NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1759029288|gb|QFI37671|]
View 

ASCH domain-containing protein [Moritella marina ATCC 15381]

Protein Classification

ASCH domain-containing protein( domain architecture ID 570)

ASCH (ASC-1 homology) domain-containing protein may bind RNA; similar to mouse CXorf40A

Gene Ontology:  GO:0003723
PubMed:  16322048

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ASCH super family cl01020
ASC-1 homology or ASCH domain, a small beta-barrel domain found in all three kingdoms of life. ...
 5-103 1.34e-37

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.


The actual alignment was detected with superfamily member PRK04980:

Pssm-ID: 445230  Cd Length: 102  Bit Score: 122.29  E-value: 1.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288   5 ITFFQRLERSILSGNKTATIRDKSDSHYLVGQMLDACTHEDNRKMCQIEILSIEYVTFSELNRAHANAEGLPfLFMLKWI 84
Cdd:PRK04980    5 ITFFERFEADILAGRKTITIRDESESHFKPGDVLRVGTFEDDRYFCTIEVLSVSPVTFDELNEKHAEQENMT-LPELKQV 83

                          90
                  ....*....|....*....
gi 1759029288  85 VRKIYPTSNDLFFISFRVV 103
Cdd:PRK04980   84 IAEIYPNLDQLYVIEFKLL 102
 
Name Accession Description Interval E-value
PRK04980 PRK04980
hypothetical protein; Provisional
 5-103 1.34e-37

hypothetical protein; Provisional


Pssm-ID: 179908  Cd Length: 102  Bit Score: 122.29  E-value: 1.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288   5 ITFFQRLERSILSGNKTATIRDKSDSHYLVGQMLDACTHEDNRKMCQIEILSIEYVTFSELNRAHANAEGLPfLFMLKWI 84
Cdd:PRK04980    5 ITFFERFEADILAGRKTITIRDESESHFKPGDVLRVGTFEDDRYFCTIEVLSVSPVTFDELNEKHAEQENMT-LPELKQV 83

                          90
                  ....*....|....*....
gi 1759029288  85 VRKIYPTSNDLFFISFRVV 103
Cdd:PRK04980   84 IAEIYPNLDQLYVIEFKLL 102
YqfB COG3097
Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown];
5-103 6.55e-37

Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown];


Pssm-ID: 442331  Cd Length: 102  Bit Score: 120.37  E-value: 6.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288   5 ITFFQRLERSILSGNKTATIRDKSDSHYLVGQMLDACTHEDNRKMCQIEILSIEYVTFSELNRAHANAEGLPfLFMLKWI 84
Cdd:COG3097     5 ITFFERFEPDILAGRKTITIRDESESHFKPGQILRVGTYEDDRYFCTIEVLSVTPVTLDELTEEHARQENMT-LDELKQV 83

                          90
                  ....*....|....*....
gi 1759029288  85 VRKIYPTSNDLFFISFRVV 103
Cdd:COG3097    84 IREIYPGEDQLYVIEFKLV 102
ASCH_yqfb_like cd06552
ASC-1 homology domain, subfamily similar to Escherichia coli Yqfb. The ASCH domain, a small ...
 5-102 4.00e-33

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: 110.79  E-value: 4.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288   5 ITFFQRLERSILSGNKTATIRDKSDSHYLVGQMLDACTHEdnRKMCQIEILSIEYVTFSELNRAHANAEGLPFLFMLKWI 84
Cdd:cd06552     2 ILFFERYEEAILSGKKTATIRDGGESHLKPGDVVEVHTGE--RIFGEAEITSVEEKTLGELTDEDARQEGFPSLEELKEA 79

                          90       100
                  ....*....|....*....|.
gi 1759029288  85 VRKIYPTSND---LFFISFRV 102
Cdd:cd06552    80 LKEIYPGLKDddeVYVIEFRL 100
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 5-104 2.87e-24

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: 88.17  E-value: 2.87e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288    5 ITFFQRLERSILSGNKTATIRDKSDSHYLVGQmLDACTHEDNRKMCQIEILSIEYVTFSELNRAHANAEGLPFLFMLKWI 84
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLENEPLPKVGD-LLIVLDGEGKPVCVIEVTSVEIIPFKDVTAEHAYLEGEGSLEEWRKV 79

                           90       100
                   ....*....|....*....|
gi 1759029288   85 VRKIYPTSNDLFFISFRVVT 104
Cdd:smart01022  80 HKEFYPEDMEVVCEEFEVVE 99
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 5-103 1.59e-22

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: 83.96  E-value: 1.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288   5 ITFFQRLERSILSGNKTATIRDKSDSHYLVGqMLDACTHEDNRKMCQIEILSIEYVTFSELNRAHANAEGlPFLFMLKWI 84
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPVVG-DLLILLDSTGRPVGVIEVTDVEIIPFEEVTEEHAYLEG-ESLEEWRKV 78

                          90       100
                  ....*....|....*....|...
gi 1759029288  85 VRKIYP----TSNDLFFISFRVV 103
Cdd:pfam04266  79 HKEFYPeekeEDEGVVVEEFELV 101
 
