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Conserved domains on  [gi|392921811|ref|NP_001256578|]
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Glutaredoxin domain-containing protein [Caenorhabditis elegans]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
219-262 9.82e-07

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 cd03028:

Pssm-ID: 469754  Cd Length: 90  Bit Score: 45.95  E-value: 9.82e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 392921811 219 IQSLNDNQIEYTIFDVSTDSEIRFISKALSDCETFPQLFVDGAF 262
Cdd:cd03028   30 VQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGEL 73
 
Name Accession Description Interval E-value
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
219-262 9.82e-07

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: 45.95  E-value: 9.82e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 392921811 219 IQSLNDNQIEYTIFDVSTDSEIRFISKALSDCETFPQLFVDGAF 262
Cdd:cd03028   30 VQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGEL 73
Glutaredoxin pfam00462
Glutaredoxin;
222-260 1.00e-05

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 42.11  E-value: 1.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 392921811  222 LNDNQIEYTIFDVSTDSEIRFISKALSDCETFPQLFVDG 260
Cdd:pfam00462  19 LKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDG 57
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
222-260 9.65e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 37.10  E-value: 9.65e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 392921811 222 LNDNQIEYTIFDVSTDSEIRFISKALSDCETFPQLFVDG 260
Cdd:COG0695   20 LDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFIGG 58
 
Name Accession Description Interval E-value
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
219-262 9.82e-07

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: 45.95  E-value: 9.82e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 392921811 219 IQSLNDNQIEYTIFDVSTDSEIRFISKALSDCETFPQLFVDGAF 262
Cdd:cd03028   30 VQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGEL 73
Glutaredoxin pfam00462
Glutaredoxin;
222-260 1.00e-05

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 42.11  E-value: 1.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 392921811  222 LNDNQIEYTIFDVSTDSEIRFISKALSDCETFPQLFVDG 260
Cdd:pfam00462  19 LKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDG 57
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
222-262 7.13e-05

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: 40.14  E-value: 7.13e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 392921811 222 LNDNQIEYTIFDVSTDSEIRFISKALSDCETFPQLFVDGAF 262
Cdd:cd02066   20 LESLGIEFEEIDILEDGELREELKELSGWPTVPQIFINGEF 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
222-260 9.65e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 37.10  E-value: 9.65e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 392921811 222 LNDNQIEYTIFDVSTDSEIRFISKALSDCETFPQLFVDG 260
Cdd:COG0695   20 LDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFIGG 58
 
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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