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Conserved domains on  [gi|489738180|ref|WP_003642275|]
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MULTISPECIES: ASCH domain-containing protein [Lactiplantibacillus]

Protein Classification

ASCH domain-containing protein( domain architecture ID 10158657)

ASCH (ASC-1 homology) domain-containing protein may bind RNA

Gene Ontology:  GO:0003723
PubMed:  16322048

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASCH_PF0470_like cd06555
ASC-1 homology domain, subfamily similar to Pyrococcus furiosus Pf0470. The ASCH domain, a ...
 4-111 3.69e-47

ASC-1 homology domain, subfamily similar to Pyrococcus furiosus Pf0470. 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: 119347  Cd Length: 109  Bit Score: 147.00  E-value: 3.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738180   4 MQLIHPQWLLIKSGLKTIEIRLNDAKRQALQVGDIVNFIDLTTGQQLTTQLIDITRFASFESLLSEYTAVQVGSApGTPV 83
Cdd:cd06555    3 MGLEEEPFELIKSGKKTIEIRLNDEKRQQIKVGDKILFNDLDTGQQLLVKVVDIRKYDSFRELLEEEGLEKVGPG-VDSI 81

                         90       100
                 ....*....|....*....|....*...
gi 489738180  84 TQMVQEMLTLYSPVQVAQSGVVALQVRP 111
Cdd:cd06555   82 EEGVKDTYKIYSKEQEKKYGVLAIEIRV 109
 
Name Accession Description Interval E-value
ASCH_PF0470_like cd06555
ASC-1 homology domain, subfamily similar to Pyrococcus furiosus Pf0470. The ASCH domain, a ...
 4-111 3.69e-47

ASC-1 homology domain, subfamily similar to Pyrococcus furiosus Pf0470. 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: 119347  Cd Length: 109  Bit Score: 147.00  E-value: 3.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738180   4 MQLIHPQWLLIKSGLKTIEIRLNDAKRQALQVGDIVNFIDLTTGQQLTTQLIDITRFASFESLLSEYTAVQVGSApGTPV 83
Cdd:cd06555    3 MGLEEEPFELIKSGKKTIEIRLNDEKRQQIKVGDKILFNDLDTGQQLLVKVVDIRKYDSFRELLEEEGLEKVGPG-VDSI 81

                         90       100
                 ....*....|....*....|....*...
gi 489738180  84 TQMVQEMLTLYSPVQVAQSGVVALQVRP 111
Cdd:cd06555   82 EEGVKDTYKIYSKEQEKKYGVLAIEIRV 109
ASCH COG4043
ASC-1 homology (ASCH) domain, predicted RNA-binding domain [General function prediction only];
1-113 7.80e-44

ASC-1 homology (ASCH) domain, predicted RNA-binding domain [General function prediction only];


Pssm-ID: 443221  Cd Length: 113  Bit Score: 138.52  E-value: 7.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738180   1 MTTMQLIHPQWLLIKSGLKTIEIRLNDAKRQALQVGDIVNFIDLTTGQQLTTQLIDITRFASFESLLSEYTAVQVGsAPG 80
Cdd:COG4043    2 THKMGLEEEYFELIKSGKKTIEGRLNDPKRKKIKVGDKIVFINLETGESLTVRVTDVRRYPTFKEMLEEEGLEKVL-PDG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489738180  81 TPVTQMVQEMLTLYSPVQVAQSGVVALQVRPLI 113
Cdd:COG4043   81 TSLEEMVKIYYKIYSKEKEKKYGVLAIEIELIG 113
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 7-112 1.33e-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: 48.49  E-value: 1.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738180     7 IHPQWL-LIKSGLKTIEIRlnDAKRQALQVGDIVNFIDLTTGQQLTTQLIDITrFASFESLLSEyTAVQVGSapgTPVTQ 85
Cdd:smart01022   3 FKDELAdLILSGKKTATIR--LENEPLPKVGDLLIVLDGEGKPVCVIEVTSVE-IIPFKDVTAE-HAYLEGE---GSLEE 75

                           90       100
                   ....*....|....*....|....*..
gi 489738180    86 MVQEMLTLYSPVQVaqsgVVALQVRPL 112
Cdd:smart01022  76 WRKVHKEFYPEDME----VVCEEFEVV 98
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 7-112 1.49e-04

