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Conserved domains on  [gi|17555914|ref|NP_497453|]
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Glutaredoxin domain-containing protein [Caenorhabditis elegans]

Protein Classification

glutaredoxin family protein( domain architecture ID 10122541)

glutaredoxin (GRX) family protein belonging to the thioredoxin superfamily, may function as a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins using an active site dithiol, present in a CXXC motif

CATH:  3.40.30.10
Gene Ontology:  GO:0015036
PubMed:  11441809|12074972|9099998|10049365|15558583|14713336
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 73-230 1.73e-59

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


:

Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 184.36  E-value: 1.73e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555914  73 GVIVYLTSCGVLRRSYDRCKNVTQLLEAFRVKYEIRDLNISNFHVAELAEKLKLNvefqkdLIFDSLPLIYVDGYFLGNE 152
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAE------LKAVSLPRVFVDGRYLGGA 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555914 153 KTIVELNDVKLLDNILGKYQNQAPSSVCSECGNRGYIVCRMCHGSRRRHQQNATssvenPFGLVLRCSSCDENGIARC 230
Cdd:cd03031  75 EEVLRLNESGELRKLLKGIRARAGGGVCEGCGGARFVPCSECNGSCKVFAENAT-----AAGGFLRCPECNENGLVRC 147
 
Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 73-230 1.73e-59

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 184.36  E-value: 1.73e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555914  73 GVIVYLTSCGVLRRSYDRCKNVTQLLEAFRVKYEIRDLNISNFHVAELAEKLKLNvefqkdLIFDSLPLIYVDGYFLGNE 152
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAE------LKAVSLPRVFVDGRYLGGA 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555914 153 KTIVELNDVKLLDNILGKYQNQAPSSVCSECGNRGYIVCRMCHGSRRRHQQNATssvenPFGLVLRCSSCDENGIARC 230
Cdd:cd03031  75 EEVLRLNESGELRKLLKGIRARAGGGVCEGCGGARFVPCSECNGSCKVFAENAT-----AAGGFLRCPECNENGLVRC 147
 
Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 73-230 1.73e-59

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 184.36  E-value: 1.73e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555914  73 GVIVYLTSCGVLRRSYDRCKNVTQLLEAFRVKYEIRDLNISNFHVAELAEKLKLNvefqkdLIFDSLPLIYVDGYFLGNE 152
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAE------LKAVSLPRVFVDGRYLGGA 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555914 153 KTIVELNDVKLLDNILGKYQNQAPSSVCSECGNRGYIVCRMCHGSRRRHQQNATssvenPFGLVLRCSSCDENGIARC 230
Cdd:cd03031  75 EEVLRLNESGELRKLLKGIRARAGGGVCEGCGGARFVPCSECNGSCKVFAENAT-----AAGGFLRCPECNENGLVRC 147
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 74-160 3.99e-06

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: 43.22  E-value: 3.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555914  74 VIVYLTS-CGvlrrsydRCKNVTQLLEAFRVKYEIRDLNISNFHVAELAEKLKLnvefqkdlifDSLPLIYVDGYFLGNE 152
Cdd:cd02066   2 VVVFSKStCP-------YCKRAKRLLESLGIEFEEIDILEDGELREELKELSGW----------PTVPQIFINGEFIGGY 64


                ....*...
gi 17555914 153 KTIVELND 160
Cdd:cd02066  65 DDLKALHE 72
 
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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