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Conserved domains on  [gi|157818479|ref|NP_001102281|]
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twisted gastrulation protein homolog 1 precursor [Rattus norvegicus]

Protein Classification

Tsg domain-containing protein( domain architecture ID 10519929)

Tsg domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tsg pfam04668
Twisted gastrulation (Tsg) protein conserved region; Tsg was identified in Drosophila as being ...
 85-221 1.89e-40

Twisted gastrulation (Tsg) protein conserved region; Tsg was identified in Drosophila as being required to specify the dorsal-most structures in the embryo, for example amnioserosa. Biochemical experiments have revealed three key properties of Tsg: it can synergistically inhibit Dpp/BMP action in both Drosophila and vertebrates by forming a tripartite complete between itself, SOG/chordin and a BMP ligand; Tsg seems to enhance the Tld/BMP-1-mediated cleavage rate of SOG/chordin and may change the preference of site utilization; Tsg can promote the dissociation of chordin cysteine-rich-containing fragments from the ligand to inhibit BMP signalling.


:

Pssm-ID: 461385  Cd Length: 99  Bit Score: 133.57  E-value: 1.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818479   85 PPTSKSTVEELHEPIPSLFRALTEG-DTQLNWNivsfpvaeelthhenlvsfletvnqphhqnvSVPSNNVHAPfpsdke 163
Cdd:pfam04668   1 PLSKKSTVEDLSDPVPSLFRALTEEdDPEQRWS-------------------------------PLKENSITVN------ 43

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157818479  164 hmCTVVYFDDCMSIHQCKISCESMGASKYRWFHNACCECVGPECIDYGSKTVKCMNCM 221
Cdd:pfam04668  44 --CTVAYFDQCMSWNKCKQSCESMGASSYRWFHDGCCECVGPDCLNYGINESRCLNCP 99
 
Name Accession Description Interval E-value
Tsg pfam04668
Twisted gastrulation (Tsg) protein conserved region; Tsg was identified in Drosophila as being ...
 85-221 1.89e-40

Twisted gastrulation (Tsg) protein conserved region; Tsg was identified in Drosophila as being required to specify the dorsal-most structures in the embryo, for example amnioserosa. Biochemical experiments have revealed three key properties of Tsg: it can synergistically inhibit Dpp/BMP action in both Drosophila and vertebrates by forming a tripartite complete between itself, SOG/chordin and a BMP ligand; Tsg seems to enhance the Tld/BMP-1-mediated cleavage rate of SOG/chordin and may change the preference of site utilization; Tsg can promote the dissociation of chordin cysteine-rich-containing fragments from the ligand to inhibit BMP signalling.


Pssm-ID: 461385  Cd Length: 99  Bit Score: 133.57  E-value: 1.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818479   85 PPTSKSTVEELHEPIPSLFRALTEG-DTQLNWNivsfpvaeelthhenlvsfletvnqphhqnvSVPSNNVHAPfpsdke 163
Cdd:pfam04668   1 PLSKKSTVEDLSDPVPSLFRALTEEdDPEQRWS-------------------------------PLKENSITVN------ 43

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157818479  164 hmCTVVYFDDCMSIHQCKISCESMGASKYRWFHNACCECVGPECIDYGSKTVKCMNCM 221
Cdd:pfam04668  44 --CTVAYFDQCMSWNKCKQSCESMGASSYRWFHDGCCECVGPDCLNYGINESRCLNCP 99
 
Name Accession Description Interval E-value
Tsg pfam04668
Twisted gastrulation (Tsg) protein conserved region; Tsg was identified in Drosophila as being ...
 85-221 1.89e-40

Twisted gastrulation (Tsg) protein conserved region; Tsg was identified in Drosophila as being required to specify the dorsal-most structures in the embryo, for example amnioserosa. Biochemical experiments have revealed three key properties of Tsg: it can synergistically inhibit Dpp/BMP action in both Drosophila and vertebrates by forming a tripartite complete between itself, SOG/chordin and a BMP ligand; Tsg seems to enhance the Tld/BMP-1-mediated cleavage rate of SOG/chordin and may change the preference of site utilization; Tsg can promote the dissociation of chordin cysteine-rich-containing fragments from the ligand to inhibit BMP signalling.


Pssm-ID: 461385  Cd Length: 99  Bit Score: 133.57  E-value: 1.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818479   85 PPTSKSTVEELHEPIPSLFRALTEG-DTQLNWNivsfpvaeelthhenlvsfletvnqphhqnvSVPSNNVHAPfpsdke 163
Cdd:pfam04668   1 PLSKKSTVEDLSDPVPSLFRALTEEdDPEQRWS-------------------------------PLKENSITVN------ 43

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157818479  164 hmCTVVYFDDCMSIHQCKISCESMGASKYRWFHNACCECVGPECIDYGSKTVKCMNCM 221
Cdd:pfam04668  44 --CTVAYFDQCMSWNKCKQSCESMGASSYRWFHDGCCECVGPDCLNYGINESRCLNCP 99
 
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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