A5U229 · DING_MYCTA

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 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

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

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).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site49-56ATP (UniProtKB | ChEBI)
Binding site120[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site192[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site198[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site204[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular FunctionATP binding
Molecular FunctionDNA binding
Molecular FunctionDNA helicase activity
Molecular Functionhydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
Molecular Functionisomerase activity
Molecular Functionmetal ion binding
Biological ProcessDNA recombination
Biological ProcessDNA repair

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent helicase DinG
  • EC number
  • Alternative names
    • DNA 5'-3' helicase DinG

Gene names

    • Name
      dinG
    • Ordered locus names
      MRA_1337

Organism names

Accessions

  • Primary accession
    A5U229

Proteomes

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis55Loss of helicase and ssDNA translocase activity, no change in DNA-binding.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004606241-664ATP-dependent helicase DinG

Structure

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain14-290Helicase ATP-binding
Motif246-249DEAH box

Sequence similarities

Belongs to the helicase family. DinG subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    664
  • Mass (Da)
    70,168
  • Last updated
    2007-07-10 v1
  • Checksum
    875A13606091CDB1
MSESVSMSVPELLAIAVAALGGTRRRGQQEMAAAVAHAFETGEHLVVQAGTGTGKSLAYLVPAIIRALCDDAPVVVSTATIALQRQLVDRDLPQLVDSLTNALPRRPKFALLKGRRNYLCLNKIHNSVTASDHDDERPQEELFDPVAVTALGRDVQRLTAWASTTVSGDRDDLKPGVGDRSWSQVSVSARECLGVARCPFGSECFSERARGAAGLADVVVTNHALLAIDAVAESAVLPEHRLLVVDEAHELADRVTSVAAAELTSATLGMAARRITRLVDPKVTQRLQAASATFSSAIHDARPGRIDCLDDEMATYLSALRDAASAARSAIDTGSDTTTASVRAEAGAVLTEISDTASRILASFAPAIPDRSDVVWLEHEDNHESARAVLRVAPLSVAELLATQVFARATTVLTSATLTIGGSFDAMATAWGLTADTPWRGLDVGSPFQHAKSGILYVAAHLPPPGRDGSGSAEQLTEIAELITAAGGRTLGLFSSMRAARAATEAMRERLSTPVLCQGDDSTSTLVEKFTADAATSLFGTLSLWQGVDVPGPSLSLVLIDRIPFPRPDDPLLSARQRAVAARGGNGFMTVAASHAALLLAQGSGRLLRRVTDRGVVAVLDSRMATARYGEFLRASLPPFWQTTNATQVRAALRRLARADAKAH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000611
EMBL· GenBank· DDBJ
ABQ73079.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp