFTKPGCPFCAKAKATLKEKGYDFEEIPLGNDARGRSLRAVTGATTVPQVFIGGKLIGGSDELEAYLA 79
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 9-160 3.22e-35

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: 122.27  E-value: 3.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201   9 RVPNVSFrvrENNEWKTVTTADlFEGKTIALFSLPGAFTPTCSsTHLPRYNELAPVFAKHGVDaILCVSVNDTFVMNEWA 88
Cdd:cd02971    1 KAPDFTL---PATDGGEVSLSD-FKGKWVVLFFYPKDFTPVCT-TELCAFRDLAEEFAKGGAE-VLGVSVDSPFSHKAWA 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519048201  89 KDQESENIVMIPDGNGEFTEGMGMLVDKTDLgfGKRSWRYSMLV-KDGVVEKMFIEPEEpgdpfKVSDADTML 160
Cdd:cd02971   75 EKEGGLNFPLLSDPDGEFAKAYGVLIEKSAG--GGLAARATFIIdPDGKIRYVEVEPLP-----TGRNAEELL 140
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 171-242 2.43e-32

Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that 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. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -> GSH reductase -> GSH -> GRX domain of hybrid -> PRX domain of hybrid -> peroxide substrate.


Pssm-ID: 239327 [Multi-domain]  Cd Length: 72  Bit Score: 112.99  E-value: 2.43e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519048201 171 DQVVVFSKVGCSFCAKAKQMLSDNGYEYIDVPLEHKVRGKVLGAVSGNMTAPQIFINGSLVGDAEALEAYLA 242
Cdd:cd03029    1 ESVSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGRSLRAVTGAMTVPQVFIDGELIGGSDDLEKYFA 72
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 6-160 1.05e-31

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 113.62  E-value: 1.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201    6 EGQRVPNVSFrVRENNEWKTVTTADlFEGKTIALFSLPGAFTPTCSSTHlPRYNELAPVFAKHGVDAILCVSVNDTF-VM 84
Cdd:pfam08534   2 AGDKAPDFTL-PDAATDGNTVSLSD-FKGKKVVLNFWPGAFCPTCSAEH-PYLEKLNELYKEKGVDVVAVNSDNDAFfVK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519048201   85 NEWAKdqESENIVMIPDGNGEFTEGMGMLVDKtDLGFGKRSWRYSMLVKDGVVEKMFIEPEepgDPFKVSDADTML 160
Cdd:pfam08534  79 RFWGK--EGLPFPFLSDGNAAFTKALGLPIEE-DASAGLRSPRYAVIDEDGKVVYLFVGPE---PGVDVSDAEAVL 148
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
172-242 1.01e-16

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 72.15  E-value: 1.01e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519048201 172 QVVVFSKVGCSFCAKAKQMLSDNG--YEYIDVPLEHKVRGKVLgAVSGNMTAPQIFINGSLVG--DAEALEAYLA 242
Cdd:COG0695    1 KVTLYTTPGCPYCARAKRLLDEKGipYEEIDVDEDPEAREELR-ERSGRRTVPVIFIGGEHLGgfDEGELDALLA 74
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 173-240 2.16e-16

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.


Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 71.34  E-value: 2.16e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201 173 VVVFSKVGCSFCAKAKQMLSDNG--YEYIDVpLEHKVRGKVLGAVSGNMTAPQIFINGSLVGDAEALEAY 240
Cdd:cd02066    2 VVVFSKSTCPYCKRAKRLLESLGieFEEIDI-LEDGELREELKELSGWPTVPQIFINGEFIGGYDDLKAL 70
Glutaredoxin pfam00462
Glutaredoxin;
173-231 5.27e-15

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 67.14  E-value: 5.27e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519048201  173 VVVFSKVGCSFCAKAKQMLSDNG--YEYIDVPLEHKVRgKVLGAVSGNMTAPQIFINGSLV 231
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGvdFEEIDVDEDPEIR-EELKELSGWPTVPQVFIDGEHI 60
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 7-140 2.59e-14

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: 2.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201    7 GQRVPNVSfrvRENNEWKTVTTADlFEGKTIALFSLPGAFTPTCsSTHLPRYNELAPVFAKHGVDaILCVSVNDTFVMNE 86
Cdd:pfam00578   2 GDKAPDFE---LPDGDGGTVSLSD-YRGKWVVLFFYPADWTPVC-TTELPALADLYEEFKKLGVE-VLGVSVDSPESHKA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 519048201   87 WAKDQEsENIVMIPDGNGEFTEGMGMLVDKTDLGfgkrsWRYSMLV-KDGVVEKM 140
Cdd:pfam00578  76 FAEKYG-LPFPLLSDPDGEVARAYGVLNEEEGGA-----LRATFVIdPDGKVRYI 124
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 173-240 1.11e-11

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.


