Annotations: 1UW0

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1uw0a_	Small proteins	Glucocorticoid receptor-like (DNA-binding domain)	Glucocorticoid receptor-like (DNA-binding domain)	PARP-type zinc finger	DNA ligase III	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	PARP-type zinc finger	8028558	4003083	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Glucocorticoid receptor-like (DNA-binding domain)	8040937	3000068	SCOP2 (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	PF00645	e1uw0A1	A: few secondary structure elements	X: Glucocorticoid receptor-like	H: LIM domain-like	T: PARP-type zinc finger	F: PF00645	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1740.10	Alpha Beta	2-Layer Sandwich	first zn-finger domain of poly(adp-ribose) polymerase-1	Zinc finger, PARP-type	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00645	Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region (zf-PARP)	Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region	Poly(ADP-ribose) polymerase is an important regulatory component of the cellular response to DNA damage. The amino-terminal region of Poly(ADP-ribose) polymerase consists of two PARP-type zinc fingers. This region acts as a DNA nick sensor.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	DNA LIGASE III	ligase activity, forming phosphoric ester bonds catalytic activity, acting on DNA catalytic activity, acting on a nucleic acid catalytic activity DNA ligase activity ligase activity DNA ligase (ATP) activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding ligase activity, forming phosphoric ester bonds catalytic activity, acting on DNA catalytic activity, acting on a nucleic acid catalytic activity DNA ligase activity ligase activity DNA ligase (ATP) activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding DNA binding nucleic acid binding cation binding transition metal ion binding zinc ion binding metal ion binding	DNA-templated DNA replication lagging strand elongation primary metabolic process DNA metabolic process nucleic acid metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process DNA strand elongation organic substance metabolic process DNA replication metabolic process DNA strand elongation involved in DNA replication macromolecule metabolic process negative regulation of biological process DNA-templated DNA replication lagging strand elongation primary metabolic process DNA metabolic process nucleic acid metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process DNA strand elongation organic substance metabolic process DNA replication metabolic process DNA strand elongation involved in DNA replication macromolecule metabolic process negative regulation of biological process mitochondrial genome maintenance mitochondrial DNA metabolic process regulation of primary metabolic process cellular component organization negative regulation of DNA-templated DNA replication negative regulation of nucleobase-containing compound metabolic process cellular component organization or biogenesis regulation of nucleobase-containing compound metabolic process mitochondrion organization negative regulation of macromolecule metabolic process regulation of biological process negative regulation of DNA replication negative regulation of metabolic process biological regulation regulation of macromolecule metabolic process organelle organization mitochondrial DNA replication negative regulation of mitochondrial DNA replication regulation of DNA-templated DNA replication cellular process negative regulation of DNA metabolic process regulation of mitochondrial DNA replication negative regulation of mitochondrial DNA metabolic process regulation of metabolic process regulation of mitochondrial DNA metabolic process regulation of DNA metabolic process regulation of DNA replication cell division cell cycle cellular biosynthetic process cellular metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid biosynthetic process biosynthetic process organic cyclic compound biosynthetic process organic substance biosynthetic process DNA biosynthetic process cellular response to stimulus response to stimulus base-excision repair, DNA ligation DNA ligation involved in DNA repair DNA ligation base-excision repair cellular response to stress DNA damage response response to stress DNA repair double-strand break repair DNA recombination recombinational repair double-strand break repair via homologous recombination mitochondrial DNA repair base-excision repair, gap-filling double-strand break repair via nonhomologous end joining double-strand break repair via alternative nonhomologous end joining	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle protein-containing complex catalytic complex nucleus nuclear protein-containing complex DNA ligase III-XRCC1 complex membrane-enclosed lumen membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle protein-containing complex catalytic complex nucleus nuclear protein-containing complex DNA ligase III-XRCC1 complex membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036599	DNA ligase, ATP-dependent, N-terminal domain superfamily	Homologous Superfamily
A	IPR036957	Zinc finger, PARP-type superfamily	Homologous Superfamily
A	IPR001357	BRCT domain	Domain
A	IPR012310	DNA ligase, ATP-dependent, central	Domain
A	IPR012308	DNA ligase, ATP-dependent, N-terminal	Domain
A	IPR036420	BRCT domain superfamily	Homologous Superfamily
A	IPR016059	DNA ligase, ATP-dependent, conserved site	Conserved Site
A	IPR000977	DNA ligase, ATP-dependent	Family
A	IPR031916	DNA ligase 3, BRCT domain	Domain
A	IPR001510	Zinc finger, PARP-type	Domain
A	IPR012340	Nucleic acid-binding, OB-fold	Homologous Superfamily
A	IPR012309	DNA ligase, ATP-dependent, C-terminal	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: P49916	atypical teratoid rhabdoid tumor large cell medulloblastoma medulloblastoma primitive neuroectodermal tumor spina bifida breast cancer lung cancer non-small cell lung carcinoma psoriasis subependymal giant cell astrocytoma colorectal cancer malignant mesothelioma osteosarcoma rheumatoid arthritis

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.