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Conserved domains on  [gi|19075206|ref|NP_587706|]
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thioredoxin-related chaperone Pmp20 [Schizosaccharomyces pombe]

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, ...
 4-154 3.44e-62

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: 188.15  E-value: 3.44e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206   4 VGSTLPKVTLWE-----NKPEEVVEFPSQGKFIIVGVPGAFTPPCSSQ-VPGYIANEKQFAAKGISGIYVVAVNDVFVTK 77
Cdd:cd03013   1 VGDKLPNVTLFEyvpgpPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQhLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075206  78 AWKKSFDGGEqsGVHFVADWNGEFTKAFDAGFDASGLLGPLRSKRYAAVVENGKVVKVFIENEVTDVDISSADKVLS 154
Cdd:cd03013  81 AWGKALGAKD--KIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENVLK 155
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 4-154 3.44e-62

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: 188.15  E-value: 3.44e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206   4 VGSTLPKVTLWE-----NKPEEVVEFPSQGKFIIVGVPGAFTPPCSSQ-VPGYIANEKQFAAKGISGIYVVAVNDVFVTK 77
Cdd:cd03013   1 VGDKLPNVTLFEyvpgpPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQhLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075206  78 AWKKSFDGGEqsGVHFVADWNGEFTKAFDAGFDASGLLGPLRSKRYAAVVENGKVVKVFIENEVTDVDISSADKVLS 154
Cdd:cd03013  81 AWGKALGAKD--KIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENVLK 155
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-156 2.56e-53

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 166.03  E-value: 2.56e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206   1 MVAVGSTLPKVTLWENKPEEVVEFPSQGKF-----IIVGVPGAFTPPCSS-QVPGYIANEKQFAAKGISGIYVVAVNDVF 74
Cdd:COG0678   1 TIKVGDKLPDVTFKTRTADGPEDVTTDDLFagkkvVLFAVPGAFTPTCSSaHLPGFVELADAFKAKGVDEIACVSVNDAF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206  75 VTKAWKKSFDGGEqsGVHFVADWNGEFTKAFDAGFDASGL-LGpLRSKRYAAVVENGKVVKVFIENEVTDVDISSADKVL 153
Cdd:COG0678  81 VMNAWGKAQGAEG--KITMLADGNGEFTKALGLEVDKSALgFG-KRSQRYAMLVEDGVVKKLNVEPAPGPFEVSDAETLL 157


                ...
gi 19075206 154 SSL 156
Cdd:COG0678 158 AQL 160
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 3-153 8.11e-28

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 100.52  E-value: 8.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206     3 AVGSTLPKVTLWE-NKPEEVV---EFPSqGKFIIVGVPGAFTPPCSSQVPgYIAN-EKQFAAKGISGIYVVAVNDVF-VT 76
Cdd:pfam08534   1 KAGDKAPDFTLPDaATDGNTVslsDFKG-KKVVLNFWPGAFCPTCSAEHP-YLEKlNELYKEKGVDVVAVNSDNDAFfVK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075206    77 KAWKKsfdggEQSGVHFVADWNGEFTKAFDAGFDASGLLGpLRSKRYAAVVENGKVVKVFIENEVTdVDISSADKVL 153
Cdd:pfam08534  79 RFWGK-----EGLPFPFLSDGNAAFTKALGLPIEEDASAG-LRSPRYAVIDEDGKVVYLFVGPEPG-VDVSDAEAVL 148
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 4-154 3.44e-62

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: 188.15  E-value: 3.44e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206   4 VGSTLPKVTLWE-----NKPEEVVEFPSQGKFIIVGVPGAFTPPCSSQ-VPGYIANEKQFAAKGISGIYVVAVNDVFVTK 77
Cdd:cd03013   1 VGDKLPNVTLFEyvpgpPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQhLPGYVENADELKAKGVDEVICVSVNDPFVMK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075206  78 AWKKSFDGGEqsGVHFVADWNGEFTKAFDAGFDASGLLGPLRSKRYAAVVENGKVVKVFIENEVTDVDISSADKVLS 154
Cdd:cd03013  81 AWGKALGAKD--KIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEDPGDVEVSSAENVLK 155
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-156 2.56e-53

