Annotations: 5FRQ

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	DNA_pol3_beta	e5frqA3	A: a+b two layers	X: DNA clamp (From Topology)	H: DNA clamp (From Topology)	T: DNA clamp	F: DNA_pol3_beta	ECOD (1.6)
A	DNA_pol3_beta_2	e5frqA2	A: a+b two layers	X: DNA clamp (From Topology)	H: DNA clamp (From Topology)	T: DNA clamp	F: DNA_pol3_beta_2	ECOD (1.6)
A	DNA_pol3_beta_3	e5frqA1	A: a+b two layers	X: DNA clamp (From Topology)	H: DNA clamp (From Topology)	T: DNA clamp	F: DNA_pol3_beta_3	ECOD (1.6)
B	DNA_pol3_beta	e5frqB2	A: a+b two layers	X: DNA clamp (From Topology)	H: DNA clamp (From Topology)	T: DNA clamp	F: DNA_pol3_beta	ECOD (1.6)
B	DNA_pol3_beta_2	e5frqB1	A: a+b two layers	X: DNA clamp (From Topology)	H: DNA clamp (From Topology)	T: DNA clamp	F: DNA_pol3_beta_2	ECOD (1.6)
B	DNA_pol3_beta_3	e5frqB3	A: a+b two layers	X: DNA clamp (From Topology)	H: DNA clamp (From Topology)	T: DNA clamp	F: DNA_pol3_beta_3	ECOD (1.6)
C	DNA_pol3_beta	e5frqC1	A: a+b two layers	X: DNA clamp (From Topology)	H: DNA clamp (From Topology)	T: DNA clamp	F: DNA_pol3_beta	ECOD (1.6)
C	DNA_pol3_beta_2	e5frqC3	A: a+b two layers	X: DNA clamp (From Topology)	H: DNA clamp (From Topology)	T: DNA clamp	F: DNA_pol3_beta_2	ECOD (1.6)
C	DNA_pol3_beta_3	e5frqC2	A: a+b two layers	X: DNA clamp (From Topology)	H: DNA clamp (From Topology)	T: DNA clamp	F: DNA_pol3_beta_3	ECOD (1.6)
D	DNA_pol3_beta	e5frqD2	A: a+b two layers	X: DNA clamp (From Topology)	H: DNA clamp (From Topology)	T: DNA clamp	F: DNA_pol3_beta	ECOD (1.6)
D	DNA_pol3_beta_2	e5frqD3	A: a+b two layers	X: DNA clamp (From Topology)	H: DNA clamp (From Topology)	T: DNA clamp	F: DNA_pol3_beta_2	ECOD (1.6)
D	DNA_pol3_beta_3	e5frqD1	A: a+b two layers	X: DNA clamp (From Topology)	H: DNA clamp (From Topology)	T: DNA clamp	F: DNA_pol3_beta_3	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.150.10	Alpha Beta	Roll	DNA Polymerase III	Chain A, domain 2	CATH (4.3.0)
B	3.10.150.10	Alpha Beta	Roll	DNA Polymerase III	Chain A, domain 2	CATH (4.3.0)
C	3.10.150.10	Alpha Beta	Roll	DNA Polymerase III	Chain A, domain 2	CATH (4.3.0)
D	3.10.150.10	Alpha Beta	Roll	DNA Polymerase III	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF02768	DNA polymerase III beta subunit, C-terminal domain (DNA_pol3_beta_3)	DNA polymerase III beta subunit, C-terminal domain	A dimer of the beta subunit of DNA polymerase beta forms a ring which encircles duplex DNA. Each monomer contains three domains of identical topology and DNA clamp fold.	Domain
A, B, C, D	PF02767	DNA polymerase III beta subunit, central domain (DNA_pol3_beta_2)	DNA polymerase III beta subunit, central domain	A dimer of the beta subunit of DNA polymerase beta forms a ring which encircles duplex DNA. Each monomer contains three domains of identical topology and DNA clamp fold.	Domain
A, B, C, D	PF00712	DNA polymerase III beta subunit, N-terminal domain (DNA_pol3_beta)	DNA polymerase III beta subunit, N-terminal domain	A dimer of the beta subunit of DNA polymerase beta forms a ring which encircles duplex DNA. Each monomer contains three domains of identical topology and DNA clamp fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