Pssm-ID: 239511 [Multi-domain]  Cd Length: 82  Bit Score: 59.09  E-value: 1.11e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519048201 173 VVVFSKVGCSFCAKAKQMLSDNGYEYIDVPLEHKVRG----KVLGAVSGNMTAPQIFINGSLVGDAEALEAY 240
Cdd:cd03419    2 VVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGseiqDYLQELTGQRTVPNVFIGGKFIGGCDDLMAL 73
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 173-239 6.79e-10

Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily.


Pssm-ID: 239510 [Multi-domain]  Cd Length: 75  Bit Score: 54.13  E-value: 6.79e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519048201 173 VVVFSKVGCSFCAKAKQMLSDNG--YEYIDVPLEHKVRGKVLGAVSGNMTAPQIFINGSLVG---DAEALEA 239
Cdd:cd03418    2 VEIYTKPNCPYCVRAKALLDKKGvdYEEIDVDGDPALREEMINRSGGRRTVPQIFIGDVHIGgcdDLYALER 73
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 172-238 2.12e-09

Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of uncharacterized proteins containing a GRX domain and additional domains DEP and DUF547, both of which have unknown functions. GRX is a glutathione (GSH) dependent reductase containing a redox active CXXC motif in a TRX fold. It has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins, GRX is involved in many cellular functions.


Pssm-ID: 239325 [Multi-domain]  Cd Length: 73  Bit Score: 52.41  E-value: 2.12e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 519048201 172 QVVVFSKVGCSFCAKAKQMLSDNGYEYIDVPLE-HKVRGKVLGAVSGNMTAPQIFINGSLVGDAEALE 238
Cdd:cd03027    2 RVTIYSRLGCEDCTAVRLFLREKGLPYVEINIDiFPERKAELEERTGSSVVPQIFFNEKLVGGLTDLK 69
PRK10638 PRK10638
glutaredoxin 3; Provisional
 173-243 1.29e-08

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 50.59  E-value: 1.29e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519048201 173 VVVFSKVGCSFCAKAKQMLSDNGYEYIDVPLE-HKVRGKVLGAVSGNMTAPQIFINGSLVGDAEALEAYLAR 243
Cdd:PRK10638   4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPIDgDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDAR 75
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
7-113 6.25e-08

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 51.23  E-value: 6.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201   7 GQRVPNVSFRVRENNEWKTVTTADlFEGKTIALFSLPGAFTPTCsSTHLPRYNELAPVFAKHGVDaILCVSVNDTFVMNE 86
Cdd:COG0450    6 GDKAPDFTAEATHGGEFKKISLSD-YKGKWVVLFFHPADFTFVC-PTELGAFAKRYEEFKKLGVE-VIGLSVDSVFSHKA 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 519048201  87 WAKD-QESENIV-----MIPDGNGEFTEGMGML 113
Cdd:COG0450   83 WHETiKEKGGIVkikfpIIADPTGKIARAYGML 115
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 5-156 1.87e-07

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: 49.19  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201   5 REGQRVPnvSFRVRENNEwKTVTTADLFEGKTIALFSLPGAFTPTCsSTHLPRYNELAPVFAKHGVDAiLCVSVNDTFVM 84
Cdd:cd03018    2 EVGDKAP--DFELPDQNG-QEVRLSEFRGRKPVVLVFFPLAFTPVC-TKELCALRDSLELFEAAGAEV-LGISVDSPFSL 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519048201  85 NEWAkDQESENIVMIPDGN--GEFTEGMGMLVDktDLGFGKRSwrySMLV-KDGVVE-KMFIEPEEPGDPFKVSDA 156
Cdd:cd03018   77 RAWA-EENGLTFPLLSDFWphGEVAKAYGVFDE--DLGVAERA---VFVIdRDGIIRyAWVSDDGEPRDLPDYDEA 146
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 173-241 5.06e-07

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.


Pssm-ID: 239274 [Multi-domain]  Cd Length: 73  Bit Score: 46.06  E-value: 5.06e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519048201 173 VVVFSKVGCSFCAKAKQMLSDNG--YEYIDVPLEHKVRGKvLGAVSGNMTAPQIFING-SLVG-DAEALEAYL 241
Cdd:cd02976    2 VTVYTKPDCPYCKATKRFLDERGipFEEVDVDEDPEALEE-LKKLNGYRSVPVVVIGDeHLSGfRPDKLRALL 73
grxA PRK11200
glutaredoxin 1; Provisional
 172-240 6.48e-07

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 46.18  E-value: 6.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201 172 QVVVFSKVGCSFCAKAKQM-------LSDNGYEYIDV--------PLEHKVrGKvlgAVSgnmTAPQIFINGSLVGDAEA 236
Cdd:PRK11200   2 FVVIFGRPGCPYCVRAKELaeklseeRDDFDYRYVDIhaegiskaDLEKTV-GK---PVE---TVPQIFVDQKHIGGCTD 74


                 ....
gi 519048201 237 LEAY 240
Cdd:PRK11200  75 FEAY 78
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 39-113 2.76e-06

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: 46.76  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201  39 LFSLPGAFTPTCsSTHLPRYNELAPVFAKHGVDaILCVSVNDTFVMNEWAKDQESENIVMIP-----DGNGEFTEGMGML 113
Cdd:cd03016   30 LFSHPADFTPVC-TTELGAFAKLAPEFKKRNVK-LIGLSVDSVESHIKWIEDIEEYTGVEIPfpiiaDPDREVAKLLGMI 107
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 173-239 3.69e-06

Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.


