A5U229 · DING_MYCTA
- ProteinATP-dependent helicase DinG
- GenedinG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids664 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
A structure-dependent 5'-3' DNA helicase that unwinds a number of substrates that resemble intermediates in DNA repair, recombination and replication. Requires 15-25 nucleotides of 3'-overhang single-stranded (ss)DNA for optimal activity (PubMed:25059658).
Unwinds 3'-flap and forked duplex DNA (PubMed:25059658).
Unwinds both lead and lagging strands in replication fork structures (may have branch migration activity) (PubMed:25059658).
Has weak Holliday junction unwinding activity (PubMed:25059658).
In vitro at high concentrations also unwinds in a 3'-5' direction (PubMed:25059658).
Binds best to ssDNA, followed by forked duplex, 3'- and 5'-overhang and 3-strand junction DNA; binds poorly if at all to blunt end double-stranded (ds)DNA substrates (PubMed:25059658).
Translocates on ssDNA with 5'-3' polarity (PubMed:25059658).
Unwinds 3'-flap and forked duplex DNA (PubMed:25059658).
Unwinds both lead and lagging strands in replication fork structures (may have branch migration activity) (PubMed:25059658).
Has weak Holliday junction unwinding activity (PubMed:25059658).
In vitro at high concentrations also unwinds in a 3'-5' direction (PubMed:25059658).
Binds best to ssDNA, followed by forked duplex, 3'- and 5'-overhang and 3-strand junction DNA; binds poorly if at all to blunt end double-stranded (ds)DNA substrates (PubMed:25059658).
Translocates on ssDNA with 5'-3' polarity (PubMed:25059658).
Unwinds G4 DNA (planar arrays of 4 guanine bases stabilized by hydrogen bonds, parallel and antiparallel arrays were tested) with both 5'- and 3'- ss-tails (PubMed:25059658).
Miscellaneous
Dimethyl sulfate protection studies on 3 short, promoter-derived oligonucleotides (18 to 46 bases long) suggest they form G4 DNA structures in vitro (PubMed:25059658).
Catalytic activity
- Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction. This creates two antiparallel DNA single strands (ssDNA). The leading ssDNA polymer is the template for DNA polymerase III holoenzyme which synthesizes a continuous strand.
- ATP + H2O = ADP + phosphate + H+
Cofactor
Activity regulation
Helicase activity on G4 DNA is inhibited by porphyrin derivatives meso-tetra (N-methyl-4-pyridyl) porphine tetra tosylate (T4) and N-methyl mesoporphyrin IX (NMM) (PubMed:25059658).
Helicase activity on forked duplexes is not inhibited by T4 or NMM (PubMed:25059658).
Helicase activity on forked duplexes is not inhibited by T4 or NMM (PubMed:25059658).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 49-56 | ATP (UniProtKB | ChEBI) | ||||
Sequence: AGTGTGKS | ||||||
Binding site | 120 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 192 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 198 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 204 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | DNA helicase activity | |
Molecular Function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides | |
Molecular Function | isomerase activity | |
Molecular Function | metal ion binding | |
Biological Process | DNA recombination | |
Biological Process | DNA repair |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent helicase DinG
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionA5U229
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 55 | Loss of helicase and ssDNA translocase activity, no change in DNA-binding. | ||||
Sequence: K → R |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000460624 | 1-664 | ATP-dependent helicase DinG | |||
Sequence: MSESVSMSVPELLAIAVAALGGTRRRGQQEMAAAVAHAFETGEHLVVQAGTGTGKSLAYLVPAIIRALCDDAPVVVSTATIALQRQLVDRDLPQLVDSLTNALPRRPKFALLKGRRNYLCLNKIHNSVTASDHDDERPQEELFDPVAVTALGRDVQRLTAWASTTVSGDRDDLKPGVGDRSWSQVSVSARECLGVARCPFGSECFSERARGAAGLADVVVTNHALLAIDAVAESAVLPEHRLLVVDEAHELADRVTSVAAAELTSATLGMAARRITRLVDPKVTQRLQAASATFSSAIHDARPGRIDCLDDEMATYLSALRDAASAARSAIDTGSDTTTASVRAEAGAVLTEISDTASRILASFAPAIPDRSDVVWLEHEDNHESARAVLRVAPLSVAELLATQVFARATTVLTSATLTIGGSFDAMATAWGLTADTPWRGLDVGSPFQHAKSGILYVAAHLPPPGRDGSGSAEQLTEIAELITAAGGRTLGLFSSMRAARAATEAMRERLSTPVLCQGDDSTSTLVEKFTADAATSLFGTLSLWQGVDVPGPSLSLVLIDRIPFPRPDDPLLSARQRAVAARGGNGFMTVAASHAALLLAQGSGRLLRRVTDRGVVAVLDSRMATARYGEFLRASLPPFWQTTNATQVRAALRRLARADAKAH |
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-290 | Helicase ATP-binding | ||||
Sequence: AIAVAALGGTRRRGQQEMAAAVAHAFETGEHLVVQAGTGTGKSLAYLVPAIIRALCDDAPVVVSTATIALQRQLVDRDLPQLVDSLTNALPRRPKFALLKGRRNYLCLNKIHNSVTASDHDDERPQEELFDPVAVTALGRDVQRLTAWASTTVSGDRDDLKPGVGDRSWSQVSVSARECLGVARCPFGSECFSERARGAAGLADVVVTNHALLAIDAVAESAVLPEHRLLVVDEAHELADRVTSVAAAELTSATLGMAARRITRLVDPKVTQRLQAA | ||||||
Motif | 246-249 | DEAH box | ||||
Sequence: DEAH |
Sequence similarities
Belongs to the helicase family. DinG subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length664
- Mass (Da)70,168
- Last updated2007-07-10 v1
- Checksum875A13606091CDB1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000611 EMBL· GenBank· DDBJ | ABQ73079.1 EMBL· GenBank· DDBJ | Genomic DNA |