9DCI | pdb_00009dci

Mycobacterium tuberculosis UvrD1 dimer: apo compact conformation.

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, B	PF21196	PcrA/UvrD tudor domain (PcrA_UvrD_tudor)	PcrA/UvrD tudor domain	The PcrA/UvrD helicase binds directly to RNA polymerase (RNAP). This entry represents the C-terminal tudor domain that mediates interaction with RNA polymerase [1-5].	Domain
A, B	PF13361	UvrD-like helicase C-terminal domain (UvrD_C)	UvrD-like helicase C-terminal domain	This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.	Domain
A, B	PF00580	UvrD/REP helicase N-terminal domain (UvrD-helicase)	UvrD/REP helicase N-terminal domain	The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyse ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near t ...	The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyse ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	ATP-dependent DNA helicase UvrD1	ATP-dependent activity, acting on DNA catalytic activity, acting on DNA catalytic activity, acting on a nucleic acid catalytic activity ATP-dependent activity nucleic acid conformation isomerase activity forked DNA-dependent helicase activity isomerase activity DNA helicase activity helicase activity macromolecular conformation isomerase activity cation binding magnesium ion binding ion binding ATP-dependent activity, acting on DNA catalytic activity, acting on DNA catalytic activity, acting on a nucleic acid catalytic activity ATP-dependent activity nucleic acid conformation isomerase activity forked DNA-dependent helicase activity isomerase activity DNA helicase activity helicase activity macromolecular conformation isomerase activity cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding DNA binding nucleic acid binding adenyl deoxyribonucleotide binding deoxyribonucleotide binding purine deoxyribonucleotide binding dATP binding single-stranded DNA helicase activity 3'-5' DNA helicase activity single-stranded 3'-5' DNA helicase activity four-way junction helicase activity 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 double-stranded DNA helicase activity	regulation of DNA recombination regulation of cellular process negative regulation of biological process regulation of primary metabolic process nucleobase-containing compound metabolic process negative regulation of strand invasion negative regulation of cellular process negative regulation of nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process regulation of strand invasion negative regulation of macromolecule metabolic process regulation of biological process DNA recombination negative regulation of metabolic process regulation of DNA recombination regulation of cellular process negative regulation of biological process regulation of primary metabolic process nucleobase-containing compound metabolic process negative regulation of strand invasion negative regulation of cellular process negative regulation of nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process regulation of strand invasion negative regulation of macromolecule metabolic process regulation of biological process DNA recombination negative regulation of metabolic process biological regulation primary metabolic process regulation of macromolecule metabolic process DNA metabolic process DNA strand invasion nucleic acid metabolic process negative regulation of DNA recombination cellular process metabolic process negative regulation of DNA metabolic process macromolecule metabolic process regulation of metabolic process regulation of DNA metabolic process response to light stimulus response to stimulus response to radiation response to abiotic stimulus response to UV UV protection cellular response to stimulus cellular response to stress DNA damage response response to stress recombinational repair DNA repair double-strand break repair	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane external encapsulating structure cell wall peptidoglycan-based cell wall protein-containing complex catalytic complex DNA helicase complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR014017	UvrD-like DNA helicase, C-terminal	Domain
A, B	IPR005751	ATP-dependent DNA helicase PcrA	Family
A, B	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A, B	IPR014016	UvrD-like helicase, ATP-binding domain	Domain
A, B	IPR000212	DNA helicase, UvrD/REP type	Family
A, B	IPR013986	DExx box DNA helicase 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.