Pssm-ID: 274023 [Multi-domain]  Cd Length: 99  Bit Score: 44.37  E-value: 3.69e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519048201  173 VVVFSKVGCSFCAKAKQMLSDNG-----YEyIDVPLEHKVRGKVLGAVSGNMTAPQIFINGSLVGDAEALEA 239
Cdd:TIGR02189  10 VVIFSRSSCCMCHVVKRLLLTLGvnpavHE-IDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMA 80
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 169-232 1.13e-05

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


Pssm-ID: 239326  Cd Length: 90  Bit Score: 42.87  E-value: 1.13e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519048201 169 KPDQVVVFSKvG------CSFCAKAKQMLSDNG--YEYIDVPLEHKVRGKvLGAVSGNMTAPQIFINGSLVG 232
Cdd:cd03028    6 KENPVVLFMK-GtpeeprCGFSRKVVQILNQLGvdFGTFDILEDEEVRQG-LKEYSNWPTFPQLYVNGELVG 75
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 7-125 3.83e-05

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: 42.57  E-value: 3.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201   7 GQRVPNVSFRvreNNEWKTVTTADlFEGKTIALFSLPGAFTPTCSsTHLPRYNELApvfAKHGVDAILCVSVNDTFVMNE 86
Cdd:cd03014    3 GDKAPDFTLV---TSDLSEVSLAD-FAGKVKVISVFPSIDTPVCA-TQTKRFNKEA---AKLDNTVVLTISADLPFAQKR 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 519048201  87 WAKDQESENIVMIPD-GNGEFTEGMGMLVDktDLGFGKRS 125
Cdd:cd03014   75 WCGAEGVDNVTTLSDfRDHSFGKAYGVLIK--DLGLLARA 112
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 173-228 5.19e-05

Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature.


Pssm-ID: 469116 [Multi-domain]  Cd Length: 70  Bit Score: 40.14  E-value: 5.19e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 519048201 173 VVVFSKVGCSFCAKAKQMLSDNG--YEYIDVPLEHKVRGKVLGAVSGNMTAPQIFING 228
Cdd:NF041212   1 VVIYTKPGCPYCAAAKEDLARRGipFEEIDVSKDPEALEEMLRLTGGERIVPVIVEGG 58
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 24-141 1.02e-04

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: 40.99  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201  24 KTVTTADlFEGKTIALFSLPGAFTPTCsSTHLPRYNELAPVFAKHGVdAILCVSVNDTFVMNEWAKDQESeNIVMIPDGN 103
Cdd:cd03017   14 ETVSLSD-LRGKPVVLYFYPKDDTPGC-TKEACDFRDLYEEFKALGA-VVIGVSPDSVESHAKFAEKYGL-PFPLLSDPD 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 519048201 104 GEFTEGMGMLVDKTDLGFG-KRSwrySMLV-KDGVVEKMF 141
Cdd:cd03017   90 GKLAKAYGVWGEKKKKYMGiERS---TFLIdPDGKIVKVW 126
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 7-100 1.21e-04

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 41.76  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201   7 GQRVPNVSFrvrenNEWKTVTTADLFEGKTIALFSLPGAFTPTCSSTHLP---RYNElapvFAKHGVDaILCVSVNDTFV 83
Cdd:PRK13190   5 GQKAPDFTV-----NTTKGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAfsrRYED----FKKLGVE-LVGLSVDSIYS 74

                         90
                 ....*....|....*..
gi 519048201  84 MNEWAKDQESENIVMIP 100
Cdd:PRK13190  75 HIAWLRDIEERFGIKIP 91
PRK13599 PRK13599
peroxiredoxin;
32-148 1.73e-03

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 38.54  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519048201  32 FEGKTIALFSLPGAFTPTCsSTHLPRYNELAPVFAKHGVDaILCVSVNDTFV---MNEWAKDQESENI--VMIPDGNGEF 106
Cdd:PRK13599  26 YAGKWFVLFSHPADFTPVC-TTEFVEFARKANDFKELNTE-LIGLSVDQVFShikWVEWIKDNTNIAIpfPVIADDLGKV 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 519048201 107 TEGMGMLvdktDLGFGKRSWRYSMLVKD-GVVEKMFIEPEEPG 148
Cdd:PRK13599 104 SNQLGMI----HPGKGTNTVRAVFIVDDkGTIRLIMYYPQEVG 142
 
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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