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Conserved domains on  [gi|24980968|gb|AAH39801|]
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3110003A17Rik protein, partial [Mus musculus]

Protein Classification

costars family protein( domain architecture ID 10631454)

costars family protein similar to Dictyostelium discoideum protein costars that modulates actin dynamics and cell motility

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Costars pfam14705
Costars; This domain is found both alone and at the C-terminus of actin-binding Rho-activating ...
 25-102 8.58e-36

Costars; This domain is found both alone and at the C-terminus of actin-binding Rho-activating protein (ABRA). It binds to actin, and in muscle regulates the actin cytoskeleton and cell motility. It has a winged helix-like fold consisting of three alpha-helices and four antiparallel beta strands. Unlike typical winged helix proteins it does not bind to DNA, but contains a hydrophobic groove which may be responsible for interaction with other proteins.


:

Pssm-ID: 464274 [Multi-domain]  Cd Length: 76  Bit Score: 116.44  E-value: 8.58e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24980968    25 NVEHEVNLLVEEIHRLGSKNADGKLSVKFGVLFqdDRCANLFEALVGTLKAAKRRKIVTYAGELLLQGVHDDVDIVLL 102
Cdd:pfam14705   1 HVDREILELCEIIKRLGTKDADGKIVVTFGVLF--ERYANISEKLVGTLLRARKHGLVDFEGEMLLQGRDDDVDITLL 76
 
Name Accession Description Interval E-value
Costars pfam14705
Costars; This domain is found both alone and at the C-terminus of actin-binding Rho-activating ...
 25-102 8.58e-36

Costars; This domain is found both alone and at the C-terminus of actin-binding Rho-activating protein (ABRA). It binds to actin, and in muscle regulates the actin cytoskeleton and cell motility. It has a winged helix-like fold consisting of three alpha-helices and four antiparallel beta strands. Unlike typical winged helix proteins it does not bind to DNA, but contains a hydrophobic groove which may be responsible for interaction with other proteins.


Pssm-ID: 464274 [Multi-domain]  Cd Length: 76  Bit Score: 116.44  E-value: 8.58e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24980968    25 NVEHEVNLLVEEIHRLGSKNADGKLSVKFGVLFqdDRCANLFEALVGTLKAAKRRKIVTYAGELLLQGVHDDVDIVLL 102
Cdd:pfam14705   1 HVDREILELCEIIKRLGTKDADGKIVVTFGVLF--ERYANISEKLVGTLLRARKHGLVDFEGEMLLQGRDDDVDITLL 76
 
Name Accession Description Interval E-value
Costars pfam14705
Costars; This domain is found both alone and at the C-terminus of actin-binding Rho-activating ...
 25-102 8.58e-36

Costars; This domain is found both alone and at the C-terminus of actin-binding Rho-activating protein (ABRA). It binds to actin, and in muscle regulates the actin cytoskeleton and cell motility. It has a winged helix-like fold consisting of three alpha-helices and four antiparallel beta strands. Unlike typical winged helix proteins it does not bind to DNA, but contains a hydrophobic groove which may be responsible for interaction with other proteins.


Pssm-ID: 464274 [Multi-domain]  Cd Length: 76  Bit Score: 116.44  E-value: 8.58e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24980968    25 NVEHEVNLLVEEIHRLGSKNADGKLSVKFGVLFqdDRCANLFEALVGTLKAAKRRKIVTYAGELLLQGVHDDVDIVLL 102
Cdd:pfam14705   1 HVDREILELCEIIKRLGTKDADGKIVVTFGVLF--ERYANISEKLVGTLLRARKHGLVDFEGEMLLQGRDDDVDITLL 76
 
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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