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Conserved domains on  [gi|1865414425|gb|KAF5473668|]
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hypothetical protein F2P56_010267 [Juglans regia]

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 ...
50-114 6.82e-16

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 cd02999:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 100  Bit Score: 68.54  E-value: 6.82e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1865414425  50 PPLQVDGDFLDraLASKGRNGYTSVLFYASRCPFSCSVLPAYKTLSSMFPQIEHLTVEKSSAMPR 114
Cdd:cd02999     1 PPEEVLNIALD--LMAFNREDYTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPS 63
 
Name Accession Description Interval E-value
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
50-114 6.82e-16

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 68.54  E-value: 6.82e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1865414425  50 PPLQVDGDFLDraLASKGRNGYTSVLFYASRCPFSCSVLPAYKTLSSMFPQIEHLTVEKSSAMPR 114
Cdd:cd02999     1 PPEEVLNIALD--LMAFNREDYTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPS 63
 
Name Accession Description Interval E-value
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
50-114 6.82e-16

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 68.54  E-value: 6.82e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1865414425  50 PPLQVDGDFLDraLASKGRNGYTSVLFYASRCPFSCSVLPAYKTLSSMFPQIEHLTVEKSSAMPR 114
Cdd:cd02999     1 PPEEVLNIALD--LMAFNREDYTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPS 63
 
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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