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: 38.12  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738180    7 IHPQWL-LIKSGLKTIEIRLNDAKRQalQVGDIVNFIDLTTGQQLTTQLIDITRFaSFESLLSEYTAvqvgsAPGTPVTQ 85
Cdd:pfam04266   3 FGQEYAdLILSGKKTAEIRVWDEPLP--VVGDLLILLDSTGRPVGVIEVTDVEII-PFEEVTEEHAY-----LEGESLEE 74

                          90       100
                  ....*....|....*....|....*..
gi 489738180   86 MVQEMLTLYSPVQVAQSGVVALQVRPL 112
Cdd:pfam04266  75 WRKVHKEFYPEEKEEDEGVVVEEFELV 101
 
Name Accession Description Interval E-value
ASCH_PF0470_like cd06555
ASC-1 homology domain, subfamily similar to Pyrococcus furiosus Pf0470. The ASCH domain, a ...
 4-111 3.69e-47

ASC-1 homology domain, subfamily similar to Pyrococcus furiosus Pf0470. 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: 119347  Cd Length: 109  Bit Score: 147.00  E-value: 3.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738180   4 MQLIHPQWLLIKSGLKTIEIRLNDAKRQALQVGDIVNFIDLTTGQQLTTQLIDITRFASFESLLSEYTAVQVGSApGTPV 83
Cdd:cd06555    3 MGLEEEPFELIKSGKKTIEIRLNDEKRQQIKVGDKILFNDLDTGQQLLVKVVDIRKYDSFRELLEEEGLEKVGPG-VDSI 81

                         90       100
                 ....*....|....*....|....*...
gi 489738180  84 TQMVQEMLTLYSPVQVAQSGVVALQVRP 111
Cdd:cd06555   82 EEGVKDTYKIYSKEQEKKYGVLAIEIRV 109
ASCH COG4043
ASC-1 homology (ASCH) domain, predicted RNA-binding domain [General function prediction only];
1-113 7.80e-44

ASC-1 homology (ASCH) domain, predicted RNA-binding domain [General function prediction only];


Pssm-ID: 443221  Cd Length: 113  Bit Score: 138.52  E-value: 7.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738180   1 MTTMQLIHPQWLLIKSGLKTIEIRLNDAKRQALQVGDIVNFIDLTTGQQLTTQLIDITRFASFESLLSEYTAVQVGsAPG 80
Cdd:COG4043    2 THKMGLEEEYFELIKSGKKTIEGRLNDPKRKKIKVGDKIVFINLETGESLTVRVTDVRRYPTFKEMLEEEGLEKVL-PDG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489738180  81 TPVTQMVQEMLTLYSPVQVAQSGVVALQVRPLI 113
Cdd:COG4043   81 TSLEEMVKIYYKIYSKEKEKKYGVLAIEIELIG 113
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 7-112 1.33e-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: 48.49  E-value: 1.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738180     7 IHPQWL-LIKSGLKTIEIRlnDAKRQALQVGDIVNFIDLTTGQQLTTQLIDITrFASFESLLSEyTAVQVGSapgTPVTQ 85
Cdd:smart01022   3 FKDELAdLILSGKKTATIR--LENEPLPKVGDLLIVLDGEGKPVCVIEVTSVE-IIPFKDVTAE-HAYLEGE---GSLEE 75

                           90       100
                   ....*....|....*....|....*..
gi 489738180    86 MVQEMLTLYSPVQVaqsgVVALQVRPL 112
Cdd:smart01022  76 WRKVHKEFYPEDME----VVCEEFEVV 98
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 7-112 1.49e-04

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: 38.12  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738180    7 IHPQWL-LIKSGLKTIEIRLNDAKRQalQVGDIVNFIDLTTGQQLTTQLIDITRFaSFESLLSEYTAvqvgsAPGTPVTQ 85
Cdd:pfam04266   3 FGQEYAdLILSGKKTAEIRVWDEPLP--VVGDLLILLDSTGRPVGVIEVTDVEII-PFEEVTEEHAY-----LEGESLEE 74

                          90       100
                  ....*....|....*....|....*..
gi 489738180   86 MVQEMLTLYSPVQVAQSGVVALQVRPL 112
Cdd:pfam04266  75 WRKVHKEFYPEEKEEDEGVVVEEFELV 101
 
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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