Summary
Structure-specific recognition protein (SSRP1)
SSRP1 has been implicated in transcriptional initiation and elongation and in DNA replication and repair [1].
Literature references
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Cao S, Bendall H, Hicks GG, Nashabi A, Sakano H, Shinkai Y, Gariglio M, Oltz EM, Ruley HE; , Mol Cell Biol. 2003;23:5301-5307.: The high-mobility-group box protein SSRP1/T160 is essential for cell viability in day 3.5 mouse embryos. PUBMED:12861016
InterPro entry IPR000969
Human structure-specific recognition protein, SSRP1, PUBMED:1372440 binds specifically to DNA modified with the anti-cancer drug cisplatin. An 81kDa protein is predicted, containing several highly-charged domains and a stretch of 75 residues that share 47% identity with a portion of the high mobility group (HMG) protein HMG1. This HMG box probably constitutes the structure recognition element for cisplatin-modified DNA, the probable recognition motif being the local duplex unwinding and bending that occurs on formation of intra-strand cross-links PUBMED:1372440. SSRP1 is the human homologue of a recently identified mouse protein that binds to recombination signal sequences PUBMED:1678855. These sequences have been postulated to form stem-loop structures, further implicating local bends and unwinding in DNA as a recognition target for HMG-box proteins. A Drosophila melanogaster cDNA encoding an HMG-box-containing protein has also been isolated PUBMED:7688122, PUBMED:8479916. This protein shares 50% sequence identity with human SSRP1. In vitro binding studies using Drosophila SSRP showed that the protein binds to single-stranded DNA and RNA, with highest affinity for nucleotides G and U. Comparison of the predicted amino acid sequences among SSRP family members reveals 48% identity, with structural conservation in the C-terminus of the HMG box, as well as domains of highly charged residues. The most highly conserved regions lie in the poorly understood N-terminus, suggesting that this portion of the protein is critical for its function PUBMED:8479916.
This entry contains Pob3 , which is a subunit of the heterodimeric yeast FACT complex (Spt16p ()-Pob3p) PUBMED:15987999. The FACT complex facilitates RNA Polymerase II transcription elongation through nucleosomes by destabilising and then reassembling nucleosome structure PUBMED:12524332, PUBMED:12934006.
Clan
This family is a member of clan SSRP1-like (CL0215), which contains the following 2 members:
Rtt106 SSrecogGene Ontology
| Cellular component | nucleus (GO:0005634) |
| Molecular function | DNA binding (GO:0003677) |
External database links
| PANDIT: | PF03531 |
| SYSTERS: | SSrecog |
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: | PRINTS |
| Previous IDs: | none |
| Type: | Family |
| Author: | Griffiths-Jones SR, Mistry J |
| Number in seed: | 7 |
| Number in full: | 194 |
| Average length of the domain: | 199.60 aa |
| Average identity of full alignment: | 42 % |
| Average coverage of the sequence by the domain: | 36.51 % |
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: | 216 | ||||||||||||
| Family (HMM) version: | 7 | ||||||||||||
| 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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Interactions
There is 1 interaction for this family. More...
SSrecogStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD 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 SSrecog domain has been found.
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