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Conserved domains on  [gi|1013181363|ref|NP_001308853|]
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activating signal cointegrator 1 isoform 2 [Homo sapiens]

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 ...
 204-317 1.71e-57

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: 182.15  E-value: 1.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013181363 204 GWCLSVHQPWASLLVRGIKRVEGRSWYTPHRGRLWIAATAKKPSPQEVSELQATYRLLRGKDVEFPNDYPSGCLLGCVDL 283
Cdd:cd06554     1 MKALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILYKLDIELPTGYPTGCLLGCVDV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1013181363 284 IDCLSQKQFKEQFPDISQEsDSPFVFICKNPQEM 317
Cdd:cd06554    81 VDCLTQEEYREQYPWGKSE-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 ...
 204-317 1.71e-57

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: 182.15  E-value: 1.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013181363 204 GWCLSVHQPWASLLVRGIKRVEGRSWYTPHRGRLWIAATAKKPSPQEVSELQATYRLLRGKDVEFPNDYPSGCLLGCVDL 283
Cdd:cd06554     1 MKALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILYKLDIELPTGYPTGCLLGCVDV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1013181363 284 IDCLSQKQFKEQFPDISQEsDSPFVFICKNPQEM 317
Cdd:cd06554    81 VDCLTQEEYREQYPWGKSE-ESPYAWVLANPRPL 113
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 207-299 3.15e-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: 50.84  E-value: 3.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013181363 207 LSVHQPWASLLVRGIKRVEGRSWYTPHR--GRLWIAATakkpspqevselqatyrllrgkdvefpndyPSGCLLGCVDLI 284
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPvvGDLLILLD------------------------------STGRPVGVIEVT 50

                          90
                  ....*....|....*
gi 1013181363 285 DCLSqKQFKEQFPDI 299
Cdd:pfam04266  51 DVEI-IPFEEVTEEH 64
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 207-301 1.87e-06

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: 45.79  E-value: 1.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013181363  207 LSVHQPWASLLVRGIKRVEGRSWYTPH--RGRLWIAATAKKPSPQEVSELQATYRLLRGKDVEFpndypsGCLLGCVDLi 284
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLENEPLpkVGDLLIVLDGEGKPVCVIEVTSVEIIPFKDVTAEH------AYLEGEGSL- 73

                           90
                   ....*....|....*..
gi 1013181363  285 DCLsQKQFKEQFPDISQ 301
Cdd:smart01022  74 EEW-RKVHKEFYPEDME 89
 
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 ...
 204-317 1.71e-57

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: 182.15  E-value: 1.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013181363 204 GWCLSVHQPWASLLVRGIKRVEGRSWYTPHRGRLWIAATAKKPSPQEVSELQATYRLLRGKDVEFPNDYPSGCLLGCVDL 283
Cdd:cd06554     1 MKALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILYKLDIELPTGYPTGCLLGCVDV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1013181363 284 IDCLSQKQFKEQFPDISQEsDSPFVFICKNPQEM 317
Cdd:cd06554    81 VDCLTQEEYREQYPWGKSE-ESPYAWVLANPRPL 113
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 207-299 3.15e-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: 50.84  E-value: 3.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013181363 207 LSVHQPWASLLVRGIKRVEGRSWYTPHR--GRLWIAATakkpspqevselqatyrllrgkdvefpndyPSGCLLGCVDLI 284
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPvvGDLLILLD------------------------------STGRPVGVIEVT 50

                          90
                  ....*....|....*
gi 1013181363 285 DCLSqKQFKEQFPDI 299
Cdd:pfam04266  51 DVEI-IPFEEVTEEH 64
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 207-301 1.87e-06

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: 45.79  E-value: 1.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013181363  207 LSVHQPWASLLVRGIKRVEGRSWYTPH--RGRLWIAATAKKPSPQEVSELQATYRLLRGKDVEFpndypsGCLLGCVDLi 284
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLENEPLpkVGDLLIVLDGEGKPVCVIEVTSVEIIPFKDVTAEH------AYLEGEGSL- 73

                           90
                   ....*....|....*..
gi 1013181363  285 DCLsQKQFKEQFPDISQ 301
Cdd:smart01022  74 EEW-RKVHKEFYPEDME 89
 
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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