6LBS

Crystal structure of yeast Stn1

External Resource: Annotation

Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF12659	Telomere capping C-terminal wHTH (Stn1_C)	Telomere capping C-terminal wHTH	This domain consists of tandem winged helix-turn-helix motifs. Stn1 and Ten1 are DNA-binding proteins with specificity for telomeric DNA substrates and both protect chromosome termini from unregulated resection and regulate telomere length. Stn1 comp ...	This domain consists of tandem winged helix-turn-helix motifs. Stn1 and Ten1 are DNA-binding proteins with specificity for telomeric DNA substrates and both protect chromosome termini from unregulated resection and regulate telomere length. Stn1 complexes with Ten1 and Cdc13 to function as a telomere-specific replication protein A (RPA)-like complex [1-4]. These three interacting proteins associate with the telomeric overhang in budding yeast, whereas a single protein known as Pot1 (protection of telomeres-1) performs this function in fission yeast, and a two-subunit complex consisting of POT1 and TPP1 associates with telomeric ssDNA in humans. S.pombe has Stn1- and Ten1-like proteins that are essential for chromosome end protection. Stn1 orthologues exist in all species that have Pot1, whereas Ten1-like proteins can be found in all fungi. Fission yeast Stn1 and Ten1 localise at telomeres in a manner that correlates with the length of the ssDNA overhang, suggesting that they specifically associate with the telomeric ssDNA. Two separate protein complexes are required for chromosome end protection in fission yeast. Protection of telomeres by multiple proteins with OB-fold domains is conserved in eukaryotic evolution [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	KLLA0C11825p	-	telomere organization chromosome organization primary metabolic process DNA metabolic process nucleic acid metabolic process telomere maintenance cellular component organization nucleobase-containing compound metabolic process organic cyclic compound metabolic process organelle organization organic substance metabolic process telomere capping cellular process metabolic process telomere organization chromosome organization primary metabolic process DNA metabolic process nucleic acid metabolic process telomere maintenance cellular component organization nucleobase-containing compound metabolic process organic cyclic compound metabolic process organelle organization organic substance metabolic process telomere capping cellular process metabolic process cellular component organization or biogenesis macromolecule metabolic process	membrane-bounded organelle protein-containing complex intracellular anatomical structure protein-DNA complex nucleus nuclear protein-containing complex chromosome cellular anatomical entity intracellular membrane-bounded organelle chromosomal region intracellular organelle organelle telomere cap complex intracellular non-membrane-bounded organelle membrane-bounded organelle protein-containing complex intracellular anatomical structure protein-DNA complex nucleus nuclear protein-containing complex chromosome cellular anatomical entity intracellular membrane-bounded organelle chromosomal region intracellular organelle organelle telomere cap complex intracellular non-membrane-bounded organelle chromosome, telomeric repeat region CST complex chromosome, telomeric region non-membrane-bounded organelle nuclear telomere cap complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR024263	Stn1, C-terminal, fungi	Domain
A, B, C, D, E A, B, C, D, E, F	IPR018856	CST complex subunit Stn1, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR038240	Stn1, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR012340	Nucleic acid-binding, OB-fold	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.