Summary
CAT RNA binding domain
This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer [1] to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin [4]. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains (PF00874) that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template [2].
Literature references
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van Tilbeurgh H, Manival X, Aymerich S, Lhoste JM, Dumas C, Kochoyan M; , EMBO J 1997;16:5030-5036.: Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis. PUBMED:9305644
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Declerck N, Vincent F, Hoh F, Aymerich S, van Tilbeurgh H; , J Mol Biol 1999;294:389-402.: RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domain from SacY and LicT. PUBMED:10610766
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Manival X, Yang Y, Strub MP, Kochoyan M, Steinmetz M, Aymerich S; , EMBO J 1997;16:5019-5029.: From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins. PUBMED:9305643
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Yang Y, Declerck N, Manival X, Aymerich S, Kochoyan M; , EMBO J. 2002;21:1987-1997.: Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT. PUBMED:11953318
InterPro entry IPR004341
The CAT RNA-binding domain is found at the amino terminus of a family of transcriptional antiterminator proteins, the Co-AntiTerminator (CAT) domain. This domain forms a dimer in the crystal structure PUBMED:9305644. Transcriptional antiterminators of the BglG/SacY family are regulatory proteins that mediate the induction of sugar metabolizing operons in Gram-positive and Gram-negative bacteria. Upon activation, these proteins bind to specific targets in nascent mRNAs, thereby preventing abortive dissociation of the RNA polymerase from the DNA template PUBMED:10610766.Gene Ontology
| Molecular function | RNA binding (GO:0003723) |
| Biological process | regulation of transcription, DNA-dependent (GO:0006355) |
External database links
| PANDIT: | PF03123 |
| SCOP: | 1h99 |
| SYSTERS: | CAT_RBD |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | P39805/1-60 Psi-blast |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Bateman A, Declerck N |
| Number in seed: | 15 |
| Number in full: | 685 |
| Average length of the domain: | 57.90 aa |
| Average identity of full alignment: | 36 % |
| Average coverage of the sequence by the domain: | 20.99 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 59 | ||||||||||||
| Family (HMM) version: | 8 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CAT_RBD domain has been found.
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