Annotations: 4D4O

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C	d4d4oc_	Small proteins	Rubredoxin-like	CSL zinc finger	automated matches	automated matches	BAKER'S YEAST (Saccharomyces cerevisiae ) [TaxId: 4932 ], BAKER'S YEAST (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	CSL zinc finger	8034996	3000501	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	CSL zinc finger	8034996	3000501	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)
B	PF00415	e4d4oB1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PF00415	ECOD (1.6)
C	PF05207	e4d4oC1	A: few secondary structure elements	X: Rubredoxin-like	H: CSL zinc finger (From Topology)	T: CSL zinc finger	F: PF05207	ECOD (1.6)
A	PF00415	e4d4oA2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PF00415	ECOD (1.6)
A	PF05207	e4d4oA1	A: few secondary structure elements	X: Rubredoxin-like	H: CSL zinc finger (From Topology)	T: CSL zinc finger	F: PF05207	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	3.10.660.10	Alpha Beta	Roll	Microbial ribonuclease fold	DPH Zinc finger	CATH (4.3.0)
A	3.10.660.10	Alpha Beta	Roll	Microbial ribonuclease fold	DPH Zinc finger	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF13540	Regulator of chromosome condensation (RCC1) repeat (RCC1_2)	Regulator of chromosome condensation (RCC1) repeat	-	Repeat
A, B, C	PF05207	CSL zinc finger (zf-CSL)	CSL zinc finger	This is a zinc binding motif which contains four cysteine residues which chelate zinc [1]. This domain is often found associated with a Pfam:PF00226 domain. This domain is named after the conserved motif of the final cysteine.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	PROTEIN ATS1, DIPHTHAMIDE BIOSYNTHESIS PROTEIN 3	oxidoreductase activity oxidoreductase activity, acting on iron-sulfur proteins as donors catalytic activity 2-(3-amino-3-carboxypropyl)histidine synthase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on iron-sulfur proteins as donors catalytic activity 2-(3-amino-3-carboxypropyl)histidine synthase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding metallochaperone activity iron chaperone activity molecular carrier activity zinc ion binding aminoacyltransferase activity ubiquitin-like protein transferase activity catalytic activity, acting on a protein acyltransferase activity ubiquitin-like protein ligase activity ubiquitin protein ligase activity ubiquitin-protein transferase activity	cellular biosynthetic process RNA metabolic process tRNA wobble uridine modification nucleobase-containing compound metabolic process organic substance metabolic process tRNA processing tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation organic substance biosynthetic process tRNA wobble base modification RNA processing cellular metabolic process tRNA modification primary metabolic process gene expression cellular biosynthetic process RNA metabolic process tRNA wobble uridine modification nucleobase-containing compound metabolic process organic substance metabolic process tRNA processing tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation organic substance biosynthetic process tRNA wobble base modification RNA processing cellular metabolic process tRNA modification primary metabolic process gene expression macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process organic cyclic compound metabolic process RNA modification biosynthetic process ncRNA metabolic process macromolecule modification nucleic acid catabolic process metabolic process cellular process macromolecule metabolic process organonitrogen compound metabolic process protein histidyl modification to diphthamide peptidyl-histidine modification peptidyl-amino acid modification protein metabolic process protein modification process organonitrogen compound catabolic process catabolic process proteolysis involved in protein catabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process organic substance catabolic process protein ubiquitination post-translational protein modification protein modification by small protein conjugation protein modification by small protein conjugation or removal	intracellular anatomical structure cytoplasm cellular anatomical entity membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR007872	DPH-type metal-binding domain	Domain
A, B, C	IPR036671	DPH-type metal-binding domain superfamily	Homologous Superfamily
A, B, C	IPR000408	Regulator of chromosome condensation, RCC1	Repeat
A, B, C	IPR009091	Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II	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.