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Conserved domains on  [gi|18399346|ref|NP_565471|]
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RNA-binding ASCH domain protein [Arabidopsis thaliana]

Protein Classification

ASCH domain-containing protein( domain architecture ID 10158652)

ASCH (ASC-1 homology) domain-containing protein resembles the RNA-binding PUA domain, and may bind RNA; similar to human activating signal cointegrator 1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASCH_ASC-1_like cd06554
ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found ...
 9-128 5.18e-50

ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery.


:

Pssm-ID: 119346  Cd Length: 113  Bit Score: 162.50  E-value: 5.18e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399346   9 PCLTMHQPWASLLVHGIKRIEGRSWPSPIRGRLWIHAASKVPDEATIKAMEEFYQQIYavdgITDIQFPQHYPVSRLIGC 88
Cdd:cd06554   2 KALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILY----KLDIELPTGYPTGCLLGC 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18399346  89 VEVVGCVTSDELQNWDALPQGVrlegQTNFCWLCEKPQKL 128
Cdd:cd06554  78 VDVVDCLTQEEYREQYPWGKSE----ESPYAWVLANPRPL 113
 
Name Accession Description Interval E-value
ASCH_ASC-1_like cd06554
ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found ...
 9-128 5.18e-50

ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery.


Pssm-ID: 119346  Cd Length: 113  Bit Score: 162.50  E-value: 5.18e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399346   9 PCLTMHQPWASLLVHGIKRIEGRSWPSPIRGRLWIHAASKVPDEATIKAMEEFYQQIYavdgITDIQFPQHYPVSRLIGC 88
Cdd:cd06554   2 KALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILY----KLDIELPTGYPTGCLLGC 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18399346  89 VEVVGCVTSDELQNWDALPQGVrlegQTNFCWLCEKPQKL 128
Cdd:cd06554  78 VDVVDCLTQEEYREQYPWGKSE----ESPYAWVLANPRPL 113
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 11-45 5.06e-08

ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 398105  Cd Length: 102  Bit Score: 50.45  E-value: 5.06e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 18399346    11 LTMHQPWASLLVHGIKRIEGRSW--PSPIRGRLWIHA 45
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWdePLPVVGDLLILL 37
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 11-69 8.36e-08

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: 49.65  E-value: 8.36e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18399346     11 LTMHQPWASLLVHGIKRIEGRSW--PSPIRGRLWIHAASKVPDEATIKAMEEFYQQIYAVD 69
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLEnePLPKVGDLLIVLDGEGKPVCVIEVTSVEIIPFKDVT 61
 
Name Accession Description Interval E-value
ASCH_ASC-1_like cd06554
ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found ...
 9-128 5.18e-50

ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery.


Pssm-ID: 119346  Cd Length: 113  Bit Score: 162.50  E-value: 5.18e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399346   9 PCLTMHQPWASLLVHGIKRIEGRSWPSPIRGRLWIHAASKVPDEATIKAMEEFYQQIYavdgITDIQFPQHYPVSRLIGC 88
Cdd:cd06554   2 KALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILY----KLDIELPTGYPTGCLLGC 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18399346  89 VEVVGCVTSDELQNWDALPQGVrlegQTNFCWLCEKPQKL 128
Cdd:cd06554  78 VDVVDCLTQEEYREQYPWGKSE----ESPYAWVLANPRPL 113
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 11-45 5.06e-08

ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 398105  Cd Length: 102  Bit Score: 50.45  E-value: 5.06e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 18399346    11 LTMHQPWASLLVHGIKRIEGRSW--PSPIRGRLWIHA 45
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWdePLPVVGDLLILL 37
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 11-69 8.36e-08

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: 49.65  E-value: 8.36e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18399346     11 LTMHQPWASLLVHGIKRIEGRSW--PSPIRGRLWIHAASKVPDEATIKAMEEFYQQIYAVD 69
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLEnePLPKVGDLLIVLDGEGKPVCVIEVTSVEIIPFKDVT 61
 
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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