Summary: SeqA protein
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SeqA protein Provide feedback
The binding of SeqA protein to hemimethylated GATC sequences is important in the negative modulation of chromosomal initiation at oriC, and in the formation of SeqA foci necessary for Escherichia coli chromosome segregation [3]. SeqA tetramers are able to aggregate or multimerise in a reversible, concentration-dependent manner [3]. Apart from its function in the control of DNA replication, SeqA may also be a specific transcription factor [4].
Literature references
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Shakibai N, Ishidate K, Reshetnyak E, Gunji S, Kohiyama M, Rothfield L; , Proc Natl Acad Sci U S A 1998;95:11117-11121.: High-affinity binding of hemimethylated oriC by Escherichia coli membranes is mediated by a multiprotein system that includes SeqA and a newly identified factor, SeqB. PUBMED:9736699 EPMC:9736699
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Slater S, Wold S, Lu M, Boye E, Skarstad K, Kleckner N; , Cell 1995;82:927-936.: E. coli SeqA protein binds oriC in two different methyl-modulated reactions appropriate to its roles in DNA replication initiation and origin sequestration. PUBMED:7553853 EPMC:7553853
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Lee H, Kang S, Bae SH, Choi BS, Hwang DS; , J Biol Chem 2001;276:34600-34606.: SeqA protein aggregation is necessary for SeqA function. PUBMED:11457824 EPMC:11457824
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Slominska M, Wegrzyn A, Konopa G, Skarstad K, Wegrzyn G; , Mol Microbiol 2001;40:1371-1379.: SeqA, the Escherichia coli origin sequestration protein, is also a specific transcription factor. PUBMED:11442835 EPMC:11442835
External database links
| PANDIT: | PF03925 |
| Pseudofam: | PF03925 |
| SCOP: | 1lrr |
| SYSTERS: | SeqA |
This tab holds annotation information from the InterPro database.
InterPro entry IPR005621
The binding of SeqA protein to hemimethylated GATC sequences is important in the negative modulation of chromosomal initiation at oriC, and in the formation of SeqA foci necessary for Escherichia coli chromosome segregation [PUBMED:11457824]. SeqA tetramers are able to aggregate or multimerize in a reversible, concentration-dependent manner [PUBMED:11457824]. Apart from its function in the control of DNA replication, SeqA may also be a specific transcription factor [PUBMED:11442835]. The C-terminal domain binds DNA, binding to fully methylated and hemimethylated GATC sequences at oriC. The structure of the C-terminal domain consists of seven alpha-helices and three-stranded beta-sheet.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | DNA binding (GO:0003677) |
| Biological process | negative regulation of DNA-dependent DNA replication initiation (GO:0032297) |
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
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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics 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 (37) |
Full (801) |
Representative proteomes | NCBI (335) |
Meta (9) |
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| RP15 (13) |
RP35 (36) |
RP55 (70) |
RP75 (101) |
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| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
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 (37) |
Full (801) |
Representative proteomes | NCBI (335) |
Meta (9) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (13) |
RP35 (36) |
RP55 (70) |
RP75 (101) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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 HMMER3.
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
| Seed source: | COG3057 |
| Previous IDs: | none |
| Type: | Family |
| Author: | Bateman A |
| Number in seed: | 37 |
| Number in full: | 801 |
| Average length of the domain: | 177.20 aa |
| Average identity of full alignment: | 64 % |
| Average coverage of the sequence by the domain: | 98.90 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 190 | ||||||||||||
| Family (HMM) version: | 8 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
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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 SeqA domain has been found. There are 13 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 seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence