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Conserved domains on  [gi|1884814991|gb|KAF6206781|]
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hypothetical protein GE061_018017 [Apolygus lucorum]

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 ...
55-111 6.22e-10

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 cd02952:

Pssm-ID: 469754  Cd Length: 119  Bit Score: 52.35  E-value: 6.22e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1884814991  55 LAENLDCKGDGVFLLFMASQREDGVRWCPDCVKAEPIIDGFLEKcsLTKKAHLIVVD 111
Cdd:cd02952    13 LKLLKSHEGKPIFILFYGDKDPDGQSWCPDCVKAEPVVREALKA--APEDCVFIYCD 67
 
Name Accession Description Interval E-value
TRP14_like cd02952
Human TRX-related protein 14 (TRP14)-like family; composed of proteins similar to TRP14, a ...
55-111 6.22e-10

Human TRX-related protein 14 (TRP14)-like family; composed of proteins similar to TRP14, a 14kD cytosolic protein that shows disulfide reductase activity in vitro with a different substrate specificity compared with another human cytosolic protein, TRX1. TRP14 catalyzes the reduction of small disulfide-containing peptides but does not reduce disulfides of ribonucleotide reductase, peroxiredoxin and methionine sulfoxide reductase, which are TRX1 substrates. TRP14 also plays a role in tumor necrosis factor (TNF)-alpha signaling pathways, distinct from that of TRX1. Its depletion promoted TNF-alpha induced activation of c-Jun N-terminal kinase and mitogen-activated protein kinases.


Pssm-ID: 239250  Cd Length: 119  Bit Score: 52.35  E-value: 6.22e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1884814991  55 LAENLDCKGDGVFLLFMASQREDGVRWCPDCVKAEPIIDGFLEKcsLTKKAHLIVVD 111
Cdd:cd02952    13 LKLLKSHEGKPIFILFYGDKDPDGQSWCPDCVKAEPVVREALKA--APEDCVFIYCD 67
DUF953 pfam06110
Eukaryotic protein of unknown function (DUF953); This family consists of several hypothetical ...
66-111 6.77e-09

Eukaryotic protein of unknown function (DUF953); This family consists of several hypothetical eukaryotic proteins of unknown function.


Pssm-ID: 399247  Cd Length: 119  Bit Score: 49.79  E-value: 6.77e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1884814991  66 VFLLFMASQREDGVRWCPDCVKAEPIIDGFLEKcsLTKKAHLIVVD 111
Cdd:pfam06110  22 IFILFSGSKDTTGESWCPDCVRAEPVIYEALKE--APEDVHFIRVD 65
 
Name Accession Description Interval E-value
TRP14_like cd02952
Human TRX-related protein 14 (TRP14)-like family; composed of proteins similar to TRP14, a ...
55-111 6.22e-10

Human TRX-related protein 14 (TRP14)-like family; composed of proteins similar to TRP14, a 14kD cytosolic protein that shows disulfide reductase activity in vitro with a different substrate specificity compared with another human cytosolic protein, TRX1. TRP14 catalyzes the reduction of small disulfide-containing peptides but does not reduce disulfides of ribonucleotide reductase, peroxiredoxin and methionine sulfoxide reductase, which are TRX1 substrates. TRP14 also plays a role in tumor necrosis factor (TNF)-alpha signaling pathways, distinct from that of TRX1. Its depletion promoted TNF-alpha induced activation of c-Jun N-terminal kinase and mitogen-activated protein kinases.


Pssm-ID: 239250  Cd Length: 119  Bit Score: 52.35  E-value: 6.22e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1884814991  55 LAENLDCKGDGVFLLFMASQREDGVRWCPDCVKAEPIIDGFLEKcsLTKKAHLIVVD 111
Cdd:cd02952    13 LKLLKSHEGKPIFILFYGDKDPDGQSWCPDCVKAEPVVREALKA--APEDCVFIYCD 67
DUF953 pfam06110
Eukaryotic protein of unknown function (DUF953); This family consists of several hypothetical ...
66-111 6.77e-09

Eukaryotic protein of unknown function (DUF953); This family consists of several hypothetical eukaryotic proteins of unknown function.


Pssm-ID: 399247  Cd Length: 119  Bit Score: 49.79  E-value: 6.77e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1884814991  66 VFLLFMASQREDGVRWCPDCVKAEPIIDGFLEKcsLTKKAHLIVVD 111
Cdd:pfam06110  22 IFILFSGSKDTTGESWCPDCVRAEPVIYEALKE--APEDVHFIRVD 65
 
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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