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Conserved domains on  [gi|446110972|ref|WP_000188827|]
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ASCH domain-containing protein [Streptococcus pneumoniae]

Protein Classification

ASCH domain-containing protein( domain architecture ID 10158648)

ASCH (ASC-1 homology) domain-containing protein may bind RNA; similar to Enterococcus faecalis Ef3133

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASCH_Ef3133_like cd06553
ASC-1 homology domain, subfamily similar to Enterococcus faecalis Ef3133. The ASCH domain, a ...
 22-144 7.19e-64

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: 191.24  E-value: 7.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446110972  22 DAWAFGVEP---DLLADLVFKGEKTATASAYDLYVLEDEPLPQVGTFDVILDSQNQSVCIVEITKVSVELFNQVSAQHAF 98
Cdd:cd06553    2 EAWAFGDSPelaDELAALVLAGKKTATCSALALYEAEEEPLPKVGDYSIILDGQGKPVCIIETTEVEVVPFNDVTEEFAY 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446110972  99 KEGEGDKSLAYWRQVHEDFFTDCLGEVGLTFTPESKVVLEEFRKVY 144
Cdd:cd06553   82 AEGEGDRSLEYWRKAHEAFFTRELEEAGKEFTEDMLVVCERFEVVY 127
 
Name Accession Description Interval E-value
ASCH_Ef3133_like cd06553
ASC-1 homology domain, subfamily similar to Enterococcus faecalis Ef3133. The ASCH domain, a ...
 22-144 7.19e-64

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: 191.24  E-value: 7.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446110972  22 DAWAFGVEP---DLLADLVFKGEKTATASAYDLYVLEDEPLPQVGTFDVILDSQNQSVCIVEITKVSVELFNQVSAQHAF 98
Cdd:cd06553    2 EAWAFGDSPelaDELAALVLAGKKTATCSALALYEAEEEPLPKVGDYSIILDGQGKPVCIIETTEVEVVPFNDVTEEFAY 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446110972  99 KEGEGDKSLAYWRQVHEDFFTDCLGEVGLTFTPESKVVLEEFRKVY 144
Cdd:cd06553   82 AEGEGDRSLEYWRKAHEAFFTRELEEAGKEFTEDMLVVCERFEVVY 127
YhfF COG4405
Predicted RNA-binding protein YhfF, contains PUA-like ASCH domain [General function prediction ...
 4-146 4.64e-63

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


Pssm-ID: 443529  Cd Length: 156  Bit Score: 190.10  E-value: 4.64e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446110972   4 QEMWNKYKQINPL--IGDEIDAWAFGVEPDL---LADLVFKGEKTATASAYDLYVLEDEPLPQVGTFDVILDSQNQSVCI 78
Cdd:COG4405    8 EAFWPDALAANPEvaAEEPPEAWAFGDSPELadeLAALVLAGKKTATSSALADYEAEGEPLPKVGDLSIVLDGDGEPVAI 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446110972  79 VEITKVSVELFNQVSAQHAFKEGEGDKSLAYWRQVHEDFFTDCLGEVGLTFTPESKVVLEEFRKVYPL 146
Cdd:COG4405   88 IRTTEVEVVPFDEVTEEFAAAEGEGDRSLEYWRKAHEAFFTRELAEIGREFSEDMPVVCERFEVVYPL 155
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 24-144 3.64e-26

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: 94.75  E-value: 3.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446110972   24 WAFGVEpdlLADLVFKGEKTATasaydlYVLEDEPLPQVGTFDVILDSQNQSVCIVEITKVSVELFNQVSAQHAFKEGEg 103
Cdd:pfam04266   1 LSFGQE---YADLILSGKKTAE------IRVWDEPLPVVGDLLILLDSTGRPVGVIEVTDVEIIPFEEVTEEHAYLEGE- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446110972  104 dkSLAYWRQVHEDFFTDCLGevgltftPESKVVLEEFRKVY 144
Cdd:pfam04266  71 --SLEEWRKVHKEFYPEEKE-------EDEGVVVEEFELVE 102
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 33-144 9.15e-25

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: 90.86  E-value: 9.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446110972    33 LADLVFKGEKTATASaydlyvLEDEPLPQVGTFDVILDSQNQSVCIVEITKVSVELFNQVSAQHAFKEGEGdkSLAYWRQ 112
Cdd:smart01022   7 LADLILSGKKTATIR------LENEPLPKVGDLLIVLDGEGKPVCVIEVTSVEIIPFKDVTAEHAYLEGEG--SLEEWRK 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 446110972   113 VHEDFftdclgevgltFTPESKVVLEEFRKVY 144
Cdd:smart01022  79 VHKEF-----------YPEDMEVVCEEFEVVE 99
 