E [auth G], F [auth L]	DNA LIGASE	ligase activity, forming phosphoric ester bonds catalytic activity, acting on DNA catalytic activity, acting on a nucleic acid catalytic activity DNA ligase (NAD+) activity DNA ligase activity ligase activity DNA binding binding organic cyclic compound binding nucleic acid binding cation binding ion binding metal ion binding ligase activity, forming phosphoric ester bonds catalytic activity, acting on DNA catalytic activity, acting on a nucleic acid catalytic activity DNA ligase (NAD+) activity DNA ligase activity ligase activity DNA binding binding organic cyclic compound binding nucleic acid binding cation binding ion binding metal ion binding small molecule binding	nucleobase-containing compound metabolic process DNA replication metabolic process primary metabolic process DNA metabolic process macromolecule metabolic process nucleic acid metabolic 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 nucleobase-containing compound metabolic process DNA replication metabolic process primary metabolic process DNA metabolic process macromolecule metabolic process nucleic acid metabolic 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 cellular process DNA repair	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol
A, B, C, D	DNA POLYMERASE III SUBUNIT BETA	catalytic activity, acting on DNA DNA-directed DNA polymerase activity DNA polymerase activity catalytic activity, acting on a nucleic acid transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups DNA binding binding organic cyclic compound binding nucleic acid binding nuclease activity hydrolase activity, acting on ester bonds catalytic activity, acting on DNA DNA-directed DNA polymerase activity DNA polymerase activity catalytic activity, acting on a nucleic acid transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups DNA binding binding organic cyclic compound binding nucleic acid binding nuclease activity hydrolase activity, acting on ester bonds 3'-5' exonuclease activity hydrolase activity exonuclease activity	nucleobase-containing compound metabolic process DNA strand elongation DNA-templated DNA replication DNA replication metabolic process primary metabolic process DNA strand elongation involved in DNA replication DNA metabolic process macromolecule metabolic process nucleic acid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity transferase complex, transferring phosphorus-containing groups DNA polymerase III complex protein-containing complex catalytic complex transferase complex DNA polymerase complex intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
E [auth G], F [auth L]	IPR001679	NAD-dependent DNA ligase	Family
E [auth G], F [auth L]	IPR010994	RuvA domain 2-like	Homologous Superfamily
E [auth G], F [auth L]	IPR001357	BRCT domain	Domain
E [auth G], F [auth L]	IPR018239	NAD-dependent DNA ligase, active site	Active Site
E [auth G], F [auth L]	IPR013840	NAD-dependent DNA ligase, N-terminal	Domain
E [auth G], F [auth L]	IPR012340	Nucleic acid-binding, OB-fold	Homologous Superfamily
E [auth G], F [auth L]	IPR013839	NAD-dependent DNA ligase, adenylation	Domain
E [auth G], F [auth L]	IPR004150	NAD-dependent DNA ligase, OB-fold	Domain
E [auth G], F [auth L]	IPR033136	NAD-dependent DNA ligase, conserved site	Conserved Site
E [auth G], F [auth L]	IPR003583	Helix-hairpin-helix DNA-binding motif, class 1	Domain
E [auth G], F [auth L]	IPR036420	BRCT domain superfamily	Homologous Superfamily
A, B, C, D	IPR046938	DNA clamp superfamily	Homologous Superfamily
A, B, C, D	IPR022637	DNA polymerase III, beta sliding clamp, central	Domain
A, B, C, D	IPR001001	DNA polymerase III, beta sliding clamp	Family
A, B, C, D	IPR022634	DNA polymerase III, beta sliding clamp, N-terminal	Domain
A, B, C, D	IPR022635	DNA polymerase III, beta sliding clamp, C-terminal	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.