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Conserved domains on  [gi|1023669756|ref|NP_001311245|]
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type I iodothyronine deiodinase isoform e [Homo sapiens]

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 ...
 8-113 7.85e-31

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 pfam00837:

Pssm-ID: 469754  Cd Length: 237  Bit Score: 109.18  E-value: 7.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023669756   8 LWLKRLWVLLEVAVHVVVGKVLLILFPDRVKRNILAMgektgMTRNPHFSHDNWiPTFFSTQYFWFVLKVRWQRLEDTTE 87
Cdd:pfam00837   1 LWLRRLWVLLQVPVFVAVGKVLLLLDPARVKKHIVAM-----NGRNPHFSYDNW-ARLYTMQYLWFVWKVQWLDLEKQTE 74

                          90       100
                  ....*....|....*....|....*..
gi 1023669756  88 LGGLAPNCPVVRLSGQR-CNIWEFMQG 113
Cdd:pfam00837  75 PGGLAPNSPVVRLSGQRgCHILDFAQG 101
 
Name Accession Description Interval E-value
T4_deiodinase pfam00837
Iodothyronine deiodinase; Iodothyronine deiodinase converts thyroxine (T4) to 3,5,3 ...
 8-113 7.85e-31

Iodothyronine deiodinase; Iodothyronine deiodinase converts thyroxine (T4) to 3,5,3'-triiodothyronine (T3).


Pssm-ID: 279210  Cd Length: 237  Bit Score: 109.18  E-value: 7.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023669756   8 LWLKRLWVLLEVAVHVVVGKVLLILFPDRVKRNILAMgektgMTRNPHFSHDNWiPTFFSTQYFWFVLKVRWQRLEDTTE 87
Cdd:pfam00837   1 LWLRRLWVLLQVPVFVAVGKVLLLLDPARVKKHIVAM-----NGRNPHFSYDNW-ARLYTMQYLWFVWKVQWLDLEKQTE 74

                          90       100
                  ....*....|....*....|....*..
gi 1023669756  88 LGGLAPNCPVVRLSGQR-CNIWEFMQG 113
Cdd:pfam00837  75 PGGLAPNSPVVRLSGQRgCHILDFAQG 101
 
Name Accession Description Interval E-value
T4_deiodinase pfam00837
Iodothyronine deiodinase; Iodothyronine deiodinase converts thyroxine (T4) to 3,5,3 ...
 8-113 7.85e-31

Iodothyronine deiodinase; Iodothyronine deiodinase converts thyroxine (T4) to 3,5,3'-triiodothyronine (T3).


Pssm-ID: 279210  Cd Length: 237  Bit Score: 109.18  E-value: 7.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023669756   8 LWLKRLWVLLEVAVHVVVGKVLLILFPDRVKRNILAMgektgMTRNPHFSHDNWiPTFFSTQYFWFVLKVRWQRLEDTTE 87
Cdd:pfam00837   1 LWLRRLWVLLQVPVFVAVGKVLLLLDPARVKKHIVAM-----NGRNPHFSYDNW-ARLYTMQYLWFVWKVQWLDLEKQTE 74

                          90       100
                  ....*....|....*....|....*..
gi 1023669756  88 LGGLAPNCPVVRLSGQR-CNIWEFMQG 113
Cdd:pfam00837  75 PGGLAPNSPVVRLSGQRgCHILDFAQG 101
 
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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