A0A4R9J718 · A0A4R9J718_9LEPT

  • Protein
    RecBCD enzyme subunit RecD
  • Gene
    recD
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit has ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-assembled RecBC greatly stimulates nuclease activity and augments holoenzyme processivity. Negatively regulates the RecA-loading ability of RecBCD.

Miscellaneous

In the RecBCD complex, RecB has a slow 3'-5' helicase, an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-3' helicase activity, while RecC stimulates the ATPase and processivity of the RecB helicase and contributes to recognition of the Chi site.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site144-151ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentexodeoxyribonuclease V complex
Molecular Function5'-3' DNA helicase activity
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent H2AZ histone chaperone activity
Molecular FunctionATP-dependent H3-H4 histone complex chaperone activity
Molecular Functionchromatin extrusion motor activity
Molecular Functioncohesin loader activity
Molecular FunctionDNA binding
Molecular FunctionDNA clamp loader activity
Molecular Functionexodeoxyribonuclease V activity
Molecular Functionisomerase activity
Molecular Functionsingle-stranded DNA helicase activity
Biological Processdouble-strand break repair via homologous recombination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    RecBCD enzyme subunit RecD
  • EC number
  • Alternative names
    • DNA 5'-3' helicase subunit RecD
    • Exonuclease V subunit RecD
      (ExoV subunit RecD
      )
    • Helicase/nuclease RecBCD subunit RecD

Gene names

    • Name
      recD
    • ORF names
      EHQ49_18610

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 201702692
  • Taxonomic lineage
    Bacteria > Spirochaetota > Spirochaetia > Leptospirales > Leptospiraceae > Leptospira

Accessions

  • Primary accession
    A0A4R9J718

Proteomes

Subcellular Location

Interaction

Subunit

Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain517-573UvrD-like helicase C-terminal

Sequence similarities

Belongs to the RecD family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    596
  • Mass (Da)
    68,842
  • Last updated
    2019-07-31 v1
  • MD5 Checksum
    ED0B3ECC820B2CC113D69EE196B6F8DB
MKQTESSYLELAKEIITYFPEIQKTHEDLVAKLIEANQNGDLYLSLMDTPSNKDFPNQFPFYIETIGTEKKLFFHKTYKEKIHFESKVKGLLLNHNEDSLNKSDLTKIESTISKLETQFRNPLAPEQKQAVIESISSTFRIIAGGPGTGKTTVVSFILKVLDELQKLPAPNHIALVAPTGRAAQRLTESIQKNLNHFSDTKELASSLRGQTIHNLLRIFPDAPKPYYGEKRYLPFDLIIMDETSMVDLSLMNLFLDSISEKTHLILLGDKNQLPSVGQGEVLRDLLAEFKKQNKFISELKTNHRSKTSSKFSLFAELVKDSFDSPDPQPTFPDPKITESLKGEEDDFIWLQKELPKPTDTIPFKDWKGEELIQFLWKDFFLPTAIKATNLNWKKENLIEEIHKTKLEEMISEHRCLTILRNGFYGIEFIQDRILELAKKQLTSTNTNPHNIEYRHLAKSFYFQGMPIIIKRNDQIRKLFNGDIGLVLKIDSELRAVFPIENRLYSFALDTLPEHEPAFFLTIHKSQGSEYNTILLYLPPIPSFDPENTKEIPLLNRRILYTAVTRAKKKVILMGDYHTWKLGLETFRKRKTGFQLF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RQGA01000021
EMBL· GenBank· DDBJ
TGL33410.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
Help