Annotations: 6THL

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	PH domain-like	8103654	3000134	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	PH domain-like	8103653	3000134	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Rtt106	e6thlA2	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: Rtt106	ECOD (1.6)
A	PH1-like_Rtt106	e6thlA1	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: PH1-like_Rtt106	ECOD (1.6)
B	F_UNCLASSIFIED	e6thlB1	A: a+b two layers	X: beta-Grasp	H: C-terminal wheel domain of Cns1 (From Topology)	T: C-terminal wheel domain of Cns1	F: F_UNCLASSIFIED	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF18469	Pleckstrin homology domain (PH_18)	Pleckstrin homology domain	This is a Pleckstrin Homology (PH) domain found on the N-terminal region of the histone chaperone Rtt106 in yeast. Rtt106 binds histone H3 acetylated at lysine 56 (H3K56ac) and facilitates nucleosome assembly during several molecular processes and th ...	This is a Pleckstrin Homology (PH) domain found on the N-terminal region of the histone chaperone Rtt106 in yeast. Rtt106 binds histone H3 acetylated at lysine 56 (H3K56ac) and facilitates nucleosome assembly during several molecular processes and this N-PH domain is shown to mediate histone binding [1].	Domain
A	PF08512	Histone chaperone Rttp106-like, middle domain (Rttp106-like_middle)	Histone chaperone Rttp106-like, middle domain	This Pleckstrin homology (PH) domain is found in the middle region of Rttp106, a histone chaperone involved in heterochromatin-mediated silencing [1]. It is also found in the final part of the middle domain of various FACT (facilitates chromatin tran ...	This Pleckstrin homology (PH) domain is found in the middle region of Rttp106, a histone chaperone involved in heterochromatin-mediated silencing [1]. It is also found in the final part of the middle domain of various FACT (facilitates chromatin transactions) complex subunits, such as Spt16 and either Pob3 (yeast) or the related SSRP1 (higher eukaryotes). This domain plays a role in DNA binding [2-4].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Rtt106p	protein binding binding histone binding DNA binding double-stranded DNA binding nucleic acid binding identical protein binding protein-containing complex binding chromatin binding nucleosome binding	cellular component organization chromatin organization DNA replication-dependent chromatin assembly cellular process cellular component organization or biogenesis regulation of cellular process negative regulation of biological process negative regulation of cellular process chromatin remodeling negative regulation of macromolecule metabolic process regulation of biosynthetic process regulation of biological process heterochromatin formation epigenetic regulation of gene expression cellular component organization chromatin organization DNA replication-dependent chromatin assembly cellular process cellular component organization or biogenesis regulation of cellular process negative regulation of biological process negative regulation of cellular process chromatin remodeling negative regulation of macromolecule metabolic process regulation of biosynthetic process regulation of biological process heterochromatin formation epigenetic regulation of gene expression negative regulation of metabolic process biological regulation regulation of macromolecule metabolic process gene expression macromolecule biosynthetic process regulation of gene expression negative regulation of gene expression biosynthetic process negative regulation of biosynthetic process negative regulation of macromolecule biosynthetic process negative regulation of gene expression, epigenetic regulation of macromolecule biosynthetic process metabolic process macromolecule metabolic process regulation of metabolic process transcription elongation by RNA polymerase II RNA metabolic process primary metabolic process nucleobase-containing compound biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription nucleic acid biosynthetic process DNA-templated transcription elongation transcription by RNA polymerase II regulation of primary metabolic process negative regulation of RNA biosynthetic process regulation of RNA metabolic process negative regulation of nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of transcription by RNA polymerase II negative regulation of DNA-templated transcription negative regulation of transcription by RNA polymerase II regulation of DNA-templated transcription negative regulation of RNA metabolic process transposition	intracellular organelle cellular anatomical structure intracellular anatomical structure organelle membraneless organelle intracellular membraneless organelle chromosome membrane-bounded organelle nucleus intracellular membrane-bounded organelle
B	Box C/D snoRNA protein 1	RNA binding binding snoRNA binding nucleic acid binding cation binding ion binding metal ion binding small molecule binding	nucleobase-containing compound metabolic process sno(s)RNA metabolic process RNA metabolic process metabolic process cellular process primary metabolic process macromolecule metabolic process nucleic acid metabolic process ribonucleoprotein complex biogenesis rRNA processing cellular component biogenesis RNA biosynthetic process ribosome biogenesis nucleic acid biosynthetic process nucleobase-containing compound metabolic process sno(s)RNA metabolic process RNA metabolic process metabolic process cellular process primary metabolic process macromolecule metabolic process nucleic acid metabolic process ribonucleoprotein complex biogenesis rRNA processing cellular component biogenesis RNA biosynthetic process ribosome biogenesis nucleic acid biosynthetic process cellular component organization or biogenesis RNA processing rRNA metabolic process gene expression nucleobase-containing compound biosynthetic process ribosomal large subunit biogenesis macromolecule biosynthetic process maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) biosynthetic process maturation of LSU-rRNA localization macromolecule localization snoRNA localization RNA localization protein-containing complex organization small nucleolar ribonucleoprotein complex assembly protein-RNA complex assembly cellular component organization protein-RNA complex organization cellular component assembly protein-containing complex assembly box C/D snoRNP assembly	protein-containing complex ribonucleoprotein complex pre-snoRNP complex cellular anatomical structure intracellular anatomical structure cytoplasm membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR050454	RTT106/SSRP1 Histone Chaperone/FACT Complex	Family
A	IPR040770	Rtt106, pleckstrin homology domain	Domain
A	IPR011993	PH-like domain superfamily	Homologous Superfamily
A	IPR040993	Histone chaperone Rtt106, N-terminal domain	Domain
A	IPR013719	Histone chaperone RTT106/FACT complex subunit SPT16-like, middle domain	Domain
A	IPR044891	Histone chaperone Rtt106, N-terminal domain superfamily	Homologous Superfamily
B	IPR051639	Box C/D snoRNA	Family
B	IPR007529	Zinc finger, HIT-type	Domain

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 R01GM157729.