Summary: 'Cold-shock' DNA-binding domain
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Cold-shock domain Edit Wikipedia article
| CSD | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| solution structure of the single-stranded dna-binding cold shock domain (csd) of human y-box protein 1 (yb1) determined by nmr (10 lowest energy structures) | |||||||||
| Identifiers | |||||||||
| Symbol | CSD | ||||||||
| Pfam | PF00313 | ||||||||
| Pfam clan | CL0021 | ||||||||
| InterPro | IPR002059 | ||||||||
| PROSITE | PDOC00304 | ||||||||
| SCOP | 1mjc | ||||||||
| SUPERFAMILY | 1mjc | ||||||||
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Im molecular biology, the cold-shock domain (CSD) is a protein domain of about 70 amino acids which has been found in prokaryotic and eukaryotic DNA-binding proteins.[1][2][3] Part of this domain is highly similar to the RNP-1 RNA-binding motif.[4]
When Escherichia coli is exposed to a temperature drop from 37 to 10 degrees Celsius, a 4-5 hour lag phase occurs, after which growth is resumed at a reduced rate.[5] During the lag phase, the expression of around 13 proteins, which contain cold shock domains is increased 2-10 fold.[6] These so-called 'cold shock' proteins are thought to help the cell to survive in temperatures lower than optimum growth temperature, by contrast with heat shock proteins, which help the cell to survive in temperatures greater than the optimum, possibly by condensation of the chromosome and organisation of the prokaryotic nucleoid.[5]
[edit] References
- ^ Doniger J, Landsman D, Gonda MA, Wistow G (April 1992). "The product of unr, the highly conserved gene upstream of N-ras, contains multiple repeats similar to the cold-shock domain (CSD), a putative DNA-binding motif". New Biol. 4 (4): 389â95. PMID 1622933.
- ^ Wistow G (April 1990). "Cold shock and DNA binding". Nature 344 (6269): 823â4. doi:10.1038/344823c0. PMID 2184368.
- ^ Jones PG, Inouye M (March 1994). "The cold-shock response--a hot topic". Mol. Microbiol. 11 (5): 811â8. doi:10.1111/j.1365-2958.1994.tb00359.x. PMID 8022259.
- ^ Landsman D (June 1992). "RNP-1, an RNA-binding motif is conserved in the DNA-binding cold shock domain". Nucleic Acids Res. 20 (11): 2861â4. doi:10.1093/nar/20.11.2861. PMC 336933. PMID 1614871. //www.ncbi.nlm.nih.gov/pmc/articles/PMC336933/.
- ^ a b Obokata J, Ohme M, Hayashida N (October 1991). "Nucleotide sequence of a cDNA clone encoding a putative glycine-rich protein of 19.7 kDa in Nicotiana sylvestris". Plant Mol. Biol. 17 (4): 953â5. PMID 1912512.
- ^ Tafuri SR, Wolffe AP (November 1990). "Xenopus Y-box transcription factors: molecular cloning, functional analysis and developmental regulation". Proc. Natl. Acad. Sci. U.S.A. 87 (22): 9028â32. doi:10.1073/pnas.87.22.9028. PMC 55094. PMID 2247479. //www.ncbi.nlm.nih.gov/pmc/articles/PMC55094/.
This article incorporates text from the public domain Pfam and InterPro IPR002059
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Literature references
-
Schindelin H, Jiang W, Inouye M, Heinemann U; , Proc Natl Acad Sci U S A 1994;91:5119-5123.: Crystal structure of CspA, the major cold shock protein of Escherichia coli. PUBMED:8197194 EPMC:8197194
Internal database links
| Similarity to PfamA using HHSearch: | OB_RNB |
External database links
| HOMSTRAD: | csp |
| PANDIT: | PF00313 |
| PRINTS: | PR00050 |
| PROSITE: | PDOC00304 |
| Pseudofam: | PF00313 |
| SCOP: | 1mjc |
| SYSTERS: | CSD |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002059
When Escherichia coli is exposed to a temperature drop from 37 to 10 degrees centigrade, a 4-5 hour lag phase occurs, after which growth is resumed at a reduced rate [PUBMED:1912512]. During the lag phase, the expression of around 13 proteins, which contain specific DNA-binding regions [PUBMED:2247479], is increased 2-10 fold. These so-called 'cold shock' proteins are thought to help the cell to survive in temperatures lower than optimum growth temperature, by contrast with heat shock proteins, which help the cell to survive in temperatures greater than the optimum, possibly by condensation of the chromosome and organisation of the prokaryotic nucleoid [PUBMED:1912512]. A conserved domain of about 70 amino acids has been found in prokaryotic and eukaryotic DNA-binding proteins [PUBMED:1622933, PUBMED:2184368, PUBMED:8022259]. This domain is known as the 'cold-shock domain' (CSD), part of which is highly similar [PUBMED:1614871] to the RNP-1 RNA-binding motif.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 | regulation of transcription, DNA-dependent (GO:0006355) |
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 OB (CL0021), which contains the following 45 members:
BOF CSD DNA_ligase_OB DUF2110 DUF223 DUF3127 DUF35 EFP eIF-1a eIF-5a EutN_CcmL EXOSC1 mRNA_cap_C OB_NTP_bind OB_RNB OmdA Phage_DNA_bind POT1 RecO_N RecO_N_2 Rep-A_N Rep_fac-A_3 Rho_RNA_bind Ribosom_S12_S23 Ribosomal_L2 Ribosomal_S17 RNA_pol_Rbc25 RNA_pol_Rpb8 RuvA_N S1 S1-like S1_2 SSB Stn1 TEBP_beta Ten1 Ten1_2 TOBE TOBE_2 TOBE_3 TRAM tRNA_anti-codon tRNA_anti-like tRNA_anti_2 tRNA_bindAlignments
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...
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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 (40) |
Full (14886) |
Representative proteomes | NCBI (7958) |
Meta (3141) |
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| RP15 (1082) |
RP35 (2120) |
RP55 (2935) |
RP75 (3740) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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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 (40) |
Full (14886) |
Representative proteomes | NCBI (7958) |
Meta (3141) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (1082) |
RP35 (2120) |
RP55 (2935) |
RP75 (3740) |
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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: | Prosite |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Finn RD |
| Number in seed: | 40 |
| Number in full: | 14886 |
| Average length of the domain: | 65.20 aa |
| Average identity of full alignment: | 46 % |
| Average coverage of the sequence by the domain: | 67.33 % |
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: | 66 | ||||||||||||
| Family (HMM) version: | 17 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
CSDStructures
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 CSD domain has been found. There are 61 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