K0F7H5 · K0F7H5_NOCB7
- ProteinRecBCD enzyme subunit RecB
- GenerecB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1141 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA.
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.
Catalytic activity
- ATP + H2O = ADP + phosphate + H+
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | exodeoxyribonuclease V complex | |
Molecular Function | 3'-5' DNA helicase activity | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | DNA binding | |
Molecular Function | exodeoxyribonuclease V activity | |
Molecular Function | isomerase activity | |
Molecular Function | magnesium ion binding | |
Biological Process | double-strand break repair via homologous recombination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRecBCD enzyme subunit RecB
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Nocardia
Accessions
- Primary accessionK0F7H5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with RecA.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-781 | DNA-binding and helicase activity, interacts with RecC | ||||
Sequence: MTVQDTSFVVPEVDGPDAFEPYGPLPTGTTVLEASAGTGKTHAIVGLAVRYVAEAVIDVAELLLVTFSRAATQELRERTRDRFVLVAAGLADPELARAHADDLVRYLAQADPAEVRRRRARLLAALSDFDAGTIATTHSFCQRMLDELGLAGEHDPGARLVESVDELVGTVADDLYLNRYARAEPPFTVKESHTLALAAVQDRHAMLVPAGESAAGERVAFATAVRAETERRKRLAGLRDFDDLLVLLHEVLADPDHGPRACRRIRARYRVALVDEFQDTDPLQWDILRLAFHGHTTMVLVGDPKQAIYAFRGAEVLSYLDAVAHADTRKELTTNWRSDAGLIAALDHLHGGAALGHKEISVYPVAATRPWSRLNGPGELCTPLRVRCLTRTGAGPLNKSGFPAVGRMRAKVADDLAADIVRLLESGTTLDTTPHRPRNSSNDAEQQRNTADADGDALPPEYRPIGPGDIAVLVRTRSQIDVVRAALDRVGVASVLAGGTSVFATSSATDWLWVLRALEQPHRADRVRLAACTPLLGVTAAEIDSGGADLVGRVSAQLRDAARLFARAGFAAVFEKISAEADLAHRLLAVENGERQLTDLRHVAQLLDQVALTESLGLTALTRWLADRVRDPASGTVADRSRRLDRDAAAVQIATVHASKGLEFPIVYLPFAWDNAKNPYPATLLFHDDNGARVLDVGGPDASGYAERKLRSEAEEAGEELRLLYVALTRAMCQVVAWWAPAITTAASPLHRMVLGRPDGGDMVPPRASVPADTAAPGLLS | ||||||
Domain | 13-339 | UvrD-like helicase ATP-binding | ||||
Sequence: VDGPDAFEPYGPLPTGTTVLEASAGTGKTHAIVGLAVRYVAEAVIDVAELLLVTFSRAATQELRERTRDRFVLVAAGLADPELARAHADDLVRYLAQADPAEVRRRRARLLAALSDFDAGTIATTHSFCQRMLDELGLAGEHDPGARLVESVDELVGTVADDLYLNRYARAEPPFTVKESHTLALAAVQDRHAMLVPAGESAAGERVAFATAVRAETERRKRLAGLRDFDDLLVLLHEVLADPDHGPRACRRIRARYRVALVDEFQDTDPLQWDILRLAFHGHTTMVLVGDPKQAIYAFRGAEVLSYLDAVAHADTRKELTTNWRSD | ||||||
Domain | 350-661 | UvrD-like helicase C-terminal | ||||
Sequence: HGGAALGHKEISVYPVAATRPWSRLNGPGELCTPLRVRCLTRTGAGPLNKSGFPAVGRMRAKVADDLAADIVRLLESGTTLDTTPHRPRNSSNDAEQQRNTADADGDALPPEYRPIGPGDIAVLVRTRSQIDVVRAALDRVGVASVLAGGTSVFATSSATDWLWVLRALEQPHRADRVRLAACTPLLGVTAAEIDSGGADLVGRVSAQLRDAARLFARAGFAAVFEKISAEADLAHRLLAVENGERQLTDLRHVAQLLDQVALTESLGLTALTRWLADRVRDPASGTVADRSRRLDRDAAAVQIATVHASKG | ||||||
Compositional bias | 428-448 | Polar residues | ||||
Sequence: TTLDTTPHRPRNSSNDAEQQR | ||||||
Region | 428-461 | Disordered | ||||
Sequence: TTLDTTPHRPRNSSNDAEQQRNTADADGDALPPE | ||||||
Region | 828-1141 | Nuclease activity, interacts with RecD and RecA | ||||
Sequence: NWRRTSYSALTAAAHGPAAVAPELEPEDGREPGDEPEDAPVAALEEVFGGVPSLMNALPYGAEFGTLVHGVLELIDTDAPDLAAEVSERCRAVIGELMAEVDPDLLAAALLAVLRTPMDIGALAGISSRDRLNELEFELPLAGGDAPRAAAATLRRIADLLRAQLPADDDLAGYADQLATLDDLPLRGYLTGSIDAVLRVADGAGTRYVIVDYKTNRLGTGDLTVEHYTRERMAAEMLRSHYPLQALLYSVALHRYLRWRLPGYDPARHLGGARYLFVRGMVGAETPPGHGVFDWDPPAPLIVALSELLAGDVR | ||||||
Region | 841-864 | Disordered | ||||
Sequence: AHGPAAVAPELEPEDGREPGDEPE |
Domain
The C-terminal domain has nuclease activity and interacts with RecD. It interacts with RecA, facilitating its loading onto ssDNA.
The N-terminal DNA-binding domain is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function. This domain interacts with RecC.
Sequence similarities
Belongs to the helicase family. UvrD subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,141
- Mass (Da)122,676
- Last updated2012-11-28 v1
- ChecksumB9800346DE9A5504
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 428-448 | Polar residues | ||||
Sequence: TTLDTTPHRPRNSSNDAEQQR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP003876 EMBL· GenBank· DDBJ | AFU03431.1 EMBL· GenBank· DDBJ | Genomic DNA |