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Conserved domains on  [gi|284813540|ref|NP_001165379|]
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protein EOLA1 isoform a [Homo sapiens]

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 ...
 6-114 4.46e-09

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: 50.80  E-value: 4.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284813540     6 LSFRQPYAGFVLNGIKTVETRWRpllsSQRNCTIAVHIAHRDWEGDawRELLVERLGMTPAQIQALLRK-GEKFGRGVIA 84
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLE----NEPLPKVGDLLIVLDGEGK--PVCVIEVTSVEIIPFKDVTAEhAYLEGEGSLE 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 284813540    85 GLVDIGETLQcpedlTPDEVVELENQAVLT 114
Cdd:smart01022  75 EWRKVHKEFY-----PEDMEVVCEEFEVVE 99
 
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 ...
 6-114 4.46e-09

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: 50.80  E-value: 4.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284813540     6 LSFRQPYAGFVLNGIKTVETRWRpllsSQRNCTIAVHIAHRDWEGDawRELLVERLGMTPAQIQALLRK-GEKFGRGVIA 84
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLE----NEPLPKVGDLLIVLDGEGK--PVCVIEVTSVEIIPFKDVTAEhAYLEGEGSLE 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 284813540    85 GLVDIGETLQcpedlTPDEVVELENQAVLT 114
Cdd:smart01022  75 EWRKVHKEFY-----PEDMEVVCEEFEVVE 99
ASCH_ASC-1_like cd06554
ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found ...
 1-28 5.94e-05

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: 40.39  E-value: 5.94e-05
                         10        20
                 ....*....|....*....|....*....
gi 284813540   1 MKfgCLSFRQPYAGFVLNGIKTVETR-WR 28
Cdd:cd06554    1 MK--ALSIHQPWASLIVRGIKRIEGRsWA 27
 
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 ...
 6-114 4.46e-09

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: 50.80  E-value: 4.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284813540     6 LSFRQPYAGFVLNGIKTVETRWRpllsSQRNCTIAVHIAHRDWEGDawRELLVERLGMTPAQIQALLRK-GEKFGRGVIA 84
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLE----NEPLPKVGDLLIVLDGEGK--PVCVIEVTSVEIIPFKDVTAEhAYLEGEGSLE 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 284813540    85 GLVDIGETLQcpedlTPDEVVELENQAVLT 114
Cdd:smart01022  75 EWRKVHKEFY-----PEDMEVVCEEFEVVE 99
ASCH_ASC-1_like cd06554
ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found ...
 1-28 5.94e-05

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: 40.39  E-value: 5.94e-05
                         10        20
                 ....*....|....*....|....*....
gi 284813540   1 MKfgCLSFRQPYAGFVLNGIKTVETR-WR 28
Cdd:cd06554    1 MK--ALSIHQPWASLIVRGIKRIEGRsWA 27
 
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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