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Conserved domains on  [gi|4759244|ref|NP_004193|]
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thymosin beta-4, Y-chromosomal [Homo sapiens]

Protein Classification

thymosin beta( domain architecture ID 10472827)

thymosin beta-4 family protein similar to Homo sapiens thymosin beta-4, thymosin beta-10 and thymosin beta-15A/15B, which play important roles in the organization of the cytoskeleton

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thymosin pfam01290
Thymosin beta-4 family;
3-41 2.77e-09

Thymosin beta-4 family;


:

Pssm-ID: 396038  Cd Length: 39  Bit Score: 46.18  E-value: 2.77e-09
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 4759244     3 DKPGMAEIEKFDKSKLKKTETQEKNPLSSKETIEQERQA 41
Cdd:pfam01290  1 DKPKVSEVESFDKSKLKKTETQEKNPLPTKEDIEQEKQH 39
 
Name Accession Description Interval E-value
Thymosin pfam01290
Thymosin beta-4 family;
3-41 2.77e-09

Thymosin beta-4 family;


Pssm-ID: 396038  Cd Length: 39  Bit Score: 46.18  E-value: 2.77e-09
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 4759244     3 DKPGMAEIEKFDKSKLKKTETQEKNPLSSKETIEQERQA 41
Cdd:pfam01290  1 DKPKVSEVESFDKSKLKKTETQEKNPLPTKEDIEQEKQH 39
THY smart00152
Thymosin beta actin-binding motif;
7-43 2.91e-05

Thymosin beta actin-binding motif;


Pssm-ID: 128457  Cd Length: 37  Bit Score: 36.03  E-value: 2.91e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4759244      7 MAEIEKFDKSKLKKTETQEKNPLSSKETIEQERQAGE 43
Cdd:smart00152  1 IDEIEHFDSENLKKTETIEKNVLPSKEDIEQEKQHLE 37
WH2_BetaT cd22059
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in beta-Thymosin, and similar ...
 3-36 5.36e-05

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in beta-Thymosin, and similar proteins; This family contains beta-thymosin (betaT; also called thymosin beta or Tbeta) domain which is similar to the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2). Proteins in the beta-thymosin family are small peptides that act as actin monomer (G-actin) sequestering factors. They bind to G-actin into a 1:1 complex, rendering G-actin resistant to polymerization into filaments (F-actin). Thymosin beta 4 (Tbeta4 or TB4) and beta10 (Tbeta10) are minor variants of betaT that bind skeletal muscle actin and inhibit actin polymerization. Thymosin beta4 can also bind to polymerized F-actin. The roles of beta-thymosins also appear to extend beyond G-actin sequestration. Thymosin beta4 has also been linked to a number of additional biological events, including angiogenesis, wound healing, inflammation, and intracellular signaling through kinase activation. Research on thymosin beta10 in breast cancer cells has suggested a relationship with actin cytoskeletal remodeling and cell motility. In addition, thymosins beta4, beta10, and beta15 are highly expressed in several tumor cells, and these have been associated with a higher metastatic potential, possibly due to their function in cell proliferation.


Pssm-ID: 409202  Cd Length: 34  Bit Score: 35.02  E-value: 5.36e-05
                       10        20        30
               ....*....|....*....|....*....|....
gi 4759244   3 DKPGMAEIEKFDKSKLKKTETQEKNPLSSKETIE 36
Cdd:cd22059  1 AENLKSQLEGFDKSKLKKTETQEKNPLPSKETIE 34
 
Name Accession Description Interval E-value
Thymosin pfam01290
Thymosin beta-4 family;
3-41 2.77e-09

Thymosin beta-4 family;


Pssm-ID: 396038  Cd Length: 39  Bit Score: 46.18  E-value: 2.77e-09
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 4759244     3 DKPGMAEIEKFDKSKLKKTETQEKNPLSSKETIEQERQA 41
Cdd:pfam01290  1 DKPKVSEVESFDKSKLKKTETQEKNPLPTKEDIEQEKQH 39
THY smart00152
Thymosin beta actin-binding motif;
7-43 2.91e-05

Thymosin beta actin-binding motif;


Pssm-ID: 128457  Cd Length: 37  Bit Score: 36.03  E-value: 2.91e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4759244      7 MAEIEKFDKSKLKKTETQEKNPLSSKETIEQERQAGE 43
Cdd:smart00152  1 IDEIEHFDSENLKKTETIEKNVLPSKEDIEQEKQHLE 37
WH2_BetaT cd22059
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in beta-Thymosin, and similar ...
 3-36 5.36e-05

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in beta-Thymosin, and similar proteins; This family contains beta-thymosin (betaT; also called thymosin beta or Tbeta) domain which is similar to the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2). Proteins in the beta-thymosin family are small peptides that act as actin monomer (G-actin) sequestering factors. They bind to G-actin into a 1:1 complex, rendering G-actin resistant to polymerization into filaments (F-actin). Thymosin beta 4 (Tbeta4 or TB4) and beta10 (Tbeta10) are minor variants of betaT that bind skeletal muscle actin and inhibit actin polymerization. Thymosin beta4 can also bind to polymerized F-actin. The roles of beta-thymosins also appear to extend beyond G-actin sequestration. Thymosin beta4 has also been linked to a number of additional biological events, including angiogenesis, wound healing, inflammation, and intracellular signaling through kinase activation. Research on thymosin beta10 in breast cancer cells has suggested a relationship with actin cytoskeletal remodeling and cell motility. In addition, thymosins beta4, beta10, and beta15 are highly expressed in several tumor cells, and these have been associated with a higher metastatic potential, possibly due to their function in cell proliferation.


Pssm-ID: 409202  Cd Length: 34  Bit Score: 35.02  E-value: 5.36e-05
                       10        20        30
               ....*....|....*....|....*....|....
gi 4759244   3 DKPGMAEIEKFDKSKLKKTETQEKNPLSSKETIE 36
Cdd:cd22059  1 AENLKSQLEGFDKSKLKKTETQEKNPLPSKETIE 34
 
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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