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Conserved domains on  [gi|74753396|sp|Q9ULW3|]
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RecName: Full=Activator of basal transcription 1; Short=hABT1; AltName: Full=Basal transcriptional activator

Protein Classification

RNA-binding protein( domain architecture ID 10188096)

RNA-binding protein recognizes RNA via an RNA recognition motif (RRM)

Gene Ontology:  GO:0003723
PubMed:  15853797|22278943|18515081
SCOP:  3000110

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RRM_ABT1_like cd12263
RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar ...
 46-149 1.99e-50

RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar proteins; This subfamily corresponds to the RRM of novel nuclear proteins termed ABT1 and its homologous counterpart, pre-rRNA-processing protein ESF2 (eighteen S factor 2), from yeast. ABT1 associates with the TATA-binding protein (TBP) and enhances basal transcription activity of class II promoters. Meanwhile, ABT1 could be a transcription cofactor that can bind to DNA in a sequence-independent manner. The yeast ABT1 homolog, ESF2, is a component of 90S preribosomes and 5' ETS-based RNPs. It is previously identified as a putative partner of the TATA-element binding protein. However, it is primarily localized to the nucleolus and physically associates with pre-rRNA processing factors. ESF2 may play a role in ribosome biogenesis. It is required for normal pre-rRNA processing, as well as for SSU processome assembly and function. Both ABT1 and ESF2 contain an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


:

Pssm-ID: 409707 [Multi-domain]  Cd Length: 98  Bit Score: 160.83  E-value: 1.99e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74753396  46 GIVYLGHIPPRFRPLHVRNLLSAYGEVGRVFFQAEDRFVRRKKKAAAAaggkkrSYTKDYTEGWVEFRDKRIAKRVAASL 125
Cdd:cd12263   1 GIVYLSRIPPGMNPAKLRQLLSQYGEVGRIYLQPEDPSKRKKRKKKGG------NKKKKFTEGWVEFEDKKVAKRVAESL 74

                        90       100
                ....*....|....*....|....
gi 74753396 126 HNTPMGARRRSPFRYDLWNLKYLH 149
Cdd:cd12263  75 NNTPIGGKKRSRFRDDLWNIKYLP 98
 
Name Accession Description Interval E-value
RRM_ABT1_like cd12263
RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar ...
 46-149 1.99e-50

RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar proteins; This subfamily corresponds to the RRM of novel nuclear proteins termed ABT1 and its homologous counterpart, pre-rRNA-processing protein ESF2 (eighteen S factor 2), from yeast. ABT1 associates with the TATA-binding protein (TBP) and enhances basal transcription activity of class II promoters. Meanwhile, ABT1 could be a transcription cofactor that can bind to DNA in a sequence-independent manner. The yeast ABT1 homolog, ESF2, is a component of 90S preribosomes and 5' ETS-based RNPs. It is previously identified as a putative partner of the TATA-element binding protein. However, it is primarily localized to the nucleolus and physically associates with pre-rRNA processing factors. ESF2 may play a role in ribosome biogenesis. It is required for normal pre-rRNA processing, as well as for SSU processome assembly and function. Both ABT1 and ESF2 contain an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409707 [Multi-domain]  Cd Length: 98  Bit Score: 160.83  E-value: 1.99e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74753396  46 GIVYLGHIPPRFRPLHVRNLLSAYGEVGRVFFQAEDRFVRRKKKAAAAaggkkrSYTKDYTEGWVEFRDKRIAKRVAASL 125
Cdd:cd12263   1 GIVYLSRIPPGMNPAKLRQLLSQYGEVGRIYLQPEDPSKRKKRKKKGG------NKKKKFTEGWVEFEDKKVAKRVAESL 74

                        90       100
                ....*....|....*....|....
gi 74753396 126 HNTPMGARRRSPFRYDLWNLKYLH 149
Cdd:cd12263  75 NNTPIGGKKRSRFRDDLWNIKYLP 98
 
Name Accession Description Interval E-value
RRM_ABT1_like cd12263
RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar ...
 46-149 1.99e-50

RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar proteins; This subfamily corresponds to the RRM of novel nuclear proteins termed ABT1 and its homologous counterpart, pre-rRNA-processing protein ESF2 (eighteen S factor 2), from yeast. ABT1 associates with the TATA-binding protein (TBP) and enhances basal transcription activity of class II promoters. Meanwhile, ABT1 could be a transcription cofactor that can bind to DNA in a sequence-independent manner. The yeast ABT1 homolog, ESF2, is a component of 90S preribosomes and 5' ETS-based RNPs. It is previously identified as a putative partner of the TATA-element binding protein. However, it is primarily localized to the nucleolus and physically associates with pre-rRNA processing factors. ESF2 may play a role in ribosome biogenesis. It is required for normal pre-rRNA processing, as well as for SSU processome assembly and function. Both ABT1 and ESF2 contain an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409707 [Multi-domain]  Cd Length: 98  Bit Score: 160.83  E-value: 1.99e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74753396  46 GIVYLGHIPPRFRPLHVRNLLSAYGEVGRVFFQAEDRFVRRKKKAAAAaggkkrSYTKDYTEGWVEFRDKRIAKRVAASL 125
Cdd:cd12263   1 GIVYLSRIPPGMNPAKLRQLLSQYGEVGRIYLQPEDPSKRKKRKKKGG------NKKKKFTEGWVEFEDKKVAKRVAESL 74

                        90       100
                ....*....|....*....|....
gi 74753396 126 HNTPMGARRRSPFRYDLWNLKYLH 149
Cdd:cd12263  75 NNTPIGGKKRSRFRDDLWNIKYLP 98
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 48-134 6.43e-04

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


Pssm-ID: 409669 [Multi-domain]  Cd Length: 72  Bit Score: 37.65  E-value: 6.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74753396  48 VYLGHIPPRFRPLHVRNLLSAYGEVGRVFFQaedrfvrrkkkaaaaaggkKRSYTKDYTEGWVEFRDKRIAKRVAASLHN 127
Cdd:cd00590   1 LFVGNLPPDTTEEDLRELFSKFGEVVSVRIV-------------------RDRDGKSKGFAFVEFESPEDAEKALEALNG 61


                ....*..
gi 74753396 128 TPMGARR 134
Cdd:cd00590  62 TELGGRP 68
 
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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