8H1E | pdb_00008h1e

Aquifex aeolicus MutL endonuclease domain complexed with manganese ions

External Resource: Annotation

Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF08676	MutL C terminal dimerisation domain (MutL_C)	MutL C terminal dimerisation domain	MutL and MutS are key components of the DNA repair machinery that corrects replication errors [1]. MutS recognises mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The ...	MutL and MutS are key components of the DNA repair machinery that corrects replication errors [1]. MutS recognises mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerisation [3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	DNA mismatch repair protein MutL	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding DNA binding double-stranded DNA binding mismatched DNA binding nucleic acid binding pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity ATP-dependent activity ATP-dependent activity, acting on DNA DNA damage sensor activity molecular sensor activity catalytic activity, acting on DNA ATP-dependent DNA damage sensor activity catalytic activity, acting on a nucleic acid molecular function regulator activity	cellular response to stimulus mismatch repair response to stimulus primary metabolic process DNA metabolic process nucleic acid metabolic process nucleobase-containing compound metabolic process cellular response to stress DNA damage response response to stress metabolic process cellular process macromolecule metabolic process DNA repair	protein-containing complex intracellular anatomical structure cellular anatomical structure mismatch repair complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR038973	DNA mismatch repair protein MutL/Mlh/Pms-like	Family
A	IPR037198	MutL, C-terminal domain superfamily	Homologous Superfamily
A	IPR013507	DNA mismatch repair protein, S5 domain 2-like	Domain
A	IPR014790	MutL, C-terminal, dimerisation	Domain
A	IPR002099	DNA mismatch repair protein MutL/Mlh/PMS	Family
A	IPR036890	Histidine kinase/HSP90-like ATPase superfamily	Homologous Superfamily
A	IPR042120	MutL, C-terminal domain, dimerisation subdomain	Homologous Superfamily
A	IPR014762	DNA mismatch repair, conserved site	Conserved Site
A	IPR020667	DNA mismatch repair protein, MutL	Family
A	IPR020568	Ribosomal protein uS5 domain 2-type superfamily	Homologous Superfamily
A	IPR014721	Small ribosomal subunit protein uS5 domain 2-type fold, subgroup	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.