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103  structures 7165  species 0  interactions 8908  sequences 106  architectures

Family: RNA_pol_A_CTD (PF03118)

Summary: Bacterial RNA polymerase, alpha chain C terminal domain

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Bacterial RNA polymerase, alpha chain C terminal domain Provide feedback

The alpha subunit of RNA polymerase consists of two independently folded domains, referred to as amino-terminal and carboxyl terminal domains. The amino terminal domain is involved in the interaction with the other subunits of the RNA polymerase. The carboxyl-terminal domain interacts with the DNA and activators. The amino acid sequence of the alpha subunit is conserved in prokaryotic and chloroplast RNA polymerases. There are three regions of particularly strong conservation, two in the amino-terminal and one in the carboxyl- terminal [2].

Literature references

  1. Jeon YH, Negishi T, Shirakawa M, Yamazaki T, Fujita N, Ishihama A, Kyogoku Y; , Science 1995;270:1495-1497.: Solution structure of the activator contact domain of the RNA polymerase alpha subunit. PUBMED:7491496 EPMC:7491496

  2. Ebright RH, Busby S; , Curr Opin Genet Dev 1995;5:197-203.: The Escherichia coli RNA polymerase alpha subunit: structure and function. PUBMED:7613089 EPMC:7613089

  3. Murakami K, Kimura M, Owens JT, Meares CF, Ishihama A; , Proc Natl Acad Sci USA 1997;94:1709-1714.: The two alpha subunits of Escherichia coli RNA polymerase are asymmetrically arranged and contact different halves of the DNA upstream element. PUBMED:9050843 EPMC:9050843


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR011260

The core of the bacterial RNA polymerase (RNAP) consists of four subunits, two alpha, a beta and a beta', which are conserved from bacteria to mammals. The alpha subunit (RpoA) initiates RNAP assembly by dimerising to form a platform on which the beta subunits can interact. The alpha subunit consists of a N-terminal domain (NTD) and a C-terminal domain (CTD), connected by a short linker. The NTD is essential for RNAP assembly, while the CTD is necessary for transcription regulation, interacting with transcription factors and promoter upstream elements. In Escherichia coli, the catabolite activator protein (CAP or CRP) was shown to exert its effect through its interactions with the CTD, where CAP binding to CTD promotes RNAP binding to promoter DNA, thereby stimulating transcription initiation at class I CAP-dependent promoters. At class II CAP-dependent promoters, the interaction of CAP with CTD is one of multiple interactions involved in activation [ PUBMED:12202833 ].

The CTD has a compact structure of four helices and two long arms enclosing its hydrophobic core, making its folding topology distinct from most other binding proteins. The upstream promoter element-binding site is formed from helices 1 and 4 [ PUBMED:7491496 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan HHH (CL0198), which has the following description:

This superfamily includes Helix-hairpin-helix DNA-binding domains.

The clan contains the following 23 members:

Cdd1 DNA_pol_B_N DNA_pol_lambd_f DUF3173 DUF3701 DUF4332 DUF655 HHH HhH-GPD HHH_2 HHH_3 HHH_4 HHH_5 HHH_6 HHH_7 HHH_8 HHH_9 IMS_HHH PsbU RNA_pol_A_CTD T2SSK TfoX_C Transposase_20

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(59)
Full
(8908)
Representative proteomes UniProt
(53915)
RP15
(1354)
RP35
(4605)
RP55
(9275)
RP75
(15721)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(59)
Full
(8908)
Representative proteomes UniProt
(53915)
RP15
(1354)
RP35
(4605)
RP55
(9275)
RP75
(15721)
Alignment:
Format:
Order:
Sequence:
Gaps:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(59)
Full
(8908)
Representative proteomes UniProt
(53915)
RP15
(1354)
RP35
(4605)
RP55
(9275)
RP75
(15721)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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's seed alignment. 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 alignment.

Note: You can also download the data file for the tree.

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 View help on the curation process

Seed source: Pfam-B_172 (release 3.0)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Finn RD , Bateman A
Number in seed: 59
Number in full: 8908
Average length of the domain: 65.90 aa
Average identity of full alignment: 44 %
Average coverage of the sequence by the domain: 19.85 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.8 23.8
Trusted cut-off 23.8 23.8
Noise cut-off 23.7 23.7
Model length: 67
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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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 RNA_pol_A_CTD domain has been found. There are 103 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0JZ49 View 3D Structure Click here
A0KF45 View 3D Structure Click here
A0L5Z8 View 3D Structure Click here
A0LIL7 View 3D Structure Click here
A0LRP8 View 3D Structure Click here
A0PXX5 View 3D Structure Click here
A0QSL8 View 3D Structure Click here
A0T0K0 View 3D Structure Click here
A0T0Z4 View 3D Structure Click here
A1A095 View 3D Structure Click here
A1ALW7 View 3D Structure Click here
A1AVM5 View 3D Structure Click here
A1B052 View 3D Structure Click here
A1BJ07 View 3D Structure Click here
A1E9V6 View 3D Structure Click here
A1KB01 View 3D Structure Click here
A1R8R5 View 3D Structure Click here
A1S243 View 3D Structure Click here
A1SNI8 View 3D Structure Click here
A1SXW8 View 3D Structure Click here
A1T0B7 View 3D Structure Click here
A1T520 View 3D Structure Click here
A1TJU2 View 3D Structure Click here
A1UBY5 View 3D Structure Click here
A1USR8 View 3D Structure Click here
A1VJ40 View 3D Structure Click here
A1W333 View 3D Structure Click here
A1WK92 View 3D Structure Click here
A1WV97 View 3D Structure Click here
A2SLD1 View 3D Structure Click here
A3CK90 View 3D Structure Click here
A3DJK1 View 3D Structure Click here
A3N382 View 3D Structure Click here
A3PF25 View 3D Structure Click here
A3Q9A7 View 3D Structure Click here
A4FPJ2 View 3D Structure Click here
A4G9R3 View 3D Structure Click here
A4GYU3 View 3D Structure Click here
A4J139 View 3D Structure Click here
A4SCT6 View 3D Structure Click here