2FHD

Crystal structure of Crb2 tandem tudor domains

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	KOG3548_1st	e2fhdA3	A: beta barrels	X: SH3	H: SH3	T: SH3	F: KOG3548_1st	ECOD (1.6)
A	KOG3548_2nd	e2fhdA2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: KOG3548_2nd	ECOD (1.6)
B	KOG3548_1st	e2fhdB3	A: beta barrels	X: SH3	H: SH3	T: SH3	F: KOG3548_1st	ECOD (1.6)
B	KOG3548_2nd	e2fhdB2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: KOG3548_2nd	ECOD (1.6)
C	KOG3548_1st	e2fhdC2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: KOG3548_1st	ECOD (1.6)
C	KOG3548_2nd	e2fhdC3	A: beta barrels	X: SH3	H: SH3	T: SH3	F: KOG3548_2nd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.30.30.140	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)
A	2.30.30.810	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)
B	2.30.30.140	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)
B	2.30.30.810	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)
C	2.30.30.140	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)
C	2.30.30.810	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF22520	Crb2, Tudor domain (Crb2_Tudor)	Crb2, Tudor domain	This entry represents a Tudor domain in the DNA repair protein Crb2 from Schizosaccharomyces pombe [1]. Crb2 possesses tandem Tudor domains which interact with histone H4 dimethylated at Lys20 (H4-K20me2).	Domain
A, B, C	PF18115	DNA repair protein Crb2 Tudor domain (Tudor_3)	DNA repair protein Crb2 Tudor domain	This is the tudor domain found in DNA repair protein crb2. Structural and functional studies of Crb2 and its mammalian homologue 53BP1 indicate that the conserved tandem-Tudor domain of 53BP1 and Crb2 preferentially interacts with H4K20me2, though it ...	This is the tudor domain found in DNA repair protein crb2. Structural and functional studies of Crb2 and its mammalian homologue 53BP1 indicate that the conserved tandem-Tudor domain of 53BP1 and Crb2 preferentially interacts with H4K20me2, though it also binds to H4K20me1 [1]. Furthermore, despite low amino acid sequence similarity, Crb2 is structurally related to 53BP1 in having two tudor domains and a conserved dimethyllysine-binding pocket, and that, like 53BP1, it directly binds H4-K20me2 [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	DNA repair protein rhp9/CRB2	protein binding binding histone binding chromatin-protein adaptor activity protein-macromolecule adaptor activity molecular adaptor activity methylated histone binding modification-dependent protein binding methylation-dependent protein binding identical protein binding	cellular response to stimulus regulation of cellular process regulation of cell cycle phase transition response to stimulus signaling G2/M transition of mitotic cell cycle negative regulation of biological process negative regulation of cell cycle cell cycle phase transition intracellular signal transduction mitotic cell cycle negative regulation of mitotic cell cycle cell communication mitotic G2/M transition checkpoint regulation of mitotic cell cycle cellular response to stimulus regulation of cellular process regulation of cell cycle phase transition response to stimulus signaling G2/M transition of mitotic cell cycle negative regulation of biological process negative regulation of cell cycle cell cycle phase transition intracellular signal transduction mitotic cell cycle negative regulation of mitotic cell cycle cell communication mitotic G2/M transition checkpoint regulation of mitotic cell cycle mitotic DNA integrity checkpoint signaling negative regulation of cellular process negative regulation of cell cycle phase transition signal transduction cell cycle DNA replication checkpoint signaling regulation of cell cycle cell cycle process cell cycle G2/M phase transition regulation of biological process mitotic DNA replication checkpoint signaling negative regulation of mitotic cell cycle phase transition regulation of G2/M transition of mitotic cell cycle regulation of cell cycle process biological regulation DNA integrity checkpoint signaling regulation of cell cycle G2/M phase transition negative regulation of cell cycle process cell cycle checkpoint signaling regulation of mitotic cell cycle phase transition mitotic cell cycle checkpoint signaling mitotic cell cycle process negative regulation of cell cycle G2/M phase transition cellular process negative regulation of G2/M transition of mitotic cell cycle mitotic cell cycle phase transition regulation of DNA recombination regulation of double-strand break repair regulation of cellular response to stress regulation of primary metabolic process nucleobase-containing compound metabolic process cellular response to stress response to stress regulation of response to stress recombinational repair regulation of nucleobase-containing compound metabolic process double-strand break repair via homologous recombination DNA repair double-strand break repair DNA recombination primary metabolic process DNA metabolic process regulation of macromolecule metabolic process nucleic acid metabolic process regulation of DNA repair regulation of double-strand break repair via homologous recombination DNA damage response regulation of response to stimulus metabolic process macromolecule metabolic process regulation of metabolic process regulation of DNA metabolic process DNA damage checkpoint signaling mitotic G2 DNA damage checkpoint signaling mitotic DNA damage checkpoint signaling signal transduction in response to DNA damage positive regulation of DNA-templated transcription positive regulation of biological process RNA metabolic process positive regulation of macromolecule biosynthetic process RNA biosynthetic process nucleic acid biosynthetic process positive regulation of metabolic process DNA-templated transcription regulation of RNA metabolic process transcription by RNA polymerase II positive regulation of biosynthetic process positive regulation of macromolecule metabolic process positive regulation of cellular process regulation of RNA biosynthetic process regulation of biosynthetic process regulation of transcription by RNA polymerase II positive regulation of nucleobase-containing compound metabolic process positive regulation of transcription by RNA polymerase II nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process positive regulation of RNA metabolic process regulation of gene expression biosynthetic process positive regulation of RNA biosynthetic process regulation of macromolecule biosynthetic process regulation of DNA-templated transcription negative regulation of nucleobase-containing compound metabolic process negative regulation of macromolecule metabolic process negative regulation of DNA replication negative regulation of metabolic process DNA replication negative regulation of DNA metabolic process regulation of DNA replication	intracellular organelle site of double-strand break cellular anatomical structure intracellular anatomical structure organelle membraneless organelle site of DNA damage intracellular membraneless organelle chromosome chromatin membrane-bounded organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR047249	TP53-binding protein 1-like, first BRCT domain	Domain
A, B, C	IPR047252	TP53-binding protein 1-like	Family
A, B, C	IPR041297	DNA repair protein Crb2, Tudor domain	Domain
A, B, C	IPR001357	BRCT domain	Domain
A, B, C	IPR055249	Crb2, Tudor domain, schizosaccharomyces	Domain
A, B, C	IPR036420	BRCT domain superfamily	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 R01GM157729.