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Conserved domains on  [gi|960139256|ref|NP_001304671|]
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SH3 domain-binding glutamic acid-rich protein isoform b [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 ...
 1-50 4.02e-21

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 pfam04908:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 92  Bit Score: 80.97  E-value: 4.02e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 960139256    1 MRENvpgekkPQNGIPLPPQIFNEEQYCGDFDSFFSAKEENIIYSFLGLA 50
Cdd:pfam04908  49 MREN------PPNGAPLPPQIFNEDQYCGDYDAFFEAVEANTLYEFLGLA 92
 
Name Accession Description Interval E-value
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
1-50 4.02e-21

SH3-binding, glutamic acid-rich protein;


Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 80.97  E-value: 4.02e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 960139256    1 MRENvpgekkPQNGIPLPPQIFNEEQYCGDFDSFFSAKEENIIYSFLGLA 50
Cdd:pfam04908  49 MREN------PPNGAPLPPQIFNEDQYCGDYDAFFEAVEANTLYEFLGLA 92
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 1-49 1.46e-19

Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a recently-identified subfamily composed of SH3BGR and similar proteins possessing significant sequence similarity to GRX, but without a redox active CXXC motif. The SH3BGR gene was cloned in an effort to identify genes mapping to chromosome 21, which could be involved in the pathogenesis of congenital heart disease affecting Down syndrome newborns. Several human SH3BGR-like (SH3BGRL) genes have been identified since, mapping to different locations in the chromosome. Of these, SH3BGRL3 was identified as a tumor necrosis factor (TNF) alpha inhibitory protein and was also named TIP-B1. Upregulation of expression of SH3BGRL3 is associated with differentiation. It has been suggested that it functions as a regulator of differentiation-related signal transduction pathways.


Pssm-ID: 239328 [Multi-domain]  Cd Length: 92  Bit Score: 76.93  E-value: 1.46e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 960139256   1 MRENVPGEkkpqNGIPLPPQIFNEEQYCGDFDSFFSAKEENIIYSFLGL 49
Cdd:cd03030   48 MRENVPNE----NGKPLPPQIFNGDEYCGDYEAFFEAKENNTLEEFLKL 92
 
Name Accession Description Interval E-value
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
1-50 4.02e-21

SH3-binding, glutamic acid-rich protein;


Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 80.97  E-value: 4.02e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 960139256    1 MRENvpgekkPQNGIPLPPQIFNEEQYCGDFDSFFSAKEENIIYSFLGLA 50
Cdd:pfam04908  49 MREN------PPNGAPLPPQIFNEDQYCGDYDAFFEAVEANTLYEFLGLA 92
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 1-49 1.46e-19

Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a recently-identified subfamily composed of SH3BGR and similar proteins possessing significant sequence similarity to GRX, but without a redox active CXXC motif. The SH3BGR gene was cloned in an effort to identify genes mapping to chromosome 21, which could be involved in the pathogenesis of congenital heart disease affecting Down syndrome newborns. Several human SH3BGR-like (SH3BGRL) genes have been identified since, mapping to different locations in the chromosome. Of these, SH3BGRL3 was identified as a tumor necrosis factor (TNF) alpha inhibitory protein and was also named TIP-B1. Upregulation of expression of SH3BGRL3 is associated with differentiation. It has been suggested that it functions as a regulator of differentiation-related signal transduction pathways.


Pssm-ID: 239328 [Multi-domain]  Cd Length: 92  Bit Score: 76.93  E-value: 1.46e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 960139256   1 MRENVPGEkkpqNGIPLPPQIFNEEQYCGDFDSFFSAKEENIIYSFLGL 49
Cdd:cd03030   48 MRENVPNE----NGKPLPPQIFNGDEYCGDYEAFFEAKENNTLEEFLKL 92
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 14-39 2.00e-04

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: 37.06  E-value: 2.00e-04
                         10        20
                 ....*....|....*....|....*.
gi 960139256  14 GIPLPPQIFNEEQYCGDFDSFFSAKE 39
Cdd:cd02066   47 GWPTVPQIFINGEFIGGYDDLKALHE 72
 
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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