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Conserved domains on  [gi|808359001|ref|NP_001294788|]
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Thioredoxin 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 ...
119-230 2.18e-06

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 cd03006:

Pssm-ID: 469754  Cd Length: 113  Bit Score: 47.08  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808359001 119 AKPFFHgvHRKLIQDNYDG----TIRLSGNQTMSVILLYSPYSIRSKWFREEYYTTArrlKKLHGNLapYFGATNCFDQN 194
Cdd:cd03006    1 PVPFFS--QRSPVLDFYKGqldyAEELRTDAEVSLVMYYAPWDAQSQAARQEFEQVA---QKLSDQV--LFVAINCWWPQ 73
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 808359001 195 SYCRRKYNLKQYPAMMAQNSALMGSVYNGPLDSVYV 230
Cdd:cd03006   74 GKCRKQKHFFYFPVIHLYYRSRGPIEYKGPMRAPYM 109
 
Name Accession Description Interval E-value
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
119-230 2.18e-06

PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase (ThOX), also called Duox. ThOX proteins are responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones. EFP1 was isolated through a yeast two-hybrid method using the EF-hand fragment of dog Duox1 as a bait. It could be one of the partners in the assembly of a multiprotein complex constituting the thyroid hydrogen peroxide generating system. EFP1 contains two TRX domains related to the redox active TRX domains of protein disulfide isomerase (PDI). This subfamily is composed of the N-terminal TRX domain of EFP1, which contains a CXXS sequence in place of the typical CXXC motif, similar to ERp44. The CXXS motif allows the formation of stable mixed disulfides, crucial for the ER-retention function of ERp44.


Pssm-ID: 239304  Cd Length: 113  Bit Score: 47.08  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808359001 119 AKPFFHgvHRKLIQDNYDG----TIRLSGNQTMSVILLYSPYSIRSKWFREEYYTTArrlKKLHGNLapYFGATNCFDQN 194
Cdd:cd03006    1 PVPFFS--QRSPVLDFYKGqldyAEELRTDAEVSLVMYYAPWDAQSQAARQEFEQVA---QKLSDQV--LFVAINCWWPQ 73
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 808359001 195 SYCRRKYNLKQYPAMMAQNSALMGSVYNGPLDSVYV 230
Cdd:cd03006   74 GKCRKQKHFFYFPVIHLYYRSRGPIEYKGPMRAPYM 109
 
Name Accession Description Interval E-value
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
119-230 2.18e-06

PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase (ThOX), also called Duox. ThOX proteins are responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones. EFP1 was isolated through a yeast two-hybrid method using the EF-hand fragment of dog Duox1 as a bait. It could be one of the partners in the assembly of a multiprotein complex constituting the thyroid hydrogen peroxide generating system. EFP1 contains two TRX domains related to the redox active TRX domains of protein disulfide isomerase (PDI). This subfamily is composed of the N-terminal TRX domain of EFP1, which contains a CXXS sequence in place of the typical CXXC motif, similar to ERp44. The CXXS motif allows the formation of stable mixed disulfides, crucial for the ER-retention function of ERp44.


Pssm-ID: 239304  Cd Length: 113  Bit Score: 47.08  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808359001 119 AKPFFHgvHRKLIQDNYDG----TIRLSGNQTMSVILLYSPYSIRSKWFREEYYTTArrlKKLHGNLapYFGATNCFDQN 194
Cdd:cd03006    1 PVPFFS--QRSPVLDFYKGqldyAEELRTDAEVSLVMYYAPWDAQSQAARQEFEQVA---QKLSDQV--LFVAINCWWPQ 73
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 808359001 195 SYCRRKYNLKQYPAMMAQNSALMGSVYNGPLDSVYV 230
Cdd:cd03006   74 GKCRKQKHFFYFPVIHLYYRSRGPIEYKGPMRAPYM 109
 
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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