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 166.03  E-value: 2.56e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206   1 MVAVGSTLPKVTLWENKPEEVVEFPSQGKF-----IIVGVPGAFTPPCSS-QVPGYIANEKQFAAKGISGIYVVAVNDVF 74
Cdd:COG0678   1 TIKVGDKLPDVTFKTRTADGPEDVTTDDLFagkkvVLFAVPGAFTPTCSSaHLPGFVELADAFKAKGVDEIACVSVNDAF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206  75 VTKAWKKSFDGGEqsGVHFVADWNGEFTKAFDAGFDASGL-LGpLRSKRYAAVVENGKVVKVFIENEVTDVDISSADKVL 153
Cdd:COG0678  81 VMNAWGKAQGAEG--KITMLADGNGEFTKALGLEVDKSALgFG-KRSQRYAMLVEDGVVKKLNVEPAPGPFEVSDAETLL 157


                ...
gi 19075206 154 SSL 156
Cdd:COG0678 158 AQL 160
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 3-153 8.11e-28

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 100.52  E-value: 8.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206     3 AVGSTLPKVTLWE-NKPEEVV---EFPSqGKFIIVGVPGAFTPPCSSQVPgYIAN-EKQFAAKGISGIYVVAVNDVF-VT 76
Cdd:pfam08534   1 KAGDKAPDFTLPDaATDGNTVslsDFKG-KKVVLNFWPGAFCPTCSAEHP-YLEKlNELYKEKGVDVVAVNSDNDAFfVK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075206    77 KAWKKsfdggEQSGVHFVADWNGEFTKAFDAGFDASGLLGpLRSKRYAAVVENGKVVKVFIENEVTdVDISSADKVL 153
Cdd:pfam08534  79 RFWGK-----EGLPFPFLSDGNAAFTKALGLPIEEDASAG-LRSPRYAVIDEDGKVVYLFVGPEPG-VDVSDAEAVL 148
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 28-153 3.34e-25

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: 93.77  E-value: 3.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206  28 GKFIIVGVPGAFTPPCSSQVPGYIANEKQFAAKGISgIYVVAVNDVFVTKAWKKSFDGgeqSGVHFVADWNGEFTKAFDA 107
Cdd:cd02971  23 KWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAE-VLGVSVDSPFSHKAWAEKEGG---LNFPLLSDPDGEFAKAYGV 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 19075206 108 GFDASGLLGplRSKRYAAVV-ENGKVVKVFIENEVTDvdiSSADKVL 153
Cdd:cd02971  99 LIEKSAGGG--LAARATFIIdPDGKIRYVEVEPLPTG---RNAEELL 140
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 27-135 1.62e-08

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: 49.92  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206    27 QGKFIIV-GVPGAFTPPCSSQVPGYIANEKQFAAKGISgIYVVAVNDVFVTKAWKKSfdggEQSGVHFVADWNGEFTKAF 105
Cdd:pfam00578  24 RGKWVVLfFYPADWTPVCTTELPALADLYEEFKKLGVE-VLGVSVDSPESHKAFAEK----YGLPFPLLSDPDGEVARAY 98

                          90       100       110
                  ....*....|....*....|....*....|
gi 19075206   106 DAGFDASGllGPLRSkrYAAVVENGKVVKV 135
Cdd:pfam00578  99 GVLNEEEG--GALRA--TFVIDPDGKVRYI 124
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 4-107 2.07e-06

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: 44.96  E-value: 2.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206   4 VGSTLPKVTLWENKPEEVV--EFPSQGKFIIVGVPGAFTPPCSSQVPGYIANEKQFAAKGIsGIYVVAVNDVFVTKAWKk 81
Cdd:cd03018   3 VGDKAPDFELPDQNGQEVRlsEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGA-EVLGISVDSPFSLRAWA- 80

                        90       100       110
                ....*....|....*....|....*....|
gi 19075206  82 sfdggEQSGVHF--VADWN--GEFTKAFDA 107
Cdd:cd03018  81 -----EENGLTFplLSDFWphGEVAKAYGV 105
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
37-139 1.38e-04

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 39.46  E-value: 1.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075206  37 GAFTPPCSSQVPGYIANEKQFAAKGISgIYVVAVNDVFVTKAWKKSFdggeqsGVHF--VADWNGEFTKAFDAgfdasgl 114
Cdd:COG1225  30 ATWCPGCTAELPELRDLYEEFKDKGVE-VLGVSSDSDEAHKKFAEKY------GLPFplLSDPDGEVAKAYGV------- 95

                        90       100
                ....*....|....*....|....*.
gi 19075206 115 lgplRSKRYAAVV-ENGKVVKVFIEN 139
Cdd:COG1225  96 ----RGTPTTFLIdPDGKIRYVWVGP 117
 
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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