NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488237974|ref|WP_002309182|]
View 

MULTISPECIES: ASCH domain-containing protein [Enterococcus]

Protein Classification

YhfF family protein( domain architecture ID 10008549)

YhfF family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YhfF COG4405
Predicted RNA-binding protein YhfF, contains PUA-like ASCH domain [General function prediction ...
 3-151 2.52e-63

Predicted RNA-binding protein YhfF, contains PUA-like ASCH domain [General function prediction only];


:

Pssm-ID: 443529  Cd Length: 156  Bit Score: 190.87  E-value: 2.52e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974   3 QKVEEYFKKFQEKYPRYQSEEL-SFFSFGNTEEMADELSGLVVKKIKTGTSSGYDLYKKEKEPLPKVGQLDVVLNGKNEP 81
Cdd:COG4405    5 ASLEAFWPDALAANPEVAAEEPpEAWAFGDSPELADELAALVLAGKKTATSSALADYEAEGEPLPKVGDLSIVLDGDGEP 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974  82 VCIIKNINVTILPFSEITEEHAWKEGEGDRTLAYWRKVHTDFFKHVYKEaLNMAFTEEKLIVYEEFEVIF 151
Cdd:COG4405   85 VAIIRTTEVEVVPFDEVTEEFAAAEGEGDRSLEYWRKAHEAFFTRELAE-IGREFSEDMPVVCERFEVVY 153
 
Name Accession Description Interval E-value
YhfF COG4405
Predicted RNA-binding protein YhfF, contains PUA-like ASCH domain [General function prediction ...
 3-151 2.52e-63

Predicted RNA-binding protein YhfF, contains PUA-like ASCH domain [General function prediction only];


Pssm-ID: 443529  Cd Length: 156  Bit Score: 190.87  E-value: 2.52e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974   3 QKVEEYFKKFQEKYPRYQSEEL-SFFSFGNTEEMADELSGLVVKKIKTGTSSGYDLYKKEKEPLPKVGQLDVVLNGKNEP 81
Cdd:COG4405    5 ASLEAFWPDALAANPEVAAEEPpEAWAFGDSPELADELAALVLAGKKTATSSALADYEAEGEPLPKVGDLSIVLDGDGEP 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974  82 VCIIKNINVTILPFSEITEEHAWKEGEGDRTLAYWRKVHTDFFKHVYKEaLNMAFTEEKLIVYEEFEVIF 151
Cdd:COG4405   85 VAIIRTTEVEVVPFDEVTEEFAAAEGEGDRSLEYWRKAHEAFFTRELAE-IGREFSEDMPVVCERFEVVY 153
ASCH_Ef3133_like cd06553
ASC-1 homology domain, subfamily similar to Enterococcus faecalis Ef3133. The ASCH domain, a ...
 25-151 1.57e-62

ASC-1 homology domain, subfamily similar to Enterococcus faecalis Ef3133. 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.


Pssm-ID: 119345  Cd Length: 127  Bit Score: 187.77  E-value: 1.57e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974  25 SFFSFGNTEEMADELSGLVVKKIKTGTSSGYDLYKKEKEPLPKVGQLDVVLNGKNEPVCIIKNINVTILPFSEITEEHAW 104
Cdd:cd06553    2 EAWAFGDSPELADELAALVLAGKKTATCSALALYEAEEEPLPKVGDYSIILDGQGKPVCIIETTEVEVVPFNDVTEEFAY 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488237974 105 KEGEGDRTLAYWRKVHTDFFKHVYKEAlNMAFTEEKLIVYEEFEVIF 151
Cdd:cd06553   82 AEGEGDRSLEYWRKAHEAFFTRELEEA-GKEFTEDMLVVCERFEVVY 127
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 35-151 1.01e-20

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: 80.85  E-value: 1.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974    35 MADELSGLVVKKIKTGTSSgydlykKEKEPLPKVGQLDVVLNGKNEPVCIIKNINVTILPFSEITEEHAWKEGEGDrtLA 114
Cdd:smart01022   3 FKDELADLILSGKKTATIR------LENEPLPKVGDLLIVLDGEGKPVCVIEVTSVEIIPFKDVTAEHAYLEGEGS--LE 74

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 488237974   115 YWRKVHTDFfkhvykealnmaFTEEKLIVYEEFEVIF 151
Cdd:smart01022  75 EWRKVHKEF------------YPEDMEVVCEEFEVVE 99
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 37-151 8.17e-19

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: 76.26  E-value: 8.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974   37 DELSGLVVKKIKTGTssgydlYKKEKEPLPKVGQLDVVLNGKNEPVCIIKNINVTILPFSEITEEHAWKEGEgdrTLAYW 116
Cdd:pfam04266   5 QEYADLILSGKKTAE------IRVWDEPLPVVGDLLILLDSTGRPVGVIEVTDVEIIPFEEVTEEHAYLEGE---SLEEW 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 488237974  117 RKVHTDFFKHVYKealnmaftEEKLIVYEEFEVIF 151
Cdd:pfam04266  76 RKVHKEFYPEEKE--------EDEGVVVEEFELVE 102
 
Name Accession Description Interval E-value
YhfF COG4405
Predicted RNA-binding protein YhfF, contains PUA-like ASCH domain [General function prediction ...
 3-151 2.52e-63