Name Accession Description Interval E-value
PRK04980 PRK04980
hypothetical protein; Provisional
 5-103 1.34e-37

hypothetical protein; Provisional


Pssm-ID: 179908  Cd Length: 102  Bit Score: 122.29  E-value: 1.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288   5 ITFFQRLERSILSGNKTATIRDKSDSHYLVGQMLDACTHEDNRKMCQIEILSIEYVTFSELNRAHANAEGLPfLFMLKWI 84
Cdd:PRK04980    5 ITFFERFEADILAGRKTITIRDESESHFKPGDVLRVGTFEDDRYFCTIEVLSVSPVTFDELNEKHAEQENMT-LPELKQV 83

                          90
                  ....*....|....*....
gi 1759029288  85 VRKIYPTSNDLFFISFRVV 103
Cdd:PRK04980   84 IAEIYPNLDQLYVIEFKLL 102
YqfB COG3097
Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown];
5-103 6.55e-37

Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown];


Pssm-ID: 442331  Cd Length: 102  Bit Score: 120.37  E-value: 6.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288   5 ITFFQRLERSILSGNKTATIRDKSDSHYLVGQMLDACTHEDNRKMCQIEILSIEYVTFSELNRAHANAEGLPfLFMLKWI 84
Cdd:COG3097     5 ITFFERFEPDILAGRKTITIRDESESHFKPGQILRVGTYEDDRYFCTIEVLSVTPVTLDELTEEHARQENMT-LDELKQV 83

                          90
                  ....*....|....*....
gi 1759029288  85 VRKIYPTSNDLFFISFRVV 103
Cdd:COG3097    84 IREIYPGEDQLYVIEFKLV 102
ASCH_yqfb_like cd06552
ASC-1 homology domain, subfamily similar to Escherichia coli Yqfb. The ASCH domain, a small ...
 5-102 4.00e-33

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: 110.79  E-value: 4.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288   5 ITFFQRLERSILSGNKTATIRDKSDSHYLVGQMLDACTHEdnRKMCQIEILSIEYVTFSELNRAHANAEGLPFLFMLKWI 84
Cdd:cd06552     2 ILFFERYEEAILSGKKTATIRDGGESHLKPGDVVEVHTGE--RIFGEAEITSVEEKTLGELTDEDARQEGFPSLEELKEA 79

                          90       100
                  ....*....|....*....|.
gi 1759029288  85 VRKIYPTSND---LFFISFRV 102
Cdd:cd06552    80 LKEIYPGLKDddeVYVIEFRL 100
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 5-104 2.87e-24

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: 88.17  E-value: 2.87e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288    5 ITFFQRLERSILSGNKTATIRDKSDSHYLVGQmLDACTHEDNRKMCQIEILSIEYVTFSELNRAHANAEGLPFLFMLKWI 84
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLENEPLPKVGD-LLIVLDGEGKPVCVIEVTSVEIIPFKDVTAEHAYLEGEGSLEEWRKV 79

                           90       100
                   ....*....|....*....|
gi 1759029288   85 VRKIYPTSNDLFFISFRVVT 104
Cdd:smart01022  80 HKEFYPEDMEVVCEEFEVVE 99
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 5-103 1.59e-22

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: 83.96  E-value: 1.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288   5 ITFFQRLERSILSGNKTATIRDKSDSHYLVGqMLDACTHEDNRKMCQIEILSIEYVTFSELNRAHANAEGlPFLFMLKWI 84
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPVVG-DLLILLDSTGRPVGVIEVTDVEIIPFEEVTEEHAYLEG-ESLEEWRKV 78

                          90       100
                  ....*....|....*....|...
gi 1759029288  85 VRKIYP----TSNDLFFISFRVV 103
Cdd:pfam04266  79 HKEFYPeekeEDEGVVVEEFELV 101
ASCH COG2411
Predicted RNA-binding protein, contains PUA-like ASCH domain [General function prediction only] ...
 5-103 2.37e-07

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


Pssm-ID: 441966  Cd Length: 103  Bit Score: 45.25  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288   5 ITFFQRLERSILSGNKTATIRdKSDSHYLVGQMLDacTHEDNRKMCQIEILSIEYVTFSELNRAHANAEGLPFLFMLKWI 84
Cdd:COG2411     4 LNFKPKYLDAILSGRKTATIR-LGDKRYKPGDEVY--VTSGGRKIAKARITSVRVKKLSELTDEDARLDGFSSVEELIEA 80

                          90       100
                  ....*....|....*....|..
gi 1759029288  85 VRKIYP--TSNDLF-FISFRVV 103
Cdd:COG2411    81 LRKIYGdiSPDDEVtVIEFEVV 102
ASCH cd06541
ASC-1 homology or ASCH domain, a small beta-barrel domain found in all three kingdoms of life. ...
 5-86 6.53e-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: 44.19  E-value: 6.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759029288   5 ITFFQRLERSILSGNKTATIRDKS--DSHYLVGQMLDACTHEdnRKMCQIEILSIE-YVTFSELNRAHANAEGLPFLFML 81
Cdd:cd06541     2 LMFGDRYGQLVVSGRKTIEIRSLDiyEQLPKAGDYLIILDGQ--QPLAIAEVVKVEiMPMVNELSEEQEQAEGEGDLTLL 79


                  ....*
gi 1759029288  82 KWIVR 86
Cdd:cd06541    80 YELKE 84
 
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