Summary: Regulatory protein Sir1
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Regulatory protein Sir1 Provide feedback
Sir1p interacts with the BAH domain of the Orc1p subunit of the origin recognition complex (ORC) resulting in the establishment of silent chromatin at HMR and HML in S.cerevisiae . The amino acids from the ORC interaction region of Sir1p are presented on a conserved, convex surface that forms a complementary interface with the Orc1 BAH domain, critical for transcriptional silencing .
Hou Z, Bernstein DA, Fox CA, Keck JL; , Proc Natl Acad Sci U S A. 2005;102:8489-8494.: Structural basis of the Sir1-origin recognition complex interaction in transcriptional silencing. PUBMED:15932939 EPMC:15932939
This tab holds annotation information from the InterPro database.
InterPro entry IPR021646
This entry represents the ORC-binding domain of Sir1. Sir1 interacts with the BAH domain of the Orc1 subunit of the origin recognition complex (ORC) resulting in the establishment of silent chromatin at HMR and HML in S.cerevisiae [PUBMED:15932939]. The amino acids from the ORC interaction region of Sir1 are presented on a conserved, convex surface that forms a complementary interface with the Orc1 BAH domain, critical for transcriptional silencing [PUBMED:15932939].
Proteins containing this domain also include Y' element ATP-dependent helicase protein 1, which catalyses DNA unwinding and is involved in telomerase-independent telomere maintenance [PUBMED:9837911].
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Curation and family details
|Number in seed:||29|
|Number in full:||104|
|Average length of the domain:||107.20 aa|
|Average identity of full alignment:||37 %|
|Average coverage of the sequence by the domain:||16.04 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Sir1 domain has been found. There are 4 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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