Name Accession Description Interval E-value
ASCH_Ef3133_like cd06553
ASC-1 homology domain, subfamily similar to Enterococcus faecalis Ef3133. The ASCH domain, a ...
 22-144 7.19e-64

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: 191.24  E-value: 7.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446110972  22 DAWAFGVEP---DLLADLVFKGEKTATASAYDLYVLEDEPLPQVGTFDVILDSQNQSVCIVEITKVSVELFNQVSAQHAF 98
Cdd:cd06553    2 EAWAFGDSPelaDELAALVLAGKKTATCSALALYEAEEEPLPKVGDYSIILDGQGKPVCIIETTEVEVVPFNDVTEEFAY 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446110972  99 KEGEGDKSLAYWRQVHEDFFTDCLGEVGLTFTPESKVVLEEFRKVY 144
Cdd:cd06553   82 AEGEGDRSLEYWRKAHEAFFTRELEEAGKEFTEDMLVVCERFEVVY 127
YhfF COG4405
Predicted RNA-binding protein YhfF, contains PUA-like ASCH domain [General function prediction ...
 4-146 4.64e-63

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


Pssm-ID: 443529  Cd Length: 156  Bit Score: 190.10  E-value: 4.64e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446110972   4 QEMWNKYKQINPL--IGDEIDAWAFGVEPDL---LADLVFKGEKTATASAYDLYVLEDEPLPQVGTFDVILDSQNQSVCI 78
Cdd:COG4405    8 EAFWPDALAANPEvaAEEPPEAWAFGDSPELadeLAALVLAGKKTATSSALADYEAEGEPLPKVGDLSIVLDGDGEPVAI 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446110972  79 VEITKVSVELFNQVSAQHAFKEGEGDKSLAYWRQVHEDFFTDCLGEVGLTFTPESKVVLEEFRKVYPL 146
Cdd:COG4405   88 IRTTEVEVVPFDEVTEEFAAAEGEGDRSLEYWRKAHEAFFTRELAEIGREFSEDMPVVCERFEVVYPL 155
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 24-144 3.64e-26

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: 94.75  E-value: 3.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446110972   24 WAFGVEpdlLADLVFKGEKTATasaydlYVLEDEPLPQVGTFDVILDSQNQSVCIVEITKVSVELFNQVSAQHAFKEGEg 103
Cdd:pfam04266   1 LSFGQE---YADLILSGKKTAE------IRVWDEPLPVVGDLLILLDSTGRPVGVIEVTDVEIIPFEEVTEEHAYLEGE- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446110972  104 dkSLAYWRQVHEDFFTDCLGevgltftPESKVVLEEFRKVY 144
Cdd:pfam04266  71 --SLEEWRKVHKEFYPEEKE-------EDEGVVVEEFELVE 102
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 33-144 9.15e-25

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: 90.86  E-value: 9.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446110972    33 LADLVFKGEKTATASaydlyvLEDEPLPQVGTFDVILDSQNQSVCIVEITKVSVELFNQVSAQHAFKEGEGdkSLAYWRQ 112
Cdd:smart01022   7 LADLILSGKKTATIR------LENEPLPKVGDLLIVLDGEGKPVCVIEVTSVEIIPFKDVTAEHAYLEGEG--SLEEWRK 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 446110972   113 VHEDFftdclgevgltFTPESKVVLEEFRKVY 144
Cdd:smart01022  79 VHKEF-----------YPEDMEVVCEEFEVVE 99
ASCH cd06541
ASC-1 homology or ASCH domain, a small beta-barrel domain found in all three kingdoms of life. ...
 24-120 4.09e-09

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: 50.74  E-value: 4.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446110972  24 WAFGvepDLLADLVFKGEKTATASAYDLYvledEPLPQVGTFDVILDSQnQSVCIVEITKVS-VELFNQVSAQHAFKEGE 102
Cdd:cd06541    2 LMFG---DRYGQLVVSGRKTIEIRSLDIY----EQLPKAGDYLIILDGQ-QPLAIAEVVKVEiMPMVNELSEEQEQAEGE 73

                         90
                 ....*....|....*...
gi 446110972 103 GDKSLAYWRQVHEDFFTD 120
Cdd:cd06541   74 GDLTLLYELKEHAAFFKE 91
 
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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