The domain within your query sequence starts at position 2 and ends at position 118; the E-value for the Ten1_2 domain shown below is 1.6e-44.
LPKPGVYYFPWEVSDGHVPEGSTLRTFGRLYLYDMARSLMTLAAPQKPDQCQLLVCTNLV EPFEAHVNFLYMVLGDLERMEGGAFVVRARLLTCVEGMDLSLLEKAILEQRRHLQKR
Ten1_2 |
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| PFAM accession number: | PF15490 |
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| Interpro abstract (IPR029146): | This entry represents the CST complex subunit Ten1 homologue from plants and animals [ (PUBMED:20697207) ]. Even though the protein sequence similarity is very low between budding yeast Ten1 ( IPR024222 ) and animal/plant Ten1, they are evolutionarily related. Two distinct telomere capping complexes have evolved: CST complex in budding yeast and shelterin complex in vertebrates. Budding yeast CST is composed of Cdc13, Ten1 and Stn1 [ (PUBMED:20697207) ]. The homologues of Ten1 and Stn1 have been identified in vertebrates and plants. The vertebrate CST complex does not appear to play a primary role in telomere protection, but may complement the function of shelterin complex [ (PUBMED:19854130) ]. Similar to budding yeast Ten1, mammalian Ten1 forms the CST complex with Stn1 homologue and binds to single strand DNA (ssDNA). However, unlike budding yeast CST, the binding of mammalian CST to ssDNA is not sequence specific. The mammalian CST complex may have both telomeric and non-telomeric functions [ (PUBMED:19854130) ]. In plants, the contribution of the CST components to chromosome end protection, telomeric DNA replication or both processes remains to be determined [ (PUBMED:20697207) ]. |
| GO component: | CST complex (GO:1990879) |
| GO function: | single-stranded DNA binding (GO:0003697) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Ten1_2