Predicted RNA-binding protein YhfF, contains PUA-like ASCH domain [General function prediction only];


Pssm-ID: 443529  Cd Length: 156  Bit Score: 190.87  E-value: 2.52e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974   3 QKVEEYFKKFQEKYPRYQSEEL-SFFSFGNTEEMADELSGLVVKKIKTGTSSGYDLYKKEKEPLPKVGQLDVVLNGKNEP 81
Cdd:COG4405    5 ASLEAFWPDALAANPEVAAEEPpEAWAFGDSPELADELAALVLAGKKTATSSALADYEAEGEPLPKVGDLSIVLDGDGEP 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974  82 VCIIKNINVTILPFSEITEEHAWKEGEGDRTLAYWRKVHTDFFKHVYKEaLNMAFTEEKLIVYEEFEVIF 151
Cdd:COG4405   85 VAIIRTTEVEVVPFDEVTEEFAAAEGEGDRSLEYWRKAHEAFFTRELAE-IGREFSEDMPVVCERFEVVY 153
ASCH_Ef3133_like cd06553
ASC-1 homology domain, subfamily similar to Enterococcus faecalis Ef3133. The ASCH domain, a ...
 25-151 1.57e-62

ASC-1 homology domain, subfamily similar to Enterococcus faecalis Ef3133. 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.


Pssm-ID: 119345  Cd Length: 127  Bit Score: 187.77  E-value: 1.57e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974  25 SFFSFGNTEEMADELSGLVVKKIKTGTSSGYDLYKKEKEPLPKVGQLDVVLNGKNEPVCIIKNINVTILPFSEITEEHAW 104
Cdd:cd06553    2 EAWAFGDSPELADELAALVLAGKKTATCSALALYEAEEEPLPKVGDYSIILDGQGKPVCIIETTEVEVVPFNDVTEEFAY 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488237974 105 KEGEGDRTLAYWRKVHTDFFKHVYKEAlNMAFTEEKLIVYEEFEVIF 151
Cdd:cd06553   82 AEGEGDRSLEYWRKAHEAFFTRELEEA-GKEFTEDMLVVCERFEVVY 127
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 35-151 1.01e-20

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: 80.85  E-value: 1.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974    35 MADELSGLVVKKIKTGTSSgydlykKEKEPLPKVGQLDVVLNGKNEPVCIIKNINVTILPFSEITEEHAWKEGEGDrtLA 114
Cdd:smart01022   3 FKDELADLILSGKKTATIR------LENEPLPKVGDLLIVLDGEGKPVCVIEVTSVEIIPFKDVTAEHAYLEGEGS--LE 74

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 488237974   115 YWRKVHTDFfkhvykealnmaFTEEKLIVYEEFEVIF 151
Cdd:smart01022  75 EWRKVHKEF------------YPEDMEVVCEEFEVVE 99
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 37-151 8.17e-19

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: 76.26  E-value: 8.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974   37 DELSGLVVKKIKTGTssgydlYKKEKEPLPKVGQLDVVLNGKNEPVCIIKNINVTILPFSEITEEHAWKEGEgdrTLAYW 116
Cdd:pfam04266   5 QEYADLILSGKKTAE------IRVWDEPLPVVGDLLILLDSTGRPVGVIEVTDVEIIPFEEVTEEHAYLEGE---SLEEW 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 488237974  117 RKVHTDFFKHVYKealnmaftEEKLIVYEEFEVIF 151
Cdd:pfam04266  76 RKVHKEFYPEEKE--------EDEGVVVEEFELVE 102
ASCH cd06541
ASC-1 homology or ASCH domain, a small beta-barrel domain found in all three kingdoms of life. ...
 37-125 7.61e-05

ASC-1 homology or ASCH domain, a small beta-barrel domain found in all three kingdoms of life. ASCH 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: 119343  Cd Length: 105  Bit Score: 39.57  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488237974  37 DELSGLVVKKIKTGTSSGYDLYKKekepLPKVGQLDVVLNGKnEPVCIIKNINVTILP-FSEITEEHAWKEGEGDRTLAY 115
Cdd:cd06541    6 DRYGQLVVSGRKTIEIRSLDIYEQ----LPKAGDYLIILDGQ-QPLAIAEVVKVEIMPmVNELSEEQEQAEGEGDLTLLY 80

                         90
                 ....*....|
gi 488237974 116 WRKVHTDFFK 125
Cdd:cd06541   81 ELKEHAAFFK 90
ASCH_yqfb_like cd06552
ASC-1 homology domain, subfamily similar to Escherichia coli Yqfb. The ASCH domain, a small ...
 60-124 1.95e-04

ASC-1 homology domain, subfamily similar to Escherichia coli Yqfb. 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.


Pssm-ID: 119344  Cd Length: 100  Bit Score: 38.38  E-value: 1.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488237974  60 KEKEPLPKVGQLdVVLNGKNEPVCIIKNINVTILPFSEITEEHAWKEGEGDRT--LAYWRKVHTDFF 124
Cdd:cd06552   23 DGGESHLKPGDV-VEVHTGERIFGEAEITSVEEKTLGELTDEDARQEGFPSLEelKEALKEIYPGLK 88
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH