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Conserved domains on  [gi|160286344|pdb|2Z0T|A]
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Chain A, Crystal structure of hypothetical protein PH0355

Protein Classification

ASCH domain-containing protein( domain architecture ID 10008206)

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

CATH:  2.30.130.30
Gene Ontology:  GO:0003723
PubMed:  16322048

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASCH COG4043
ASC-1 homology (ASCH) domain, predicted RNA-binding domain [General function prediction only];
1-108 3.19e-43

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


:

Pssm-ID: 443221  Cd Length: 113  Bit Score: 136.59  E-value: 3.19e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0T_A        1 MKWEMGLQEEYIELIKAGKKKIEGRLYDEKRRQIKPGDIIIFE----GGKLKVKVKGIRVYSSFKEMLEKEGIENVLPGV 76
Cdd:COG4043   1 MTHKMGLEEEYFELIKSGKKTIEGRLNDPKRKKIKVGDKIVFInletGESLTVRVTDVRRYPTFKEMLEEEGLEKVLPDG 80

                        90       100       110
                ....*....|....*....|....*....|..
2Z0T_A       77 KSIEEGVKVYRQFYDEEREKKYGVVAIEIEPI 108
Cdd:COG4043  81 TSLEEMVKIYYKIYSKEKEKKYGVLAIEIELI 112
 
Name Accession Description Interval E-value
ASCH COG4043
ASC-1 homology (ASCH) domain, predicted RNA-binding domain [General function prediction only];
1-108 3.19e-43

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


Pssm-ID: 443221  Cd Length: 113  Bit Score: 136.59  E-value: 3.19e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0T_A        1 MKWEMGLQEEYIELIKAGKKKIEGRLYDEKRRQIKPGDIIIFE----GGKLKVKVKGIRVYSSFKEMLEKEGIENVLPGV 76
Cdd:COG4043   1 MTHKMGLEEEYFELIKSGKKTIEGRLNDPKRKKIKVGDKIVFInletGESLTVRVTDVRRYPTFKEMLEEEGLEKVLPDG 80

                        90       100       110
                ....*....|....*....|....*....|..
2Z0T_A       77 KSIEEGVKVYRQFYDEEREKKYGVVAIEIEPI 108
Cdd:COG4043  81 TSLEEMVKIYYKIYSKEKEKKYGVLAIEIELI 112
ASCH_PF0470_like cd06555
ASC-1 homology domain, subfamily similar to Pyrococcus furiosus Pf0470. The ASCH domain, a ...
 3-107 3.23e-43

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: 136.60  E-value: 3.23e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0T_A        3 WEMGLQEEYIELIKAGKKKIEGRLYDEKRRQIKPGDIIIF----EGGKLKVKVKGIRVYSSFKEMLEKEGIENVLPGVKS 78
Cdd:cd06555   1 HEMGLEEEPFELIKSGKKTIEIRLNDEKRQQIKVGDKILFndldTGQQLLVKVVDIRKYDSFRELLEEEGLEKVGPGVDS 80

                        90       100
                ....*....|....*....|....*....
2Z0T_A       79 IEEGVKVYRQFYDEEREKKYGVVAIEIEP 107
Cdd:cd06555  81 IEEGVKDTYKIYSKEQEKKYGVLAIEIRV 109
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 5-109 2.39e-15

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: 65.86  E-value: 2.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0T_A          5 MGLQEEYIELIKAGKKKIEGRLYDEKRRQIKPGDIIIFEGGKL--KVKVKGIRVYsSFKEMLEKEGIenvlPGVKSIEEG 82
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPVVGDLLILLDSTGRPvgVIEVTDVEII-PFEEVTEEHAY----LEGESLEEW 75

                          90       100
                  ....*....|....*....|....*..
2Z0T_A         83 VKVYRQFYDEEREKKYGVVAIEIEPIE 109
Cdd:pfam04266  76 RKVHKEFYPEEKEEDEGVVVEEFELVE 102
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 5-109 2.64e-10

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: 52.73  E-value: 2.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0T_A           5 MGLQEEYIELIKAGKKKIEGRlyDEKRRQIKPGDIIIFE--GGKLKVKVKGIRV-YSSFKEMLEKEGienVLPGVKSIEE 81
Cdd:smart01022   1 LSFKDELADLILSGKKTATIR--LENEPLPKVGDLLIVLdgEGKPVCVIEVTSVeIIPFKDVTAEHA---YLEGEGSLEE 75

                           90       100
                   ....*....|....*....|....*...
2Z0T_A          82 GVKVYRQFYDEEREkkygVVAIEIEPIE 109
Cdd:smart01022  76 WRKVHKEFYPEDME----VVCEEFEVVE 99
 
Name Accession Description Interval E-value
ASCH COG4043
ASC-1 homology (ASCH) domain, predicted RNA-binding domain [General function prediction only];
1-108 3.19e-43

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


Pssm-ID: 443221  Cd Length: 113  Bit Score: 136.59  E-value: 3.19e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0T_A        1 MKWEMGLQEEYIELIKAGKKKIEGRLYDEKRRQIKPGDIIIFE----GGKLKVKVKGIRVYSSFKEMLEKEGIENVLPGV 76
Cdd:COG4043   1 MTHKMGLEEEYFELIKSGKKTIEGRLNDPKRKKIKVGDKIVFInletGESLTVRVTDVRRYPTFKEMLEEEGLEKVLPDG 80

                        90       100       110
                ....*....|....*....|....*....|..
2Z0T_A       77 KSIEEGVKVYRQFYDEEREKKYGVVAIEIEPI 108
Cdd:COG4043  81 TSLEEMVKIYYKIYSKEKEKKYGVLAIEIELI 112
ASCH_PF0470_like cd06555
ASC-1 homology domain, subfamily similar to Pyrococcus furiosus Pf0470. The ASCH domain, a ...
 3-107 3.23e-43

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: 136.60  E-value: 3.23e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0T_A        3 WEMGLQEEYIELIKAGKKKIEGRLYDEKRRQIKPGDIIIF----EGGKLKVKVKGIRVYSSFKEMLEKEGIENVLPGVKS 78
Cdd:cd06555   1 HEMGLEEEPFELIKSGKKTIEIRLNDEKRQQIKVGDKILFndldTGQQLLVKVVDIRKYDSFRELLEEEGLEKVGPGVDS 80

                        90       100
                ....*....|....*....|....*....
2Z0T_A       79 IEEGVKVYRQFYDEEREKKYGVVAIEIEP 107
Cdd:cd06555  81 IEEGVKDTYKIYSKEQEKKYGVLAIEIRV 109
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 5-109 2.39e-15

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: 65.86  E-value: 2.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0T_A          5 MGLQEEYIELIKAGKKKIEGRLYDEKRRQIKPGDIIIFEGGKL--KVKVKGIRVYsSFKEMLEKEGIenvlPGVKSIEEG 82
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPVVGDLLILLDSTGRPvgVIEVTDVEII-PFEEVTEEHAY----LEGESLEEW 75

                          90       100
                  ....*....|....*....|....*..
2Z0T_A         83 VKVYRQFYDEEREKKYGVVAIEIEPIE 109
Cdd:pfam04266  76 RKVHKEFYPEEKEEDEGVVVEEFELVE 102
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 5-109 2.64e-10

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: 52.73  E-value: 2.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0T_A           5 MGLQEEYIELIKAGKKKIEGRlyDEKRRQIKPGDIIIFE--GGKLKVKVKGIRV-YSSFKEMLEKEGienVLPGVKSIEE 81
Cdd:smart01022   1 LSFKDELADLILSGKKTATIR--LENEPLPKVGDLLIVLdgEGKPVCVIEVTSVeIIPFKDVTAEHA---YLEGEGSLEE 75

                           90       100
                   ....*....|....*....|....*...
2Z0T_A          82 GVKVYRQFYDEEREkkygVVAIEIEPIE 109
Cdd:smart01022  76 WRKVHKEFYPEDME----VVCEEFEVVE 99
ASCH cd06541
ASC-1 homology or ASCH domain, a small beta-barrel domain found in all three kingdoms of life. ...
 7-106 1.94e-07

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: 45.35  E-value: 1.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0T_A        7 LQEEYIELIKAGKKKIEGRLYDEKRRQIKPGDIIIF---EGGKLKVKVKGIRVYSSFKEMLEkEGIENVLPGVKSIEEGV 83
Cdd:cd06541   4 FGDRYGQLVVSGRKTIEIRSLDIYEQLPKAGDYLIIldgQQPLAIAEVVKVEIMPMVNELSE-EQEQAEGEGDLTLLYEL 82

                        90       100
                ....*....|....*....|...
2Z0T_A       84 KVYRQFYDEEREKKYGVVAIEIE 106
Cdd:cd06541  83 KEHAAFFKEELAPDMLLYAISFE 105
 
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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