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Conserved domains on  [gi|17535651|ref|NP_496154|]
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Peroxiredoxin-like 2A [Caenorhabditis elegans]

Protein Classification

peroxiredoxin-like family protein( domain architecture ID 10121943)

peroxiredoxin (PRX)-like family protein containing a CXXC motif, with the second cysteine in the motif corresponding to the peroxidatic cysteine of PRX, however, it does not contain the other two residues of the catalytic triad of PRXs; similar to vertebrate peroxiredoxin-like 2A, 2B (prostamide/prostaglandin F synthase) and 2C

CATH:  3.40.30.10
PubMed:  15518547|12517450|10049365
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 59-196 2.84e-29

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


:

Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 106.67  E-value: 2.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535651  59 EQFTADSLFKKGPIMVMAVRRPGCMLCRREAAELHTLLPLLKEKGIELAAVVHETRGANE--FKSWFSGGDVYLDTDRTF 136
Cdd:cd02970  13 ETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESPEKLEafDKGKFLPFPVYADPDRKL 92

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535651 137 YGpnerwlpvWMGFLRFGTYSNVY----KAKKAKVEGNMEGEGRLLGGVYLIANND-IVFTHLEK 196
Cdd:cd02970  93 YR--------ALGLVRSLPWSNTPralwKNAAIGFRGNDEGDGLQLPGVFVIGPDGtILFAHVDR 149
 
Name Accession Description Interval E-value
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 59-196 2.84e-29

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


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 106.67  E-value: 2.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535651  59 EQFTADSLFKKGPIMVMAVRRPGCMLCRREAAELHTLLPLLKEKGIELAAVVHETRGANE--FKSWFSGGDVYLDTDRTF 136
Cdd:cd02970  13 ETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESPEKLEafDKGKFLPFPVYADPDRKL 92

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535651 137 YGpnerwlpvWMGFLRFGTYSNVY----KAKKAKVEGNMEGEGRLLGGVYLIANND-IVFTHLEK 196
Cdd:cd02970  93 YR--------ALGLVRSLPWSNTPralwKNAAIGFRGNDEGDGLQLPGVFVIGPDGtILFAHVDR 149
AhpC-TSA_2 pfam13911
AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide ...
 91-197 2.92e-23

AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 433575  Cd Length: 114  Bit Score: 90.06  E-value: 2.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535651    91 ELHTLLPLLKEKGIELAAVVHETRG-ANEF-KSWFSGGDVYLDTDRTFYGPNERWLPVW----MGFLRFGTYSNVYKAKK 164
Cdd:pfam13911   1 RLSSLKPELDAAGIRLVAIGCGTPGrIEEFiKLTGFPFPVYVDPSRKLYRALGLKRGLSggllPGFLGKGLRNMTRRAKA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17535651   165 AKVEGNMEGEGRLLGGVYLIAN-NDIVFTHLEKE 197
Cdd:pfam13911  81 IGIPGNLGGDGTQLGGTFVFDKgGEILYEHRDRG 114
 
Name Accession Description Interval E-value
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 59-196 2.84e-29

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


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 106.67  E-value: 2.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535651  59 EQFTADSLFKKGPIMVMAVRRPGCMLCRREAAELHTLLPLLKEKGIELAAVVHETRGANE--FKSWFSGGDVYLDTDRTF 136
Cdd:cd02970  13 ETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESPEKLEafDKGKFLPFPVYADPDRKL 92

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535651 137 YGpnerwlpvWMGFLRFGTYSNVY----KAKKAKVEGNMEGEGRLLGGVYLIANND-IVFTHLEK 196
Cdd:cd02970  93 YR--------ALGLVRSLPWSNTPralwKNAAIGFRGNDEGDGLQLPGVFVIGPDGtILFAHVDR 149
AhpC-TSA_2 pfam13911
AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide ...
 91-197 2.92e-23

AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 433575  Cd Length: 114  Bit Score: 90.06  E-value: 2.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535651    91 ELHTLLPLLKEKGIELAAVVHETRG-ANEF-KSWFSGGDVYLDTDRTFYGPNERWLPVW----MGFLRFGTYSNVYKAKK 164
Cdd:pfam13911   1 RLSSLKPELDAAGIRLVAIGCGTPGrIEEFiKLTGFPFPVYVDPSRKLYRALGLKRGLSggllPGFLGKGLRNMTRRAKA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17535651   165 AKVEGNMEGEGRLLGGVYLIAN-NDIVFTHLEKE 197
Cdd:pfam13911  81 IGIPGNLGGDGTQLGGTFVFDKgGEILYEHRDRG 114
 
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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