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Conserved domains on  [gi|1515054363|gb|ROK32952|]
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RNA-binding protein [Escherichia coli]

Protein Classification

ASCH domain-containing protein( domain architecture ID 10659984)

ASCH (ASC-1 homology) domain-containing protein may bind RNA; similar to human protein EOLA2

Gene Ontology:  GO:0003723
PubMed:  16322048

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 6-53 1.68e-03

The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


:

Pssm-ID: 214979  Cd Length: 99  Bit Score: 35.01  E-value: 1.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1515054363    6 LAVKSEYFDAMIRGEKTEEYRLcndyWNKRImFREYDRLIITKGYPKR 53
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRL----ENEPL-PKVGDLLIVLDGEGKP 43
 
Name Accession Description Interval E-value
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 6-53 1.68e-03

The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 214979  Cd Length: 99  Bit Score: 35.01  E-value: 1.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1515054363    6 LAVKSEYFDAMIRGEKTEEYRLcndyWNKRImFREYDRLIITKGYPKR 53
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRL----ENEPL-PKVGDLLIVLDGEGKP 43
 
Name Accession Description Interval E-value
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 6-53 1.68e-03

The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 214979  Cd Length: 99  Bit Score: 35.01  E-value: 1.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1515054363    6 LAVKSEYFDAMIRGEKTEEYRLcndyWNKRImFREYDRLIITKGYPKR 53
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRL----ENEPL-PKVGDLLIVLDGEGKP 43
 
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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