Q1YLZ8 · Q1YLZ8_AURMS

Function

function

The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA2B2 complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.

Caution

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

Features

Showing features for binding site.

111021002003004005006007008009001,0001,100
TypeIDPosition(s)Description
Binding site226-233ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentexcinuclease repair complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionDNA binding
Molecular Functionexcinuclease ABC activity
Molecular Functionhelicase activity
Biological Processnucleotide-excision repair
Biological ProcessSOS response

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    UvrABC system protein B
  • Short names
    Protein UvrB
  • Alternative names
    • Excinuclease ABC subunit B

Gene names

    • Name
      uvrB
    • ORF names
      SI859A1_02399

Organism names

Accessions

  • Primary accession
    Q1YLZ8

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex.

Family & Domains

Features

Showing features for region, compositional bias, domain, motif, coiled coil.

TypeIDPosition(s)Description
Region1-126Disordered
Compositional bias103-121Polar residues
Domain213-361Helicase ATP-binding
Motif279-302Beta-hairpin
Coiled coil444-471
Domain618-784Helicase C-terminal
Coiled coil808-835
Domain812-847UVR
Region850-871Disordered
Region892-1102Disordered
Compositional bias904-934Basic and acidic residues
Compositional bias993-1019Basic and acidic residues
Compositional bias1035-1059Polar residues
Compositional bias1061-1091Basic and acidic residues

Domain

The beta-hairpin motif is involved in DNA binding.

Sequence similarities

Belongs to the UvrB family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,102
  • Mass (Da)
    119,932
  • Last updated
    2006-05-02 v1
  • Checksum
    0048FF0745B33C2C
MASRSRTTRSRPASDTAEDEAPFDPGAPARRGGFAEAPQADFEAAREFAGPVSGWADEIAQGLETTAEHVADGDNPAPAAAEPEPAKAKAKPAAKSSKAAASTGARPGKTSRGTSMGGTSDPKQRAAAGLNPVAGMDLSLEDAKGLPEGGVTATVDALTKLISEGDPLLKNGEIWVPHRPARPDKSEGGVPFRIASDYTPQGDQPTAIADLVSGITDHDQTQVLLGVTGSGKTFSVANVIERTQRPALILAPNKTLAAQLYGEFKNFFPDNAVEYFVSYYDYYQPEAYVPRSDTFIEKESSINEQIDRMRHAATRALLERDDVIIVASVSCIYGIGSVETYTAMTFQMSIGDRLDQRQLLADLVAQQYKRRDMDFQRGSFRVRGDTIEIFPAHLEDRAWRISLFGDEIESIQEFDPLTGQKTDSLKSVKIYANSHYVTPRPTLNQAVRLIKEELRHRLVELEKAGRLLEAQRLEQRTRFDIEMIEATGSCPGIENYSRYLTGRQPGHPPPTLFEYLPDNALVFIDESHVTVPQIGAMYRGDFRRKATLAEYGFRLPSCMDNRPLRFEEWNAMRPQTVAVSATPGSWEMEEAGGVFAEQVIRPTGLIDPPVEIRPARSQVDDLVGEIRDTVDKGYRVLATVLTKRMAEDLTEYLHEQGIRVRYMHSDIDTLERIEIIRDLRLGAFDVLVGINLLREGLDIPECGLVAILDADKEGFLRSETSLIQTIGRAARNIDGKVILYADRTTGSMERAIAETNRRREKQEAYNAEHGITPASVKAQIADILDSYYEKDHVRVDVGPGAKEGAMVGNNLKSHLEHLEKQMRDAAADLDFETAARLRDEIKRLQAKELEFGGLPGGDSGSGGKKARGGGNVVDAADPMAIAAELEEEAISPVTGRSKYGRKTKRDRQPAGGERFGPRGEPLKPRGEGSDRRPAPLARPPRPGDAAASPAGHDASAPSDGASGQHGGDTAAGSYFQKPSLDDMGPGTDTARPDRPGLFRKNSLDEMTVGRTEKPVGKPAPKKPAPRKPADTASPKADTGSGTGPGMGKSTNTNAPHGEPVEPRTSSDDAAPIRRERIGRGSYEDPTDQKRKRRPGKTGRPGR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias103-121Polar residues
Compositional bias904-934Basic and acidic residues
Compositional bias993-1019Basic and acidic residues
Compositional bias1035-1059Polar residues
Compositional bias1061-1091Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAPJ01000001
EMBL· GenBank· DDBJ
EAS51583.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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