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Conserved domains on  [gi|1178431661|ref|NP_001337229|]
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WRB-SH3BGR readthrough isoform 2 [Homo sapiens]

Protein Classification

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 ...
 112-195 4.06e-43

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: 141.45  E-value: 4.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431661 112 QIRKKQQEVVGFLEANKIDFKELDIAGDEDNRRWMRENvpgekkPQNGIPLPPQIFNEEQYCGDFDSFFSAKEENIIYSF 191
Cdd:pfam04908  15 EIKKKQQRVLMILDANKIPFDEVDITKDEEQRRWMREN------PPNGAPLPPQIFNEDQYCGDYDAFFEAVEANTLYEF 88


                  ....
gi 1178431661 192 LGLA 195
Cdd:pfam04908  89 LGLA 92
CHD5 super family cl04507
CHD5-like protein; Members of this family are probably coiled-coil proteins that are similar ...
 17-111 1.10e-24

CHD5-like protein; Members of this family are probably coiled-coil proteins that are similar to the CHD5 (Congenital heart disease 5) protein. In Saccharomyces cerevisiae this protein localizes to the ER and is thought to play a homeostatic role.


The actual alignment was detected with superfamily member pfam04420:

Pssm-ID: 427938  Cd Length: 158  Bit Score: 96.10  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431661  17 FVFGCNVLRILLPSFSSFMSRVLQ----------KDAEQESQMRAEIQDMKQELSTVNMMDEFARYARLERKINKMTDKL 86
Cdd:pfam04420   1 VVFLLILLIKLINTIGKDTINNLLwllylklstsKLAKEQRKLKAEILKLKEELNATSAQDEFAKWAKLNRKHDKLLEEL 80

                          90       100
                  ....*....|....*....|....*
gi 1178431661  87 KTHVKARTAQLAKIKWVISVAFYVL 111
Cdd:pfam04420  81 EKLKKSLSSAKSSFDKLLKKVRWVL 105
 
Name Accession Description Interval E-value
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
112-195 4.06e-43

SH3-binding, glutamic acid-rich protein;


Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 141.45  E-value: 4.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431661 112 QIRKKQQEVVGFLEANKIDFKELDIAGDEDNRRWMRENvpgekkPQNGIPLPPQIFNEEQYCGDFDSFFSAKEENIIYSF 191
Cdd:pfam04908  15 EIKKKQQRVLMILDANKIPFDEVDITKDEEQRRWMREN------PPNGAPLPPQIFNEDQYCGDYDAFFEAVEANTLYEF 88


                  ....
gi 1178431661 192 LGLA 195
Cdd:pfam04908  89 LGLA 92
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 113-194 3.27e-42

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: 138.94  E-value: 3.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431661 113 IRKKQQEVVGFLEANKIDFKELDIAGDEDNRRWMRENVPGEkkpqNGIPLPPQIFNEEQYCGDFDSFFSAKEENIIYSFL 192
Cdd:cd03030    15 IKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPNE----NGKPLPPQIFNGDEYCGDYEAFFEAKENNTLEEFL 90


                  ..
gi 1178431661 193 GL 194
Cdd:cd03030    91 KL 92
CHD5 pfam04420
CHD5-like protein; Members of this family are probably coiled-coil proteins that are similar ...
 17-111 1.10e-24

CHD5-like protein; Members of this family are probably coiled-coil proteins that are similar to the CHD5 (Congenital heart disease 5) protein. In Saccharomyces cerevisiae this protein localizes to the ER and is thought to play a homeostatic role.


Pssm-ID: 427938  Cd Length: 158  Bit Score: 96.10  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431661  17 FVFGCNVLRILLPSFSSFMSRVLQ----------KDAEQESQMRAEIQDMKQELSTVNMMDEFARYARLERKINKMTDKL 86
Cdd:pfam04420   1 VVFLLILLIKLINTIGKDTINNLLwllylklstsKLAKEQRKLKAEILKLKEELNATSAQDEFAKWAKLNRKHDKLLEEL 80

                          90       100
                  ....*....|....*....|....*
gi 1178431661  87 KTHVKARTAQLAKIKWVISVAFYVL 111
Cdd:pfam04420  81 EKLKKSLSSAKSSFDKLLKKVRWVL 105
 
Name Accession Description Interval E-value
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
112-195 4.06e-43

SH3-binding, glutamic acid-rich protein;


Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 141.45  E-value: 4.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431661 112 QIRKKQQEVVGFLEANKIDFKELDIAGDEDNRRWMRENvpgekkPQNGIPLPPQIFNEEQYCGDFDSFFSAKEENIIYSF 191
Cdd:pfam04908  15 EIKKKQQRVLMILDANKIPFDEVDITKDEEQRRWMREN------PPNGAPLPPQIFNEDQYCGDYDAFFEAVEANTLYEF 88


                  ....
gi 1178431661 192 LGLA 195
Cdd:pfam04908  89 LGLA 92
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 113-194 3.27e-42

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: 138.94  E-value: 3.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431661 113 IRKKQQEVVGFLEANKIDFKELDIAGDEDNRRWMRENVPGEkkpqNGIPLPPQIFNEEQYCGDFDSFFSAKEENIIYSFL 192
Cdd:cd03030    15 IKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPNE----NGKPLPPQIFNGDEYCGDYEAFFEAKENNTLEEFL 90


                  ..
gi 1178431661 193 GL 194
Cdd:cd03030    91 KL 92
CHD5 pfam04420
CHD5-like protein; Members of this family are probably coiled-coil proteins that are similar ...
 17-111 1.10e-24

CHD5-like protein; Members of this family are probably coiled-coil proteins that are similar to the CHD5 (Congenital heart disease 5) protein. In Saccharomyces cerevisiae this protein localizes to the ER and is thought to play a homeostatic role.


Pssm-ID: 427938  Cd Length: 158  Bit Score: 96.10  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431661  17 FVFGCNVLRILLPSFSSFMSRVLQ----------KDAEQESQMRAEIQDMKQELSTVNMMDEFARYARLERKINKMTDKL 86
Cdd:pfam04420   1 VVFLLILLIKLINTIGKDTINNLLwllylklstsKLAKEQRKLKAEILKLKEELNATSAQDEFAKWAKLNRKHDKLLEEL 80

                          90       100
                  ....*....|....*....|....*
gi 1178431661  87 KTHVKARTAQLAKIKWVISVAFYVL 111
Cdd:pfam04420  81 EKLKKSLSSAKSSFDKLLKKVRWVL 105
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 115-184 8.38e-18

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: 75.20  E-value: 8.38e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431661 115 KKQQEVVGFLEANKIDFKELDIAGDEDNRRWMRENVpgekkpqnGIPLPPQIFNEEQYCGDFDSFFSAKE 184
Cdd:cd02066    11 PYCKRAKRLLESLGIEFEEIDILEDGELREELKELS--------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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